|
Name |
Accession |
Description |
Interval |
E-value |
| ZUO1 |
COG5269 |
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ... |
75-368 |
2.86e-70 |
|
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227594 [Multi-domain] Cd Length: 379 Bit Score: 232.23 E-value: 2.86e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 75 MLKTLDPKDWKNQDHYAVLGLGHVRYKATQRQIKAAHKTMVLKHHPDKRKAAGEpikEGDNDYFTCITKAYEMLSDPVKR 154
Cdd:COG5269 31 LYTREDFKNWKKVDLYALLGLSKYRTKAIPPQILKAHKKKVYKYHPDKTAAGGN---KGCDEFFKLIQKAREVLGDRKLR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 155 RAFNSVDptFDNSVPS-KSEAKENFFQVFSPVFERNSRWSNKKNVPKLGDMNSSFEDVDAFYSFWYNFDSWREFSYLDEE 233
Cdd:COG5269 108 LQYDSND--FDADVPPpRIYTPDEFFEVWEPVFEREARFSKKQPVPSLGPSDSSLKEVEEFYEFWSNFDSWRTFEPLDED 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 234 EKEKAECRDERKWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEGKAKKEAEKRAKAEARRKEQEAKEKQR 313
Cdd:COG5269 186 YPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRIKSFKEQEKEMKKIRKWEREAGARLKALAALKGK 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 158138509 314 QAEleavrlaKEKEEEEVRQQALLA---KKEKEIQKKAIKKERQKLRNSCKNWNHFSD 368
Cdd:COG5269 266 AEA-------KNKAEIEAEALASATavkKKAKEVMKKALKMEKKAIKNAAKDADYFGD 316
|
|
| RAC_head |
pfam16717 |
Ribosome-associated complex head domain; The RAC head domain is involved in ribosome binding. |
344-420 |
6.15e-17 |
|
Ribosome-associated complex head domain; The RAC head domain is involved in ribosome binding.
Pssm-ID: 435537 Cd Length: 87 Bit Score: 76.15 E-value: 6.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 344 IQKKAIKKERQKLRNSCKNWNHFSDNEADRVKM----MEEVEKLCDRLELASLQCLNEILASST-REVGKAALEKQIEEV 418
Cdd:pfam16717 1 AAKKALKKNKRVLRGSVKDANYFADGEAEKAAVidgvLADVDLLCEKLDDEELAELAEKLEGAKdAEAVKAVFEEEVKEL 80
|
..
gi 158138509 419 NE 420
Cdd:pfam16717 81 VD 82
|
|
| DnaJ |
pfam00226 |
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
88-158 |
6.29e-14 |
|
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.
Pssm-ID: 395170 [Multi-domain] Cd Length: 63 Bit Score: 66.73 E-value: 6.29e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158138509 88 DHYAVLGLGHvryKATQRQIKAAHKTMVLKHHPDKrkaagEPIKEGDNDYFTCITKAYEMLSDPVKRRAFN 158
Cdd:pfam00226 1 DYYEILGVSP---DASDEEIKKAYRKLALKYHPDK-----NPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
|
|
| DnaJ |
cd06257 |
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
88-150 |
1.79e-11 |
|
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.
Pssm-ID: 99751 [Multi-domain] Cd Length: 55 Bit Score: 59.48 E-value: 1.79e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158138509 88 DHYAVLGlghVRYKATQRQIKAAHKTMVLKHHPDKRkaagePIKEGDNDYFTCITKAYEMLSD 150
Cdd:cd06257 1 DYYDILG---VPPDASDEEIKKAYRKLALKYHPDKN-----PDDPEAEEKFKEINEAYEVLSD 55
|
|
| DnaJ |
smart00271 |
DnaJ molecular chaperone homology domain; |
87-153 |
2.49e-11 |
|
DnaJ molecular chaperone homology domain;
Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 59.17 E-value: 2.49e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158138509 87 QDHYAVLGLGHvryKATQRQIKAAHKTMVLKHHPDKRKAAgepiKEGDNDYFTCITKAYEMLSDPVK 153
Cdd:smart00271 1 TDYYEILGVPR---DASLDEIKKAYRKLALKYHPDKNPGD----KEEAEEKFKEINEAYEVLSDPEK 60
|
|
| PRK10767 |
PRK10767 |
chaperone protein DnaJ; Provisional |
87-157 |
2.04e-10 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 62.85 E-value: 2.04e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158138509 87 QDHYAVLGlghVRYKATQRQIKAAHKTMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAF 157
Cdd:PRK10767 4 RDYYEVLG---VSRNASEDEIKKAYRKLAMKYHPDRNpgdKEAEEKFKE--------IKEAYEVLSDPQKRAAY 66
|
|
| SANT |
cd00167 |
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ... |
553-600 |
4.40e-10 |
|
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.
Pssm-ID: 238096 [Multi-domain] Cd Length: 45 Bit Score: 55.27 E-value: 4.40e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 158138509 553 PWTTEEQKLLEQALKTYPVNtpeRWEKIAEAVPGRTKKDCMRRYKELV 600
Cdd:cd00167 1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELPGRTPKQCRERWRNLL 45
|
|
| SANT |
smart00717 |
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains; |
553-602 |
3.21e-09 |
|
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
Pssm-ID: 197842 [Multi-domain] Cd Length: 49 Bit Score: 53.00 E-value: 3.21e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 158138509 553 PWTTEEQKLLEQALKTYPVNtpeRWEKIAEAVPGRTKKDCMRRYKELVEM 602
Cdd:smart00717 3 EWTEEEDELLIELVKKYGKN---NWEKIAKELPGRTAEQCRERWRNLLKP 49
|
|
| Myb_DNA-binding |
pfam00249 |
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ... |
553-599 |
3.62e-08 |
|
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.
Pssm-ID: 459731 [Multi-domain] Cd Length: 46 Bit Score: 49.81 E-value: 3.62e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 158138509 553 PWTTEEQKLLEQALKTYPvntpERWEKIAEAVPGRTKKDCMRRYKEL 599
Cdd:pfam00249 3 PWTPEEDELLLEAVEKLG----NRWKKIAKLLPGRTDNQCKNRWQNY 45
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
232-355 |
3.86e-06 |
|
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: 49.46 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 232 EEEKEKAECRDERKWIEKQNRATRAQRKKEEMNRIRtlvdnayscdPRIKKFKEEGKAKKEAEKRAKAEARRKEQEAKEK 311
Cdd:TIGR02794 79 EAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQA----------EEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEA 148
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 158138509 312 QRQAELEAvrLAKEKEEEEVRQQALLAKKEKEIQKKAIKKERQK 355
Cdd:TIGR02794 149 AKQAEEEA--KAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAK 190
|
|
| SANT |
cd00167 |
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ... |
453-506 |
1.95e-03 |
|
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.
Pssm-ID: 238096 [Multi-domain] Cd Length: 45 Bit Score: 36.40 E-value: 1.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 158138509 453 NWSEDDLQLLIKAVNLFPAGtnsRWEVIANYMNihsssgvKRTAKDVIGKAKSL 506
Cdd:cd00167 1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELP-------GRTPKQCRERWRNL 44
|
|
| zuotin_NTD |
cd23953 |
N-terminal domain of fungal ribosome associated J-protein zuotin and similar proteins; Zuotin, ... |
13-47 |
3.22e-03 |
|
N-terminal domain of fungal ribosome associated J-protein zuotin and similar proteins; Zuotin, also known as DnaJ-related protein ZUO1, J protein ZUO1, or heat shock protein 40 homolog ZUO1, is a component of the ribosome-associated complex (RAC), which is a heterodimer of the Hsp70/DnaK-type chaperone SSZ1 and the Hsp40/DnaJ-type chaperone ZUO1. The RAC chaperone complex plays a role in regulating accurate translation termination and folding or maintaining nascent polypeptides in a folding-competent state. The ATPase activity of the ribosome-associated pool of Hsp70-type chaperones SSB1/SSB2 that bind to the nascent polypeptide chain is stimulated by the RAC chaperone complex. ZUO1 acts as a J-protein for SSB1/SSB2 only when it is associated with SSZ1. The N-terminal domain (NTD) of ZUO1 is responsible for its interaction with SSZ1, and it contains a conserved LP-motif that binds to the SSZ1 C-terminal SBD (substrate binding domain) beta-lid domain in the same way as canonical Hsp70s bind to their substrates.
