|
Name |
Accession |
Description |
Interval |
E-value |
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
392-694 |
0e+00 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 529.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 392 FFARLKKGLLKTRVNIGSGFASIFSG-KKIDDELFEELETQLLTADLGVDTTMKLIDNLTDAADRKQLKDGDALYELMKQ 470
Cdd:COG0552 1 FFERLKEGLSKTRSGLGEKLKSLFSGkKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKKLKDPEELKEALKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 471 EMASMLKTAEQPLVVSnDKKPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVI 550
Cdd:COG0552 81 ELLEILDPVDKPLAIE-EKKPFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFRAAAIEQLEVWGERVGVPVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 551 AQHTGADSASVVFDAFQAAKARNVDVLIADTAGRLQNKDNLMQELEKIARVMKKIDPDAPHEVMLTIDAGTGQNAISQVK 630
Cdd:COG0552 160 AQKEGADPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVIKKLDPDAPHEVLLVLDATTGQNALSQAK 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201083 631 LFNECVGLTGITLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFIDALFSQD 694
Cdd:COG0552 240 VFNEAVGVTGIVLTKLDGTAKGGVVLAIADELGIPIKFIGVGEGIDDLRPFDAEEFVDALFGEE 303
|
|
| PRK10416 |
PRK10416 |
signal recognition particle-docking protein FtsY; Provisional |
385-695 |
0e+00 |
|
signal recognition particle-docking protein FtsY; Provisional
Pssm-ID: 236686 [Multi-domain] Cd Length: 318 Bit Score: 529.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 385 EKPKKEGFFARLKKGLLKTRVNIGSGFASIFSGKKIDDELFEELETQLLTADLGVDTTMKLIDNLTDAADRKQLKDGDAL 464
Cdd:PRK10416 9 KKEKKEGWFERLKKGLSKTRENFGEGINGLFAKKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKNLKDPEEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 465 YELMKQEMASMLKTAEQPLVVsNDKKPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGER 544
Cdd:PRK10416 89 KELLKEELAEILEPVEKPLNI-EEKKPFVILVVGVNGVGKTTTIGKLAHKYKAQGKKVLLAAGDTFRAAAIEQLQVWGER 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 545 NSIPVIAQHTGADSASVVFDAFQAAKARNVDVLIADTAGRLQNKDNLMQELEKIARVMKKIDPDAPHEVMLTIDAGTGQN 624
Cdd:PRK10416 168 VGVPVIAQKEGADPASVAFDAIQAAKARGIDVLIIDTAGRLHNKTNLMEELKKIKRVIKKADPDAPHEVLLVLDATTGQN 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 625 AISQVKLFNECVGLTGITLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFIDALFSQDE 695
Cdd:PRK10416 248 ALSQAKAFHEAVGLTGIILTKLDGTAKGGVVFAIADELGIPIKFIGVGEGIDDLQPFDAEEFVDALLGGED 318
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
419-691 |
4.51e-128 |
|
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: 380.45 E-value: 4.51e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 419 KIDDELFEELETQLLTADLGVDTTMKLIDNLTDAADRKQLKDGDALYELMKQEMASMLKTAE----QPLVVSNDKKPFVI 494
Cdd:TIGR00064 1 KDDEDFFEELEEILLESDVGYEVVEKIIEALKKELKGKKVKDAEKLKEILKEYLKEILKEDLlkntDLELIVEENKPNVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 495 LMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKARNV 574
Cdd:TIGR00064 81 LFVGVNGVGKTTTIAKLANKLKKQGKSVLLAAGDTFRAAAIEQLEEWAKRLGVDVIKQKEGADPAAVAFDAIQKAKARNI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 575 DVLIADTAGRLQNKDNLMQELEKIARVMKKIDPDAPHEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGTAKGGV 654
Cdd:TIGR00064 161 DVVLIDTAGRLQNKVNLMDELKKIKRVIKKVDKDAPDEVLLVLDATTGQNALEQAKVFNEAVGLTGIILTKLDGTAKGGI 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 1952201083 655 IFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFIDALF 691
Cdd:TIGR00064 241 ILSIAYELKLPIKFIGVGEKIDDLAPFDADWFVEALF 277
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
492-690 |
4.52e-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: 331.07 E-value: 4.52e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 492 FVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKA 571
Cdd:cd17874 1 FVILFVGVNGVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAVEQLEEWAERLGVPVISQNEGADPAAVAFDAIQAAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 572 RNVDVLIADTAGRLQNKDNLMQELEKIARVMKKIDPDAPHEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGTAK 651
Cdd:cd17874 81 RGIDVVLIDTAGRLHTKKNLMEELKKIKRVIKKKDPEAPHEVLLVLDATTGQNALEQAKEFNEAVGLTGIILTKLDGTAK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1952201083 652 GGVIFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFIDAL 690
Cdd:cd17874 161 GGIVLSIADELKIPVKFVGVGEGIDDLRPFDPEAFVEAL 199
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
491-691 |
1.98e-97 |
|
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: 298.17 E-value: 1.98e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 491 PFVILMVGVNGVGKTTTIGKLAKQFQ-NEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAA 569
Cdd:smart00962 1 PGVILLVGPNGVGKTTTIAKLAARLKlKGGKKVLLVAADTFRAAAVEQLKTYAEILGVVPVAGGEGADPVAVAKDAVELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 570 KARNVDVLIADTAGRLQNKDNLMQELEKIARVMKkidpdaPHEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGT 649
Cdd:smart00962 81 KARGYDVVLIDTAGRLHNDENLMEELKKIKRVIK------PDEVLLVSDATTGQDAVEQAKAFNEALGLTGIILTKLDGT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1952201083 650 AKGGVIFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFIDALF 691
Cdd:smart00962 155 AKGGAALSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLL 196
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
492-690 |
1.37e-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: 282.89 E-value: 1.37e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 492 FVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKA 571
Cdd:pfam00448 1 NVILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQLAEKLGVPVFGSKTGADPAAVAFDAVEKAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 572 RNVDVLIADTAGRLQNKDNLMQELEKIARVMKkidpdaPHEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGTAK 651
Cdd:pfam00448 81 ENYDVVLVDTAGRLQNDKNLMDELKKIKRVVA------PDEVLLVLDATTGQNAVNQAKAFNEAVGITGVILTKLDGDAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1952201083 652 GGVIFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFIDAL 690
Cdd:pfam00448 155 GGAALSIVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
492-690 |
1.61e-82 |
|
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: 259.23 E-value: 1.61e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 492 FVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKA 571
Cdd:cd03115 1 NVILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAADTFRAAAVEQLKTLAEKLGVPVFESYTGTDPASIAQEAVEKAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 572 RNVDVLIADTAGRLQNKDNLMQELEKIARVmkkidpDAPHEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGTAK 651
Cdd:cd03115 81 EGYDVLLVDTAGRLQKDEPLMEELKKVKEV------ESPDEVLLVLDATTGQEALSQAKAFNEAVGLTGVILTKLDGTAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1952201083 652 GGVIFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFIDAL 690
Cdd:cd03115 155 GGAALSIVAETKKPIKFIGVGEKPEDLEPFDPERFVSAL 193
|
|
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
357-692 |
2.00e-75 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 246.04 E-value: 2.00e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 357 ERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFFARLKkgllktrvnigsgfASIFSGKKIDDELfEELETQLLTAD 436
Cdd:PRK14974 14 EKVEEKIEEEEEEEAPEAEEEEEEEDEEEKKEKPGFFDKAK--------------ITEIKEKDIEDLL-EELELELLESD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 437 LGVDTTMKLIDNLTDAADRKQLKDGDALYELMKQ-------EMASMLKTAEQPLVVSNDKKPFVILMVGVNGVGKTTTIG 509
Cdd:PRK14974 79 VALEVAEEILESLKEKLVGKKVKRGEDVEEIVKNalkeallEVLSVGDLFDLIEEIKSKGKPVVIVFVGVNGTGKTTTIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 510 KLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKARNVDVLIADTAGRLQNKD 589
Cdd:PRK14974 159 KLAYYLKKNGFSVVIAAGDTFRAGAIEQLEEHAERLGVKVIKHKYGADPAAVAYDAIEHAKARGIDVVLIDTAGRMHTDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 590 NLMQELEKIARVMKkidpdaPHEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGTAKGGVIFAVADKFNIPIRYI 669
Cdd:PRK14974 239 NLMDELKKIVRVTK------PDLVIFVGDALAGNDAVEQAREFNEAVGIDGVILTKVDADAKGGAALSIAYVIGKPILFL 312
|
330 340
....*....|....*....|...
gi 1952201083 670 GVGEGIDDLRTFNSSDFIDALFS 692
Cdd:PRK14974 313 GVGQGYDDLIPFDPDWFVDKLLG 335
|
|
| Ffh |
COG0541 |
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ... |
406-682 |
2.62e-63 |
|
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440307 [Multi-domain] Cd Length: 423 Bit Score: 216.43 E-value: 2.62e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 406 NIGSGFASIF---SGK-KID----DELFEELETQLLTADLGVDTTMKLIDNLTDAA----DRKQLKDGDALYELMKQEMA 473
Cdd:COG0541 4 NLSERLQGAFkklRGKgRLTeeniKEALREVRRALLEADVNLKVVKDFIERVKERAlgeeVLKSLTPGQQVIKIVHDELV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 474 SMLKTAEQPLVVSNdKKPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQH 553
Cdd:COG0541 84 ELLGGENEELNLAK-KPPTVIMMVGLQGSGKTTTAAKLAKYLKKKGKKPLLVAADVYRPAAIEQLKTLGEQIGVPVFPEE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 554 TGADSASVVFDAFQAAKARNVDVLIADTAGRLQNKDNLMQELEKIARVMKkidpdaPHEVMLTIDAGTGQNAISQVKLFN 633
Cdd:COG0541 163 DGKDPVDIAKRALEYAKKNGYDVVIVDTAGRLHIDEELMDELKAIKAAVN------PDETLLVVDAMTGQDAVNVAKAFN 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1952201083 634 ECVGLTGITLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGIDDLRTFN 682
Cdd:COG0541 237 EALGLTGVILTKLDGDARGGAALSIRAVTGKPIKFIGTGEKLDDLEPFH 285
|
|
| SRP_G |
cd18539 |
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ... |
493-681 |
1.07e-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: 198.98 E-value: 1.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 493 VILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKAR 572
Cdd:cd18539 2 VILLVGLQGSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAAIEQLQTLGEQVGVPVFESGDGQSPVDIAKRALEKAKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 573 NVDVLIADTAGRLQNKDNLMQELEKIARVMKkidpdaPHEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGTAKG 652
Cdd:cd18539 82 GFDVVIVDTAGRLHIDEELMDELKEIKEVLN------PDEVLLVVDAMTGQDAVNVAKAFNERLGLTGVVLTKLDGDARG 155
|
170 180
....*....|....*....|....*....
gi 1952201083 653 GVIFAVADKFNIPIRYIGVGEGIDDLRTF 681
Cdd:cd18539 156 GAALSIRHVTGKPIKFIGVGEKIEDLEPF 184
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
406-687 |
2.43e-53 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 190.03 E-value: 2.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 406 NIGSGFASIFSGKKIDDELFEE----LETQLLTADLGVDTTMKLIDNLTDAADRKQLKDG----DALYELMKQEMASMLK 477
Cdd:PRK00771 4 SLRDALKKLAGKSRIDEKTVKEvvkdIQRALLQADVNVKLVKELSKSIKERALEEEPPKGltprEHVIKIVYEELVKLLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 478 TAEQPLVvsNDKKPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGAD 557
Cdd:PRK00771 84 EETEPLV--LPLKPQTIMLVGLQGSGKTTTAAKLARYFKKKGLKVGLVAADTYRPAAYDQLKQLAEKIGVPFYGDPDNKD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 558 SASVVFDAFQAAKarNVDVLIADTAGRLQNKDNLMQELEKIARVMKkidpdaPHEVMLTIDAGTGQNAISQVKLFNECVG 637
Cdd:PRK00771 162 AVEIAKEGLEKFK--KADVIIVDTAGRHALEEDLIEEMKEIKEAVK------PDEVLLVIDATIGQQAKNQAKAFHEAVG 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1952201083 638 LTGITLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFI 687
Cdd:PRK00771 234 IGGIIITKLDGTAKGGGALSAVAETGAPIKFIGTGEKIDDLERFDPDRFI 283
|
|
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
492-690 |
2.62e-47 |
|
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: 165.87 E-value: 2.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 492 FVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKA 571
Cdd:cd17876 1 YVIVFCGVNGVGKSTNLAKIAYWLLSNGFRVLIAACDTFRSGAVEQLRTHARRLGVELYEKGYGKDPAAVAKEAIKYARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 572 RNVDVLIADTAGRLQNKDNLMQELEKIARVMKkidPDApheVMLTIDAGTGQNAISQVKLFNECV----------GLTGI 641
Cdd:cd17876 81 QGFDVVLIDTAGRMQNNEPLMRALAKLIKENN---PDL---VLFVGEALVGNDAVDQLKKFNQALadyspsdnprLIDGI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 642 TLSKLDgTA--KGGVIFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFIDAL 690
Cdd:cd17876 155 VLTKFD-TIddKVGAALSMVYATGQPIVFVGTGQTYTDLKKLNVKAVVNSL 204
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
492-687 |
1.07e-46 |
|
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: 163.90 E-value: 1.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 492 FVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKA 571
Cdd:cd17875 1 NVIMFVGLQGSGKTTTAAKLAYYYQKKGYKVGLVCADTFRAGAFDQLKQNATKARVPFYGSYTEKDPVKIAKEGVEKFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 572 RNVDVLIADTAGRLQNKDNLMQELEKIARVMKkidpdaPHEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGTAK 651
Cdd:cd17875 81 EKFDIIIVDTSGRHKQEEELFEEMKQISDAVK------PDEVILVIDASIGQAAEDQAKAFKEAVDIGSVIITKLDGHAK 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1952201083 652 -GGVIFAVAdKFNIPIRYIGVGEGIDDLRTFNSSDFI 687
Cdd:cd17875 155 gGGALSAVA-ATGAPIIFIGTGEHIDDLEPFDPKRFV 190
|
|
| SRP54_euk |
TIGR01425 |
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ... |
407-690 |
4.02e-37 |
|
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: 144.21 E-value: 4.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 407 IGSGFASIFSGKKIDDE----LFEELETQLLTADLGVDTTMKLIDNLTDAADRKQLKDGDALYELMKQ----EMASMLKT 478
Cdd:TIGR01425 9 LVTALRSMSSATVIDEEvintMLKEICTALLESDVNPKLVRQMRNNIKKKINLEDIASGINKRKLIQDavfeELCNLVDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 479 AEQPLVVSNDKkPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADS 558
Cdd:TIGR01425 89 GVEAFTPKKGK-TCVIMFVGLQGAGKTTTCTKLAYYYKRRGFKPALVCADTFRAGAFDQLKQNATKAGIPFYGSYEESDP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 559 ASVVFDAFQAAKARNVDVLIADTAGRLQNKDNLMQELEKIARVMKkidpdaPHEVMLTIDAGTGQNAISQVKLFNECVGL 638
Cdd:TIGR01425 168 VKIASEGVEKFRKEKFDIIIVDTSGRHKQEKELFEEMQQVREAIK------PDSIIFVMDGSIGQAAFGQAKAFKDSVEV 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1952201083 639 TGITLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFIDAL 690
Cdd:TIGR01425 242 GSVIITKLDGHAKGGGALSAVAATKSPIIFIGTGEHVDEFEIFDAEPFVSKL 293
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
367-691 |
3.45e-33 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 131.14 E-value: 3.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 367 EQAEAERLEQEKVAQAAAEKPKKEGFFARLKKGLLKTRVNIGSGFASIFSGKKIDDELFEELETQLLTADLGVDTTMKLI 446
Cdd:COG1419 50 DEDEAEKAPAAAAAPAAASAAAEEEELEELRRELAELKELLEEQLSGLAGESARLPPELAELLERLLEAGVSPELARELL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 447 DNLtdaadrKQLKDGDALYELMKQEMASMLKTAEQPLVvsndKKPFVILMVGVNGVGKTTTIGKLAKQF-QNEGKSVMLA 525
Cdd:COG1419 130 EKL------PEDLSAEEAWRALLEALARRLPVAEDPLL----DEGGVIALVGPTGVGKTTTIAKLAARFvLRGKKKVALI 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 526 AGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVfdafqaAKARNVDVLIADTAGRLQNKDNLMQELEKIARVMKKI 605
Cdd:COG1419 200 TTDTYRIGAVEQLKTYARILGVPVEVAYDPEELKEAL------ERLRDKDLVLIDTAGRSPRDPELIEELKALLDAGPPI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 606 dpdaphEVMLTIDAGT-GQNAISQVKLFNEcVGLTGITLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGI-DDLRTFNS 683
Cdd:COG1419 274 ------EVYLVLSATTkYEDLKEIVEAFSS-LGLDGLILTKLDETASLGSILNLLIRTGLPLSYITNGQRVpEDIEVADP 346
|
....*...
gi 1952201083 684 SDFIDALF 691
Cdd:COG1419 347 ERLARLLL 354
|
|
| FlhF |
cd17873 |
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ... |
493-678 |
1.25e-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: 113.03 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 493 VILMVGVNGVGKTTTIGKLAKQFQ-NEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAqhtgADSAsvvfDAFQAAKA 571
Cdd:cd17873 2 VIALVGPTGVGKTTTLAKLAARYVlKKGKKVALITTDTYRIGAVEQLKTYAEIMGIPVEV----AEDP----EDLADALE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 572 R--NVDVLIADTAGRLQNKDNLMQELEKIARVMKKIdpdaphEVMLTIDAGT-GQNAISQVKLFnECVGLTGITLSKLDG 648
Cdd:cd17873 74 RlsDRDLILIDTAGRSPRDKEQLEELKELLGAGEDI------EVHLVLSATTkAKDLKEIIERF-SPLGYRGLILTKLDE 146
|
170 180 190
....*....|....*....|....*....|.
gi 1952201083 649 TAKGGVIFAVADKFNIPIRYIGVGEGI-DDL 678
Cdd:cd17873 147 TTSLGSVLSVLAESQLPVSYVTTGQRVpEDI 177
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
315-679 |
3.66e-23 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 102.66 E-value: 3.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 315 EQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFFA 394
Cdd:PRK05703 55 ETPKKNPVLREEKRKPAKSILSLQALLEKRPSRTNSQDALLQAENALPEWKKELEKPSEPKEEEPKAAAESKVVQKELDE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 395 RLK-----KGLLKTRVnigsgfASIFSGKKIDDElFEELETQLLTADLG---VDTTMKLIDNLTDAADRkqlkdgdALYE 466
Cdd:PRK05703 135 LRDelkelKNLLEDQL------SGLRQVERIPPE-FAELYKRLKRSGLSpeiAEKLLKLLLEHMPPRER-------TAWR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 467 LMKQEMASMLKTAEQPLVvsndKKPFVILMVGVNGVGKTTTIGKLAKQF--QNEGKSVMLAAGDTFRAAAVEQLQVWGER 544
Cdd:PRK05703 201 YLLELLANMIPVRVEDIL----KQGGVVALVGPTGVGKTTTLAKLAARYalLYGKKKVALITLDTYRIGAVEQLKTYAKI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 545 NSIPVIaqhtgadsasVVFDAFQAAKA----RNVDVLIADTAGRLQNKDNLMQELEKIARvmkkiDPDAPHEVMLTIDAg 620
Cdd:PRK05703 277 MGIPVE----------VVYDPKELAKAleqlRDCDVILIDTAGRSQRDKRLIEELKALIE-----FSGEPIDVYLVLSA- 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201083 621 TGQN----AIsqVKLFNECvGLTGITLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGI-DDLR 679
Cdd:PRK05703 341 TTKYedlkDI--YKHFSRL-PLDGLIFTKLDETSSLGSILSLLIESGLPISYLTNGQRVpDDIK 401
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
17-392 |
1.16e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.86 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 17 DKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLE 96
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 97 QERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEA 176
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 177 ERLeQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQ 256
Cdd:COG1196 546 AAL-QNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 257 ERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAA 336
Cdd:COG1196 625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEE 704
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1952201083 337 EKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGF 392
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
15-377 |
2.75e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.32 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 15 KSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAE-RLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE 93
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRlELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 94 RLEQERIAAERRDAERvEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEK 173
Cdd:COG1196 320 ELEEELAELEEELEEL-EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 174 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER 253
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 254 LEQERIAAEKAEAERLEQERIAAE--------KAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAE 325
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEADyegflegvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEV 558
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1952201083 326 AERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQE 377
Cdd:COG1196 559 AAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLRE 610
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
18-390 |
5.70e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.55 E-value: 5.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 18 KQQAEQAAKEADNQKQIEEQQ------RIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE--- 88
Cdd:COG1196 206 ERQAEKAERYRELKEELKELEaellllKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELElee 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 89 KAEAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQ 168
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 169 AAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEK 248
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 249 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAE------KAEAERLEQERIVAE 322
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflegvKAALLLAGLRGLAGA 525
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952201083 323 KAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:COG1196 526 VAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALA 593
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
15-399 |
2.49e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 93.28 E-value: 2.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 15 KSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERI---AAEKAEAERLEQEriAAEKAE 91
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELkkaAAAKKKADEAKKK--AEEKKK 1432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 92 AERLEQEriAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAA 171
Cdd:PTZ00121 1433 ADEAKKK--AEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKK 1510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 172 EKAEAERLEQERIAAEKAEAE---RLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE-KAEAERLEQERIAAE 247
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEeakKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEdKNMALRKAEEAKKAE 1590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 248 KAEAERLEQERIAAEKAEAERL---EQERIAAE---KAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVA 321
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAkkaEEAKIKAEelkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA 1670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 322 E----KAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAA--AEKPKKEGFFAR 395
Cdd:PTZ00121 1671 EedkkKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKkeAEEDKKKAEEAK 1750
|
....
