|
Name |
Accession |
Description |
Interval |
E-value |
| ANTH |
pfam07651 |
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ... |
30-299 |
8.02e-93 |
|
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.
Pssm-ID: 400137 Cd Length: 272 Bit Score: 286.89 E-value: 8.02e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 30 TQAISISKAINTQEAPVKEKHARRIILGTHH-EKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLHDCQRY 108
Cdd:pfam07651 1 DLEVAVVKATSHDEAPPKEKHVREILVGTSSsAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 109 RSNIREIGDLWGH-LHDRYGQLVNVYTKLLLTKISFHLKHPQFPAGLEVTDEVLeKAAGTDVNNIFqLTVEMFDYMDCEL 187
Cdd:pfam07651 81 RRRISSLLRISSFsLSWDYGAFIRAYAKYLDERLDFHRKLPRDPGTFERVEYGS-LVAVGDPNERY-LTMSMEDLLDSIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 188 KLSESVFRQLNTAIAVSQMsSGQCRLAPLIQVIQDCSHLYHYTVKLLFKLHSCLP------ADTLQGHRDRFHEQFHSLR 261
Cdd:pfam07651 159 KLQKLLFRLLKCRPTGNAL-SNECIIAALILLVKESFGLYRAINEGIINLLEKFFelskpdADRALGIYKRFVKQFERLK 237
|
250 260 270
....*....|....*....|....*....|....*...
gi 733605517 262 NFFRRASDMLYFKRLIqIPRLPEGPPNFLRasALAEHI 299
Cdd:pfam07651 238 EFYEVCKNLGYFRSLE-IPKLPHIPPNLLE--ALEEYL 272
|
|
| ANTH_N_HIP1R |
cd17014 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
31-144 |
4.90e-83 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1-related protein; Huntingtin-interacting protein 1-related protein (HIP1R), also called HIP12, promotes clathrin assembly in vitro. It is an endocytic protein involved in receptor trafficking, including regulating cell surface expression of receptor tyrosine kinases. Low HIP1R protein expression is associated with worse survival in diffuse large B-cell lymphoma (DLBCL) patients; it is preferentially expressed in germinal center B-cell (GCB)-like DLBCL, and may be potentially useful in subtyping DLBCL cases. HIP1R contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of mammalian HIP1R was found to preferentially bind PtdIns(3,5)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1-related protein.
Pssm-ID: 340811 Cd Length: 114 Bit Score: 255.56 E-value: 4.90e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 31 QAISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLHDCQRYRS 110
Cdd:cd17014 1 QAISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLQDCQRYRS 80
|
90 100 110
....*....|....*....|....*....|....
gi 733605517 111 NIREIGDLWGHLHDRYGQLVNVYTKLLLTKISFH 144
Cdd:cd17014 81 NIRETGSLWGHLHDRYGQLVSLYTKLLCTKIEFH 114
|
|
| ANTH_N_HIP1_like |
cd17006 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
31-144 |
1.23e-65 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1 and related proteins; This subfamily includes Huntingtin-interacting protein 1 (HIP1), HIP1-related protein (HIP1R), and similar proteins. Mammalian HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 is expressed only in neurons while HIP1R is ubiquitously expressed. Together with its interacting partner HIPPI, HIP1 regulates apoptosis and gene expression. Both HIP1 and HIP1R promote clathrin assembly in vitro, and they share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. Mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively, instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of the ANTH domain of Huntingtin-interacting protein 1 and related proteins.
Pssm-ID: 340803 Cd Length: 114 Bit Score: 210.22 E-value: 1.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 31 QAISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLHDCQRYRS 110
Cdd:cd17006 1 QAISINKAINPQEVPVKEKHVRSIIIGTHQEKGASTFWSIVSRLPLQGNPIVCWKFCHLLHKLLREGHPSVLRDSQRYRS 80
|
90 100 110
....*....|....*....|....*....|....
gi 733605517 111 NIREIGDLWGHLHDRYGQLVNVYTKLLLTKISFH 144
Cdd:cd17006 81 RLKELGKLWGHLKDGYGKLIAQYCKLLITKLEFH 114
|
|
| ANTH_N_HIP1 |
cd17013 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
31-144 |
1.72e-52 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1; Huntingtin-interacting protein 1 (HIP1) was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 promotes clathrin assembly in vitro. Together with its interacting partner HIPPI, it regulates apoptosis and gene expression. HIP1 contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of mammalian HIP1 was found to preferentially bind PtdIns(3,4)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1.