Pssm-ID: 467935 Cd Length: 38 Bit Score: 35.56 E-value: 3.22e-03
10 20 30
....*....|....*....|....*....|....*..
gi 158138509 13 TAITHALTSASAVCQVEPVGRWFEAFV--KRRNRNAS 47
Cdd:cd23953 2 SAVVHASLSAPVTRKLEPVGPAFLAHArrKLHNRTFS 38
|
|
| SANT |
smart00717 |
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains; |
452-508 |
5.52e-03 |
|
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
Pssm-ID: 197842 [Multi-domain] Cd Length: 49 Bit Score: 35.28 E-value: 5.52e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 158138509 452 KNWSEDDLQLLIKAVNLFPAGtnsRWEVIANYMNihsssgvKRTAKDVIGKAKSLQK 508
Cdd:smart00717 2 GEWTEEEDELLIELVKKYGKN---NWEKIAKELP-------GRTAEQCRERWRNLLK 48
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZUO1 |
COG5269 |
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ... |
75-368 |
2.86e-70 |
|
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227594 [Multi-domain] Cd Length: 379 Bit Score: 232.23 E-value: 2.86e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 75 MLKTLDPKDWKNQDHYAVLGLGHVRYKATQRQIKAAHKTMVLKHHPDKRKAAGEpikEGDNDYFTCITKAYEMLSDPVKR 154
Cdd:COG5269 31 LYTREDFKNWKKVDLYALLGLSKYRTKAIPPQILKAHKKKVYKYHPDKTAAGGN---KGCDEFFKLIQKAREVLGDRKLR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 155 RAFNSVDptFDNSVPS-KSEAKENFFQVFSPVFERNSRWSNKKNVPKLGDMNSSFEDVDAFYSFWYNFDSWREFSYLDEE 233
Cdd:COG5269 108 LQYDSND--FDADVPPpRIYTPDEFFEVWEPVFEREARFSKKQPVPSLGPSDSSLKEVEEFYEFWSNFDSWRTFEPLDED 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 234 EKEKAECRDERKWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEGKAKKEAEKRAKAEARRKEQEAKEKQR 313
Cdd:COG5269 186 YPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRIKSFKEQEKEMKKIRKWEREAGARLKALAALKGK 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 158138509 314 QAEleavrlaKEKEEEEVRQQALLA---KKEKEIQKKAIKKERQKLRNSCKNWNHFSD 368
Cdd:COG5269 266 AEA-------KNKAEIEAEALASATavkKKAKEVMKKALKMEKKAIKNAAKDADYFGD 316
|
|
| RAC_head |
pfam16717 |
Ribosome-associated complex head domain; The RAC head domain is involved in ribosome binding. |
344-420 |
6.15e-17 |
|
Ribosome-associated complex head domain; The RAC head domain is involved in ribosome binding.
Pssm-ID: 435537 Cd Length: 87 Bit Score: 76.15 E-value: 6.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 344 IQKKAIKKERQKLRNSCKNWNHFSDNEADRVKM----MEEVEKLCDRLELASLQCLNEILASST-REVGKAALEKQIEEV 418
Cdd:pfam16717 1 AAKKALKKNKRVLRGSVKDANYFADGEAEKAAVidgvLADVDLLCEKLDDEELAELAEKLEGAKdAEAVKAVFEEEVKEL 80
|
..
gi 158138509 419 NE 420
Cdd:pfam16717 81 VD 82
|
|
| DnaJ |
pfam00226 |
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
88-158 |
6.29e-14 |
|
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.
Pssm-ID: 395170 [Multi-domain] Cd Length: 63 Bit Score: 66.73 E-value: 6.29e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158138509 88 DHYAVLGLGHvryKATQRQIKAAHKTMVLKHHPDKrkaagEPIKEGDNDYFTCITKAYEMLSDPVKRRAFN 158
Cdd:pfam00226 1 DYYEILGVSP---DASDEEIKKAYRKLALKYHPDK-----NPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
|
|
| DnaJ |
cd06257 |
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
88-150 |
1.79e-11 |
|
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.
Pssm-ID: 99751 [Multi-domain] Cd Length: 55 Bit Score: 59.48 E-value: 1.79e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158138509 88 DHYAVLGlghVRYKATQRQIKAAHKTMVLKHHPDKRkaagePIKEGDNDYFTCITKAYEMLSD 150
Cdd:cd06257 1 DYYDILG---VPPDASDEEIKKAYRKLALKYHPDKN-----PDDPEAEEKFKEINEAYEVLSD 55
|
|
| DnaJ |
smart00271 |
DnaJ molecular chaperone homology domain; |
87-153 |
2.49e-11 |
|
DnaJ molecular chaperone homology domain;
Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 59.17 E-value: 2.49e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158138509 87 QDHYAVLGLGHvryKATQRQIKAAHKTMVLKHHPDKRKAAgepiKEGDNDYFTCITKAYEMLSDPVK 153
Cdd:smart00271 1 TDYYEILGVPR---DASLDEIKKAYRKLALKYHPDKNPGD----KEEAEEKFKEINEAYEVLSDPEK 60
|
|
| CbpA |
COG2214 |
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; |
87-157 |
1.18e-10 |
|
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
Pssm-ID: 441816 [Multi-domain] Cd Length: 91 Bit Score: 58.19 E-value: 1.18e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158138509 87 QDHYAVLGLGHvryKATQRQIKAAHKTMVLKHHPDKrkaaGEPIKEGDNDYFTCITKAYEMLSDPVKRRAF 157
Cdd:COG2214 5 KDHYAVLGVPP---DASLEEIRQAYRRLAKLLHPDR----GGELKALAEELFQRLNEAYEVLSDPERRAEY 68
|
|
| PRK10767 |
PRK10767 |
chaperone protein DnaJ; Provisional |
87-157 |
2.04e-10 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 62.85 E-value: 2.04e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158138509 87 QDHYAVLGlghVRYKATQRQIKAAHKTMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAF 157
Cdd:PRK10767 4 RDYYEVLG---VSRNASEDEIKKAYRKLAMKYHPDRNpgdKEAEEKFKE--------IKEAYEVLSDPQKRAAY 66
|
|
| DnaJ |
COG0484 |
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
88-157 |
2.68e-10 |
|
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440252 [Multi-domain] Cd Length: 139 Bit Score: 58.95 E-value: 2.68e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158138509 88 DHYAVLGlghVRYKATQRQIKAAHKTMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAF 157
Cdd:COG0484 1 DYYEILG---VSRDASAEEIKKAYRKLAKKYHPDRNpgdPEAEEKFKE--------INEAYEVLSDPEKRAAY 62
|
|
| SANT |
cd00167 |
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ... |
553-600 |
4.40e-10 |
|
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.
Pssm-ID: 238096 [Multi-domain] Cd Length: 45 Bit Score: 55.27 E-value: 4.40e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 158138509 553 PWTTEEQKLLEQALKTYPVNtpeRWEKIAEAVPGRTKKDCMRRYKELV 600
Cdd:cd00167 1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELPGRTPKQCRERWRNLL 45
|
|
| PRK14282 |
PRK14282 |
chaperone protein DnaJ; Provisional |
87-209 |
1.15e-09 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184603 [Multi-domain] Cd Length: 369 Bit Score: 60.58 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 87 QDHYAVLGlghVRYKATQRQIKAAHKTMVLKHHPDK----RKAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFNSVDP 162
Cdd:PRK14282 4 KDYYEILG---VSRNATQEEIKRAYKRLVKEWHPDRhpenRKEAEQKFKE--------IQEAYEVLSDPQKRAMYDRFGY 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158138509 163 TFDNSVPSKSEAKENFFQ-------------VFSPVFERNSRWSNKKNVPKLG-DMNSSFE 209
Cdd:PRK14282 73 VGEQPPYQETESGGGFFEdifkdfenifnrdIFDIFFGERRTQEEQREYARRGeDIRYEIE 133
|
|
| SANT |
smart00717 |
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains; |
553-602 |
3.21e-09 |
|
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
Pssm-ID: 197842 [Multi-domain] Cd Length: 49 Bit Score: 53.00 E-value: 3.21e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 158138509 553 PWTTEEQKLLEQALKTYPVNtpeRWEKIAEAVPGRTKKDCMRRYKELVEM 602
Cdd:smart00717 3 EWTEEEDELLIELVKKYGKN---NWEKIAKELPGRTAEQCRERWRNLLKP 49
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
281-442 |
9.15e-09 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 58.25 E-value: 9.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 281 KKFKE-EGKAK---KEAEKRAKAEARRKEQEAKEKQRQAELEAVRLAKEKEEEEVRQQALLAKKEKEIQKK--AIKKERQ 354
Cdd:PRK12704 31 AKIKEaEEEAKrilEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKleLLEKREE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 355 KLRNSCKNWNHfsdneadRVKMMEEVEKLCDRLELASLQCLNEIlASSTREVGKAALEKQIE-----EVNELMRKEKEEA 429
Cdd:PRK12704 111 ELEKKEKELEQ-------KQQELEKKEEELEELIEEQLQELERI-SGLTAEEAKEILLEKVEeearhEAAVLIKEIEEEA 182
|
170
....*....|...