gi 1952201083 396 LKKG 399
Cdd:PTZ00121 1751 KDEE 1754
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
17-422 |
3.51e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 92.90 E-value: 3.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 17 DKQQAEQAAKEAD-NQKQIEEQQRIEAEKAEAERLEQEriAAEKAEAERLEQERIAAEKAEaerlEQERIAAEKAEAERL 95
Cdd:PTZ00121 1389 EKKKADEAKKKAEeDKKKADELKKAAAAKKKADEAKKK--AEEKKKADEAKKKAEEAKKAD----EAKKKAEEAKKAEEA 1462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 96 EQEriAAERRDAErvEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAE 175
Cdd:PTZ00121 1463 KKK--AEEAKKAD--EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE 1538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 176 AERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE---KAEAE 252
Cdd:PTZ00121 1539 AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEeakKAEEA 1618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 253 RLEQERIAAEKAEAERLEQ--ERIAAEKAEAERL---EQERIAAEKAEADRLEQERIAAEKA----EAERLEQERIVAEK 323
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQlkKKEAEEKKKAEELkkaEEENKIKAAEEAKKAEEDKKKAEEAkkaeEDEKKAAEALKKEA 1698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 324 AEAERLEQERIAAE----KAEADRLEQE--RIAAEKAEAERLEQERIAEEqAEAERLEQEKVAQAAAEKPKKEGFFARLK 397
Cdd:PTZ00121 1699 EEAKKAEELKKKEAeekkKAEELKKAEEenKIKAEEAKKEAEEDKKKAEE-AKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
410 420
....*....|....*....|....*
gi 1952201083 398 KGLLKTRVNIGSGFASIFSGKKIDD 422
Cdd:PTZ00121 1778 EAVIEEELDEEDEKRRMEVDKKIKD 1802
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
26-390 |
3.26e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 89.82 E-value: 3.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 26 KEADNQKQIEEQQRIEAEK--AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE 103
Cdd:PTZ00121 1194 RKAEDARKAEAARKAEEERkaEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK 1273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 104 RRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLEQER 183
Cdd:PTZ00121 1274 AEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 184 IAAEKAEAERlEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQEriAAEK 263
Cdd:PTZ00121 1354 AAADEAEAAE-EKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKK--AEEK 1430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 264 AEAERLEQEriAAEKAEAERLEQERIAAEKAEadrlEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADR 343
Cdd:PTZ00121 1431 KKADEAKKK--AEEAKKADEAKKKAEEAKKAE----EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKK 1504
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1952201083 344 LEQERIAAEkaEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:PTZ00121 1505 AAEAKKKAD--EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD 1549
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
15-390 |
4.48e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 89.43 E-value: 4.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 15 KSDKQQAEQAAKEADNQKQIEEQQRIEaekaEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAaekAEAER 94
Cdd:PTZ00121 1147 KAEDAKRVEIARKAEDARKAEEARKAE----DAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKA---EEARK 1219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 95 LEQERIAAERRDAERVEQERIAAEKAEAERlaqEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKA 174
Cdd:PTZ00121 1220 AEDAKKAEAVKKAEEAKKDAEEAKKAEEER---NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK 1296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 175 EAERLEQERIAAEKA-EAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER 253
Cdd:PTZ00121 1297 KAEEKKKADEAKKKAeEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 254 LEQERIAAEKAEAERLEQE-RIAAEKAEAERLEQERIAAEKAEADRLEQEriAAEKAEAERLEQERIVAEKA-EAERLEQ 331
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEaKKKAEEDKKKADELKKAAAAKKKADEAKKK--AEEKKKADEAKKKAEEAKKAdEAKKKAE 1454
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1952201083 332 ERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD 1513
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
18-390 |
7.55e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 88.66 E-value: 7.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 18 KQQAEQAAKEADNQKQIEEQQRIEAEKA--EAERLEQERIAAEKAEAERLEQERIAAEKAEAER--------LEQERIAA 87
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAadEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKkadeakkkAEEDKKKA 1407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 88 EKAEAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAE 167
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE 1487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 168 QAAAEKAEAERLEQERIAAEkaEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE 247
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAE--AKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK 1565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 248 KAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEkaEADRLEQERIAAE---KAEAERLEQERIVAEKA 324
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE--EAKKAEEAKIKAEelkKAEEEKKKVEQLKKKEA 1643
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952201083 325 EAERLEQERIAAEKAEADRLEQERIAAE--KAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKKAEedKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
15-390 |
8.44e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 88.66 E-value: 8.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 15 KSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAeAER 94
Cdd:PTZ00121 1195 KAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQA-AIK 1273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 95 LEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKA 174
Cdd:PTZ00121 1274 AEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 175 EAErlEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE--KAEAERLEQERI---AAEKA 249
Cdd:PTZ00121 1354 AAA--DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADElkKAAAAKKKADEAkkkAEEKK 1431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 250 EAERLEQERIAAEKA-EAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAER 328
Cdd:PTZ00121 1432 KADEAKKKAEEAKKAdEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK 1511
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952201083 329 LEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:PTZ00121 1512 ADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE 1573
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
17-390 |
1.07e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 88.27 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 17 DKQQAEQAAKEADNQKQIEEQQRiEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAErlE 96
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKK-KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE--A 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 97 QERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQ-EAAMKLEQERAAAEQAQREAEQAAAEKAE 175
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKaEEKKKADEAKKKAEEAKKADEAKKKAEEA 1456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 176 AERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKA----EAERLEQERIAAEKAEA 251
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAkkaeEAKKADEAKKAEEAKKA 1536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 252 ERLEQERIAAEKAEAERLEQERIAAEKAEAERleqeriaAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQ 331
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKAEEKKKAEE-------AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952201083 332 ERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERL---EQEKVAQAAAEKPKKE 390
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELkkaEEENKIKAAEEAKKAE 1671
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
15-377 |
2.00e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.91 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 15 KSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAEr 94
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE- 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 95 leqeriaAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAA-MKLEQERAAAEQAQREAEQAAAEK 173
Cdd:COG1196 499 -------AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAaLQNIVVEDDEVAAAAIEYLKAAKA 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 174 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER 253
Cdd:COG1196 572 GRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTL 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 254 LEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQER 333
Cdd:COG1196 652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1952201083 334 IAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQE 377
Cdd:COG1196 732 AEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
11-402 |
2.40e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 87.12 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 11 FGFGKSDKQQAEQAAKEAdnQKQIEEQQRIEAEKAEAERLEQEriAAEKAEAERleqeriaaEKAEAERLEQERIAAEKA 90
Cdd:PTZ00121 1079 FDFDAKEDNRADEATEEA--FGKAEEAKKTETGKAEEARKAEE--AKKKAEDAR--------KAEEARKAEDARKAEEAR 1146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 91 EAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAA 170
Cdd:PTZ00121 1147 KAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKA 1226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 171 AEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERL----EQERIAA 246
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAkkaeEKKKADE 1306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 247 EKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAE-KAE 325
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAaKKK 1386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 326 AERLEQERIAAEKAEADRLEQERI---AAEKAEAERLEQEriAEEQAEAERLEQEKVAQAAAEKPKKEGFFARLKKGLLK 402
Cdd:PTZ00121 1387 AEEKKKADEAKKKAEEDKKKADELkkaAAAKKKADEAKKK--AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKK 1464
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
15-404 |
1.23e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.81 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 15 KSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAE---RLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAE 91
Cdd:PTZ00121 1279 KADELKKAEEKKKADEAKKAEEKKKADEAKKKAEeakKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 92 AERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEqaaa 171
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAD---- 1434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 172 ekaeaerlEQERIAAEKAEAERLEQERIAAEKAEaerlEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEA 251
Cdd:PTZ00121 1435 --------EAKKKAEEAKKADEAKKKAEEAKKAE----EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA 1502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 252 ERLEQERIAAEKA----EAERLEQERIAAEKAEAERLeqeRIAAEKAEADRL---EQERIAAE--KAEAERLEQERIVAE 322
Cdd:PTZ00121 1503 KKAAEAKKKADEAkkaeEAKKADEAKKAEEAKKADEA---KKAEEKKKADELkkaEELKKAEEkkKAEEAKKAEEDKNMA 1579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 323 KAEAERLEQ-ERIAAEKAEADRLEQERIAAE---KAEAERLEQERIAEEQAEAERLEQEKVAQA----AAEKPKKEGFFA 394
Cdd:PTZ00121 1580 LRKAEEAKKaEEARIEEVMKLYEEEKKMKAEeakKAEEAKIKAEELKKAEEEKKKVEQLKKKEAeekkKAEELKKAEEEN 1659
|
410
....*....|
gi 1952201083 395 RLKKGLLKTR 404
Cdd:PTZ00121 1660 KIKAAEEAKK 1669
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
17-402 |
2.20e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.04 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 17 DKQQAEQAAKEADNQKQIEEQQRIEAEK--AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER 94
Cdd:PTZ00121 1113 EARKAEEAKKKAEDARKAEEARKAEDARkaEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEE 1192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 95 L---EQERIAAERRDAE---RVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQ 168
Cdd:PTZ00121 1193 LrkaEDARKAEAARKAEeerKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAI 1272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 169 AAAEKAEAERL---EQERIAAEKAEAERLEQERIAAEKA-EAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERI 244
Cdd:PTZ00121 1273 KAEEARKADELkkaEEKKKADEAKKAEEKKKADEAKKKAeEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEA 1352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 245 AAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQEriAAEKAEADRLEQERI---AAEKAEAERLEQERIVA 321
Cdd:PTZ00121 1353 EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE--AKKKAEEDKKKADELkkaAAAKKKADEAKKKAEEK 1430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 322 EKAEaerlEQERIAAEKAEADRLEQERIAAEKAEaerlEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFFARLKKGLL 401
Cdd:PTZ00121 1431 KKAD----EAKKKAEEAKKADEAKKKAEEAKKAE----EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA 1502
|
.
gi 1952201083 402 K 402
Cdd:PTZ00121 1503 K 1503
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
15-390 |
6.74e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 82.50 E-value: 6.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 15 KSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQE-RIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE 93
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADElKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKK 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 94 RLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQ----EAAMKLEQERAAAEQAQREAEQA 169
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkkaDAAKKKAEEKKKADEAKKKAEED 1403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 170 AAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQE--RIAAEKAEAERLEQERIAAE 247
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEakKKAEEAKKADEAKKKAEEAK 1483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 248 KAEAERLEQERIAAEKAEAERLEQERIAAEKA----EAERLEQERIAAEKAEADRLeqeRIAAEKAEAERLEQERIVAEK 323
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAkkaeEAKKADEAKKAEEAKKADEA---KKAEEKKKADELKKAEELKKA 1560
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952201083 324 AEAERLEQERIAAE-KAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEdKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA 1628
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
334-583 |
1.19e-15 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 77.76 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 334 IAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFfARLKKGLLKTRVNIGSGFAS 413
Cdd:TIGR03499 48 AAIDEEEAAAASAEEEASKALEQADPKPLSATAEPLELPAPQEEPAAPAAQAAEPLLPE-EELRKELEALRELLERLLAG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 414 IfsGKKIDDELFEELETQLLTADLGVDTTMKLIDNLtdaadrKQLKDGDALYELMKQEMASML--KTAEQPLvvsnDKKP 491
Cdd:TIGR03499 127 L--AWLQRPPERAKLYERLLEAGVSEELARELLEKL------PEDADAEDAWRWLREALEGMLpvKPEEDPI----LEQG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 492 FVILMVGVNGVGKTTTIGKLAKQF--QNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADsasvvfdaFQAA 569
Cdd:TIGR03499 195 GVIALVGPTGVGKTTTLAKLAARFalEHGKKKVALITTDTYRIGAVEQLKTYAEILGIPVKVARDPKE--------LREA 266
|
250
....*....|....*.
gi 1952201083 570 KA--RNVDVLIADTAG 583
Cdd:TIGR03499 267 LDrlRDKDLILIDTAG 282
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
17-390 |
4.54e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.33 E-value: 4.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 17 DKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLE 96
Cdd:PTZ00121 1051 DIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKA 1130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 97 QERIAAErrDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKleqERAAAEQAQREAEQAAAEKAEA 176
Cdd:PTZ00121 1131 EEARKAE--DARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARK---AEEVRKAEELRKAEDARKAEAA 1205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 177 ERLEQERIAaekAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQ 256
Cdd:PTZ00121 1206 RKAEEERKA---EEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADE 1282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 257 ERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAE-KAEAERLEQERIVAEKAEAERLEQERIA 335
Cdd:PTZ00121 1283 LKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAaKKKAEEAKKAAEAAKAEAEAAADEAEAA 1362
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1952201083 336 AEKAEADRL----EQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:PTZ00121 1363 EEKAEAAEKkkeeAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD 1421
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
30-387 |
1.11e-13 |
|
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: 74.39 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 30 NQKQIEEQQRIEaekaEAERLEQERIAAEKAEAER-LEQERIAAEKAEAERLEQERIAAEKAEAERL------EQERIAA 102
Cdd:pfam17380 280 HQKAVSERQQQE----KFEKMEQERLRQEKEEKAReVERRRKLEEAEKARQAEMDRQAAIYAEQERMamererELERIRQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 103 E--RRDAERVEQERIAAEkaeAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAaeqaqreaeqaaaekaeaerlE 180
Cdd:pfam17380 356 EerKRELERIRQEEIAME---ISRMRELERLQMERQQKNERVRQELEAARKVKILEEE---------------------R 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 181 QERIAAEKAEAERLEQERIAAEKAEAERLEQERiaaeKAEAERLEQEriaaEKAEAERLEQERIAAEKAEAERLEQERIA 260
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEER----AREMERVRLE----EQERQQQVERLRQQEEERKRKKLELEKEK 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 261 AEKAEAErlEQERIAAEKAEAERleQERIAAEKAEADRLEQERIAAEKAEAErlEQERIVAEKAEAERLEQERIAAEKAE 340
Cdd:pfam17380 484 RDRKRAE--EQRRKILEKELEER--KQAMIEEERKRKLLEKEMEERQKAIYE--EERRREAEEERRKQQEMEERRRIQEQ 557
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1952201083 341 ADRLEQERIAAEKAEAERLEQERIAEeqAEAERLEQEKVAQAAAEKP 387
Cdd:pfam17380 558 MRKATEERSRLEAMEREREMMRQIVE--SEKARAEYEATTPITTIKP 602
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
186-390 |
2.69e-13 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 73.44 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 186 AEKAEAERLEQERIAAEKAEaERLE--QERIAAEKAE-AERLEQ--ERIAAEKAEAERLEQERIAAEKAEAerleqERIA 260
Cdd:PRK05035 433 QAKAEIRAIEQEKKKAEEAK-ARFEarQARLEREKAArEARHKKaaEARAAKDKDAVAAALARVKAKKAAA-----TQPI 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 261 AEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAA--EKAEAERLEQERIVAEKAEAERLEQERIAA-- 336
Cdd:PRK05035 507 VIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAaiARAKAKKAAQQAANAEAEEEVDPKKAAVAAai 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1952201083 337 EKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:PRK05035 587 ARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEP 640
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
57-317 |
1.24e-12 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 71.13 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 57 AEKAEAERLEQERIAAEKAeaerleQERIAAEKAEAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQR 136
Cdd:PRK05035 433 QAKAEIRAIEQEKKKAEEA------KARFEARQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPI 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 137 QEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLEQERIAaeKAEAERLEQERIAAEKAEAERLEQERIAA 216
Cdd:PRK05035 507 VIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIA--RAKAKKAAQQAANAEAEEEVDPKKAAVAA 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 217 --EKAEAERLEQERIAAEKAEAERLEQERIAA-----EKAEAERLEQERiAAEKAEAERLEQERIAAE--KAEAERLEQE 287
Cdd:PRK05035 585 aiARAKAKKAAQQAASAEPEEQVAEVDPKKAAvaaaiARAKAKKAEQQA-NAEPEEPVDPRKAAVAAAiaRAKARKAAQQ 663
|
250 260 270
....*....|....*....|....*....|..
gi 1952201083 288 RIAAEKAEADRLEQERIAAE--KAEAERLEQE 317
Cdd:PRK05035 664 QANAEPEEAEDPKKAAVAAAiaRAKAKKAAQQ 695
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
490-616 |
3.42e-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: 64.70 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 490 KPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVwgernsIPVIAQHTGADSASVVFDAFQAA 569
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLL------IIVGGKKASGSGELRLRLALALA 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1952201083 570 KARNVDVLIADTAGRLQNKDNLMQELEKI-ARVMKKIDPDAPHEVMLT 616
Cdd:smart00382 75 RKLKPDVLILDEITSLLDAEQEALLLLLEeLRLLLLLKSEKNLTVILT 122
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
88-390 |
4.50e-12 |
|
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: 69.38 E-value: 4.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 88 EKAEAERLEQERIaaerrdaERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAE 167
Cdd:pfam17380 281 QKAVSERQQQEKF-------EKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 168 QAAAEKAEAERLEQERIAAEKA---EAERLEQERiaaeKAEAERLEQERIAAEKAEAERLEQER-IAAEKAEAERLEQER 243
Cdd:pfam17380 354 RQEERKRELERIRQEEIAMEISrmrELERLQMER----QQKNERVRQELEAARKVKILEEERQRkIQQQKVEMEQIRAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 244 IAAEKAEAERLEQERiaaeKAEAERLEQEriaaEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAErlEQERIVAEK 323
Cdd:pfam17380 430 EEARQREVRRLEEER----AREMERVRLE----EQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE--EQRRKILEK 499
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 324 AEAER----LEQERiAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:pfam17380 500 ELEERkqamIEEER-KRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE 569
|
|
| SRP54_N |
smart00963 |
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle ... |
406-476 |
7.67e-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: 61.41 E-value: 7.67e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201083 406 NIGSGFASIFSGKKIDDELFEELETQLLTADLGVDTTMKLIDNLTDAADR---KQLKDGDALYELMKQEMASML 476
Cdd:smart00963 4 ALGKLLGELFLTEKDDEELLEELEEALLEADVGVEVVKEIIERVKEKAKGevlKGLTPKQEVKKILKEELVKIL 77
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
228-333 |
9.64e-12 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 68.61 E-value: 9.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 228 RIAAEKAEAERLEQERIAAEKAEAERLEQERIA-AEKAEAERLEQERIaaEKAEAERLEQERIAAEKAEADRLEQERIaa 306
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKILEKKRIErLEREERERLERERM--ERIERERLERERLERERLERDRLERDRL-- 504
|
90 100
....*....|....*....|....*..
gi 1952201083 307 ekaeaERLEQERIvaEKAEAERLEQER 333
Cdd:PTZ00266 505 -----DRLERERV--DRLERDRLEKAR 524
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
183-288 |
1.17e-11 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 68.23 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 183 RIAAEKAEAERLEQERIAAEKAEAERLEQERIA-AEKAEAERLEQERIaaEKAEAERLEQERIAAEKAEAERLEQERIaa 261
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKILEKKRIErLEREERERLERERM--ERIERERLERERLERERLERDRLERDRL-- 504
|
90 100
....*....|....*....|....*..
gi 1952201083 262 ekaeaERLEQERIaaEKAEAERLEQER 288
Cdd:PTZ00266 505 -----DRLERERV--DRLERDRLEKAR 524
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
76-386 |
1.18e-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: 66.48 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 76 EAERLEQERIAAEKAEAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQE 155
Cdd:pfam13868 25 DAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 156 RAAAEQAQREAEQAAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKA- 234
Cdd:pfam13868 105 EIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEr 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 235 EAERL--EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAE 312
Cdd:pfam13868 185 EIARLraQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFE 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201083 313 RLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEK 386
Cdd:pfam13868 265 RMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
258-363 |
1.45e-11 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 67.84 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 258 RIAAEKAEAERLEQERIAAEKAEAERLEQERIA-AEKAEADRLEQERIaaEKAEAERLEQERIVAEKAEAERLEQERIaa 336
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKILEKKRIErLEREERERLERERM--ERIERERLERERLERERLERDRLERDRL-- 504
|
90 100
....*....|....*....|....*..