Pssm-ID: 340810 Cd Length: 114 Bit Score: 175.61 E-value: 1.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 31 QAISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLHDCQRYRS 110
Cdd:cd17013 1 QTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 80
|
90 100 110
....*....|....*....|....*....|....
gi 733605517 111 NIREIGDLWGHLHDRYGQLVNVYTKLLLTKISFH 144
Cdd:cd17013 81 ELSDMSRMWGHLSEGYGQLCSIYLKLLITKMEFH 114
|
|
| ENTH |
smart00273 |
Epsin N-terminal homology (ENTH) domain; |
30-151 |
2.59e-37 |
|
Epsin N-terminal homology (ENTH) domain;
Pssm-ID: 214594 Cd Length: 127 Bit Score: 134.68 E-value: 2.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 30 TQAISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSS--ILSWKFCHVLHKVLRDGHPNVLHDCQR 107
Cdd:smart00273 2 DLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTKnwRVVYKALILLHYLLRNGSPRVILEALR 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 733605517 108 YRSNIREIGDLWGHLHD--RYGQLVNVYTKLLLTKISFHLKHPQFP 151
Cdd:smart00273 82 NRNRILNLSDFQDIDSRgkDQGANIRTYAKYLLERLEDDRRLKEER 127
|
|
| HIP1_clath_bdg |
pfam16515 |
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ... |
461-559 |
3.33e-34 |
|
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil region of Huntington-interacting proteins 1. It carries a highly conserved HADLLRKN sequence motif at its N-terminus which effects the binding of HIP1R to clathrin light-chain EED regulatory site. this binding then stimulates clathrin lattice assembly. Huntingtin-interacting protein 1 (HIP1) is an obligate binding partner for Huntungtin, and loss of this interaction triggers the cascade of events that results in the apoptosis of neuronal cells and the onset of Hungtinton's disease. Clathrin light-chain binds to a flexible coiled-coil domain in HIP1 and induces a compact state that is refractory to actin binding.
Pssm-ID: 465154 [Multi-domain] Cd Length: 99 Bit Score: 125.12 E-value: 3.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 461 HAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRESELKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQ 540
Cdd:pfam16515 1 HADLLRKNAETTKQLTVAQQAQEEVEREKKQLEFELERAKEEAQMKLEEQKEELERLKRELESSRAELATLQSTLQSSEQ 80
|
90
....*....|....*....
gi 733605517 541 SKSELSSRLDTLSAEKDAL 559
Cdd:pfam16515 81 SGSQLSSQLAALQAEKEGL 99
|
|
| ANTH_N_Sla2p_HIP1_like |
cd16986 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; ... |
34-144 |
1.58e-23 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; Members of the Sla2p/HIP1/HIP1R subfamily share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. Both HIP1 and HIP1R promote clathrin assembly in vitro. Yeast Sla2p, is a regulator of membrane cytoskeleton assembly. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. While the ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome, mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively. This model describes the N-terminal region of ANTH domains of the Sla2p/HIP1/HIP1R subfamily.
Pssm-ID: 340783 Cd Length: 117 Bit Score: 95.91 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 34 SISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLHDCQRYRSNIR 113
Cdd:cd16986 4 AVNKATNKTDSPPKPKHVRTIIVKSWTHQKGPQFYEELSKRLLLNNPVVQFKALVTLHKVLRDGPPELSLLGGYLDAWLP 83
|
90 100 110
....*....|....*....|....*....|....
gi 733605517 114 EIGDL---WGHLHDRYGQLVNVYTKLLLTKISFH 144
Cdd:cd16986 84 ELVRVkntQQSLSEFYSQLIKKYVRYLELKVVFH 117
|
|
| ANTH_N_Sla2p |
cd17007 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; ... |
33-144 |
2.31e-21 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; This subfamily is composed of Saccharomyces cerevisiae Sla2 protein (Sla2p, also called transmembrane protein MOP2), Schizosaccharomyces pombe endocytosis protein End4 (End4p, also called Sla2 protein homolog), and similar proteins. In yeast, cells lacking Sla2p have severe defects in actin organization, cell morphology, and endocytosis, suggesting roles in these processes. Sla2p regulates the Eps15-like Arp2/3 complex activator, Pan1p, controlling actin polymerization during endocytosis. In fission yeast, End4p has been implicated in cellular morphogenesis. Sla2p contains an N-terminal ANTH, a central colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domains f Sla2p and similar proteins.
Pssm-ID: 340804 Cd Length: 115 Bit Score: 89.67 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 33 ISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLHDCQRYRSNI 112
Cdd:cd17007 3 VAIKKACSSDETAPKRKHVRACIVYTWDHKSSKPFWNALKTQPLLSDEVQCFKALITIHKVLQEGHPSALKEAIRNIEWL 82
|
90 100 110
....*....|....*....|....*....|...
gi 733605517 113 REIGDLW-GHLHDRYGQLVNVYTKLLLTKISFH 144
Cdd:cd17007 83 ESLGRQSsGSGAKGYGRLIKEYVRYLLDKLAFH 115
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
355-606 |
6.80e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 94.23 E-value: 6.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 355 QIESLKREVE------MLRSELEKIKLEAQ-RYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLR----AAQ 423
Cdd:COG1196 201 QLEPLERQAEkaeryrELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRleleELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 424 LEGERSQGLREEAERKASATEARYNKLKEKHSELvhvHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAfQVEQVKRES 503
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRREL---EERLEELEEELAELEEELEELEEELEELEEELE-EAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 504 ELKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAA 583
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
250 260
....*....|....*....|...