gi 158138509 430 darMRQASKNAEK 442
Cdd:PRK12704 183 ---KEEADKKAKE 192
|
|
| PRK14276 |
PRK14276 |
chaperone protein DnaJ; Provisional |
86-210 |
1.44e-08 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237653 [Multi-domain] Cd Length: 380 Bit Score: 57.02 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 86 NQDHYAVLGlghVRYKATQRQIKAAHKTMVLKHHPDKRKAAG--EPIKEgdndyftcITKAYEMLSDPVKRRAFNSVDPT 163
Cdd:PRK14276 3 NTEYYDRLG---VSKDASQDEIKKAYRKLSKKYHPDINKEPGaeEKYKE--------VQEAYETLSDPQKRAAYDQYGAA 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158138509 164 ---------------FDNsvpskSEAKENFFQVFSPVFERNSRWSNkKNVPKLGD-----MNSSFED 210
Cdd:PRK14276 72 ganggfgggaggfggFDG-----SGGFGGFEDIFSSFFGGGGARRN-PNAPRQGDdlqyrVNLDFEE 132
|
|
| PRK14291 |
PRK14291 |
chaperone protein DnaJ; Provisional |
87-217 |
1.94e-08 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237661 [Multi-domain] Cd Length: 382 Bit Score: 56.70 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 87 QDHYAVLGlghVRYKATQRQIKAAHKTMVLKHHPD--KRKAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFNSvdptF 164
Cdd:PRK14291 3 KDYYEILG---VSRNATQEEIKKAYRRLARKYHPDfnKNPEAEEKFKE--------INEAYQVLSDPEKRKLYDQ----F 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 158138509 165 DNSVPSKSEAKENFFQVFSPVFERNsrwsnkknvpkLGDMnssFEDVDAFYSF 217
Cdd:PRK14291 68 GHAAFSGSGQQQQGQEGFSDFGGGN-----------IEDI---LEDVFDIFGF 106
|
|
| PRK14295 |
PRK14295 |
molecular chaperone DnaJ; |
82-167 |
2.32e-08 |
|
molecular chaperone DnaJ;
Pssm-ID: 237665 [Multi-domain] Cd Length: 389 Bit Score: 56.40 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 82 KDWKNQDHYAVLGlghVRYKATQRQIKAAHKTMVLKHHPDKRKaaGEPIKEgdnDYFTCITKAYEMLSDPVKRRAFNSVD 161
Cdd:PRK14295 4 KDYIEKDYYKVLG---VPKDATEAEIKKAYRKLAREYHPDANK--GDAKAE---ERFKEISEAYDVLSDEKKRKEYDEAR 75
|
....*.
gi 158138509 162 PTFDNS 167
Cdd:PRK14295 76 SLFGNG 81
|
|
| PRK14299 |
PRK14299 |
chaperone protein DnaJ; Provisional |
87-159 |
3.20e-08 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237667 [Multi-domain] Cd Length: 291 Bit Score: 55.33 E-value: 3.20e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158138509 87 QDHYAVLGlghVRYKATQRQIKAAHKTMVLKHHPDKRKAAGEPIKegdndyFTCITKAYEMLSDPVKRRAFNS 159
Cdd:PRK14299 4 KDYYAILG---VPKNASQDEIKKAFKKLARKYHPDVNKSPGAEEK------FKEINEAYTVLSDPEKRRIYDT 67
|
|
| Myb_DNA-binding |
pfam00249 |
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ... |
553-599 |
3.62e-08 |
|
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.
Pssm-ID: 459731 [Multi-domain] Cd Length: 46 Bit Score: 49.81 E-value: 3.62e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 158138509 553 PWTTEEQKLLEQALKTYPvntpERWEKIAEAVPGRTKKDCMRRYKEL 599
Cdd:pfam00249 3 PWTPEEDELLLEAVEKLG----NRWKKIAKLLPGRTDNQCKNRWQNY 45
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
233-621 |
4.16e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 233 EEKEKAecrDERKWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEGKAKKEAEKRAKAEARRKEQEAKEKQ 312
Cdd:PTZ00121 1287 EEKKKA---DEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAE 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 313 RQAELEAVRLAKEKEE-EEVRQQALLAKKEKEIQKKA----IKKERQKLRNSCKNWNHFSDNEADRVKMMEEVEKLCDRL 387
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKaDAAKKKAEEKKKADEAKKKAeedkKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA 1443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 388 ELASLQCLNEILASSTREVGKAALEKQIEEVNELMRKEKEEADarmrQASKNAEKSTGRSGSGSKNWSEDDlqlliKAVN 467
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD----EAKKKAEEAKKKADEAKKAAEAKK-----KADE 1514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 468 LFPAGTNSRWEvianymniHSSSGVKRTAKDVIGKAKSLQKLDPHQKDDINKKAFDKFKKEHGVAPQADSAAPSERFEgp 547
Cdd:PTZ00121 1515 AKKAEEAKKAD--------EAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE-- 1584
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158138509 548 cidsiPWTTEEQKLLEQALKTYPVNTPERWEKIAEAVPGRTKKDCMRRYKELVEMV-KAKKAAQEQVLNASRARK 621
Cdd:PTZ00121 1585 -----EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVeQLKKKEAEEKKKAEELKK 1654
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
233-457 |
4.49e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 233 EEKEKAEcrDERKWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEGKAKKEAEKRAKAEARRKEQEAK--E 310
Cdd:PTZ00121 1454 EEAKKAE--EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKkaE 1531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 311 KQRQAE----------LEAVRLAKEKEEEEVRQQALLAKKEKEIQKKAIKK-------ERQKLRNSCKNWNHFSDNEADR 373
Cdd:PTZ00121 1532 EAKKADeakkaeekkkADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaeeakkaEEARIEEVMKLYEEEKKMKAEE 1611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 374 VKMMEEVEKLCDRLELAS--LQCLNEILASSTREVGKAALEKQIEEVNELMRKE---KEEADARMRQASKNAEKSTGRSG 448
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKKAEeeKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEeakKAEEDKKKAEEAKKAEEDEKKAA 1691
|
....*....