gi 1952201083 337 ekaeaDRLEQERIaaEKAEAERLEQER 363
Cdd:PTZ00266 505 -----DRLERERV--DRLERDRLEKAR 524
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
89-398 |
5.85e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 5.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 89 KAEAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQ 168
Cdd:PTZ00121 1061 EAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDAR 1140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 169 AAAEKAEAERLEQERIAAEKAEAERLEQERIAAEkaeAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEk 248
Cdd:PTZ00121 1141 KAEEARKAEDAKRVEIARKAEDARKAEEARKAED---AKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEE- 1216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 249 aeAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAER 328
Cdd:PTZ00121 1217 --ARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADE 1294
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 329 LeqeRIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFFARLKK 398
Cdd:PTZ00121 1295 A---KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
|
| flhF |
PRK14722 |
flagellar biosynthesis regulator FlhF; Provisional |
326-677 |
7.55e-11 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173185 [Multi-domain] Cd Length: 374 Bit Score: 64.36 E-value: 7.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 326 AERLEQERIAAEKAeADRLEQERIAAE----KAEAERLEQERIAEEQAEAERLEQEKVAQAA-AEKPKKEGFFARLKKGL 400
Cdd:PRK14722 5 ARRLPADEPAAAKP-ALRLPEDTAAAVadavKARIERIVNDTVMQELGSLRELMEEQFAGLMwNERQRRNPVHGALTKYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 401 lktrvnigsgFASIFSGKKIddelfeeletqlltadlgvdttMKLIDNLTDAADRKQLkdgDALYELMKQEMASMLktae 480
Cdd:PRK14722 84 ----------FAAGFSAQLV----------------------RMIVDNLPEGEGYDTL---DAAADWAQSVLAANL---- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 481 qPLVVSND---KKPFVILMVGVNGVGKTTTIGKLAKQ--FQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTG 555
Cdd:PRK14722 125 -PVLDSEDalmERGGVFALMGPTGVGKTTTTAKLAARcvMRFGASKVALLTTDSYRIGGHEQLRIFGKILGVPVHAVKDG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 556 ADSASVVfdafqaAKARNVDVLIADTAGRLQNKDNLMQELEKIArvmkkiDPDAPHEVMLTIDAGTGQNAISQV-KLFNE 634
Cdd:PRK14722 204 GDLQLAL------AELRNKHMVLIDTIGMSQRDRTVSDQIAMLH------GADTPVQRLLLLNATSHGDTLNEVvQAYRS 271
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 635 CVG--------LTGITLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGIDD 677
Cdd:PRK14722 272 AAGqpkaalpdLAGCILTKLDEASNLGGVLDTVIRYKLPVHYVSTGQKVPE 322
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
14-114 |
1.28e-10 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 64.76 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 14 GKSDKQQAEQAAKEADN------QKQIEEQQRIE-AEKAEAERLEQERIaaekaeaERLEQERIAAEKAEAERLEQERIa 86
Cdd:PTZ00266 428 GRVDKDHAERARIEKENahrkalEMKILEKKRIErLEREERERLERERM-------ERIERERLERERLERERLERDRL- 499
|
90 100
....*....|....*....|....*...
gi 1952201083 87 aEKAEAERLEQERIaaERRDAERVEQER 114
Cdd:PTZ00266 500 -ERDRLDRLERERV--DRLERDRLEKAR 524
|
|
| PRK12726 |
PRK12726 |
flagellar biosynthesis regulator FlhF; Provisional |
493-677 |
1.70e-10 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183704 [Multi-domain] Cd Length: 407 Bit Score: 63.60 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 493 VILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAqhtgADSASVVFDAFQAAKAR 572
Cdd:PRK12726 208 IISLIGQTGVGKTTTLVKLGWQLLKQNRTVGFITTDTFRSGAVEQFQGYADKLDVELIV----ATSPAELEEAVQYMTYV 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 573 N-VDVLIADTAGRlqnkdNLMQElEKIARVMKKIDPDAPHEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGTAK 651
Cdd:PRK12726 284 NcVDHILIDTVGR-----NYLAE-ESVSEISAYTDVVHPDLTCFTFSSGMKSADVMTILPKLAEIPIDGFIITKMDETTR 357
|
170 180
....*....|....*....|....*.
gi 1952201083 652 GGVIFAVADKFNIPIRYIGVGEGIDD 677
Cdd:PRK12726 358 IGDLYTVMQETNLPVLYMTDGQNITE 383
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
187-389 |
1.98e-10 |
|
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: 63.82 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 187 EKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQEriaaekaEAERLEQERIAAEKAEA 266
Cdd:pfam15709 326 EKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELE-------QQRRFEEIRLRKQRLEE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 267 ERLEQERIAAEKAEAERLEQERIAAEKAEADR-LEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADRLE 345
Cdd:pfam15709 399 ERQRQEEEERKQRLQLQAAQERARQQQEEFRRkLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLE 478
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1952201083 346 QERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKK 389
Cdd:pfam15709 479 YQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
288-395 |
2.98e-10 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 63.60 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 288 RIAAEKAEADRLEQERIAAEKAEAERLEQERIV-AEKAEAERLEQERIaaEKAEADRLEQERIAAEKAEAERLEQERIAE 366
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKILEKKRIErLEREERERLERERM--ERIERERLERERLERERLERDRLERDRLDR 506
|
90 100 110
....*....|....*....|....*....|
gi 1952201083 367 -EQAEAERLEQEKVaqaaaEKPKKEGFFAR 395
Cdd:PTZ00266 507 lERERVDRLERDRL-----EKARRNSYFLK 531
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
493-687 |
3.24e-10 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 63.09 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 493 VILMVGVNGVGKTTTIGKLAKQF--QNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPViaqHTgADSASVVFDAFQaaK 570
Cdd:PRK12727 352 VIALVGPTGAGKTTTIAKLAQRFaaQHAPRDVALVTTDTQRVGGREQLHSYGRQLGIAV---HE-ADSAESLLDLLE--R 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 571 ARNVDVLIADTAGRLQNKDNLMQELE--KIARVMKKidpdaphevMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDG 648
Cdd:PRK12727 426 LRDYKLVLIDTAGMGQRDRALAAQLNwlRAARQVTS---------LLVLPANAHFSDLDEVVRRFAHAKPQGVVLTKLDE 496
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1952201083 649 TAKGGVIFAVADKFNIPIRYIGVGEGI-DDLRTFNSSDFI 687
Cdd:PRK12727 497 TGRFGSALSVVVDHQMPITWVTDGQRVpDDLHRANAASLV 536
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
72-382 |
4.49e-10 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 63.04 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 72 AEKAEAERLEQERIAAEKAEaERLE--QERIaaerrdaERVEQERIAAEKAEAERLAQEQQAAEQqrqeqqarlaeqeAA 149
Cdd:PRK05035 433 QAKAEIRAIEQEKKKAEEAK-ARFEarQARL-------EREKAAREARHKKAAEARAAKDKDAVA-------------AA 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 150 MkleqeraaaeqaqreaeqaaaEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERI 229
Cdd:PRK05035 492 L---------------------ARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAV 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 230 AA--EKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAErleqeriaAEKAEAERLEQERIAAEKAEADRLEQERIAAE 307
Cdd:PRK05035 551 AAaiARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAK--------AKKAAQQAASAEPEEQVAEVDPKKAAVAAAIA 622
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952201083 308 KAEAERLEQERiVAEKAEAERLEQERIAAE--KAEADRLEQERIAAEKAEAERLEQERIAeeqAEAERLEQEKVAQA 382
Cdd:PRK05035 623 RAKAKKAEQQA-NAEPEEPVDPRKAAVAAAiaRAKARKAAQQQANAEPEEAEDPKKAAVA---AAIARAKAKKAAQQ 695
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
28-362 |
5.55e-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: 61.47 E-value: 5.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 28 ADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERiaaEKAEAERLEQERIAAEKAEAERLEQERIAAERRDA 107
Cdd:pfam13868 22 KERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEK---EEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 108 ERVEQERIAAEKAEAERlaqeqqaaeqqrQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLEQERIAAE 187
Cdd:pfam13868 99 EREQMDEIVERIQEEDQ------------AEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 188 KAEAERLEQERIAAEKAEaeRLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE 267
Cdd:pfam13868 167 REEEREAEREEIEEEKER--EIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 268 RLEQERIAAEKAEAERLEQERIAAEKAEADRLEQEriAAEKAEAERL----EQERIVAEKAEAERLEQERIAAEKAEADR 343
Cdd:pfam13868 245 IELKERRLAEEAEREEEEFERMLRKQAEDEEIEQE--EAEKRRMKRLehrrELEKQIEEREEQRAAEREEELEEGERLRE 322
|
330
....*....|....*....
gi 1952201083 344 LEQERIAAEKAEAERLEQE 362
Cdd:pfam13868 323 EEAERRERIEEERQKKLKE 341
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
17-317 |
1.73e-09 |
|
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: 59.93 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 17 DKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAA--EKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER 94
Cdd:pfam13868 40 EEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEqiEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 95 LEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKA 174
Cdd:pfam13868 120 EKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 175 EAerlEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERL 254
Cdd:pfam13868 200 KA---ERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEI 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952201083 255 EQERIA--AEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQE 317
Cdd:pfam13868 277 EQEEAEkrRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
15-297 |
1.90e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 15 KSDKQQAEQAAKEADNQKQIEEQQRI-EAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIaaekAEAE 93
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKAdELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI----EEVM 1598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 94 RLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEK 173
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE 1678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 174 AEAERLEQERIAAEKAEAErlEQERIAAEKAEAERLEQERIAAE--KAEAERLEQERIAAEKAEAERLEQERIAAEKAEA 251
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKE--AEEAKKAEELKKKEAEEKKKAEElkKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1952201083 252 ERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAD 297
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
185-404 |
2.35e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.93 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 185 AAEKAEAERLEQERIAAEkaEAERLEQERIAAEKAEAE---RLEQER---IAAEKAEAERLEQERIAAEKAEAERLEQER 258
Cdd:PTZ00121 1120 AKKKAEDARKAEEARKAE--DARKAEEARKAEDAKRVEiarKAEDARkaeEARKAEDAKKAEAARKAEEVRKAEELRKAE 1197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 259 IAAEKAEAERLEQERIAaekAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEK 338
Cdd:PTZ00121 1198 DARKAEAARKAEEERKA---EEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA 1274
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952201083 339 AEADRLEQERIAAEKAEAERLeqeRIAEEQAEAERLEQEKVAQAAAEKPKKEGFFARLKKGLLKTR 404
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKADEA---KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKK 1337
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
39-125 |
5.74e-09 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 59.75 E-value: 5.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 39 RIEAEKAEAERLEQERIAAEKAEAERLEQERIA-AEKAEAERLEQERIaaEKAEAERLEQERIAAERRDAERVEQERI-A 116
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKILEKKRIErLEREERERLERERM--ERIERERLERERLERERLERDRLERDRLdR 506
|
....*....
gi 1952201083 117 AEKAEAERL 125
Cdd:PTZ00266 507 LERERVDRL 515
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
174-389 |
8.13e-09 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 58.81 E-value: 8.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 174 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER 253
Cdd:PRK05035 465 EKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAAD 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 254 LEQERIAA--EKAEAERLEQERIAAEKAEAERLEQERIAA--EKAEADRLEQERIAAEKAEAERLEQERIVA-----EKA 324
Cdd:PRK05035 545 PKKAAVAAaiARAKAKKAAQQAANAEAEEEVDPKKAAVAAaiARAKAKKAAQQAASAEPEEQVAEVDPKKAAvaaaiARA 624
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952201083 325 EAERLEQERIAAEKAEAD-RLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAE-KPKK 389
Cdd:PRK05035 625 KAKKAEQQANAEPEEPVDpRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARaKAKK 691
|
|
| SRP54_N |
pfam02881 |
SRP54-type protein, helical bundle domain; |
407-472 |
9.74e-09 |
|
SRP54-type protein, helical bundle domain;
Pssm-ID: 460734 [Multi-domain] Cd Length: 75 Bit Score: 52.47 E-value: 9.74e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 407 IGSGFASIFSGKKIDDELFEE----LETQLLTADLGVDTTMKLIDNLTDAA-DRKQLKDGDALYELMKQEM 472
Cdd:pfam02881 5 LSSLFKGLRGKGKIDEEDLEEalkeLEEALLEADVGVEVVKKIIERLREKAvGEKKLKPPQEVKKILKEEL 75
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
179-258 |
1.02e-08 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 58.60 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 179 LEQERIA-AEKAEAERLEQERIaaEKAEAERLEQERIAAEKAEAERLEQERIaaekaeaERLEQERIaaEKAEAERLEQE 257
Cdd:PTZ00266 455 LEKKRIErLEREERERLERERM--ERIERERLERERLERERLERDRLERDRL-------DRLERERV--DRLERDRLEKA 523
|
.
gi 1952201083 258 R 258
Cdd:PTZ00266 524 R 524
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
18-325 |
1.03e-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: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 18 KQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERL---EQERIAAEKAEAER 94
Cdd:pfam13868 35 KAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLqerEQMDEIVERIQEED 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 95 LEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAeka 174
Cdd:pfam13868 115 QAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRA--- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 175 eaerlEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERL 254
Cdd:pfam13868 192 -----QQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERM 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 255 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAE 325
Cdd:pfam13868 267 LRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQK 337
|
|
| flhF |
PRK06731 |
flagellar biosynthesis regulator FlhF; Validated |
488-675 |
1.38e-08 |
|
flagellar biosynthesis regulator FlhF; Validated
Pssm-ID: 75717 [Multi-domain] Cd Length: 270 Bit Score: 56.68 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 488 DKKPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHtgaDSASVVFDAFQ 567
Cdd:PRK06731 72 EKEVQTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAVR---DEAAMTRALTY 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 568 AAKARNVDVLIADTAGRLQNKDnlmQELEKIARVMKKIDPDApheVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLD 647
Cdd:PRK06731 149 FKEEARVDYILIDTAGKNYRAS---ETVEEMIETMGQVEPDY---ICLTLSASMKSKDMIEIITNFKDIHIDGIVFTKFD 222
|
170 180
....*....|....*....|....*...
gi 1952201083 648 GTAKGGVIFAVADKFNIPIRYIGVGEGI 675
Cdd:PRK06731 223 ETASSGELLKIPAVSSAPIVLMTDGQDV 250
|
|
| PRK12724 |
PRK12724 |
flagellar biosynthesis regulator FlhF; Provisional |
493-675 |
1.62e-08 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183703 [Multi-domain] Cd Length: 432 Bit Score: 57.28 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 493 VILMVGVNGVGKTTTIGKLA-KQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTgadsasvvFDAFQAAKA 571
Cdd:PRK12724 225 VVFFVGPTGSGKTTSIAKLAaKYFLHMGKSVSLYTTDNYRIAAIEQLKRYADTMGMPFYPVKD--------IKKFKETLA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 572 RNVDVLI-ADTAGRLQNKdnlMQELEKIARVMKKIDPDAPHEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGTA 650
Cdd:PRK12724 297 RDGSELIlIDTAGYSHRN---LEQLERMQSFYSCFGEKDSVENLLVLSSTSSYHHTLTVLKAYESLNYRRILLTKLDEAD 373
|
170 180
....*....|....*....|....*
gi 1952201083 651 KGGVIFAVADKFNIPIRYIGVGEGI 675
Cdd:PRK12724 374 FLGSFLELADTYSKSFTYLSVGQEV 398
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
63-388 |
2.55e-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: 57.33 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 63 ERLEQERIAAEKAEAErLEQERIAAEKAEAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQAR 142
Cdd:NF033838 99 EYLYELNVLKEKSEAE-LTSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPTNTYKTLELE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 143 LAEQEAAMKLEQERAAAEQAQREAEQAAAEKAeaerleQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE 222
Cdd:NF033838 178 IAESDVEVKKAELELVKEEAKEPRDEEKIKQA------KAKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEK 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 223 RLEQERIAAEKAEAER--LEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEkAEAERLEQERIAAEKAEADRLE 300
Cdd:NF033838 252 NVATSEQDKPKRRAKRgvLGEPATPDKKENDAKSSDSSVGEETLPSPSLKPEKKVAE-AEKKVEEAKKKAKDQKEEDRRN 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 301 QERIAAEKAEAERLEQERIVAEkAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLE----QERIAEEQAEAERLEQ 376
Cdd:NF033838 331 YPTNTYKTLELEIAESDVKVKE-AELELVKEEAKEPRNEEKIKQAKAKVESKKAEATRLEkiktDRKKAEEEAKRKAAEE 409
|
330
....*....|..
gi 1952201083 377 EKVAQAAAEKPK 388
Cdd:NF033838 410 DKVKEKPAEQPQ 421
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
15-257 |
3.22e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 56.88 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 15 KSDKQQAEQAAKEADNQKQIEE--QQRIEAEKAE-AERLEQ--ERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE- 88
Cdd:PRK05035 435 KAEIRAIEQEKKKAEEAKARFEarQARLEREKAArEARHKKaaEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARp 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 89 ------KAEAERLEQERIAAERRDAERVEQERIAA-----EKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERA 157
Cdd:PRK05035 515 dnsaviAAREARKAQARARQAEKQAAAAADPKKAAvaaaiARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKA 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 158 AAEQAQREAEQAAAEKAEAERLEQERIAAEKAEAERLEQERIAAEkAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE 237
Cdd:PRK05035 595 AQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEE-PVDPRKAAVAAAIARAKARKAAQQQANAEPEEAE 673
|
250 260
....*....|....*....|..
gi 1952201083 238 RLEQERIAAE--KAEAERLEQE 257
Cdd:PRK05035 674 DPKKAAVAAAiaRAKAKKAAQQ 695
|
|
| flhF |
PRK11889 |
flagellar biosynthesis protein FlhF; |
488-675 |
3.32e-08 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 183360 [Multi-domain] Cd Length: 436 Bit Score: 56.61 E-value: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 488 DKKPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHtgaDSASVVFDAFQ 567
Cdd:PRK11889 238 EKEVQTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAVR---DEAAMTRALTY 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 568 AAKARNVDVLIADTAGRlqnKDNLMQELEKIARVMKKIDPDApheVMLTIDAG-TGQNAISQVKLFNEcVGLTGITLSKL 646
Cdd:PRK11889 315 FKEEARVDYILIDTAGK---NYRASETVEEMIETMGQVEPDY---ICLTLSASmKSKDMIEIITNFKD-IHIDGIVFTKF 387
|
170 180
....*....|....*....|....*....
gi 1952201083 647 DGTAKGGVIFAVADKFNIPIRYIGVGEGI 675
Cdd:PRK11889 388 DETASSGELLKIPAVSSAPIVLMTDGQDV 416
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
233-390 |
5.04e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 56.03 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 233 KAEAERLEQERIAaeKAEAERLEQERIA-----AEKAEAERlEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAE 307
Cdd:COG2268 192 RKIAEIIRDARIA--EAEAERETEIAIAqanreAEEAELEQ-EREIETARIAEAEAELAKKKAEERREAETARAEAEAAY 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 308 KAEAERLEQERI----VAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAErleqeriAEEQAEAERLEQEKVAQAA 383
Cdd:COG2268 269 EIAEANAEREVQrqleIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAE-------AEAEAEAEAIRAKGLAEAE 341
|
....*..