gi 158138509 449 SGSKNWSED 457
Cdd:PTZ00121 1692 EALKKEAEE 1700
|
|
| PTZ00037 |
PTZ00037 |
DnaJ_C chaperone protein; Provisional |
86-158 |
4.63e-08 |
|
DnaJ_C chaperone protein; Provisional
Pssm-ID: 240236 [Multi-domain] Cd Length: 421 Bit Score: 55.60 E-value: 4.63e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158138509 86 NQDHYAVLGLGHvryKATQRQIKAAHKTMVLKHHPDKrkaagepikEGDNDYFTCITKAYEMLSDPVKRRAFN 158
Cdd:PTZ00037 27 NEKLYEVLNLSK---DCTTSEIKKAYRKLAIKHHPDK---------GGDPEKFKEISRAYEVLSDPEKRKIYD 87
|
|
| PRK14278 |
PRK14278 |
chaperone protein DnaJ; Provisional |
88-155 |
5.81e-08 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237654 [Multi-domain] Cd Length: 378 Bit Score: 55.06 E-value: 5.81e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 88 DHYAVLGlghVRYKATQRQIKAAHKTMVLKHHPD--KRKAAGEPIKEgdndyftcITKAYEMLSDPVKRR 155
Cdd:PRK14278 4 DYYGLLG---VSRNASDAEIKRAYRKLARELHPDvnPDEEAQEKFKE--------ISVAYEVLSDPEKRR 62
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
232-433 |
7.36e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 7.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 232 EEEKEKAEcrDERKWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEGKAKKEAEK-RAKAEARRKEQEAK- 309
Cdd:PTZ00121 1374 EEAKKKAD--AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEaKKKAEEAKKADEAKk 1451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 310 --EKQRQAELEAVRLAKEKEEEEVRQQALLAKKEKEIQKKA--IKKERQKLRNSCKNWNHFSD-NEADRVKMMEEVEKLC 384
Cdd:PTZ00121 1452 kaEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAeeAKKKADEAKKAAEAKKKADEaKKAEEAKKADEAKKAE 1531
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 158138509 385 DRLELASLQCLNEIlaSSTREVGKAALEKQIEEVNELMRKEKEEADARM 433
Cdd:PTZ00121 1532 EAKKADEAKKAEEK--KKADELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
|
| PRK14286 |
PRK14286 |
chaperone protein DnaJ; Provisional |
86-158 |
1.40e-07 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172774 [Multi-domain] Cd Length: 372 Bit Score: 53.84 E-value: 1.40e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158138509 86 NQDHYAVLGlghVRYKATQRQIKAAHKTMVLKHHPDKRKAAGEPikegdNDYFTCITKAYEMLSDPVKRRAFN 158
Cdd:PRK14286 3 ERSYYDILG---VSKSANDEEIKSAYRKLAIKYHPDKNKGNKES-----EEKFKEATEAYEILRDPKKRQAYD 67
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
231-428 |
1.42e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 231 DEEEKEKAE----CRDERKWIEKQNRATRAQRKKEEmnrirtlvdnayscdpRIKKFKEEGKAKKEAEKRAKAEARRKEQ 306
Cdd:PTZ00121 1615 AEEAKIKAEelkkAEEEKKKVEQLKKKEAEEKKKAE----------------ELKKAEEENKIKAAEEAKKAEEDKKKAE 1678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 307 EAKEKQRQAELEAVRLakEKEEEEVRQQALLAKKEKEIQKKAIKKERQKLRNSCKNWNHFSDNEADRVKMMEEVEKLCDR 386
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEAL--KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 158138509 387 LELASLQCLNEILASSTREVGKAALEKQIEEVNELMRKEKEE 428
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| PRK14277 |
PRK14277 |
chaperone protein DnaJ; Provisional |
87-158 |
1.44e-07 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184599 [Multi-domain] Cd Length: 386 Bit Score: 54.04 E-value: 1.44e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158138509 87 QDHYAVLGlghVRYKATQRQIKAAHKTMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFN 158
Cdd:PRK14277 5 KDYYEILG---VDRNATEEEIKKAYRRLAKKYHPDLNpgdKEAEQKFKE--------INEAYEILSDPQKRAQYD 68
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
232-443 |
1.65e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 232 EEEKEKAEcrDERKWIEKQNRATRAQRKKEEMNRIRTL---VDNAYSCDPRIKKFKEEGKA----KKEAEKRAKAEARRK 304
Cdd:PTZ00121 1414 AAAKKKAD--EAKKKAEEKKKADEAKKKAEEAKKADEAkkkAEEAKKAEEAKKKAEEAKKAdeakKKAEEAKKADEAKKK 1491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 305 EQEAKEKQRqaelEAVRLAKEKEEEEVRQQALLAKKEKEIQKKAIKKERQKLRNSCKNWNHFSDNEADRVKMMEEVEKlc 384
Cdd:PTZ00121 1492 AEEAKKKAD----EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK-- 1565
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 158138509 385 drLELASLQCLNEILASSTREVGKAALEKQIEEVNELMRKEKEEADARMRQASKNAEKS 443
Cdd:PTZ00121 1566 --AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
|
| PRK14298 |
PRK14298 |
chaperone protein DnaJ; Provisional |
87-158 |
3.55e-07 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184612 [Multi-domain] Cd Length: 377 Bit Score: 52.93 E-value: 3.55e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158138509 87 QDHYAVLGLGHvryKATQRQIKAAHKTMVLKHHPDKRKAAGEpikegdNDYFTCITKAYEMLSDPVKRRAFN 158
Cdd:PRK14298 5 RDYYEILGLSK---DASVEDIKKAYRKLAMKYHPDKNKEPDA------EEKFKEISEAYAVLSDAEKRAQYD 67
|
|
| PRK14297 |
PRK14297 |
molecular chaperone DnaJ; |
86-154 |
4.27e-07 |
|
molecular chaperone DnaJ;
Pssm-ID: 184611 [Multi-domain] Cd Length: 380 Bit Score: 52.48 E-value: 4.27e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158138509 86 NQDHYAVLGLghvRYKATQRQIKAAHKTMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKR 154
Cdd:PRK14297 3 SKDYYEVLGL---EKGASDDEIKKAFRKLAIKYHPDKNkgnKEAEEKFKE--------INEAYQVLSDPQKK 63
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
232-357 |
6.20e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 52.18 E-value: 6.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 232 EEEKEKAEC-RDERKWIEKQNRAT---RAQRKKEEMNRIrtlvdnayscdprikkfkeegKAKKEAEKR-AKAEARRKEQ 306
Cdd:COG2268 200 DARIAEAEAeRETEIAIAQANREAeeaELEQEREIETAR---------------------IAEAEAELAkKKAEERREAE 258
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 158138509 307 EAKEKQRQAeleaVRLAKEKEEEEVRQQALLAKKEKEI--QKKAIKKERQKLR 357
Cdd:COG2268 259 TARAEAEAA----YEIAEANAEREVQRQLEIAEREREIelQEKEAEREEAELE 307
|
|
| PRK14294 |
PRK14294 |
chaperone protein DnaJ; Provisional |
87-187 |
8.09e-07 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237664 [Multi-domain] Cd Length: 366 Bit Score: 51.69 E-value: 8.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 87 QDHYAVLGlghVRYKATQRQIKAAHKTMVLKHHPDKR---KAAGEPIKEGdndyftciTKAYEMLSDPVKRRAFNSVDPT 163
Cdd:PRK14294 4 RDYYEILG---VTRDASEEEIKKSYRKLAMKYHPDRNpgdKEAEELFKEA--------AEAYEVLSDPKKRGIYDQYGHE 72
|
90 100
....*....|....*....|....*
gi 158138509 164 -FDNSVPSKSEAKENFFQVFSPVFE 187
Cdd:PRK14294 73 gLSGTGFSGFSGFDDIFSSFGDIFE 97
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
232-441 |
8.42e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 8.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 232 EEEKEKAECRDERKWIEKQNRATRAQRKKEEMNRIRTlvdnayscdpRIKKFKEEGKAKKEAEKRAKAEARRKEQE-AKE 310
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRL----------ELEELELELEEAQAEEYELLAELARLEQDiARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 311 KQRQAELEAVRLAKEKEEEEVRQQALLAKKEKEIQKKAIKKERQKLRNSCKNWNHFSDNEADRVKMMEEVEKLCDRLELA 390
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 158138509 391 SLQCLNEILASSTREVGKAALEKQIEEVNELMRKEKEEADARMRQASKNAE 441
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
|
| PRK14280 |
PRK14280 |
molecular chaperone DnaJ; |
87-210 |
8.67e-07 |
|
molecular chaperone DnaJ;
Pssm-ID: 237656 [Multi-domain] Cd Length: 376 Bit Score: 51.65 E-value: 8.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 87 QDHYAVLGLGHvryKATQRQIKAAHKTMVLKHHPDKRKAAG--EPIKEgdndyftcITKAYEMLSDPVKRR---AFNSVD 161
Cdd:PRK14280 4 RDYYEVLGVSK---SASKDEIKKAYRKLSKKYHPDINKEEGadEKFKE--------ISEAYEVLSDDQKRAqydQFGHAG 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 158138509 162 P--TFDNSVPSKSEAKENF-FQ-VFSPVFERNSRwSNKKNVPKLGD-----MNSSFED 210
Cdd:PRK14280 73 PnqGFGGGGFGGGDFGGGFgFEdIFSSFFGGGGR-RRDPNAPRQGAdlqytMTLTFEE 129
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
232-442 |
9.90e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 9.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 232 EEEKEKAECRDERKWIEKQNRATRAQRKKEEMNRI-RTLVDNAYSCDPRIKKFKEEgKAKKEAEKRAKAEARRKEQEAKE 310
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAeEARIEEVMKLYEEEKKMKAE-EAKKAEEAKIKAEELKKAEEEKK 1633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 311 KQRQ---AELEAVRLAKE--KEEEEVR-QQALLAKKEKEIQKKAikKERQKLRNSCKNWNHFSDNEADRVKMMEEVEKlc 384
Cdd:PTZ00121 1634 KVEQlkkKEAEEKKKAEElkKAEEENKiKAAEEAKKAEEDKKKA--EEAKKAEEDEKKAAEALKKEAEEAKKAEELKK-- 1709
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158138509 385 drlelaslqclneilaSSTREVGKAALEKQIEEVN----ELMRKEKEEADARMRQASKNAEK 442
Cdd:PTZ00121 1710 ----------------KEAEEKKKAEELKKAEEENkikaEEAKKEAEEDKKKAEEAKKDEEE 1755
|
|
| PRK14284 |
PRK14284 |
chaperone protein DnaJ; Provisional |
88-158 |
1.36e-06 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237658 [Multi-domain] Cd Length: 391 Bit Score: 51.00 E-value: 1.36e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158138509 88 DHYAVLGlghVRYKATQRQIKAAHKTMVLKHHPDKRKAAGEPIKEgdndyFTCITKAYEMLSDPVKRRAFN 158
Cdd:PRK14284 2 DYYTILG---VSKTASPEEIKKAYRKLAVKYHPDKNPGDAEAEKR-----FKEVSEAYEVLSDAQKRESYD 64
|
|
| PRK14290 |
PRK14290 |
chaperone protein DnaJ; Provisional |
87-158 |
1.73e-06 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172778 [Multi-domain] Cd Length: 365 Bit Score: 50.70 E-value: 1.73e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158138509 87 QDHYAVLGlghVRYKATQRQIKAAHKTMVLKHHPD----KRKAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFN 158
Cdd:PRK14290 3 KDYYKILG---VDRNASQEDIKKAFRELAKKWHPDlhpgNKAEAEEKFKE--------ISEAYEVLSDPQKRRQYD 67
|
|
| PRK14281 |
PRK14281 |
chaperone protein DnaJ; Provisional |
87-158 |
1.88e-06 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237657 [Multi-domain] Cd Length: 397 Bit Score: 50.58 E-value: 1.88e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158138509 87 QDHYAVLGLGHvryKATQRQIKAAHKTMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFN 158
Cdd:PRK14281 3 RDYYEVLGVSR---SADKDEIKKAYRKLALKYHPDKNpdnKEAEEHFKE--------VNEAYEVLSNDDKRRRYD 66
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
232-355 |
3.86e-06 |
|
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: 49.46 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 232 EEEKEKAECRDERKWIEKQNRATRAQRKKEEMNRIRtlvdnayscdPRIKKFKEEGKAKKEAEKRAKAEARRKEQEAKEK 311
Cdd:TIGR02794 79 EAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQA----------EEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEA 148
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 158138509 312 QRQAELEAvrLAKEKEEEEVRQQALLAKKEKEIQKKAIKKERQK 355
Cdd:TIGR02794 149 AKQAEEEA--KAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAK 190
|
|
| PRK14292 |
PRK14292 |
chaperone protein DnaJ; Provisional |
88-154 |
4.49e-06 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237662 [Multi-domain] Cd Length: 371 Bit Score: 49.12 E-value: 4.49e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158138509 88 DHYAVLGlghVRYKATQRQIKAAHKTMVLKHHPDKRKaagepiKEGDNDYFTCITKAYEMLSDPVKR 154
Cdd:PRK14292 3 DYYELLG---VSRTASADEIKSAYRKLALKYHPDRNK------EKGAAEKFAQINEAYAVLSDAEKR 60
|
|
| PRK14293 |
PRK14293 |
molecular chaperone DnaJ; |
88-154 |
1.13e-05 |
|
molecular chaperone DnaJ;
Pssm-ID: 237663 [Multi-domain] Cd Length: 374 Bit Score: 48.06 E-value: 1.13e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158138509 88 DHYAVLGlghVRYKATQRQIKAAHKTMVLKHHPDKRKaagEPikeGDNDYFTCITKAYEMLSDPVKR 154
Cdd:PRK14293 4 DYYEILG---VSRDADKDELKRAYRRLARKYHPDVNK---EP---GAEDRFKEINRAYEVLSDPETR 61
|
|
| PRK14289 |
PRK14289 |
molecular chaperone DnaJ; |
87-158 |
2.23e-05 |
|
molecular chaperone DnaJ;
Pssm-ID: 237660 [Multi-domain] Cd Length: 386 Bit Score: 47.13 E-value: 2.23e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158138509 87 QDHYAVLGlghVRYKATQRQIKAAHKTMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFN 158
Cdd:PRK14289 5 RDYYEVLG---VSKTATVDEIKKAYRKKAIQYHPDKNpgdKEAEEKFKE--------AAEAYDVLSDPDKRSRYD 68
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
230-352 |
2.31e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.11 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 230 LDEEEKEKAECRDERKWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIK---------------KFKEEGKAKKEAE 294
Cdd:PRK09510 103 LKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKraaaaakkaaaeakkKAEAEAAKKAAAE 182
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 158138509 295 KRAKAEARRKEQEAKEKQRQAELEavrlAKEKEEEEVRQQALLAKKEKEIQKKAIKKE 352
Cdd:PRK09510 183 AKKKAEAEAAAKAAAEAKKKAEAE----AKKKAAAEAKKKAAAEAKAAAAKAAAEAKA 236
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
229-621 |
2.39e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 229 YLDEEEKEKAECRDERKWIEKQNRATRAQRKKEEMNR---IRTLVDNAYSCDPRIKKFKEEGKAKKEAEKRA-----KAE 300
Cdd:PTZ00121 1208 AEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKaeeERNNEEIRKFEEARMAHFARRQAAIKAEEARKadelkKAE 1287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 301 ARRKEQEAK--EKQRQAELEAVRLAKEKEEEEVRQQALLAKKEKEIQKKaiKKERQKlrnscknwnhfsdnEADRVKMME 378
Cdd:PTZ00121 1288 EKKKADEAKkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKK--KAEEAK--------------KAAEAAKAE 1351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 379 EvEKLCDRLELASLQCLNEILASSTREVGKAALEKQIEEVnelmrKEKEEADARMRQASKNAEKSTGRSGSGSKnwsEDD 458
Cdd:PTZ00121 1352 A-EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK-----KKADEAKKKAEEDKKKADELKKAAAAKKK---ADE 1422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 459 LQllikavnlfpagtnSRWEVIANYMNIHSSSGVKRTAKDVIGKAKSLQKLDPHQKDDINKKAFDKFKKEHGVAPQADSA 538
Cdd:PTZ00121 1423 AK--------------KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEA 1488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 539 APSERFEGPCIDSIPWTTEEQKLLEQALKTYPVNTPERWEKIAEAvpgrTKKDCMRRYKELVEMVKAKKAaqEQVLNASR 618
Cdd:PTZ00121 1489 KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEA----KKADEAKKAEEKKKADELKKA--EELKKAEE 1562
|
...
gi 158138509 619 ARK 621
Cdd:PTZ00121 1563 KKK 1565
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
278-442 |
2.47e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 278 PRIKKFKEEGKAKKEAEKRAKAEARRKEQEAKEKQRQAELEAVRLAKEKEEEEVRQQalLAKKEKEIQKKAIKKERQKLR 357
Cdd:COG4717 61 PQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREE--LEKLEKLLQLLPLYQELEALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 358 NS----CKNWNHFSDNEADRVKMMEEVEKLCDRLELASLQClnEILASSTREVGKAALEKQIEEVNELmRKEKEEADARM 433
Cdd:COG4717 139 AElaelPERLEELEERLEELRELEEELEELEAELAELQEEL--EELLEQLSLATEEELQDLAEELEEL-QQRLAELEEEL 215
|
....*....