gi 1952201083 384 AEKPKKE 390
Cdd:COG2268 342 GKRALAE 348
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
189-390 |
1.05e-07 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 55.38 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 189 AEAERLEQE--RIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE--KAEAERLEQERIAAEKAEAERL----EQERIA 260
Cdd:PRK14900 842 AETARVDKEigKVDQDLAVLERKLQNPSFVQNAPPAVVEKDRARAEelREKRGKLEAHRAMLSGSEANSArrdtMEIQNE 921
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 261 AEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAE 340
Cdd:PRK14900 922 QKPTQDGPAAEAQPAQENTVVESAEKAVAAVSEAAQQAATAVASGIEKVAEAVRKTVRRSVKKAAATRAAMKKKVAKKAP 1001
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1952201083 341 ADRLEQERIAAEKAEAerleqERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:PRK14900 1002 AKKAAAKKAAAKKAAA-----KKKVAKKAPAKKVARKPAAKKAAKKPARK 1046
|
|
| PRK12723 |
PRK12723 |
flagellar biosynthesis regulator FlhF; Provisional |
490-675 |
1.32e-07 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183702 [Multi-domain] Cd Length: 388 Bit Score: 54.52 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 490 KPFVILMVGVNGVGKTTTIGKLAKQF----QNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDa 565
Cdd:PRK12723 173 KKRVFILVGPTGVGKTTTIAKLAAIYginsDDKSLNIKIITIDNYRIGAKKQIQTYGDIMGIPVKAIESFKDLKEEITQ- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 566 fqaakARNVDVLIADTAGRlQNKDNLmqELEKIARVMKKIDPDAphEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSK 645
Cdd:PRK12723 252 -----SKDFDLVLVDTIGK-SPKDFM--KLAEMKELLNACGRDA--EFHLAVSSTTKTSDVKEIFHQFSPFSYKTVIFTK 321
|
170 180 190
....*....|....*....|....*....|
gi 1952201083 646 LDGTAKGGVIFAVADKFNIPIRYIGVGEGI 675
Cdd:PRK12723 322 LDETTCVGNLISLIYEMRKEVSYVTDGQIV 351
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
180-409 |
1.33e-07 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 54.66 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 180 EQERIAAEKAEAERLEQERIAAEKAEAERL---EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQ 256
Cdd:COG3064 15 QERLEQAEAEKRAAAEAEQKAKEEAEEERLaelEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 257 ERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAA 336
Cdd:COG3064 95 AEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952201083 337 EKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFFARLKKGLLKTRVNIGS 409
Cdd:COG3064 175 AAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGG 247
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
212-660 |
1.49e-07 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 54.66 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 212 ERIAAEKAEAERLEQERiAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAA 291
Cdd:COG3064 6 EEKAAEAAAQERLEQAE-AEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 292 EKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEA 371
Cdd:COG3064 85 AAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 372 ERLEQEKVAQAAAEKPKKEGFFARLKKGLLKTRVNIGSGFASIFSGKKIDDELFEELETQLLTADLGVDTTMKLIDNLTD 451
Cdd:COG3064 165 AAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 452 AADRKQLKDGDALYELMKQEMASMLKTAEQPLVVSNDKkpfVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFR 531
Cdd:COG3064 245 LGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVA---AALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 532 AAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKARNVDVLIADTAGRLQNKDNLMQELEKIARVMKKIDPDAPH 611
Cdd:COG3064 322 AAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLL 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1952201083 612 EVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGTAKGGVIFAVAD 660
Cdd:COG3064 402 GLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVG 450
|
|
| flhF |
PRK14723 |
flagellar biosynthesis regulator FlhF; Provisional |
493-691 |
1.69e-07 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 237802 [Multi-domain] Cd Length: 767 Bit Score: 54.81 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 493 VILMVGVNGVGKTTTIGKLAKQF-QNEGKS-VMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADsasvVFDAFQAAK 570
Cdd:PRK14723 187 VLALVGPTGVGKTTTTAKLAARCvAREGADqLALLTTDSFRIGALEQLRIYGRILGVPVHAVKDAAD----LRFALAALG 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 571 ARNVdVLIaDTAGRLQNKDNLMQELEKIARVmkkidpDAPHEVMLTIdagtgqNAISQVKLFNECV---------GLTGI 641
Cdd:PRK14723 263 DKHL-VLI-DTVGMSQRDRNVSEQIAMLCGV------GRPVRRLLLL------NAASHGDTLNEVVhayrhgageDVDGC 328
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 642 TLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGI-DDLRTFNSSDFIDALF 691
Cdd:PRK14723 329 IITKLDEATHLGPALDTVIRHRLPVHYVSTGQKVpEHLELAQADELVDRAF 379
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
187-390 |
1.93e-07 |
|
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: 53.77 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 187 EKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEA 266
Cdd:pfam13868 83 EEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 267 ERLEQERIAAEKAEAERLEQERIAAEKAEadrlEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQ 346
Cdd:pfam13868 163 EKAEREEEREAEREEIEEEKEREIARLRA----QQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQ 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1952201083 347 ERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:pfam13868 239 QAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAE 282
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
200-410 |
2.26e-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: 53.31 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 200 AAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKA 279
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 280 EaeRLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERL 359
Cdd:TIGR02794 126 A--KQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKA 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 360 EQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFFARLKKGLLKTRVNIGSG 410
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARG 254
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
179-376 |
2.78e-07 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 54.23 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 179 LEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE-------KAEAER---LEQERIAAEKAEAErlEQERIAAEK 248
Cdd:TIGR00927 630 LSKGDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEqegetetKGENESegeIPAERKGEQEGEGE--IEAKEADHK 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 249 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIA----AEKAEADRLEQERIAAEKAEAERLEQE-RIVAEK 323
Cdd:TIGR00927 708 GETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAegkhEVETEGDRKETEHEGETEAEGKEDEDEgEIQAGE 787
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952201083 324 ----------AEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQ 376
Cdd:TIGR00927 788 dgemkgdegaEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEK 850
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
10-366 |
4.06e-07 |
|
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: 53.44 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 10 WFGFGKSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEK 89
Cdd:pfam02463 657 GLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINE 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 90 AEAERLEQERIAAERRDAERVEQERIAAEKAEAE--RLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAE 167
Cdd:pfam02463 737 ELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSlkEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAEL 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 168 QAAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE 247
Cdd:pfam02463 817 LEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEK 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 248 KAEAERLEQERIAAEKAEAERLEQERIAAEK-------AEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIV 320
Cdd:pfam02463 897 EEKKELEEESQKLNLLEEKENEIEERIKEEAeillkyeEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVN 976
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1952201083 321 AEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAE 366
Cdd:pfam02463 977 LMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEF 1022
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
19-385 |
4.48e-07 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 53.32 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 19 QQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQE 98
Cdd:COG3899 726 RYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGD 805
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 99 RIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAER 178
Cdd:COG3899 806 YEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAA 885
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 179 LEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQER 258
Cdd:COG3899 886 LAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAA 965
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 259 IAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEK 338
Cdd:COG3899 966 AAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALAL 1045
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1952201083 339 AEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAE 385
Cdd:COG3899 1046 LAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAAL 1092
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
180-375 |
5.84e-07 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 53.08 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 180 EQERIAAEKAEAErLEQERIAAEKAEAErlEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERI 259
Cdd:TIGR00927 672 ETETKGENESEGE-IPAERKGEQEGEGE--IEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGE 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 260 A----AEKAEAERLEQERIAAEKAEAERLEQE-RIAAEK----------AEADRLEQERIAAEKAEAERLEQERIVAEKA 324
Cdd:TIGR00927 749 AegkhEVETEGDRKETEHEGETEAEGKEDEDEgEIQAGEdgemkgdegaEGKVEHEGETEAGEKDEHEGQSETQADDTEV 828
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201083 325 EAERLEQERIAAEKAEA-------------DRLEQERIAAEKAEAERLEQERIAEEQAEAERLE 375
Cdd:TIGR00927 829 KDETGEQELNAENQGEAkqdekgvdggggsDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEE 892
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
15-371 |
5.95e-07 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 52.73 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 15 KSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER 94
Cdd:COG3064 12 AAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 95 LEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKA 174
Cdd:COG3064 92 KAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 175 EAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERL 254
Cdd:COG3064 172 ARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 255 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERI 334
Cdd:COG3064 252 ADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRG 331
|
330 340 350
....*....|....*....|....*....|....*..
gi 1952201083 335 AAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEA 371
Cdd:COG3064 332 GGAASLEAALSLLAAGAAAAAAGAGALATGALGDALA 368
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
183-372 |
7.90e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 51.73 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 183 RIAAEKAEAERLEQERIAAEKAEAERLEQErIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE 262
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQK-QAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 263 KAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEAD 342
Cdd:PRK09510 145 AKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAK 224
|
170 180 190
....*....|....*....|....*....|
gi 1952201083 343 RLEQERIAAEKAEAERLEQERIAEEQAEAE 372
Cdd:PRK09510 225 AAAAKAAAEAKAAAEKAAAAKAAEKAAAAK 254
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
13-405 |
9.85e-07 |
|
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: 52.28 E-value: 9.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 13 FGKSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEA 92
Cdd:pfam02463 625 VEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKK 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 93 ERLEQERIAAERRDAERVEQERI--AAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAA 170
Cdd:pfam02463 705 EQREKEELKKLKLEAEELLADRVqeAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTE 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 171 AEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAE 250
Cdd:pfam02463 785 KLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEIT 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 251 AERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKA--EAERLEQERIVAEKAEAER 328
Cdd:pfam02463 865 KEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIkeEAEILLKYEEEPEELLLEE 944
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952201083 329 LEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFFARLKKGLLKTRV 405
Cdd:pfam02463 945 ADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
17-385 |
1.20e-06 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 51.58 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 17 DKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERL-------EQERIAAEKAEAERLEQERIAAEK 89
Cdd:COG3064 37 EEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAaaeaekkAAAEKAKAAKEAEAAAAAEKAAAA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 90 AEAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQA 169
Cdd:COG3064 117 AEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 170 AAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKA 249
Cdd:COG3064 197 AAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 250 EAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERL 329
Cdd:COG3064 277 GLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAG 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1952201083 330 EQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAE 385
Cdd:COG3064 357 ALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALL 412
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
143-396 |
1.29e-06 |
|
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: 51.98 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 143 LAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE 222
Cdd:TIGR02168 689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 223 RLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQEriAAEKAEAERLEQERIAAEKAEADRLEQe 302
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE--AANLRERLESLERRIAATERRLEDLEE- 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 303 RIAAEKAEAERLEQErIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQA 382
Cdd:TIGR02168 846 QIEELSEDIESLAAE-IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
250
....*....|....
gi 1952201083 383 AAEKPKKEGFFARL 396
Cdd:TIGR02168 925 AQLELRLEGLEVRI 938
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
186-411 |
1.30e-06 |
|
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: 51.98 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 186 AEKAEAERLEQERIAAEKAEAERLEQE-RIAAEKAEAERLEQERIAA--EKAEAERLEQERIAAEKAEAERLEQERIAAE 262
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISRLEQQkQILRERLANLERQLEELEAqlEELESKLDELAEELAELEEKLEELKEELESL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 263 KAEAERLEQERIAAEKAEAErLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEA-ERLEQERIAAEKAEA 341
Cdd:TIGR02168 357 EAELEELEAELEELESRLEE-LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLqQEIEELLKKLEEAEL 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 342 DRLeQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFFARLKKGLLKTRVNIGSGF 411
Cdd:TIGR02168 436 KEL-QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF 504
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
180-390 |
1.69e-06 |
|
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: 50.69 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 180 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQER---------IAAEKAEAERLEQERIAAEKAE 250
Cdd:pfam13868 52 ERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEReqmdeiverIQEEDQAEAEEKLEKQRQLREE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 251 AERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAA------EKAEAERLEQERIVAEKA 324
Cdd:pfam13868 132 IDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIArlraqqEKAQDEKAERDELRAKLY 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952201083 325 EAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:pfam13868 212 QEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIE 277
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
11-344 |
1.70e-06 |
|
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: 51.60 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 11 FGFGKSDKQQAEQAAKEADNQKQIEEQQRIEAE--------KAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQ 82
Cdd:TIGR02168 663 GGSAKTNSSILERRREIEELEEKIEELEEKIAElekalaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 83 ERIAAEKAEAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQqrqeqqarlaeQEAAMKLEQERAAAEQA 162
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL-----------KEELKALREALDELRAE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 163 QREAEQAAAEKAEAERLEQERIAAEKAEAERLEQeRIAAEKAEAERLEQERIAAEkaeaERLEQERIAAEKAEAERLEQE 242
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLEDLEE-QIEELSEDIESLAAEIEELE----ELIEELESELEALLNERASLE 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 243 RIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEkaeaERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAE 322
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELR----EKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENK 962
|
330 340
....*....|....*....|..
gi 1952201083 323 KAEAERLEQERIAAEKAEADRL 344
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKEL 984
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
17-267 |
1.90e-06 |
|
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: 51.28 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 17 DKQQAEQAAKEADNQKQIEEQQRIEAE--KAEAERLEQERIAAEKA---EAERLEQERiaaeKAEAERLEQERIAAEKAE 91
Cdd:pfam17380 330 DRQAAIYAEQERMAMERERELERIRQEerKRELERIRQEEIAMEISrmrELERLQMER----QQKNERVRQELEAARKVK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 92 AERLEQER-IAAERRDAERVEQERIAAEKAEAERLAQEQQ-------AAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQ 163
Cdd:pfam17380 406 ILEEERQRkIQQQKVEMEQIRAEQEEARQREVRRLEEERAremervrLEEQERQQQVERLRQQEEERKRKKLELEKEKRD 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 164 REAEQAAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQER 243
Cdd:pfam17380 486 RKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEER 565
|
250 260
....*....|....*....|....*
gi 1952201083 244 IAAEKAEAER-LEQERIAAEKAEAE 267
Cdd:pfam17380 566 SRLEAMEREReMMRQIVESEKARAE 590
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
181-400 |
2.19e-06 |
|
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: 50.53 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 181 QERIAAEKAEAERLEQERIAAEKaEAERLEQERIAAEKAEAERleQERIAAEKAEAERLEQERIAAEKAEAERleQERIA 260
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLK-QLAALERRIAALARRIRAL--EQELAALEAELAELEKEIAELRAELEAQ--KEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 261 AEKAEAERLEQERIAAEKAEAERLEQ----ERIAAEKAEADRLEQERIAAEKAEAERLEQErIVAEKAEAERLEQERIAA 336
Cdd:COG4942 108 ELLRALYRLGRQPPLALLLSPEDFLDavrrLQYLKYLAPARREQAEELRADLAELAALRAE-LEAERAELEALLAELEEE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952201083 337 EKA-EADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQE----KVAQAAAEKPKKEGFFARLKKGL 400
Cdd:COG4942 187 RAAlEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiarlEAEAAAAAERTPAAGFAALKGKL 255
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
194-391 |
2.64e-06 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 50.76 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 194 LEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEaerlEQERIAAEKAEAErLEQERIAAEKAEAErlEQER 273
Cdd:TIGR00927 630 LSKGDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEG----ETETKGENESEGE-IPAERKGEQEGEGE--IEAK 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 274 IAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQER----IVAEKAEAERLEQERIAAEKAEADRLEQE-- 347
Cdd:TIGR00927 703 EADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGeaegKHEVETEGDRKETEHEGETEAEGKEDEDEge 782
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 348 -------RIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEG 391
Cdd:TIGR00927 783 iqagedgEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETG 833
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
198-385 |
4.13e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.80 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 198 RIAAEKAEAERLEQERIAAEKAEAERLEQErIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERlEQERIAAE 277
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQK-QAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAE-EAAAKAAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 278 KAEAERLEQERIAAE-----KAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAE 352
Cdd:PRK09510 144 AAKAKAEAEAKRAAAaakkaAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEA 223
|
170 180 190
....*....|....*....|....*....|...
gi 1952201083 353 KAEAERLEQERIAEEQAEAERLEQEKVAQAAAE 385
Cdd:PRK09510 224 KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
180-356 |
6.68e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.03 E-value: 6.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 180 EQERIAAEKAEAERLEQErIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEK---AEAERLEQERIAAEKAEAERLEQ 256
Cdd:PRK09510 78 EEQRKKKEQQQAEELQQK-QAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKqkqAEEAAAKAAAAAKAKAEAEAKRA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 257 ERIAAE-KAEAERLEQERIAAEKAEAERLEQERIAAEKAEAD-RLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERI 334
Cdd:PRK09510 157 AAAAKKaAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEaKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKA 236
|
170 180
....*....|....*....|..
gi 1952201083 335 AAEKAEADRLEQERIAAEKAEA 356
Cdd:PRK09510 237 AAEKAAAAKAAEKAAAAKAAAE 258
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
23-396 |
8.75e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 8.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 23 QAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAA------EKAEAERLEQERIAAEKAEAE---RLEQERIAAEKA--E 91
Cdd:PRK02224 264 RETIAETEREREELAEEVRDLRERLEELEEERDDLlaeaglDDADAEAVEARREELEDRDEElrdRLEECRVAAQAHneE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 92 AERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAA 171
Cdd:PRK02224 344 AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 172 EKAEAERLEQERIAAEK--AEAERL-------EQERIAAEKAEAERLEQERIAAEKAEAE----RLEQERIAAEKAEAER 238
Cdd:PRK02224 424 LREREAELEATLRTARErvEEAEALleagkcpECGQPVEGSPHVETIEEDRERVEELEAEledlEEEVEEVEERLERAED 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 239 L-EQERIAAEKAEAERLEQERIAAEKAEAERlEQERIAAEKAEAERLEQEriaAEKAEADRLEQERIAAEKAEAERLEQE 317
Cdd:PRK02224 504 LvEAEDRIERLEERREDLEELIAERRETIEE-KRERAEELRERAAELEAE---AEEKREAAAEAEEEAEEAREEVAELNS 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 318 RIVAEKAEAERLE-----QERIAAEKAEADRLEQERiaAEKAEAERLEQERIAEE----QAEAERLEQEKVAQAAAEKPK 388
Cdd:PRK02224 580 KLAELKERIESLErirtlLAAIADAEDEIERLREKR--EALAELNDERRERLAEKrerkRELEAEFDEARIEEAREDKER 657
|
....*...
gi 1952201083 389 KEGFFARL 396
Cdd:PRK02224 658 AEEYLEQV 665
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
15-372 |
9.00e-06 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.88 E-value: 9.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 15 KSDKQQAEQAAKEADNQKQIEE-QQRIEAEKA----EAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEK 89
Cdd:COG3064 67 RAAELAAEAAKKLAEAEKAAAEaEKKAAAEKAkaakEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 90 AEAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQA 169
Cdd:COG3064 147 EAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 170 AAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKA 249
Cdd:COG3064 227 AASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 250 EAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERL 329
Cdd:COG3064 307 LLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEA 386
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1952201083 330 EQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAE 372
Cdd:COG3064 387 AGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGA 429
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
18-390 |
9.78e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 9.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 18 KQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLE-QERIAAEKAEAERLeQERIAAEKAEAERLEQERIAAeKAEAERLE 96
Cdd:PRK02224 229 REQARETRDEADEVLEEHEERREELETLEAEIEDlRETIAETEREREEL-AEEVRDLRERLEELEEERDDL-LAEAGLDD 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 97 QERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEA 176
Cdd:PRK02224 307 ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEI 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 177 ERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE-RLEQERIAAEKAE-------------------- 235
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEaTLRTARERVEEAEalleagkcpecgqpvegsph 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 236 AERLEQERIAAEKAEAE----RLEQERIAAEKAEAERL-EQERIAAEKAEAERLEQERIAAEKAEADRlEQERIAAEKAE 310
Cdd:PRK02224 467 VETIEEDRERVEELEAEledlEEEVEEVEERLERAEDLvEAEDRIERLEERREDLEELIAERRETIEE-KRERAEELRER 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 311 AERLEQErivAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLE-----QERIAEEQAEAERLEQEKVAQAAAE 385
Cdd:PRK02224 546 AAELEAE---AEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLErirtlLAAIADAEDEIERLREKREALAELN 622
|
....*
gi 1952201083 386 KPKKE 390
Cdd:PRK02224 623 DERRE 627
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
180-356 |
1.16e-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: 47.92 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 180 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAErleQERIAAEKAEAERLEQERIAAEKAEAERLEQERI 259
Cdd:TIGR02794 87 EQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQA---AEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 260 AAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKA 339
Cdd:TIGR02794 164 AKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASG 243
|
170
....*....|....*..
gi 1952201083 340 EADRLEQERIAAEKAEA 356
Cdd:TIGR02794 244 SNAEKQGGARGAAAGSE 260
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
46-382 |
1.17e-05 |
|
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: 48.68 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 46 EAERLEQERIAAEKAEAERLEqeRIAAEKAEAERLEQERIAAEKAEAE--RLEQERIAAERRDAERvEQERIAAEKAEAE 123
Cdd:pfam12128 214 PKSRLNRQQVEHWIRDIQAIA--GIMKIRPEFTKLQQEFNTLESAELRlsHLHFGYKSDETLIASR-QEERQETSAELNQ 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 124 RLAQEQQAAEQQRQEQQARLAEQEAAMKleqeraaaeqaqREAEQAAAEKAEAERLEQERIAAEKAEAERLEQERIAAEK 203
Cdd:pfam12128 291 LLRTLDDQWKEKRDELNGELSAADAAVA------------KDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELEN 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 204 AEAE-RLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE-RLEQERIAAEKAEA 281
Cdd:pfam12128 359 LEERlKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESElREQLEAGKLEFNEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 282 ERLEQERIAAEKAeadrleqeRIAAEKAEAERLEQERIVAEKAEAERLEQEriaAEKAEADRLEQERIAAEKA-----EA 356
Cdd:pfam12128 439 EYRLKSRLGELKL--------RLNQATATPELLLQLENFDERIERAREEQE---AANAEVERLQSELRQARKRrdqasEA 507
|
330 340
....*....|....*....|....*.