gi 158138509 434 RQASKNAEK 442
Cdd:COG4717 216 EEAQEELEE 224
|
|
| PRK14285 |
PRK14285 |
chaperone protein DnaJ; Provisional |
87-187 |
9.26e-05 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172773 [Multi-domain] Cd Length: 365 Bit Score: 44.98 E-value: 9.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 87 QDHYAVLGLGHvryKATQRQIKAAHKTMVLKHHPDKRKAAGEPikegdNDYFTCITKAYEMLSDPVKRRAFNSvdptFDN 166
Cdd:PRK14285 3 RDYYEILGLSK---GASKDEIKKAYRKIAIKYHPDKNKGNKEA-----ESIFKEATEAYEVLIDDNKRAQYDR----FGH 70
|
90 100
....*....|....*....|....
gi 158138509 167 SVPSKSEAKENF---FQVFSPVFE 187
Cdd:PRK14285 71 TAFEGGGGFEGFsggFSGFSDIFE 94
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
252-442 |
1.01e-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: 45.43 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 252 RATRAQRKKEEMN--RIRTLVDnayscdpRIKKFKEEGKAKKEAEKRAkaEARRKEQEAKEKQRQAELEAVRLAK-EKEE 328
Cdd:TIGR02168 211 KAERYKELKAELRelELALLVL-------RLEELREELEELQEELKEA--EEELEELTAELQELEEKLEELRLEVsELEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 329 EEVRQQALL-----AKKEKEIQKKAIKKERQKLRNSCKNWNHFSDN-EADRVKMMEEVEKLCDRLELASLQCLNEILASS 402
Cdd:TIGR02168 282 EIEELQKELyalanEISRLEQQKQILRERLANLERQLEELEAQLEElESKLDELAEELAELEEKLEELKEELESLEAELE 361
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 158138509 403 TREVGKAALEKQIEEVNELMRKEKEEADARMRQASKNAEK 442
Cdd:TIGR02168 362 ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
231-355 |
1.47e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.41 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 231 DEEEKEKAECRDERKWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRiKKFKEEGKAKKEAE-KRAKAEARRKEQEAK 309
Cdd:PRK09510 90 EELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAA-AKAAAAAKAKAEAEaKRAAAAAKKAAAEAK 168
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 158138509 310 EK-QRQAELEAVRLAKEKEEEEVRQQALL---AKKEKEIQKKAIKKERQK 355
Cdd:PRK09510 169 KKaEAEAAKKAAAEAKKKAEAEAAAKAAAeakKKAEAEAKKKAAAEAKKK 218
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
230-345 |
1.81e-04 |
|
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: 44.73 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 230 LDEEEKEKAECRDERKWIEKQNRATRAQRKKEEMNRiRTLVDnayscdpriKKFKEEGKAKKEAEKRAKAEA-RRKEQEA 308
Cdd:pfam17380 479 LEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERK-RKLLE---------KEMEERQKAIYEEERRREAEEeRRKQQEM 548
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 158138509 309 KEKQR------QAELEAVRL-AKEKEEEEVRQQALLAKKEKEIQ 345
Cdd:pfam17380 549 EERRRiqeqmrKATEERSRLeAMEREREMMRQIVESEKARAEYE 592
|
|
| DjlA |
COG1076 |
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; |
87-151 |
2.56e-04 |
|
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440694 [Multi-domain] Cd Length: 75 Bit Score: 39.78 E-value: 2.56e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158138509 87 QDHYAVLGLGHvryKATQRQIKAAHKTMVLKHHPDkRKAAGEPIKEGD--NDYFTCITKAYEMLSDP 151
Cdd:COG1076 4 DDAFELLGLPP---DADDAELKRAYRKLQREHHPD-RLAAGLPEEEQRlaLQKAAAINEAYETLKDP 66
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
231-348 |
2.68e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 231 DEEEKEKAECRDERKWIEKQNRATRAQRkkEEMNRIRTLVDNAYSCDPRIKKFKEEgKAKKEAEKRAKAEARRKEQEAKE 310
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELL--EALRAAAELAAQLEELEEAEEALLER-LERLEEELEELEEALAELEEEEE 438
|
90 100 110
....*....|....*....|....*....|....*...
gi 158138509 311 KQRQAELEAVRLAKEKEEEEVRQQALLAKKEKEIQKKA 348
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
230-436 |
3.78e-04 |
|
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: 43.57 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 230 LDEEEKEKAECRDERKWIEKQNRATRAqrkkeEMNRIRTLvdnaYSCDPRIKKFKE-EGKAKKEAEKRAKAEARRKEQEA 308
Cdd:pfam17380 301 LRQEKEEKAREVERRRKLEEAEKARQA-----EMDRQAAI----YAEQERMAMERErELERIRQEERKRELERIRQEEIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 309 KEKQRQAELEAVRLAKEKEEEEVRQQALLAKKEKEIQKKAIKKERQKLRNSCKNWNHFSDNEADRVKMME-----EVEKL 383
Cdd:pfam17380 372 MEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEeerarEMERV 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 158138509 384 cdRLELASLQCLNEILASSTREVGKAALEKQIEE-----VNELMRKEKEEADARMRQA 436
Cdd:pfam17380 452 --RLEEQERQQQVERLRQQEEERKRKKLELEKEKrdrkrAEEQRRKILEKELEERKQA 507
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
203-621 |
4.65e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 203 DMNSSF--EDVDAFYSFWYNFDSWREFSYLDEEEKEKAECRDERKWIEKQNRATRAQRKKEEMNRIR-TLVDNAYScdpr 279
Cdd:PTZ00121 1019 DFNQNFniEKIEELTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEdNRADEATE---- 1094
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 280 ikkfkeegKAKKEAEKRAKAEARRKEQEAKEKQRQAELEAVRLAKE-KEEEEVR--QQALLAKKEKEIQKKAIKKERQKL 356
Cdd:PTZ00121 1095 --------EAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEaRKAEDARkaEEARKAEDAKRVEIARKAEDARKA 1166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 357 RNSCKNWNHFSDNEADR---VKMMEEVEKLCDRLELASLQCLNEIlaSSTREVGKAALEKQIEEVNELMRKEKEEADARM 433
Cdd:PTZ00121 1167 EEARKAEDAKKAEAARKaeeVRKAEELRKAEDARKAEAARKAEEE--RKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKK 1244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 434 RQASKNAEKStgRSGSGSKNWSEDDLQLLIKAVNLFPAGTNSRWEVIANYMNIHSSSGVKRtAKDVIGKAKSLQKLDPHQ 513
Cdd:PTZ00121 1245 AEEERNNEEI--RKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK-ADEAKKKAEEAKKADEAK 1321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 514 K---------DDINKKAFDKFKKEHGVAPQADSAAPSERFEGPCIDSIPWTTEEQKLLEQALKTYPVNTPERWEKIAEAV 584
Cdd:PTZ00121 1322 KkaeeakkkaDAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE 1401
|
410 420 430
....*....|....*....|....*....|....*..
gi 158138509 585 PGRTKKDCMRRYKELVEMVKAKKAAQEQVLNASRARK 621
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK 1438
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
246-355 |
4.86e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 246 WIEKQNRATRAQRKKEEmnriRTLVDNAYSCDPRIKKFKEEGKAKKEAEKRAKAEARRKEQE-----AKEKQRQAELEAV 320
Cdd:PRK09510 64 YNRQQQQQKSAKRAEEQ----RKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEeaakqAALKQKQAEEAAA 139
|
90 100 110
....*....|....*....|....*....|....*....
gi 158138509 321 RL---AKEKEEEEVRQQALLAKK-EKEIQKKAIKKERQK 355
Cdd:PRK09510 140 KAaaaAKAKAEAEAKRAAAAAKKaAAEAKKKAEAEAAKK 178
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
288-353 |
5.32e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 42.18 E-value: 5.32e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158138509 288 KAKKEAEKRAKAEARRKEQEAKEkQRQAELEAVRLAKEKEEEEVRQQaLLAKKEKEIQKKAIKKER 353
Cdd:cd16269 196 KEKEIEAERAKAEAAEQERKLLE-EQQRELEQKLEDQERSYEEHLRQ-LKEKMEEERENLLKEQER 259
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
294-442 |
5.59e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 294 EKRAKAEARRKEQEAKEKQRQAELEAVrlakEKEEEEVRQQALLAKKEKEIQKKAIKKERQKLRNSCKNWNHF----SDN 369
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAEL----EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLeerrREL 314
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158138509 370 EADRVKMMEEVEKLCDRLELASLQCLNEILASSTREVGKAALEKQIEEVNELMRKEKEEADARMRQASKNAEK 442
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
232-621 |
5.61e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 232 EEEKEKAECRDERKWIEKQNRATRAQ--RKKEEMNRIRTlvDNAYSCDPRIKKFKEEGKAKKEAEKRAKAEARRKEQEAK 309
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARKAEEARKAEdaRKAEEARKAED--AKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRK 1189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 310 EKQRQAELEAVRLAKEKEEEEVRQQALLAKKEKEIQKKAIKKERQKLRNScknwnhfsdNEADRVKMMEEVEKLCDRLEL 389
Cdd:PTZ00121 1190 AEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDA---------EEAKKAEEERNNEEIRKFEEA 1260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 390 ASLQCLNEILASSTREVGKAALEKQIEEVNELMRKEKEEADARMRQASKNAEKStgRSGSGSKNWSEDDLQlliKAVNLF 469
Cdd:PTZ00121 1261 RMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA--KKADEAKKKAEEAKK---KADAAK 1335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 470 PAGTNSRWEVIAnymnihsSSGVKRTAKDVIGKAKSLQKLDPHQKDDINKKAfDKFKKEHGVAPQADSAAPSERFEGPCI 549
Cdd:PTZ00121 1336 KKAEEAKKAAEA-------AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA-DAAKKKAEEKKKADEAKKKAEEDKKKA 1407
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158138509 550 DSIPWTTEEQKLLEQALKtypvntpeRWEKIAEAVPGRTKKDCMRRYKELVEMVKAKKAAQEQVLNASRARK 621
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKK--------KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
293-355 |
6.69e-04 |
|
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.
Pssm-ID: 462322 Cd Length: 323 Bit Score: 42.17 E-value: 6.69e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158138509 293 AEKRAKAEARRKEQEAK-----EKQRQAELEAVRLAKEKEEEEvrqqALLAKKEKEIQKKAIKKERQK 355
Cdd:pfam07946 256 PEALKKAKKTREEEIEKikkaaEEERAEEAQEKKEEAKKKERE----EKLAKLSPEEQRKYEEKERKK 319
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
224-370 |
7.63e-04 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 42.15 E-value: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 224 WREFSYLDEEEKEKAECRDERKwiEKQnRATRAQRKKEEMNRIRTLVDnayscdP-RIKKFKEEGKAKKEAekrakaear 302
Cdd:PRK00247 274 ERKYPLTDEFKEHHAEQRAQYR--EKQ-KEKKAFLWTLRRNRLRMIIT------PwRAPELHAENAEIKKT--------- 335
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158138509 303 RKEQEAKEKQRQAELEAVRLAKEKEEEEVRQQALLAKKEKEIQK-KAIKKERQKLRNSCKNWNHFSDNE 370
Cdd:PRK00247 336 RTAEKNEAKARKKEIAQKRRAAEREINREARQERAAAMARARARrAAVKAKKKGLIDASPNEDTPSENE 404
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
232-342 |
9.81e-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: 41.75 E-value: 9.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 232 EEEKEKAECRDERKWIEKQNRATRAQRKKEEMnrirtlvdnayscdPRIKKFKEEGKAKKEAEKRAKAEARRK--EQEAK 309
Cdd:TIGR02794 130 AEAKAKAEAEAERKAKEEAAKQAEEEAKAKAA--------------AEAKKKAEEAKKKAEAEAKAKAEAEAKakAEEAK 195
|
90 100 110
....*....|....*....|....*....|...
gi 158138509 310 EKQRQAELEAVRLAKEKEEEEVRQQALLAKKEK 342
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERK 228
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
219-430 |
1.03e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.27 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 219 YNFDSWREFSYLDEEEKEKAECRDERKWIEKqnRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEGKAKKEaeKRAK 298
Cdd:pfam02463 256 SKQEIEKEEEKLAQVLKENKEEEKEKKLQEE--ELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE--KELK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 299 AE-----ARRKEQEAKEKQRQAELEAV-RLAKEKEEEEVRQQALLAKKEKEIQKKAIKKERQKLRNSCKNWNHFSDNEAD 372
Cdd:pfam02463 332 KEkeeieELEKELKELEIKREAEEEEEeELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLL 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 158138509 373 RVKMMEEVEKLCDRLELASLqcLNEILASSTREVGKAALEKQIEEVNELMRKEKEEAD 430
Cdd:pfam02463 412 ELARQLEDLLKEEKKEELEI--LEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
|
|
| SANT_CDC5_II |
cd11659 |
SANT/myb-like DNA-binding domain of Cell Division Cycle 5-Like Protein repeat II; In humans, ... |
547-601 |
1.04e-03 |
|
SANT/myb-like DNA-binding domain of Cell Division Cycle 5-Like Protein repeat II; In humans, cell division cycle 5-like protein (CDC5) functions in pre-mRNA splicing in cell cycle control. The DNA-binding, myb-like domain of CDC5 is a member of the SANT/myb group. SANT is named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. The SANT domain resembles the 3 alpha-helix bundle of DNA-binding Myb domains and is found in a diverse set of proteins.
Pssm-ID: 212557 [Multi-domain] Cd Length: 53 Bit Score: 37.29 E-value: 1.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 158138509 547 PCIDSIPWTTEEQKLLEQALKTYPvntpERWEKIAEAVpGRTKKDCMRRYKELVE 601
Cdd:cd11659 1 PSIKKTEWTREEDEKLLHLAKLLP----TQWRTIAPIV-GRTAQQCLERYNKLLD 50
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
295-431 |
1.14e-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: 42.35 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 295 KRAKAEARRKEQEAKEKQRQAELEAVRLAKEKEEEEVRqQALLAKKEKEIQKKAIKKERQKLRNSCKNWNH-FSDNEADR 373
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELE-QLRKELEELSRQISALRKDLARLEAEVEQLEErIAQLSKEL 756
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 158138509 374 VKMMEEVEKLCDRLELASlqclneiLASSTREVGKAALEKQIEEVNELMRKEKEEADA 431
Cdd:TIGR02168 757 TELEAEIEELEERLEEAE-------EELAEAEAEIEELEAQIEQLKEELKALREALDE 807
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
230-447 |
1.17e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.03 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 230 LDEEEKEKAECRDER--KWIEKQNRATRAQRKKEEMN-RIRTLVDNAyscdpRIKKFKEEGKAKKEAEKRAKAEARRKEQ 306
Cdd:pfam17380 355 QEERKRELERIRQEEiaMEISRMRELERLQMERQQKNeRVRQELEAA-----RKVKILEEERQRKIQQQKVEMEQIRAEQ 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 307 EAK--------EKQRQAELEAVRLAK----------EKEEEEVRQQALLAKKEKEIQKKAIKKERQKLRNscknwnhfsD 368
Cdd:pfam17380 430 EEArqrevrrlEEERAREMERVRLEEqerqqqverlRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK---------E 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158138509 369 NEADRVKMMEEVEKlcdrlelaslqclNEILASSTREVGKAALEKQIEEVNELMRKEKEEADARMRQASKNAEKSTGRS 447
Cdd:pfam17380 501 LEERKQAMIEEERK-------------RKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERS 566
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
231-354 |
1.27e-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: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 231 DEEEKEKAECRDERKWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEGKAKKEAEKRAKAEARRKEQEAKE 310
Cdd:pfam05672 8 DAEEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEE 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 158138509 311 KQRQAELEAVRLAKEKEEEEVRQQALLAKK--EKEIQKKAIKKERQ 354
Cdd:pfam05672 88 REQREQEEQERLQKQKEEAEAKAREEAERQrqEREKIMQQEEQERL 133
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
243-446 |
1.35e-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: 41.97 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 243 ERKWIEKQNRATRAQRKKEEMNRIRTLVDNayscdpRIKKFKEEGKAKKEAEKRAKAEARRKEQEAKEKQRQAElEAVRL 322
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELES------KLDELAEELAELEEKLEELKEELESLEAELEELEAELE-ELESR 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 323 AKEKEEEEVRQQALLAKKEKEIqkKAIKKERQKLRnscknwNHFSDNEADRVKMMEEVEKLCDRLELASLQCLNEILASS 402
Cdd:TIGR02168 374 LEELEEQLETLRSKVAQLELQI--ASLNNEIERLE------ARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 158138509 403 TREVGKAALEK-QIEEVNELMRKEKEEADARMRQASKNAEKSTGR 446
Cdd:TIGR02168 446 EEELEELQEELeRLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
|
| SANT |
cd00167 |
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ... |
453-506 |
1.95e-03 |
|
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.