gi 1952201083 357 ERLEQERIAEEQAEAERLEQEKVAQA 382
Cdd:pfam12128 508 LRQASRRLEERQSALDELELQLFPQA 533
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
17-377 |
1.26e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 17 DKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLE 96
Cdd:COG4717 120 KLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 97 -----QERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMkLEQERAAAEQAQREAEQAAA 171
Cdd:COG4717 200 eleelQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAAL-LALLGLGGSLLSLILTIAGV 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 172 EKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEA 251
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 252 ERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQ 331
Cdd:COG4717 359 LEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELE 438
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1952201083 332 ERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQE 377
Cdd:COG4717 439 EELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAE 484
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
182-391 |
1.27e-05 |
|
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: 48.68 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 182 ERIAAEKAEAERLEQEriaaEKAEA--ERLEQER------IAAEKAEAERLEQERIAAeKAEAER----LEQERIAAEKA 249
Cdd:NF012221 1549 KHAKQDDAAQNALADK----ERAEAdrQRLEQEKqqqlaaISGSQSQLESTDQNALET-NGQAQRdailEESRAVTKELT 1623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 250 E-AERLEQERIAAEKAE----------AERLeQERIAAEKAEAERLEQERIAAEK-AEADRLEQERIAAEKAEA--ERLE 315
Cdd:NF012221 1624 TlAQGLDALDSQATYAGesgdqwrnpfAGGL-LDRVQEQLDDAKKISGKQLADAKqRHVDNQQKVKDAVAKSEAgvAQGE 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 316 QERIVAE------KAEAERLEQERIAAEKAEADRLEQERIAAEKAEaERLEQE-RIAEEQAEAERLEQEKVAQAAAEKPK 388
Cdd:NF012221 1703 QNQANAEqdiddaKADAEKRKDDALAKQNEAQQAESDANAAANDAQ-SRGEQDaSAAENKANQAQADAKGAKQDESDKPN 1781
|
...
gi 1952201083 389 KEG 391
Cdd:NF012221 1782 RQG 1784
|
|
| Agg_substance |
NF033875 |
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ... |
181-366 |
1.40e-05 |
|
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: 48.55 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 181 QERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQER-IAAEKAEAERLEQ-ERIAAEKAEAERL---- 254
Cdd:NF033875 80 QKDTTSQPTKVEEVASEKNGAEQSSATPNDTTNAQQPTVGAEKSAQEQpVVSPETTNEPLGQpTEVAPAENEANKStsip 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 255 -EQERIAAEKAEAERLEQERIAAEKAEAERL---EQERIAAEKAEADRLEQEriaaekaeaerleQERIVAEKAEAERLE 330
Cdd:NF033875 160 kEFETPDVDKAVDEAKKDPNITVVEKPAEDLgnvSSKDLAAKEKEVDQLQKE-------------QAKKIAQQAAELKAK 226
|
170 180 190
....*....|....*....|....*....|....*..
gi 1952201083 331 QERIAAEKAEadrleqerIAAE-KAEAERLEQErIAE 366
Cdd:NF033875 227 NEKIAKENAE--------IAAKnKAEKERYEKE-VAE 254
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
261-391 |
1.58e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.95 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 261 AEKAEAERLEQERIAAEKAEAE----RLEQERI--AAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQErI 334
Cdd:COG2268 201 ARIAEAEAERETEIAIAQANREaeeaELEQEREieTARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAERE-V 279
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952201083 335 AAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEG 391
Cdd:COG2268 280 QRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKG 336
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
228-389 |
1.79e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.49 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 228 RIAAEKAEAERLEQERIAAEKAEAERLEQErIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEK---AEADRLEQERI 304
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQK-QAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKqkqAEEAAAKAAAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 305 AAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAA 384
Cdd:PRK09510 145 AKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAK 224
|
....*
gi 1952201083 385 EKPKK 389
Cdd:PRK09510 225 AAAAK 229
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
168-328 |
1.79e-05 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 47.98 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 168 QAAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERlEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE 247
Cdd:PRK12678 64 AAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEA-APAARAAAAAAAEAASAPEAAQARERRERGEAARRGAA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 248 KAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERiaaekaEADRLEQERIAAEKAEAERLEQERIVAEKAEAE 327
Cdd:PRK12678 143 RKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQA------EAERGERGRREERGRDGDDRDRRDRREQGDRRE 216
|
.
gi 1952201083 328 R 328
Cdd:PRK12678 217 E 217
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
45-385 |
2.37e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 47.93 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 45 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAERRDAERVEQERIAAEKAEAER 124
Cdd:COG3899 722 AEALRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLL 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 125 LAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKA 204
Cdd:COG3899 802 LLGDYEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAA 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 205 EAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERL 284
Cdd:COG3899 882 AAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALA 961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 285 EQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERI 364
Cdd:COG3899 962 AAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAA 1041
|
330 340
....*....|....*....|.
gi 1952201083 365 AEEQAEAERLEQEKVAQAAAE 385
Cdd:COG3899 1042 ALALLAALAAAAAAAAAAAAL 1062
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
18-463 |
2.47e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 47.34 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 18 KQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERI----AAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE 93
Cdd:COG3064 7 EKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLaeleAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 94 RLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEK 173
Cdd:COG3064 87 AEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 174 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERiAAEKAEAERLEQERIAAEKAEAER 253
Cdd:COG3064 167 AAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAV-AARAAAASREAALAAVEATEEAAL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 254 LEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQER 333
Cdd:COG3064 246 GGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 334 IAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFFARLKKGLLKTRVNIGSGFAS 413
Cdd:COG3064 326 ALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRL 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1952201083 414 IFSGKKIDDELFEELETQLLTADLGVDTTMKLIDNLTDAADRKQLKDGDA 463
Cdd:COG3064 406 DLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKAL 455
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
42-284 |
2.89e-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: 47.07 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 42 AEKAEAERLEQERIAAEKAEAErlEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAERRDAERVEQERIAAEKAE 121
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAE--LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 122 AERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLEQerIAAEKAEAERLEQERIAA 201
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE--LRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 202 EKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEA 281
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
...
gi 1952201083 282 ERL 284
Cdd:COG4942 253 GKL 255
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
282-392 |
3.45e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 282 ERLEQERIAAEK--AEADRLEQEriaAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERL 359
Cdd:PRK00409 523 ASLEELERELEQkaEEAEALLKE---AEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKG 599
|
90 100 110
....*....|....*....|....*....|...
gi 1952201083 360 EQERIAEEQAEAERLEQEKVAQAAAEKPKKEGF 392
Cdd:PRK00409 600 GYASVKAHELIEARKRLNKANEKKEKKKKKQKE 632
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
17-287 |
3.52e-05 |
|
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: 47.36 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 17 DKQQAEQAAKEADNQKQIEEQQRiEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQE-RIAAEKAEAERL 95
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTA-ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 96 EQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAE 175
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 176 AERLEQERIAAEKAEAERleqeRIAAEKAEAERLEQERIAAEKAEAerleQERIAAEKAEAERLEQERIAAEKAEAERLE 255
Cdd:TIGR02168 397 SLNNEIERLEARLERLED----RRERLQQEIEELLKKLEEAELKEL----QAELEELEEELEELQEELERLEEALEELRE 468
|
250 260 270
....*....|....*....|....*....|..
gi 1952201083 256 QERIAAEKAEAERLEQERIAAEKAEAERLEQE 287
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQARLDSLERLQEN 500
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
101-390 |
3.84e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 46.96 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 101 AAERRDAERVEQERIaaEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLE 180
Cdd:COG3064 4 ALEEKAAEAAAQERL--EQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 181 QERiaaEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIA 260
Cdd:COG3064 82 AEK---AAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 261 AEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAE 340
Cdd:COG3064 159 AAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1952201083 341 ADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:COG3064 239 ATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGL 288
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
43-238 |
3.93e-05 |
|
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: 46.87 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 43 EKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE---KAEAERLEQERIAAERRDAERVEQERIAAEK 119
Cdd:pfam15709 326 EKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAekmREELELEQQRRFEEIRLRKQRLEEERQRQEE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 120 AEAERLAQEQQAAEQQRQEQQARlaeQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLEQERIAAEKAEAERLEQERI 199
Cdd:pfam15709 406 EERKQRLQLQAAQERARQQQEEF---RRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQ 482
|
170 180 190
....*....|....*....|....*....|....*....
gi 1952201083 200 AAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER 238
Cdd:pfam15709 483 KQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQAR 521
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
28-396 |
3.98e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 46.82 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 28 ADNQKQIEE----QQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE 103
Cdd:COG5278 100 ADNPEQQARldelEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 104 RRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLEQER 183
Cdd:COG5278 180 LALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALAL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 184 IAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEK 263
Cdd:COG5278 260 AALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAA 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 264 AEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADR 343
Cdd:COG5278 340 AAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAA 419
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1952201083 344 LEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFFARL 396
Cdd:COG5278 420 EALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVA 472
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
15-364 |
4.34e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 46.57 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 15 KSDKQQAEQAAKEADNQKQIEEQQRIE--AEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEA 92
Cdd:COG3064 85 AAAEAEKKAAAEKAKAAKEAEAAAAAEkaAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 93 ERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAE 172
Cdd:COG3064 165 AAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 173 KAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE 252
Cdd:COG3064 245 LGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 253 RLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQE 332
Cdd:COG3064 325 GALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLR 404
|
330 340 350
....*....|....*....|....*....|..
gi 1952201083 333 RIAAEKAEADRLEQERIAAEKAEAERLEQERI 364
Cdd:COG3064 405 LDLGAALLEAASAVELRVLLALAGAAGAVVAL 436
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
34-379 |
4.74e-05 |
|
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: 46.98 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 34 IEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERlEQERIAAEKAEAERlEQERIAAERRDAERVEQE 113
Cdd:TIGR02169 192 IIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALER-QKEAIERQLASLEE-ELEKLTEEISELEKRLEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 114 RIAAEKAEAERLAQEQQAAEqqrqeqqarLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLEQERIAAEKAEAER 193
Cdd:TIGR02169 270 IEQLLEELNKKIKDLGEEEQ---------LRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 194 LEqERIAAEKAEAERLeQERIAAEKAEAERLEQEriAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQER 273
Cdd:TIGR02169 341 LE-REIEEERKRRDKL-TEEYAELKEELEDLRAE--LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 274 IAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAErleqerIAAEKAEADRLEQERIAAEK 353
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE------LYDLKEEYDRVEKELSKLQR 490
|
330 340
....*....|....*....|....*.
gi 1952201083 354 aEAERLEQERIAEEQAEAERLEQEKV 379
Cdd:TIGR02169 491 -ELAEAEAQARASEERVRGGRAVEEV 515
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
16-361 |
5.05e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 16 SDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQE--RIAAEKAEAe 93
Cdd:PRK04863 324 SDLEQDYQAASDHLNLVQTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEvdELKSQLADY- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 94 rleQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEK 173
Cdd:PRK04863 403 ---QQALDVQQTRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAY 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 174 AEAERL--EQERIAAEKAEAERLEQERiaAEKAEAERLEQ--------ERIAAEKAEAERLEQE---RIAAEKAEAERLE 240
Cdd:PRK04863 480 QLVRKIagEVSRSEAWDVARELLRRLR--EQRHLAEQLQQlrmrlselEQRLRQQQRAERLLAEfckRLGKNLDDEDELE 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 241 QERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAeADRLeQERIAAEKAEAERLEQERI- 319
Cdd:PRK04863 558 QLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDA-LARL-REQSGEEFEDSQDVTEYMQq 635
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1952201083 320 VAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQ 361
Cdd:PRK04863 636 LLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNA 677
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
14-270 |
5.49e-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: 46.53 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 14 GKSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAErlEQERIAAEKAEAERLEQERIAAEKAEAE 93
Cdd:TIGR00927 649 GERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGE--IEAKEADHKGETEAEEVEHEGETEAEGT 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 94 RLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKleqeraaaeQAQREAEQAAAEK 173
Cdd:TIGR00927 727 EDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQ---------AGEDGEMKGDEGA 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 174 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQ---ERIAAEKAEAERLEQERIAAEKAE 250
Cdd:TIGR00927 798 EGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKgvdGGGGSDGGDSEEEEEEEEEEEEEE 877
|
250 260
....*....|....*....|
gi 1952201083 251 AERLEQERIAAEKAEAERLE 270
Cdd:TIGR00927 878 EEEEEEEEEEEENEEPLSLE 897
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
188-358 |
5.60e-05 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 46.52 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 188 KAEAERLEQERIAAE--KAEAERLEQERIAAEKAEAERL----EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAA 261
Cdd:PRK14900 873 NAPPAVVEKDRARAEelREKRGKLEAHRAMLSGSEANSArrdtMEIQNEQKPTQDGPAAEAQPAQENTVVESAEKAVAAV 952
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 262 EKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKA-- 339
Cdd:PRK14900 953 SEAAQQAATAVASGIEKVAEAVRKTVRRSVKKAAATRAAMKKKVAKKAPAKKAAAKKAAAKKAAAKKKVAKKAPAKKVar 1032
|
170
....*....|....*....
gi 1952201083 340 EADRLEQERIAAEKAEAER 358
Cdd:PRK14900 1033 KPAAKKAAKKPARKAAGRK 1051
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
23-269 |
5.71e-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: 45.91 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 23 QAAKEADNQKQIEE-QQRIEAEKAEAERLEQERIAAEKaEAERLEQERIAAEKAEAERleQERIAAEKAEAERLEQERIA 101
Cdd:COG4942 18 QADAAAEAEAELEQlQQEIAELEKELAALKKEEKALLK-QLAALERRIAALARRIRAL--EQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 102 AERRDAERveQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAeaerleQ 181
Cdd:COG4942 95 LRAELEAQ--KEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL------R 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 182 ERIAAEKAEAERLEQERIAAEKA-EAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIA 260
Cdd:COG4942 167 AELEAERAELEALLAELEEERAAlEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
....*....
gi 1952201083 261 AEKAEAERL 269
Cdd:COG4942 247 GFAALKGKL 255
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
234-302 |
5.87e-05 |
|
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: 44.66 E-value: 5.87e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 234 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER-LEQERIAAEKAEADRLEQE 302
Cdd:pfam15927 1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELKHlLEERKEALEKLRAEAREEA 70
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
219-287 |
6.39e-05 |
|
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: 44.66 E-value: 6.39e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 219 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER-LEQERIAAEKAEAERLEQE 287
Cdd:pfam15927 1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELKHlLEERKEALEKLRAEAREEA 70
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
204-272 |
6.39e-05 |
|
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: 44.66 E-value: 6.39e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 204 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER-LEQERIAAEKAEAERLEQE 272
Cdd:pfam15927 1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELKHlLEERKEALEKLRAEAREEA 70
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
189-257 |
6.39e-05 |
|
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: 44.66 E-value: 6.39e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 189 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER-LEQERIAAEKAEAERLEQE 257
Cdd:pfam15927 1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELKHlLEERKEALEKLRAEAREEA 70
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
66-313 |
7.43e-05 |
|
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: 46.10 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 66 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAE 145
Cdd:pfam15709 314 ERSEEDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRK 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 146 QEaamkleqeraaaeqaqreaeqaaaekaeaerLEQERIAAEKAEAERLEQERIAAEKAeaeRLEQERIAAEKAEAERLE 225
Cdd:pfam15709 394 QR-------------------------------LEEERQRQEEEERKQRLQLQAAQERA---RQQQEEFRRKLQELQRKK 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 226 QERiAAEKAEAERLEQERIAAEKAEaerlEQERIaAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIA 305
Cdd:pfam15709 440 QQE-EAERAEAEKQRQKELEMQLAE----EQKRL-MEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAM 513
|
....*...
gi 1952201083 306 AEKAEAER 313
Cdd:pfam15709 514 KQAQEQAR 521
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
39-315 |
9.63e-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: 45.76 E-value: 9.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 39 RIEAEkAEAERLEQERIAAEKAEAERLEQERIAAEKAEaerlEQERIAAEKAEAErleqerIAAERRDAERVEQErIAAE 118
Cdd:TIGR00927 635 VAEAE-HTGERTGEEGERPTEAEGENGEESGGEAEQEG----ETETKGENESEGE------IPAERKGEQEGEGE-IEAK 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 119 KAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKlEQERAAAEQAQREAEQAAAEKAEAERLEQERIAAEKAEAERLEQE- 197
Cdd:TIGR00927 703 EADHKGETEAEEVEHEGETEAEGTEDEGEIETG-EEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEg 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 198 RIAAEKAEAERLEQERIAAEKAEAERLEqeriaAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAErlEQERIAAE 277
Cdd:TIGR00927 782 EIQAGEDGEMKGDEGAEGKVEHEGETEA-----GEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAK--QDEKGVDG 854
|
250 260 270
....*....|....*....|....*....|....*...
gi 1952201083 278 KAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLE 315
Cdd:TIGR00927 855 GGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEE 892
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
243-390 |
1.04e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 243 RIAAEKAEAERLEQERIAAEKAEAERLEQErIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEK---AEAERLEQERI 319
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQK-QAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKqkqAEEAAAKAAAA 144
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 320 VAEKAEAERlEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:PRK09510 145 AKAKAEAEA-KRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAE 214
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
181-432 |
1.07e-04 |
|
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: 45.83 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 181 QERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEkaeaERLEQERIAAEKAEAERLEQERia 260
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE----EEKLKERLEELEEDLSSLEQEI-- 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 261 aekaEAERLEQERIAAEKAEAER-LEQERIAAEKAEAD----RLEQERIAAEKAEAERLEQERIVAE-KAEAERLEQERI 334
Cdd:TIGR02169 754 ----ENVKSELKELEARIEELEEdLHKLEEALNDLEARlshsRIPEIQAELSKLEEEVSRIEARLREiEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 335 AAEKAEADRLEQERIAAEKAEAERLEQE----RIAEEQAEAERLEQEkVAQAAAEKPKKEGFFARLKKGLLKTRVNIGSG 410
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKEQIKSIEKEIEnlngKKEELEEELEELEAA-LRDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
250 260
....*....|....*....|..
gi 1952201083 411 FASIFSGKKIDDELFEELETQL 432
Cdd:TIGR02169 909 EAQIEKKRKRLSELKAKLEALE 930
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
249-317 |
1.08e-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: 1.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 249 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEA-DRLEQERIAAEKAEAERLEQE 317
Cdd:pfam15927 1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELkHLLEERKEALEKLRAEAREEA 70
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
187-313 |
1.11e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 187 EKAEAERLEQERiAAEKAEAERLEQERIAAE-KAEAERLeQERIAAEKAEAERLEQERIAAEKAEAerleqERIAAEKAE 265
Cdd:PRK00409 523 ASLEELERELEQ-KAEEAEALLKEAEKLKEElEEKKEKL-QEEEDKLLEEAEKEAQQAIKEAKKEA-----DEIIKELRQ 595
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1952201083 266 AERLEQERIAAEKAEaERLEQERIAAEKAEADRLEQERIAAEKAEAER 313
Cdd:PRK00409 596 LQKGGYASVKAHELI-EARKRLNKANEKKEKKKKKQKEKQEELKVGDE 642
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
18-347 |
1.12e-04 |
|
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: 45.39 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 18 KQQAEQAAKEADNQKqiEEQQR------------------IEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER 79
Cdd:NF033838 145 TKKVEEAEKKAKDQK--EEDRRnyptntyktleleiaesdVEVKKAELELVKEEAKEPRDEEKIKQAKAKVESKKAEATR 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 80 LEQERIAAEKAEAErleqeriaaerrdaerveqeriAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAA 159
Cdd:NF033838 223 LEKIKTDREKAEEE----------------------AKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKE 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 160 EQAQREAEQAAAEKAEAERLEQERIAAEkAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQErIAAEKAEAERL 239
Cdd:NF033838 281 NDAKSSDSSVGEETLPSPSLKPEKKVAE-AEKKVEEAKKKAKDQKEEDRRNYPTNTYKTLELEIAESD-VKVKEAELELV 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 240 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAerlEQERIAAE--KAEADRLEQERIAAEKAEAERLEQE 317
Cdd:NF033838 359 KEEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEE---EAKRKAAEedKVKEKPAEQPQPAPAPQPEKPAPKP 435
|
330 340 350
....*....|....*....|....*....|
gi 1952201083 318 RIVAEKAEAERLEQERiaAEKAEADRLEQE 347
Cdd:NF033838 436 EKPAEQPKAEKPADQQ--AEEDYARRSEEE 463
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
232-358 |
1.17e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 232 EKAEAERLEQERiAAEKAEAERLEQERIAAE-KAEAERLeQERIAAEKAEAERLEQERIAAEKAEADrleqeRIAAEKAE 310
Cdd:PRK00409 523 ASLEELERELEQ-KAEEAEALLKEAEKLKEElEEKKEKL-QEEEDKLLEEAEKEAQQAIKEAKKEAD-----EIIKELRQ 595
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1952201083 311 AERLEQERIVAEKAEaERLEQERIAAEKAEADRLEQERIAAEKAEAER 358
Cdd:PRK00409 596 LQKGGYASVKAHELI-EARKRLNKANEKKEKKKKKQKEKQEELKVGDE 642
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
215-371 |
1.35e-04 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 44.97 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 215 AAEKAEAERLEQEriAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKA 294
Cdd:PRK13108 287 GSEYVVDEALERE--PAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVE 364
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952201083 295 EADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEA 371
Cdd:PRK13108 365 ETSEADIEREQPGDLAGQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDP 441
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
196-346 |
1.36e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 45.39 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 196 QEriAAEKAEAERLEQEriaaekaEAERLEQERIAaEKAEAErleQERIAAEKAEAERLEQERIAAEKAEAERLEQERIA 275
Cdd:PTZ00491 664 QE--AAARHQAELLEQE-------ARGRLERQKMH-DKAKAE---EQRTKLLELQAESAAVESSGQSRAEALAEAEARLI 730
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201083 276 aeKAEAErLEQERIaaeKAEADRLEQEriaaekAEAERLEQERIVAEKAEAERLEQERI---AAEKAEADRLEQ 346
Cdd:PTZ00491 731 --EAEAE-VEQAEL---RAKALRIEAE------AELEKLRKRQELELEYEQAQNELEIAkakELADIEATKFER 792
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
15-389 |
1.49e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 15 KSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQ--ERIAAEKAEA 92
Cdd:PRK03918 196 KEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIREleERIEELKKEI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 93 ERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAE 172
Cdd:PRK03918 276 EELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 173 KAEAERLEQERIAAEKAEAERLEQER--IAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAE 250
Cdd:PRK03918 356 ELEERHELYEEAKAKKEELERLKKRLtgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 251 AE-----RLEQERIAAEKAEAERLEQERIAAEKAEA-ERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKA 324
Cdd:PRK03918 436 GKcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIeEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKY 515
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952201083 325 EAERLEqeriaaEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKK 389
Cdd:PRK03918 516 NLEELE------KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAE 574
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
240-390 |
1.61e-04 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 45.03 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 240 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAErleqERIAAEKAEADRLEQERIAAEKAEAERLEQERI 319
Cdd:PRK10811 855 VEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEE----PVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQV 930
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952201083 320 VAEKAEAERLEQERIAAE-KAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:PRK10811 931 ITESDVAVAQEVAEHAEPvVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVA 1002
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
35-98 |
1.82e-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: 43.12 E-value: 1.82e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952201083 35 EEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER-LEQERIAAEKAEAERLEQE 98
Cdd:pfam15927 6 EEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELKHlLEERKEALEKLRAEAREEA 70
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
235-367 |
1.90e-04 |
|
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: 42.34 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 235 EAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEaERL 314
Cdd:pfam05672 11 EAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAE-ERE 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1952201083 315 EQERIVAEKAEAERLEQERIAAEKAEADRLEQERIaAEKAEAERLEQERIAEE 367
Cdd:pfam05672 90 QREQEEQERLQKQKEEAEAKAREEAERQRQEREKI-MQQEEQERLERKKRIEE 141
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
45-113 |
1.92e-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: 43.12 E-value: 1.92e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 45 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER-LEQERIAAERRDAERVEQE 113
Cdd:pfam15927 1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELKHlLEERKEALEKLRAEAREEA 70
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
31-332 |
2.39e-04 |
|
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: 44.66 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 31 QKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERlEQERIAAEKAEAERLEQERIAAEKAEAERLEqeriaaERRDAERV 110
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELALLVLRLEELRE-ELEELQEELKEAEEELEELTAELQELEEKLE------ELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 111 EQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLE-QERIAAEKA 189
Cdd:TIGR02168 279 LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElKEELESLEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 190 EAERLEQERIAAEKAEAErLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEA-ERLEQERIAAEKAEAER 268
Cdd:TIGR02168 359 ELEELEAELEELESRLEE-LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLqQEIEELLKKLEEAELKE 437
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201083 269 LeQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQE 332
Cdd:TIGR02168 438 L-QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
83-298 |
2.57e-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: 43.68 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 83 ERIAAEKAEAERLEQERIAAERRDAERVEQERIAAEKAEAErlaqeqqAAEQQRQEQQARLAEQEAAMKLEQERAAAEQA 162
Cdd:TIGR02794 53 NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKE-------LEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 163 QREAEQAAAEKAEAERLEQERIAAEKAEAERLEQERIAAE-KAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQ 241
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKkKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKA 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1952201083 242 ERIAAEKAEAERLEQERIAAE-KAEAERLEQERIAAEKAEAERLEQERIAAEKAEADR 298
Cdd:TIGR02794 206 AAEAAAKAEAEAAAAAAAEAErKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
294-362 |
2.86e-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: 42.73 E-value: 2.86e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 294 AEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEA-DRLEQERIAAEKAEAERLEQE 362
Cdd:pfam15927 1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELkHLLEERKEALEKLRAEAREEA 70
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
264-310 |
3.12e-04 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 44.09 E-value: 3.12e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 264 AEAERLEQERIAAEKAEAERL--EQERIAAEKA--EADRLEQERIAAEKAE 310
Cdd:PLN02316 251 LEEKRRELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEKRRE 301
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
201-296 |
3.27e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.17 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 201 AEKAEAERLEQERIAAEKAEAERLEQERIAAEkAEAERLEQERIAAEKaeaerLEQERIAAEKAEAERLEQERIAAEKAE 280
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQ-ALAEAQQQELVALEG-----LAAELEEKQQELEAQLEQLQEKAAETS 211
|
90
....*....|....*.
gi 1952201083 281 AERLEQERIAAEKAEA 296
Cdd:PRK11448 212 QERKQKRKEITDQAAK 227
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
182-384 |
3.31e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 182 ERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAA 261
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 262 EKAEAERLEQERIAAEKAEAERLEQ--ERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQ-ERIAAEK 338
Cdd:COG4717 129 PLYQELEALEAELAELPERLEELEErlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEElEELQQRL 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1952201083 339 AEADR-LEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAA 384
Cdd:COG4717 209 AELEEeLEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIA 255
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
181-270 |
3.53e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.17 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 181 QERIAAEKAEAERLEQERIAAEkAEAERLEQERIAAEKaeaerLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIA 260
Cdd:PRK11448 148 QQEVLTLKQQLELQAREKAQSQ-ALAEAQQQELVALEG-----LAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEI 221
|
90
....*....|
gi 1952201083 261 AEKAeAERLE 270
Cdd:PRK11448 222 TDQA-AKRLE 230
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
238-366 |
3.54e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.92 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 238 RLEQERIAAEKAEAERleqeRIAAEKAEAERLEQERIAAEKAEAERLEQErIAAEKAEADRLEqeriaaEKAEAERLEQE 317
Cdd:COG0542 403 RMEIDSKPEELDELER----RLEQLEIEKEALKKEQDEASFERLAELRDE-LAELEEELEALK------ARWEAEKELIE 471
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1952201083 318 RIVAEKAEAERLEQERIAAEKaEADRLEQERIAAEKAEAERLEQERIAE 366
Cdd:COG0542 472 EIQELKEELEQRYGKIPELEK-ELAELEEELAELAPLLREEVTEEDIAE 519
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
18-385 |
3.70e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 18 KQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLeQERIAAEKAEAERLEQ 97
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA-QEELEELEEELEQLEN 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 98 ERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAE 177
Cdd:COG4717 235 ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 178 RLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQE 257
Cdd:COG4717 315 ELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 258 RIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAE 337
Cdd:COG4717 395 EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAEL 474
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1952201083 338 KAEADRLEQE-RIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAE 385
Cdd:COG4717 475 LQELEELKAElRELAEEWAALKLALELLEEAREEYREERLPPVLERASE 523
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
180-242 |
3.71e-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: 42.35 E-value: 3.71e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201083 180 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER-LEQERIAAEKAEAERLEQE 242
Cdd:pfam15927 7 EEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELKHlLEERKEALEKLRAEAREEA 70
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
60-106 |
3.73e-04 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 44.09 E-value: 3.73e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 60 AEAERLEQERIAAEKAEAERL--EQERIAAEKA--EAERLEQERIAAERRD 106
Cdd:PLN02316 251 LEEKRRELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEKRRE 301
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
17-124 |
4.01e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 17 DKQQAEQAAKEADNQKQIEEQQRIEAEKA--EAERLEQERiaaeKAEAERLeQERIAAEKAEAERLEQERIAAEKAEAer 94
Cdd:PRK00409 514 DKEKLNELIASLEELERELEQKAEEAEALlkEAEKLKEEL----EEKKEKL-QEEEDKLLEEAEKEAQQAIKEAKKEA-- 586
|
90 100 110
....*....|....*....|....*....|
gi 1952201083 95 leqERIAAERRDAERVEQERIAAEKAEAER 124
Cdd:PRK00409 587 ---DEIIKELRQLQKGGYASVKAHELIEAR 613
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
179-298 |
4.29e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 179 LEQERIAAE--KAEAERLEQERiaaeKAEAERLeQERIAAEKAEAERLEQERIAAEKAEAerleqERIAAEKAEAERLEQ 256
Cdd:PRK00409 532 LEQKAEEAEalLKEAEKLKEEL----EEKKEKL-QEEEDKLLEEAEKEAQQAIKEAKKEA-----DEIIKELRQLQKGGY 601
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1952201083 257 ERIAAEKAEaERLEQERIAAEKAEAERLEQERIAAEKAEADR 298
Cdd:PRK00409 602 ASVKAHELI-EARKRLNKANEKKEKKKKKQKEKQEELKVGDE 642
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
279-347 |
4.30e-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: 41.96 E-value: 4.30e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 279 AEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAER-LEQERIAAEKAEADRLEQE 347
Cdd:pfam15927 1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELKHlLEERKEALEKLRAEAREEA 70
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
181-395 |
4.53e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 43.66 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 181 QERIAAEKAEAERLEQEriAAEKAEAERLEQERIAAE-KAEAERLEQERIAAEKAEAERL----EQERIAAEKAEAE-RL 254
Cdd:NF041483 523 EETLERTRAEAERLRAE--AEEQAEEVRAAAERAARElREETERAIAARQAEAAEELTRLhteaEERLTAAEEALADaRA 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 255 EQERIAAEKAEaerlEQERIAAEKAEAERLEQeriAAEKAEADRLEQEriAAEKAEAERLEQERIVAEKAEAERLEQERI 334
Cdd:NF041483 601 EAERIRREAAE----ETERLRTEAAERIRTLQ---AQAEQEAERLRTE--AAADASAARAEGENVAVRLRSEAAAEAERL 671
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952201083 335 AAEKAE-ADRLEQE-RIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFFAR 395
Cdd:NF041483 672 KSEAQEsADRVRAEaAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAR 734
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
86-311 |
4.75e-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: 42.91 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 86 AAEKAEAERLEQERIAAERRDAERVEQERIAAEKAEAERlaqeqqaaeqqRQEQQARLAEQEAAMKLEQERAAAEQAQRE 165
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQR-----------AAEQARQKELEQRAAAEKAAKQAEQAAKQA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 166 AEQAAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIA 245
Cdd:TIGR02794 115 EEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEA 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952201083 246 AEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEA 311
Cdd:TIGR02794 195 KAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
174-388 |
5.12e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.94 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 174 AEAerlEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQErIAAEKAEAERLEQERIAAEKAEAER 253
Cdd:COG2268 228 LEQ---EREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAERE-VQRQLEIAEREREIELQEKEAEREE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 254 LEQERIAAEKAEAERLEQERIAAEKAEAERleqeriAAEKAEADRLEQERIAAEKAEAERLEQ------ERIVAEKAEA- 326
Cdd:COG2268 304 AELEADVRKPAEAEKQAAEAEAEAEAEAIR------AKGLAEAEGKRALAEAWNKLGDAAILLmlieklPEIAEAAAKPl 377
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952201083 327 ERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPK 388
Cdd:COG2268 378 EKIDKITIIDGGNGGNGAGSAVAEALAPLLESLLEETGLDLPGLLKGLTGAGAAAPAGEPAE 439
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
17-361 |
5.24e-04 |
|
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: 43.40 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 17 DKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLE 96
Cdd:COG3096 316 EELSARESDLEQDYQAASDHLNLVQTALRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLK 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 97 ------QERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAA 170
Cdd:COG3096 396 sqladyQQALDVQQTRAIQYQQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFE 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 171 AEKAEAERL--EQERIAAEKAEAERLEQERiaAEKAEAERLEQerIAAEKAEAERLEQERiaaekAEAERLEQE---RIA 245
Cdd:COG3096 476 KAYELVCKIagEVERSQAWQTARELLRRYR--SQQALAQRLQQ--LRAQLAELEQRLRQQ-----QNAERLLEEfcqRIG 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 246 AEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAeAERLEQE--RIVAEK 323
Cdd:COG3096 547 QQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDA-LERLREQsgEALADS 625
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1952201083 324 AE-----AERLEQERIAaeKAEADRLEQERIAAEKaEAERLEQ 361
Cdd:COG3096 626 QEvtaamQQLLEREREA--TVERDELAARKQALES-QIERLSQ 665
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
69-228 |
5.39e-04 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 43.57 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 69 RIAAEKAEAERLEQERIAAEKAEAERLEQERIA-AERRDAERVEQERIaaekaeaerlaqeqqaaeqqrqeqqarlaeqe 147
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKILEKKRIErLEREERERLERERM-------------------------------- 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 148 aamkleqeraaaeqaqreaeqaaaekaeaerleqERIAAEKAEAERLEQERIAAEKAEAERLEQ-ERIAAEKAEAERLEQ 226
Cdd:PTZ00266 477 ----------------------------------ERIERERLERERLERERLERDRLERDRLDRlERERVDRLERDRLEK 522
|
..
gi 1952201083 227 ER 228
Cdd:PTZ00266 523 AR 524
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
16-360 |
5.74e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 16 SDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE-RLEQERIAAEKAEAER 94
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEaTLRTARERVEEAEALL 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 95 LEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKA 174
Cdd:PRK02224 450 EAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERR 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 175 EAERLEQERIAAEKAEAERLEQEriaAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLE-----QERIAAEKA 249
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEAE---AEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLErirtlLAAIADAED 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 250 EAERLEQERiaAEKAEAERLEQERIAaekaeaERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERL 329
Cdd:PRK02224 607 EIERLREKR--EALAELNDERRERLA------EKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDD 678
|
330 340 350
....*....|....*....|....*....|...
gi 1952201083 330 EQERIAAEKAEADRLE--QERIAAEKAEAERLE 360
Cdd:PRK02224 679 LQAEIGAVENELEELEelRERREALENRVEALE 711
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
230-391 |
5.86e-04 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 43.04 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 230 AAEKAEAERLEQEriAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKA 309
Cdd:PRK13108 287 GSEYVVDEALERE--PAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 310 EAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKK 389
Cdd:PRK13108 365 ETSEADIEREQPGDLAGQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPAEP 444
|
..
gi 1952201083 390 EG 391
Cdd:PRK13108 445 DG 446
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
279-325 |
6.11e-04 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 43.32 E-value: 6.11e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 279 AEAERLEQERIAAEKAEADRL--EQERIAAEKA--EAERLEQERIVAEKAE 325
Cdd:PLN02316 251 LEEKRRELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEKRRE 301
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
185-373 |
6.39e-04 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 42.66 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 185 AAEKAEAERLEQEriAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKA 264
Cdd:PRK13108 287 GSEYVVDEALERE--PAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 265 EAERLEQERIAAEKaeaerleqerIAAEKAEADRLEQERIAAEKAEAERLEqerivAEKAEAERLEQERIAAEKAEADRL 344
Cdd:PRK13108 365 ETSEADIEREQPGD----------LAGQAPAAHQVDAEAASAAPEEPAALA-----SEAHDETEPEVPEKAAPIPDPAKP 429
|
170 180
....*....|....*....|....*....
gi 1952201083 345 EQERIAAEKAEAERLEQERIAEEQAEAER 373
Cdd:PRK13108 430 DELAVAGPGDDPAEPDGIRRQDDFSSRRR 458
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
15-300 |
7.18e-04 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 43.06 E-value: 7.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 15 KSDKQQAEQAAKEADNQKQIEEQqrieaekAEAERLEQERIAAEKAEaerlEQERIAAEKAEAErLEQERIAAEKAEAER 94
Cdd:TIGR00927 632 KGDVAEAEHTGERTGEEGERPTE-------AEGENGEESGGEAEQEG----ETETKGENESEGE-IPAERKGEQEGEGEI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 95 LEQERIAAERRDAERVEQEriaaEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKA 174
Cdd:TIGR00927 700 EAKEADHKGETEAEEVEHE----GETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGK 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 175 EAERlEQERIAAEKAEAERLEQERIAAEKAEAERleqeriAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERL 254
Cdd:TIGR00927 776 EDED-EGEIQAGEDGEMKGDEGAEGKVEHEGETE------AGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQD 848
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1952201083 255 EQ---ERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLE 300
Cdd:TIGR00927 849 EKgvdGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLE 897
|
|
| HC2 |
pfam07382 |
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like ... |
226-358 |
7.22e-04 |
|
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like nucleoprotein HC2 (approximately 200 residues long), which seems to be found mostly in Chlamydia. HC2 functions in DNA condensation, although it has been suggested that it also has other roles.
Pssm-ID: 369339 [Multi-domain] Cd Length: 187 Bit Score: 41.30 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 226 QERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIA 305
Cdd:pfam07382 5 QKKRSSKKTAAKKAAVRKPAAKKAAAKKTVVRKVAAKKPAARKTVAKKTVAAKKPAAKKAAKKAVAKKVVAKKPVAKKAV 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1952201083 306 AEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAER 358
Cdd:pfam07382 85 AKKATAKKVAAKKVVAKKTVAKKAAAKKPAAKKAVAKKAVARKPAAKKAVAKK 137
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
268-379 |
7.51e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 7.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 268 RLEQERIAAEKAEAER----LEQERIAAEKaEADRLEQERIAAEKAEAERLEQERIVAEKA-EAERLEQERIAAEKAEAD 342
Cdd:COG0542 403 RMEIDSKPEELDELERrleqLEIEKEALKK-EQDEASFERLAELRDELAELEEELEALKARwEAEKELIEEIQELKEELE 481
|
90 100 110
....*....|....*....|....*....|....*..
gi 1952201083 343 RLEQERIAAEKAEAERLEQEriaeeqAEAERLEQEKV 379
Cdd:COG0542 482 QRYGKIPELEKELAELEEEL------AELAPLLREEV 512
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
230-383 |
7.55e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 42.55 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 230 AAEKAEAERLEQERIAAEKAEAERLEQE-RIAAEKAEAErleqerIAAEKAEAERLEQERIAAEkAEADRLEQERIAAEK 308
Cdd:PRK12472 181 KAEALAAAPARAETLAREAEDAARAADEaKTAAAAAARE------AAPLKASLRKLERAKARAD-AELKRADKALAAAKT 253
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952201083 309 AEAerleqerivaeKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAErLEQERIAEEQAEAERLEQEKVAQAA 383
Cdd:PRK12472 254 DEA-----------KARAEERQQKAAQQAAEAATQLDTAKADAEAKRAA-AAATKEAAKAAAAKKAETAKAATDA 316
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
47-348 |
7.60e-04 |
|
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: 43.13 E-value: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 47 AERLEQERIAAEKAEAERLeQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAERRDAERVEQERIAAE-KAEAERL 125
Cdd:TIGR02169 661 APRGGILFSRSEPAELQRL-RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEeEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 126 AQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLEQERIAAEKAEAERLEQERIAAE-KA 204
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREiEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 205 EAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERL 284
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952201083 285 EQERIAAEKAEADRLEQERIAAEKAEAERLEQE--RIVAEKAEAERLEQERIAAEKAEADRLEQER 348
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEElsEIEDPKGEDEEIPEEELSLEDVQAELQRVEE 965
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
208-336 |
7.77e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 208 RLEQERIAAEKAEAERleqeRIAAEKAEAERLEQERIAAEKAEAERLEQErIAAEKAEAERLEqeriaaEKAEAERLEQE 287
Cdd:COG0542 403 RMEIDSKPEELDELER----RLEQLEIEKEALKKEQDEASFERLAELRDE-LAELEEELEALK------ARWEAEKELIE 471
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1952201083 288 RIAAEKAEADRLEQERIAAEKAEAErLEQERIVAEKAEAERLEQERIAA 336
Cdd:COG0542 472 EIQELKEELEQRYGKIPELEKELAE-LEEELAELAPLLREEVTEEDIAE 519
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
264-332 |
7.83e-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: 7.83e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 264 AEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAER-LEQERIVAEKAEAERLEQE 332
Cdd:pfam15927 1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELKHlLEERKEALEKLRAEAREEA 70
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
71-536 |
8.37e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 42.33 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 71 AAEKAEAERLEQERIA-AEKAEAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAA 149
Cdd:COG3064 4 ALEEKAAEAAAQERLEqAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 150 MKLEQERAAAEQAQREAEQAAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERI 229
Cdd:COG3064 84 KAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 230 AAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKA 309
Cdd:COG3064 164 AAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 310 EAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKK 389
Cdd:COG3064 244 ALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 390 EGFFARLKKGLLKTRVNIGSGFASIFSGKKIDDELFEELETQLLTADLGVDTTMKLIDNLTDAADRKQLKDGDALYELMK 469
Cdd:COG3064 324 AGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGL 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952201083 470 QEMASMLKTAEQPLVVSNDKKPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVE 536
Cdd:COG3064 404 RLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVA 470
|
|
| HC2 |
pfam07382 |
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like ... |
181-313 |
8.62e-04 |
|
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like nucleoprotein HC2 (approximately 200 residues long), which seems to be found mostly in Chlamydia. HC2 functions in DNA condensation, although it has been suggested that it also has other roles.