Pssm-ID: 238096 [Multi-domain] Cd Length: 45 Bit Score: 36.40 E-value: 1.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 158138509 453 NWSEDDLQLLIKAVNLFPAGtnsRWEVIANYMNihsssgvKRTAKDVIGKAKSL 506
Cdd:cd00167 1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELP-------GRTPKQCRERWRNL 44
|
|
| PLN03086 |
PLN03086 |
PRLI-interacting factor K; Provisional |
281-339 |
2.15e-03 |
|
PRLI-interacting factor K; Provisional
Pssm-ID: 178635 [Multi-domain] Cd Length: 567 Bit Score: 41.01 E-value: 2.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 158138509 281 KKFKEEGKAKKEAEKRAKAEARRKEQEAKEKQRQAELEAVRlAKEKEEEEVRQQALLAK 339
Cdd:PLN03086 17 RERKQRAKLKLERERKAKEEAAKQREAIEAAQRSRRLDAIE-AQIKADQQMQESLQAGR 74
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
232-356 |
2.23e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.56 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 232 EEEKEKAECRDERKWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEE-GKAKKEAEKRAKAEARRKEQEAKE 310
Cdd:PRK09510 135 EEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAeAAAKAAAEAKKKAEAEAKKKAAAE 214
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 158138509 311 KQRQAELEAvRLAKEKEEEEVRQQALLAKKEKEIQKKAIKKERQKL 356
Cdd:PRK09510 215 AKKKAAAEA-KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
257-355 |
3.20e-03 |
|
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.
Pssm-ID: 462259 [Multi-domain] Cd Length: 353 Bit Score: 39.97 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 257 QRKKEEMNRIRTlvdnayscdpRIKKFKEEGKAKkEAEKRAKAEaRRKEQEAKEKQRQAELEAVRLAKEKEEEEVRQ-QA 335
Cdd:pfam07767 212 LKEEEKLERVLE----------KIAESAATAEAR-EEKRKTKAQ-RNKEKRRKEEEREAKEEKALKKKLAQLERLKEiAK 279
|
90 100
....*....|....*....|
gi 158138509 336 LLAKKEKEIQKKAIKKERQK 355
Cdd:pfam07767 280 EIAEKEKEREEKAEARKREK 299
|
|
| zuotin_NTD |
cd23953 |
N-terminal domain of fungal ribosome associated J-protein zuotin and similar proteins; Zuotin, ... |
13-47 |
3.22e-03 |
|
N-terminal domain of fungal ribosome associated J-protein zuotin and similar proteins; Zuotin, also known as DnaJ-related protein ZUO1, J protein ZUO1, or heat shock protein 40 homolog ZUO1, is a component of the ribosome-associated complex (RAC), which is a heterodimer of the Hsp70/DnaK-type chaperone SSZ1 and the Hsp40/DnaJ-type chaperone ZUO1. The RAC chaperone complex plays a role in regulating accurate translation termination and folding or maintaining nascent polypeptides in a folding-competent state. The ATPase activity of the ribosome-associated pool of Hsp70-type chaperones SSB1/SSB2 that bind to the nascent polypeptide chain is stimulated by the RAC chaperone complex. ZUO1 acts as a J-protein for SSB1/SSB2 only when it is associated with SSZ1. The N-terminal domain (NTD) of ZUO1 is responsible for its interaction with SSZ1, and it contains a conserved LP-motif that binds to the SSZ1 C-terminal SBD (substrate binding domain) beta-lid domain in the same way as canonical Hsp70s bind to their substrates.
Pssm-ID: 467935 Cd Length: 38 Bit Score: 35.56 E-value: 3.22e-03
10 20 30
....*....|....*....|....*....|....*..
gi 158138509 13 TAITHALTSASAVCQVEPVGRWFEAFV--KRRNRNAS 47
Cdd:cd23953 2 SAVVHASLSAPVTRKLEPVGPAFLAHArrKLHNRTFS 38
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
286-377 |
3.48e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 40.39 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 286 EGKAKKEAEkrAKAEARRKEQEAKEKQRQAELEAVRLAKEKEEEEVRQ-QALLAKKEKEIQKKAIKKERQklrnscknwn 364
Cdd:PTZ00491 714 SGQSRAEAL--AEAEARLIEAEAEVEQAELRAKALRIEAEAELEKLRKrQELELEYEQAQNELEIAKAKE---------- 781
|
90
....*....|...
gi 158138509 365 hFSDNEADRVKMM 377
Cdd:PTZ00491 782 -LADIEATKFERI 793
|
|
| SANT |
smart00717 |
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains; |
452-508 |
5.52e-03 |
|
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
Pssm-ID: 197842 [Multi-domain] Cd Length: 49 Bit Score: 35.28 E-value: 5.52e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 158138509 452 KNWSEDDLQLLIKAVNLFPAGtnsRWEVIANYMNihsssgvKRTAKDVIGKAKSLQK 508
Cdd:smart00717 2 GEWTEEEDELLIELVKKYGKN---NWEKIAKELP-------GRTAEQCRERWRNLLK 48
|
|
| eIF3_subunit |
pfam08597 |
Translation initiation factor eIF3 subunit; This is a family of proteins which are subunits of ... |
284-343 |
6.00e-03 |
|
Translation initiation factor eIF3 subunit; This is a family of proteins which are subunits of the eukaryotic translation initiation factor 3 (eIF3). In yeast it is called Hcr1. The Saccharomyces cerevisiae protein Swiss:Q05775 has been shown to be required for processing of 20S pre-rRNA and binds to 18S rRNA and eIF3 subunits Rpg1p and Prt1p.
Pssm-ID: 462530 Cd Length: 239 Bit Score: 38.81 E-value: 6.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158138509 284 KEEGKAKKEAEKRAKAEARRKEQEAKEKQ--RQAELEAVRLAKEKEEEEVRQQALLAKKEKE 343
Cdd:pfam08597 45 EEKEKAAKAAAAKAKKKKKSKKQKIAEKEaeRKAEEEAEEEEELTPEDEAARKLRLRKAEEE 106
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
225-371 |
7.64e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 39.34 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 225 REFSYLDEEEKEKAEC-----RDERKWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEGKAK---KEAEKR 296
Cdd:pfam17380 446 REMERVRLEEQERQQQverlrQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKlleKEMEER 525
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158138509 297 AKAEARRKEQEAKEKQRQAEleavrlaKEKEEEEVRQQALLAKKEKEIQKKAIKKERQKLRNSCKNWNHFSDNEA 371
Cdd:pfam17380 526 QKAIYEEERRREAEEERRKQ-------QEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEA 593
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
247-375 |
8.00e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.42 E-value: 8.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158138509 247 IEK-QNRATRAQRKKEEMNRIRTLVDnayscdprikKFKEEGKAKKEAEKRAKAEARRK-EQEAKEKQRQAELEAVRLAK 324
Cdd:PRK00409 522 IASlEELERELEQKAEEAEALLKEAE----------KLKEELEEKKEKLQEEEDKLLEEaEKEAQQAIKEAKKEADEIIK 591
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 158138509 325 EKEEEEVRQQALLAKKE-KEIQK---KAIKKERQKLRNSCKNWNHFsdNEADRVK 375
Cdd:PRK00409 592 ELRQLQKGGYASVKAHElIEARKrlnKANEKKEKKKKKQKEKQEEL--KVGDEVK 644
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
291-359 |
8.08e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 37.03 E-value: 8.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158138509 291 KEAEKrAKAEARRKEQEAKEKQRQAELEAVRL------AKEKEEEEVRQQALL-AKKEKEIQKKAIKKERQKLRNS 359
Cdd:cd06503 40 EEAEK-AKEEAEELLAEYEEKLAEARAEAQEIieearkEAEKIKEEILAEAKEeAERILEQAKAEIEQEKEKALAE 114
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