Pssm-ID: 369339 [Multi-domain] Cd Length: 187 Bit Score: 40.92 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 181 QERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIA 260
Cdd:pfam07382 5 QKKRSSKKTAAKKAAVRKPAAKKAAAKKTVVRKVAAKKPAARKTVAKKTVAAKKPAAKKAAKKAVAKKVVAKKPVAKKAV 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1952201083 261 AEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAER 313
Cdd:pfam07382 85 AKKATAKKVAAKKVVAKKTVAKKAAAKKPAAKKAVAKKAVARKPAAKKAVAKK 137
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
186-313 |
1.02e-03 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 42.15 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 186 AEKAEAERLEQERIAAEKAEAERLEQERIA------------AEKAEAERLEQERIAAEKAEAERLEQERIAAEKaeaeR 253
Cdd:PRK00247 285 EHHAEQRAQYREKQKEKKAFLWTLRRNRLRmiitpwrapelhAENAEIKKTRTAEKNEAKARKKEIAQKRRAAER----E 360
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952201083 254 LEQERIAAEKAEAERLEQERIAAEKA-----EAERLEQERIAAEKAEADRLEQERIAAEKAEAER 313
Cdd:PRK00247 361 INREARQERAAAMARARARRAAVKAKkkgliDASPNEDTPSENEESKGSPPQVEATTTAEPNREP 425
|
|
| flhF |
PRK14721 |
flagellar biosynthesis regulator FlhF; Provisional |
493-691 |
1.11e-03 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173184 [Multi-domain] Cd Length: 420 Bit Score: 41.86 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 493 VILMVGVNGVGKTTTIGKLAKQ--FQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPViaqHTGADSASVVFdAFQAAK 570
Cdd:PRK14721 193 VYALIGPTGVGKTTTTAKLAARavIRHGADKVALLTTDSYRIGGHEQLRIYGKLLGVSV---RSIKDIADLQL-MLHELR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 571 ARNVdVLIaDTAGRLQNKDNLMQELEKIARVMKKIdpdaphEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGTA 650
Cdd:PRK14721 269 GKHM-VLI-DTVGMSQRDQMLAEQIAMLSQCGTQV------KHLLLLNATSSGDTLDEVISAYQGHGIHGCIITKVDEAA 340
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1952201083 651 KGGVIFAVADKFNIPIRYIGVGEGI-DDLRTFNSSDFIDALF 691
Cdd:PRK14721 341 SLGIALDAVIRRKLVLHYVTNGQKVpEDLHEANSRYLLHRIF 382
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
42-266 |
1.13e-03 |
|
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: 41.75 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 42 AEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAERRDAERVEQERIAAEKAE 121
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 122 AERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAaaekaeaerleQERIAAEKAEAERLEQERIAA 201
Cdd:TIGR02794 127 KQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKK-----------AEAEAKAKAEAEAKAKAEEAK 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952201083 202 EKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEA 266
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
20-397 |
1.21e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 20 QAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQEriAAEKAEAERLEQERIAAE-KAEAERLEQERIAAEKAEAERLEQE 98
Cdd:NF041483 287 EAKEAAAKQLASAESANEQRTRTAKEEIARLVGE--ATKEAEALKAEAEQALADaRAEAEKLVAEAAEKARTVAAEDTAA 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 99 RIAAERRDAERV-------EQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAA 171
Cdd:NF041483 365 QLAKAARTAEEVltkasedAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAKDDTKEYRAKTVELQEEARR 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 172 EKAEAERLEQEriAAEKAEAERLEQERIAAEK-AEAERLEQERIAAEKAEAERLEQeriaAEKAEAERLEQEriAAEKAE 250
Cdd:NF041483 445 LRGEAEQLRAE--AVAEGERIRGEARREAVQQiEEAARTAEELLTKAKADADELRS----TATAESERVRTE--AIERAT 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 251 AERLE-QERIAAEKAEAERLEQEriAAEKAEAERLEQERIAAE-KAEADRLEQERIAAEKAEAERL----EQERIVAEKA 324
Cdd:NF041483 517 TLRRQaEETLERTRAEAERLRAE--AEEQAEEVRAAAERAARElREETERAIAARQAEAAEELTRLhteaEERLTAAEEA 594
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201083 325 EAE-RLEQERIAAEKAEadrlEQERIAAEKAEAERLEQeriAEEQAEAERLEQEKVAQAAAEKPKKEGFFARLK 397
Cdd:NF041483 595 LADaRAEAERIRREAAE----ETERLRTEAAERIRTLQ---AQAEQEAERLRTEAAADASAARAEGENVAVRLR 661
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
189-300 |
1.22e-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: 40.02 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 189 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEaERLEQERIAAEKAEAER 268
Cdd:pfam05672 25 EQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAE-EREQREQEEQERLQKQK 103
|
90 100 110
....*....|....*....|....*....|..
gi 1952201083 269 LEQERIAAEKAEAERLEQERIaAEKAEADRLE 300
Cdd:pfam05672 104 EEAEAKAREEAERQRQEREKI-MQQEEQERLE 134
|
|
| HC2 |
pfam07382 |
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like ... |
196-328 |
1.33e-03 |
|
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like nucleoprotein HC2 (approximately 200 residues long), which seems to be found mostly in Chlamydia. HC2 functions in DNA condensation, although it has been suggested that it also has other roles.
Pssm-ID: 369339 [Multi-domain] Cd Length: 187 Bit Score: 40.53 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 196 QERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIA 275
Cdd:pfam07382 5 QKKRSSKKTAAKKAAVRKPAAKKAAAKKTVVRKVAAKKPAARKTVAKKTVAAKKPAAKKAAKKAVAKKVVAKKPVAKKAV 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1952201083 276 AEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAER 328
Cdd:pfam07382 85 AKKATAKKVAAKKVVAKKTVAKKAAAKKPAAKKAVAKKAVARKPAAKKAVAKK 137
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
265-381 |
1.38e-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: 39.64 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 265 EAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADRl 344
Cdd:pfam05672 11 EAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEERE- 89
|
90 100 110
....*....|....*....|....*....|....*..
gi 1952201083 345 EQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQ 381
Cdd:pfam05672 90 QREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQ 126
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
231-330 |
1.49e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.86 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 231 AEKAEAERLEQERIAAEKAEAERLEQERIAAEkAEAERLEQERIAAEKaeaerLEQERIAAEKAEADRLEQERIAAEKAE 310
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQ-ALAEAQQQELVALEG-----LAAELEEKQQELEAQLEQLQEKAAETS 211
|
90 100
....*....|....*....|
gi 1952201083 311 AERLEQERIVAEKAeAERLE 330
Cdd:PRK11448 212 QERKQKRKEITDQA-AKRLE 230
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
189-235 |
1.56e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 41.78 E-value: 1.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 189 AEAERLEQERIAAEKAEAERL--EQERIAAEKA--EAERLEQERIAAEKAE 235
Cdd:PLN02316 251 LEEKRRELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEKRRE 301
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
45-91 |
1.56e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 41.78 E-value: 1.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 45 AEAERLEQERIAAEKAEAERL--EQERIAAEKA--EAERLEQERIAAEKAE 91
Cdd:PLN02316 251 LEEKRRELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEKRRE 301
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
204-250 |
1.56e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 41.78 E-value: 1.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 204 AEAERLEQERIAAEKAEAERL--EQERIAAEKA--EAERLEQERIAAEKAE 250
Cdd:PLN02316 251 LEEKRRELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEKRRE 301
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
219-265 |
1.56e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 41.78 E-value: 1.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 219 AEAERLEQERIAAEKAEAERL--EQERIAAEKA--EAERLEQERIAAEKAE 265
Cdd:PLN02316 251 LEEKRRELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEKRRE 301
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
234-280 |
1.56e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 41.78 E-value: 1.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 234 AEAERLEQERIAAEKAEAERL--EQERIAAEKA--EAERLEQERIAAEKAE 280
Cdd:PLN02316 251 LEEKRRELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEKRRE 301
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
249-295 |
1.56e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 41.78 E-value: 1.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 249 AEAERLEQERIAAEKAEAERL--EQERIAAEKA--EAERLEQERIAAEKAE 295
Cdd:PLN02316 251 LEEKRRELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEKRRE 301
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
309-378 |
1.56e-03 |
|
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: 40.42 E-value: 1.56e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 309 AEAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAER-LEQERIAEEQAEAERLEQEK 378
Cdd:pfam15927 1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELKHlLEERKEALEKLRAEAREEAE 71
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
212-382 |
1.62e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 212 ERIAAEKA-EAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQEriaaekAEAERLEQERIAAEKAEAERLEQERIA 290
Cdd:PRK12704 26 KKIAEAKIkEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNE------FEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 291 AEKAEADRLEQERIAAEKAEAER---LEQERIVAEKAEAERLEQ-ERIAAEKAEADRLEQERIAAEKAEAERLEQERIAE 366
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKqqeLEKKEEELEELIEEQLQElERISGLTAEEAKEILLEKVEEEARHEAAVLIKEIE 179
|
170
....*....|....*...
gi 1952201083 367 EQA--EAERLEQEKVAQA 382
Cdd:PRK12704 180 EEAkeEADKKAKEILAQA 197
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
283-391 |
1.62e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 283 RLEQERIAAEKAEADRleqeRIAAEKAEAERLEQERIVAEKAEAERLEQErIAAEKAEADRLEqERIAAEKAEAERLEQE 362
Cdd:COG0542 403 RMEIDSKPEELDELER----RLEQLEIEKEALKKEQDEASFERLAELRDE-LAELEEELEALK-ARWEAEKELIEEIQEL 476
|
90 100
....*....|....*....|....*....
gi 1952201083 363 RIAEEQAEAERLEQEKVAQAAAEKPKKEG 391
Cdd:COG0542 477 KEELEQRYGKIPELEKELAELEEELAELA 505
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
324-370 |
1.71e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 41.78 E-value: 1.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 324 AEAERLEQERIAAEKAEADRL--EQERIAAEKA--EAERLEQERIAEEQAE 370
Cdd:PLN02316 251 LEEKRRELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEKRRE 301
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
17-362 |
1.82e-03 |
|
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: 41.88 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 17 DKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQ-ERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERL 95
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARiEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 96 EQERIAAERrdaeRVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAE 175
Cdd:TIGR00618 313 HTELQSKMR----SRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 176 AERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKaeAERLEQERIAAEKAEAERLEQERIAaekaeAERLE 255
Cdd:TIGR00618 389 TTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKK--QQELQQRYAELCAAAITCTAQCEKL-----EKIHL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 256 QERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAaeKAEAERLEQERIVAEKAEAERLEQERIA 335
Cdd:TIGR00618 462 QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCI--HPNPARQDIDNPGPLTRRMQRGEQTYAQ 539
|
330 340 350
....*....|....*....|....*....|..
gi 1952201083 336 AEKAEAD-----RLEQERIAAEKAEAERLEQE 362
Cdd:TIGR00618 540 LETSEEDvyhqlTSERKQRASLKEQMQEIQQS 571
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
200-347 |
1.85e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 41.39 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 200 AAEKAEAERLEQERIAAEKAEAERLEQE-RIAAEKAEAErleqerIAAEKAEAERLEQERIAAEkAEAERLEQERIAAE- 277
Cdd:PRK12472 181 KAEALAAAPARAETLAREAEDAARAADEaKTAAAAAARE------AAPLKASLRKLERAKARAD-AELKRADKALAAAKt 253
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201083 278 ---KAEAERLEQERIAAEKAEADRLEQERIAAEKAEAErleqerIVAEKAEAERLEQERIAAEKAEAD-RLEQE 347
Cdd:PRK12472 254 deaKARAEERQQKAAQQAAEAATQLDTAKADAEAKRAA------AAATKEAAKAAAAKKAETAKAATDaKLALE 321
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
180-313 |
1.90e-03 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 41.52 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 180 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERI 259
Cdd:PRK14900 916 MEIQNEQKPTQDGPAAEAQPAQENTVVESAEKAVAAVSEAAQQAATAVASGIEKVAEAVRKTVRRSVKKAAATRAAMKKK 995
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1952201083 260 AAEKAEAERLEQERIAAEKAEAERLEQERIAAEKA--EADRLEQERIAAEKAEAER 313
Cdd:PRK14900 996 VAKKAPAKKAAAKKAAAKKAAAKKKVAKKAPAKKVarKPAAKKAAKKPARKAAGRK 1051
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
15-404 |
1.98e-03 |
|
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: 41.75 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 15 KSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAE-RLEQERIAAEKAEAERLEQERIAAEKAEAE 93
Cdd:pfam12128 314 DAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERlKALTGKHQDVTAKYNRRRSKIKEQNNRDIA 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 94 RLEQERIAAERRDAERVEQERIAAEKAEAE-RLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAE 172
Cdd:pfam12128 394 GIKDKLAKIREARDRQLAVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERI 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 173 KAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE 252
Cdd:pfam12128 474 ERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGK 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 253 RLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE---------KAEADRLEqERIAAEKAEAERLEQERIVAEK 323
Cdd:pfam12128 554 VISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPewaaseeelRERLDKAE-EALQSAREKQAAAEEQLVQANG 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 324 AEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFFARLKKGLLKT 403
Cdd:pfam12128 633 ELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREA 712
|
.
gi 1952201083 404 R 404
Cdd:pfam12128 713 R 713
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
277-364 |
2.07e-03 |
|
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: 40.74 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 277 EKAEAER------LEQERIAAEKAEADRLEQeRIAAEK-AEAERLEQERIVAEKaEAERLEQE-----RIAAEKAEAD-- 342
Cdd:cd03406 169 EAMEAEKtklliaEQHQKVVEKEAETERKRA-VIEAEKdAEVAKIQMQQKIMEK-EAEKKISEiedemHLAREKARADae 246
|
90 100
....*....|....*....|....*
gi 1952201083 343 --RLEQERIAAE-KAEAERLEQERI 364
Cdd:cd03406 247 yyRALREAEANKlKLTPEYLELKKY 271
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
68-271 |
2.13e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 68 ERIAAEKAEAERLEQERIAAEKAEA--ERLEQ-----ERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQ 140
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREqiELLEPirelaERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 141 ARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAE 220
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAA 384
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 221 AERLEQERIAAEKAEAERLEQERIAAEKAEAErlEQERIAAEKAEAERLEQ 271
Cdd:COG4913 385 LRAEAAALLEALEEELEALEEALAEAEAALRD--LRRELRELEAEIASLER 433
|
|
| HC2 |
pfam07382 |
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like ... |
211-343 |
2.18e-03 |
|
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like nucleoprotein HC2 (approximately 200 residues long), which seems to be found mostly in Chlamydia. HC2 functions in DNA condensation, although it has been suggested that it also has other roles.
Pssm-ID: 369339 [Multi-domain] Cd Length: 187 Bit Score: 39.76 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 211 QERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIA 290
Cdd:pfam07382 5 QKKRSSKKTAAKKAAVRKPAAKKAAAKKTVVRKVAAKKPAARKTVAKKTVAAKKPAAKKAAKKAVAKKVVAKKPVAKKAV 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1952201083 291 AEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADR 343
Cdd:pfam07382 85 AKKATAKKVAAKKVVAKKTVAKKAAAKKPAAKKAVAKKAVARKPAAKKAVAKK 137
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
181-291 |
2.22e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 181 QERIAAEKAEAERLEQERIAAEKAEAERLEQErIAAEKAEAERLEqeriaaEKAEAERLEQERIAAEKAEAERLEQERIA 260
Cdd:COG0542 417 ERRLEQLEIEKEALKKEQDEASFERLAELRDE-LAELEEELEALK------ARWEAEKELIEEIQELKEELEQRYGKIPE 489
|
90 100 110
....*....|....*....|....*....|.
gi 1952201083 261 AEKAEAErLEQERIAAEKAEAERLEQERIAA 291
Cdd:COG0542 490 LEKELAE-LEEELAELAPLLREEVTEEDIAE 519
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
200-285 |
2.26e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.48 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 200 AAEKAEAERLEQ--ERIAAEKAEAERLeQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE 277
Cdd:PRK11448 145 HALQQEVLTLKQqlELQAREKAQSQAL-AEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEITD 223
|
....*...
gi 1952201083 278 KAeAERLE 285
Cdd:PRK11448 224 QA-AKRLE 230
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
13-218 |
2.34e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 13 FGKSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERiAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEA 92
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE-AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 93 ERLEQERiaaERRDAERVEQERIAAEKAEAERlaqeQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAE 172
Cdd:PTZ00121 1680 AKKAEED---EKKAAEALKKEAEEAKKAEELK----KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1952201083 173 KAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEK 218
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
35-385 |
2.35e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 35 EEQQRIEAEKAEAERLEQEriAAEKAEAERLEQERIAAEKAEAERLeQERIAAEKAEAERLeQERIAAERRDAERVEQER 114
Cdd:PRK02224 220 EEIERYEEQREQARETRDE--ADEVLEEHEERREELETLEAEIEDL-RETIAETEREREEL-AEEVRDLRERLEELEEER 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 115 IAAeKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLEQERIAAEKAEAERL 194
Cdd:PRK02224 296 DDL-LAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 195 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE-RLEQERIAAEKAEAERLE--- 270
Cdd:PRK02224 375 AREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEaTLRTARERVEEAEALLEAgkc 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 271 -------QERIAAEKAEAERLEQERIAAEKAEAdRLEQERIAAEKAEAERL-EQERIVAEKAEAERLEQERIAAEKAEAD 342
Cdd:PRK02224 455 pecgqpvEGSPHVETIEEDRERVEELEAELEDL-EEEVEEVEERLERAEDLvEAEDRIERLEERREDLEELIAERRETIE 533
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1952201083 343 RlEQERIAAEKAEAERLEQE-RIAEEQAEAERLEQEKVAQAAAE 385
Cdd:PRK02224 534 E-KRERAEELRERAAELEAEaEEKREAAAEAEEEAEEAREEVAE 576
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
179-337 |
2.35e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.95 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 179 LEQERIAAEKAEAERLEQERIAAEK---AEAERLEQERIAAEKAEAERLEQERIAAE-KAEAERLEQERIAAEKAEAERL 254
Cdd:PRK09510 106 LEKERLAAQEQKKQAEEAAKQAALKqkqAEEAAAKAAAAAKAKAEAEAKRAAAAAKKaAAEAKKKAEAEAAKKAAAEAKK 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 255 EQERIAAEKAEAErleqeriAAEKAEAERLEQeriAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERI 334
Cdd:PRK09510 186 KAEAEAAAKAAAE-------AKKKAEAEAKKK---AAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
...
gi 1952201083 335 AAE 337
Cdd:PRK09510 256 AAE 258
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
216-358 |
2.36e-03 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 40.99 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 216 AEKAEAERLEQERIAAEKAEAERLEQERIAAekaeaeRLEQERIAAEKAEAERLEQER---IAAEKAEAERLEQERIAAE 292
Cdd:PRK00247 285 EHHAEQRAQYREKQKEKKAFLWTLRRNRLRM------IITPWRAPELHAENAEIKKTRtaeKNEAKARKKEIAQKRRAAE 358
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 293 KaEADRleqERIAAEKAEAERLEQERIVAEKA-----EAERLEQERIAAEKAEADRLEQERIAAEKAEAER 358
Cdd:PRK00247 359 R-EINR---EARQERAAAMARARARRAAVKAKkkgliDASPNEDTPSENEESKGSPPQVEATTTAEPNREP 425
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
23-115 |
2.46e-03 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 40.59 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 23 QAAKEADNQKQIEEQQRiEAEKAEAERLEQERIAAEKAEAERLEQEriaaekAEAERleQERIAAEKAEAERLEQerIAA 102
Cdd:COG0330 167 EEVQDAMEDRMKAERER-EAAILEAEGYREAAIIRAEGEAQRAIIE------AEAYR--EAQILRAEGEAEAFRI--VAE 235
|
90
....*....|...
gi 1952201083 103 ERRDAERVEQERI 115
Cdd:COG0330 236 AYSAAPFVLFYRS 248
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
246-390 |
2.57e-03 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 40.99 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 246 AEKAEAERLEQERIAAEKAEAERLEQERIAAekaeaeRLEQERIAAEKAEADRLEQER---IAAEKAEAERLEQERIVAE 322
Cdd:PRK00247 285 EHHAEQRAQYREKQKEKKAFLWTLRRNRLRM------IITPWRAPELHAENAEIKKTRtaeKNEAKARKKEIAQKRRAAE 358
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952201083 323 KaEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEqAEAERLEQEKVAQAAAEKPKKE 390
Cdd:PRK00247 359 R-EINREARQERAAAMARARARRAAVKAKKKGLIDASPNEDTPSE-NEESKGSPPQVEATTTAEPNRE 424
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
35-390 |
2.70e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 40.79 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 35 EEQQRIEAEKAEAERLEQERiAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQEriaaERRDAERVEQER 114
Cdd:COG3064 3 EALEEKAAEAAAQERLEQAE-AEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAE----QRAAELAAEAAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 115 IAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLEQERIAAEKAEAERL 194
Cdd:COG3064 78 KLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 195 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERiAAEKAEAERLEQERI 274
Cdd:COG3064 158 RAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAV-AARAAAASREAALAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 275 AAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKA 354
Cdd:COG3064 237 VEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEA 316
|
330 340 350
....*....|....*....|....*....|....*.
gi 1952201083 355 EAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:COG3064 317 VLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAA 352
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
182-328 |
2.73e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 40.73 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 182 ERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAA 261
Cdd:PRK13108 312 ASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADIEREQPGDLAGQAPAAHQVDA 391
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952201083 262 EKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAER 328
Cdd:PRK13108 392 EAASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPAEPDGIRRQDDFSSRRR 458
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
182-337 |
2.80e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 40.73 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 182 ERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAA 261
Cdd:PRK13108 297 EREPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADIEREQP 376
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952201083 262 EKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQerIVAEKAEAERLEQERIAAE 337
Cdd:PRK13108 377 GDLAGQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAKPDE--LAVAGPGDDPAEPDGIRRQ 450
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
17-382 |
3.07e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.96 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 17 DKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLE 96
Cdd:NF041483 527 ERTRAEAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALADARAEAERIR 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 97 QEriAAERRDAERVE-QERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAE 175
Cdd:NF041483 607 RE--AAEETERLRTEaAERIRTLQAQAEQEAERLRTEAAADASAARAEGENVAVRLRSEAAAEAERLKSEAQESADRVRA 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 176 AERLEQERIAAEKAEAERLEQERIAAEKAEAERL--------EQERIAAEKAEAERLEQERIAAEKAEAERL----EQER 243
Cdd:NF041483 685 EAAAAAERVGTEAAEALAAAQEEAARRRREAEETlgsaraeaDQERERAREQSEELLASARKRVEEAQAEAQrlveEADR 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 244 IAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRL------EQERIAAEKAEAERLEQE 317
Cdd:NF041483 765 RATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEHAAERTRTEAQEEADRVrsdayaERERASEDANRLRREAQE 844
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 318 RIVAEKAEAERL------EQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQA 382
Cdd:NF041483 845 ETEAAKALAERTvseaiaEAERLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSDAAAQA 915
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
37-122 |
3.12e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.09 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 37 QQRIEAEKAEAERLEQERIAAEkAEAERLEQERIAAEKaeaerLEQERIAAEKAEAERLEQERIAAERRDAERVEQERIA 116
Cdd:PRK11448 148 QQEVLTLKQQLELQAREKAQSQ-ALAEAQQQELVALEG-----LAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEI 221
|
....*.
gi 1952201083 117 AEKAEA 122
Cdd:PRK11448 222 TDQAAK 227
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
232-321 |
3.16e-03 |
|
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: 39.97 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 232 EKAEAER------LEQERIAAEKAEAERLEQeRIAAEK-AEAERLEQERIAAEKaEAERLEQE-----RIAAEKAEAD-- 297
Cdd:cd03406 169 EAMEAEKtklliaEQHQKVVEKEAETERKRA-VIEAEKdAEVAKIQMQQKIMEK-EAEKKISEiedemHLAREKARADae 246
|
90 100
....*....|....*....|....*..
gi 1952201083 298 --RLEQERIAAE-KAEAERLEQERIVA 321
Cdd:cd03406 247 yyRALREAEANKlKLTPEYLELKKYQA 273
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
37-124 |
3.18e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 37 QQRIEAEKAEAERLEQERIAAEKAEAERLEQErIAAEKAEAERLEqERIAAEKAEAERLEQERIAAERRDAERVEQERIA 116
Cdd:COG0542 417 ERRLEQLEIEKEALKKEQDEASFERLAELRDE-LAELEEELEALK-ARWEAEKELIEEIQELKEELEQRYGKIPELEKEL 494
|
....*...
gi 1952201083 117 AEKAEAER 124
Cdd:COG0542 495 AELEEELA 502
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
225-386 |
3.63e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 40.79 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 225 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERL-EQERIAAEKAEAERLEQERIAA---EKAEADRLE 300
Cdd:PRK10811 855 VEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVvVAEPQPEEVVVVETTHPEVIAApvtEQPQVITES 934
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 301 QERIAAEKAEaerlEQERIVAEKAEAERLEQeriAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVA 380
Cdd:PRK10811 935 DVAVAQEVAE----HAEPVVEPQDETADIEE---AAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVP 1007
|
....*.
gi 1952201083 381 QAAAEK 386
Cdd:PRK10811 1008 EATVEH 1013
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
261-360 |
3.70e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.71 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 261 AEKAEAERLEQERIAAEKAEAERLEQERIAAEkAEADRLEQERIAAEKAEAErLEQERivaeKAEAERLEQERIAAEKAE 340
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQ-ALAEAQQQELVALEGLAAE-LEEKQ----QELEAQLEQLQEKAAETS 211
|
90 100
....*....|....*....|
gi 1952201083 341 ADRLEQERIAAEKAeAERLE 360
Cdd:PRK11448 212 QERKQKRKEITDQA-AKRLE 230
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
180-335 |
4.06e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 40.41 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 180 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERL-EQERIAAEKAEAERLEQERIAAEKAEAERLEQER 258
Cdd:PRK10811 855 VEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVvVAEPQPEEVVVVETTHPEVIAAPVTEQPQVITES 934
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952201083 259 IAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIA 335
Cdd:PRK10811 935 DVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEATV 1011
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
276-375 |
4.24e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.71 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 276 AEKAEAERLEQERIAAEKAEADRLEQERIAAEkAEAERLEQERivaekAEAERLEQERIAAEKAEADRLEQERIAAEKAE 355
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQ-ALAEAQQQEL-----VALEGLAAELEEKQQELEAQLEQLQEKAAETS 211
|
90 100
....*....|....*....|
gi 1952201083 356 AERLEQERIAEEQAeAERLE 375
Cdd:PRK11448 212 QERKQKRKEITDQA-AKRLE 230
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
17-123 |
4.30e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 40.24 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 17 DKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQE--RIAAEKA-EAERLEQERIAAEKAEAERLEQErIAAEKAEAE 93
Cdd:COG2268 222 EAEEAELEQEREIETARIAEAEAELAKKKAEERREAEtaRAEAEAAyEIAEANAEREVQRQLEIAERERE-IELQEKEAE 300
|
90 100 110
....*....|....*....|....*....|
gi 1952201083 94 RLEQERIAAERRDAERVEQERIAAEKAEAE 123
Cdd:COG2268 301 REEAELEADVRKPAEAEKQAAEAEAEAEAE 330
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
489-601 |
4.31e-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: 38.30 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 489 KKPFVILmVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAgDTFRAAAVeqLqvwGERNSIPV--IAQHTGADSASVVFDaF 566
Cdd:cd17933 11 RNRVSVL-TGGAGTGKTTTLKALLAALEAEGKRVVLAA-PTGKAAKR--L---SESTGIEAstIHRLLGINPGGGGFY-Y 82
|
90 100 110
....*....|....*....|....*....|....*....
gi 1952201083 567 QAAKARNVDVLIADTAG----RLQNKdnLMQELEKIARV 601
Cdd:cd17933 83 NEENPLDADLLIVDEASmvdtRLMAA--LLSAIPAGARL 119
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
75-125 |
4.33e-03 |
|
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: 38.88 E-value: 4.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 75 AEAERLEQERIAAEKAEAERLEQERIAAERRDAERVEQERIAAEKAEAERL 125
Cdd:pfam15927 1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELKHL 51
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
18-111 |
4.35e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 18 KQQAEQAAKEADNQKQieEQQRIEAE-KAEAERLeQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERL- 95
Cdd:PRK00409 529 ERELEQKAEEAEALLK--EAEKLKEElEEKKEKL-QEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVk 605
|
90
....*....|....*.
gi 1952201083 96 EQERIAAERRDAERVE 111
Cdd:PRK00409 606 AHELIEARKRLNKANE 621
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
339-389 |
4.60e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 40.24 E-value: 4.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1952201083 339 AEADRLEQERIAAEKAEAERL--EQERIAEEQA--EAERleqekvAQAAAEKPKK 389
Cdd:PLN02316 251 LEEKRRELEKLAKEEAERERQaeEQRRREEEKAamEADR------AQAKAEVEKR 299
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
215-367 |
4.93e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 39.85 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 215 AAEKAEAERLEQERIAAEKAEAERLEQE-RIAAEKAEAErleqerIAAEKAEAERLEQERIAAEkAEAERLEQERIAAEK 293
Cdd:PRK12472 181 KAEALAAAPARAETLAREAEDAARAADEaKTAAAAAARE------AAPLKASLRKLERAKARAD-AELKRADKALAAAKT 253
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201083 294 AEAdrleqeriaaeKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADrLEQERIAAEKAEAERLEQERIAEE 367
Cdd:PRK12472 254 DEA-----------KARAEERQQKAAQQAAEAATQLDTAKADAEAKRAA-AAATKEAAKAAAAKKAETAKAATD 315
|
|
| flhF |
PRK06995 |
flagellar biosynthesis protein FlhF; |
275-672 |
5.15e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235904 [Multi-domain] Cd Length: 484 Bit Score: 39.95 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 275 AAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERleqeRIAAEKAEADRLeQERIAAEKA 354
Cdd:PRK06995 79 PAAEPAPWLVEHAKRLTAQREQLVARAAAPAAPEAQAPAAPAERAAAENAARRL----ARAAAAAPRPRV-PADAAAAVA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 355 EAERLEQERIAEEQAEAE------RLEQEKVAQAAAEKPKKEGFFARLKKGLLktrvniGSGFASIFSGKKIDDelfeel 428
Cdd:PRK06995 154 DAVKARIERIVNDTVMQElrslrgMLEEQLASLAWGERQRRDPVRAALLKHLL------AAGFSAQLVRMLVDN------ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 429 etqlLTADLGVDTTMK-----LIDNLTDAADRKQLKDGDALYELMkqemasmlktaeqplvvsndkkpfvilmvGVNGVG 503
Cdd:PRK06995 222 ----LPEGDDAEAALDwvqsaLAKNLPVLDSEDALLDRGGVFALM-----------------------------GPTGVG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 504 KTTTIGKLAKQF-QNEGKS-VMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVfdafqaAKARNVDVLIADT 581
Cdd:PRK06995 269 KTTTTAKLAARCvMRHGASkVALLTTDSYRIGGHEQLRIYGKILGVPVHAVKDAADLRLAL------SELRNKHIVLIDT 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 582 AGRLQnKDNLMqeLEKIArvmkkidpdaphevMLtidAGTGQ--------NAISQVKLFNECV------GLTGITLSKLD 647
Cdd:PRK06995 343 IGMSQ-RDRMV--SEQIA--------------ML---HGAGApvkrllllNATSHGDTLNEVVqayrgpGLAGCILTKLD 402
|
410 420
....*....|....*....|....*
gi 1952201083 648 GTAKGGVIFAVADKFNIPIRYIGVG 672
Cdd:PRK06995 403 EAASLGGALDVVIRYKLPLHYVSNG 427
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
22-149 |
5.39e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 39.86 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 22 EQAAKEADNQKQIEEQQRiEAEKAEAERlEQERIAAEKAEAERLEQERIAAEKAEAERleqeriAAEKAEAErLEQERIA 101
Cdd:COG2268 204 AEAEAERETEIAIAQANR-EAEEAELEQ-EREIETARIAEAEAELAKKKAEERREAET------ARAEAEAA-YEIAEAN 274
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1952201083 102 AER---RDAERVEQER-IAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAA 149
Cdd:COG2268 275 AERevqRQLEIAEREReIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAE 326
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
230-315 |
5.51e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.32 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 230 AAEKAEAERLEQ--ERIAAEKAEAERLeQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAE 307
Cdd:PRK11448 145 HALQQEVLTLKQqlELQAREKAQSQAL-AEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEITD 223
|
....*...
gi 1952201083 308 KAeAERLE 315
Cdd:PRK11448 224 QA-AKRLE 230
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
18-222 |
6.01e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 39.40 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 18 KQQAEQAAKEADNQKQIEEQQRIEAEKAEAErleQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQ 97
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAEEQRKKKEQQQAEEL---QQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 98 ERIAAERRDAERVEQERIAAEKAEAErlaqeqQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAE 177
Cdd:PRK09510 139 AKAAAAAKAKAEAEAKRAAAAAKKAA------AEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAA 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1952201083 178 RLEQERIAAE-KAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE 222
Cdd:PRK09510 213 AEAKKKAAAEaKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
13-367 |
6.25e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 13 FGKSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEaERLEQERIAAEKAEA 92
Cdd:COG4372 16 FGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE-EELEELNEQLQAAQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 93 ERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAE 172
Cdd:COG4372 95 ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 173 KAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE 252
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 253 RLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQE 332
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI 334
|
330 340 350
....*....|....*....|....*....|....*
gi 1952201083 333 RIAAEKAEADRLEQERIAAEKAEAERLEQERIAEE 367
Cdd:COG4372 335 LLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
60-124 |
6.55e-03 |
|
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: 38.50 E-value: 6.55e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952201083 60 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAERRDAERV-EQERIAAEKAEAER 124
Cdd:pfam15927 1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELKHLlEERKEALEKLRAEA 66
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
271-390 |
6.88e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 39.62 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 271 QEriAAEKAEAERLEQEriaaekaEADRLEQERIAAE-KAEAERLEQERIVAEKAEAERLEQERIAAE-KAEADRLEQE- 347
Cdd:PTZ00491 664 QE--AAARHQAELLEQE-------ARGRLERQKMHDKaKAEEQRTKLLELQAESAAVESSGQSRAEALaEAEARLIEAEa 734
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1952201083 348 --RIAAEKAEAERLEQEriaeeqAEAERLEQEKVAQAAAEKPKKE 390
Cdd:PTZ00491 735 evEQAELRAKALRIEAE------AELEKLRKRQELELEYEQAQNE 773
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
86-316 |
7.06e-03 |
|
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: 39.36 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 86 AAEKAEAERLEQERIAAERRDAErvEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQRE 165
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAE--LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 166 AEQAAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQerIAAEKAEAERLEQERIAAEKAEAERLEQERIA 245
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ--YLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 246 AEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQ 316
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
294-355 |
7.29e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 39.85 E-value: 7.29e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952201083 294 AEADRLEQERIAAEKAEAERleqerivaEKAEAERLEQERIAaekAEADRLEQERIAAEKAE 355
Cdd:PLN02316 251 LEEKRRELEKLAKEEAERER--------QAEEQRRREEEKAA---MEADRAQAKAEVEKRRE 301
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
193-350 |
7.33e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 39.31 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 193 RLEQERIAAEKAEAERLEQERIAAEKAEAERLE-QERIAAEKAEAERLEQERIAAEKAEAERLEQ--ERIAAEKAEAERL 269
Cdd:PRK12705 24 LLKKRQRLAKEAERILQEAQKEAEEKLEAALLEaKELLLRERNQQRQEARREREELQREEERLVQkeEQLDARAEKLDNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 270 EQERIAAEKAEAERlEQERIAAEKAEADRLEQeriaAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADrLEQERI 349
Cdd:PRK12705 104 ENQLEEREKALSAR-ELELEELEKQLDNELYR----VAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEAD-LEAERK 177
|
.
gi 1952201083 350 A 350
Cdd:PRK12705 178 A 178
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
16-224 |
7.90e-03 |
|
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: 39.65 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 16 SDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAErLEQERIAAEKAEAERL 95
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE-LEEQLETLRSKVAQLE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 96 EQERIAAERRDAERVEQERIAAEKaeaERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAE 175
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRR---ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 176 AERLEQERIAAEKAEAERleQERIAAEKAEAERLE--QERIAAEKAEAERL 224
Cdd:TIGR02168 470 LEEAEQALDAAERELAQL--QARLDSLERLQENLEgfSEGVKALLKNQSGL 518
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
27-244 |
7.95e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 39.09 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 27 EADNQKQIEEQQRiEAEKAEAERLEQERIAAEKAEAErleqeriaAEKAEAERlEQERIAAEKAEAERLEQERIAAERRD 106
Cdd:COG2268 187 DALGRRKIAEIIR-DARIAEAEAERETEIAIAQANRE--------AEEAELEQ-EREIETARIAEAEAELAKKKAEERRE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 107 AERVEQERIAA-EKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEqeraaaeqaqreaeqaaaekaeaerlEQERIA 185
Cdd:COG2268 257 AETARAEAEAAyEIAEANAEREVQRQLEIAEREREIELQEKEAEREEA--------------------------ELEADV 310
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1952201083 186 AEKAEAERLEQERIAAEKAEAERleqeriAAEKAEAERLEQERIAAEKAEAERLEQERI 244
Cdd:COG2268 311 RKPAEAEKQAAEAEAEAEAEAIR------AKGLAEAEGKRALAEAWNKLGDAAILLMLI 363
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
180-220 |
9.25e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 39.47 E-value: 9.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1952201083 180 EQERIAAEKAEAERL--EQERIAAEKA--EAERLEQERIAAEKAE 220
Cdd:PLN02316 257 ELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEKRRE 301
|
|
| HC2 |
pfam07382 |
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like ... |
241-373 |
9.30e-03 |
|
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like nucleoprotein HC2 (approximately 200 residues long), which seems to be found mostly in Chlamydia. HC2 functions in DNA condensation, although it has been suggested that it also has other roles.
Pssm-ID: 369339 [Multi-domain] Cd Length: 187 Bit Score: 37.84 E-value: 9.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 241 QERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIV 320
Cdd:pfam07382 5 QKKRSSKKTAAKKAAVRKPAAKKAAAKKTVVRKVAAKKPAARKTVAKKTVAAKKPAAKKAAKKAVAKKVVAKKPVAKKAV 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1952201083 321 AEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAER 373
Cdd:pfam07382 85 AKKATAKKVAAKKVVAKKTVAKKAAAKKPAAKKAVAKKAVARKPAAKKAVAKK 137
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
54-282 |
9.52e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 39.02 E-value: 9.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 54 RIAAEKAEAERLEQERIAAEKAEAERLEQErIAAEKAEAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAE 133
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQK-QAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 134 QQRQEQQARLAEQEAAMKLeqeraaaeqaqreaeqaaaekaeaerleqeriaaeKAEAERLEQERIAAEKAEAERLEQER 213
Cdd:PRK09510 145 AKAKAEAEAKRAAAAAKKA-----------------------------------AAEAKKKAEAEAAKKAAAEAKKKAEA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952201083 214 IAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE 282
Cdd:PRK09510 190 EAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
180-384 |
9.56e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 39.19 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 180 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERiaAEKAEAERLEQERI 259
Cdd:PRK07735 13 EAARRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAK--QKREGTEEVTEEEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 260 AAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKA 339
Cdd:PRK07735 91 AKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1952201083 340 EADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAA 384
Cdd:PRK07735 171 AAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKA 215
|
|
|