gi 733605517 584 LSREQQRSSQEQGELQGRLAERV 606
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEE 459
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
354-605 |
3.12e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.23 E-value: 3.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 354 LQIESLKREVEMLRSELEKIKLEAQRYIAQL---KSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRAA-QLEGERS 429
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELaelEAELEELRLELEELELELEEAQAEEYELLAELARLEQDiARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 430 QGLREEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRESELKLEE 509
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 510 KSDQLEKLKRELEAKAgELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAALSREQQ 589
Cdd:COG1196 392 LRAAAELAAQLEELEE-AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250
....*....|....*.
gi 733605517 590 RSSQEQGELQGRLAER 605
Cdd:COG1196 471 EAALLEAALAELLEEL 486
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
350-605 |
4.20e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.29 E-value: 4.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 350 DDRDLQIESLKREVEMLRSELEKIKLEAQRY---IAQLKSQVNALEGELEEQRKQKQKALVD----NEQLRHELAQLRAA 422
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELeaeLEELRLELEELELELEEAQAEEYELLAElarlEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 423 QLEGERSQGLREEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRE 502
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 503 selkLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEA 582
Cdd:COG1196 395 ----AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260
....*....|....*....|...
gi 733605517 583 ALSREQQRSSQEQGELQGRLAER 605
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARL 493
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
350-606 |
1.48e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.37 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 350 DDRDLQIESLKREVEMLRSELEkiklEAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRA----AQLE 425
Cdd:COG1196 263 AELEAELEELRLELEELELELE----EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEeleeLEEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 426 GERSQGLREEAERKASATEARYNKLKEKHSELVHVHAELLRknadTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRESEL 505
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE----ELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 506 KLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAALS 585
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
250 260
....*....|....*....|.
gi 733605517 586 REQQRSSQEQGELQGRLAERV 606
Cdd:COG1196 495 LLLEAEADYEGFLEGVKAALL 515
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
355-605 |
1.93e-14 |
|
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: 77.02 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 355 QIESLKREVEMLRSELEKIKLEAQRY---IAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRAAQLEG----- 426
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELeeeLEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELeaeie 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 427 ------ERSQGLREEAERKASATEARYNKLKEKH----SELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQV 496
Cdd:TIGR02168 765 eleerlEEAEEELAEAEAEIEELEAQIEQLKEELkalrEALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 497 EQVKRESElKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAqsl 576
Cdd:TIGR02168 845 EQIEELSE-DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL--- 920
|
250 260
....*....|....*....|....*....
gi 733605517 577 vRETEAALSREQQRSSQEQGELQGRLAER 605
Cdd:TIGR02168 921 -REKLAQLELRLEGLEVRIDNLQERLSEE 948
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
356-604 |
1.99e-14 |
|
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: 77.02 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 356 IESLKREVEMLRSELEKikleAQRYIaqlksqvnalegELEEQRKQKQKALVDNEQLRHElAQLRAAQLEGERSQGLREE 435
Cdd:TIGR02168 195 LNELERQLKSLERQAEK----AERYK------------ELKAELRELELALLVLRLEELR-EELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 436 AERKASATEARYNKLKEKHSELvhvhaellrkNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKReSELKLEEKSDQLE 515
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSEL----------EEEIEELQKELYALANEISRLEQQKQILRERLAN-LERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 516 KLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLV---RETEAALSREQQRSS 592
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVaqlELQIASLNNEIERLE 406
|
250
....*....|..
gi 733605517 593 QEQGELQGRLAE 604
Cdd:TIGR02168 407 ARLERLEDRRER 418
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
352-584 |
6.39e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.36 E-value: 6.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 352 RDLQIESLKREVEMLRSELEKIKLEAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRAAQLEGERSQG 431
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 432 LREEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRESELKLEEKS 511
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 733605517 512 DQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQ-READLLAAQSLVRETEAAL 584
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvKAALLLAGLRGLAGAVAVL 529
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
352-604 |
1.10e-13 |
|
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: 74.71 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 352 RDLQIESLKREVEMLRSELEKIKL---EAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRAAQleger 428
Cdd:TIGR02168 223 RELELALLVLRLEELREELEELQEelkEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI----- 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 429 sQGLREEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAfQVEQVKRESELKLE 508
Cdd:TIGR02168 298 -SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE-ELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 509 EKSDQLEKLKRE-------LEAKAGELARAQEALSHTEQSKSELSSRLDTL-----SAEKDALSGAVRQREADLLAAQSL 576
Cdd:TIGR02168 376 ELEEQLETLRSKvaqlelqIASLNNEIERLEARLERLEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEE 455
|
250 260
....*....|....*....|....*...
gi 733605517 577 VRETEAALSREQQRSSQEQGELQGRLAE 604
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERE 483
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
353-607 |
1.37e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 353 DLQIESLKREVEMLRSELEK----IKLEAQRyIAQLKSQVNALEGELEEQRKQKQKAlvdNEQLRHELAQLRAAQLEGER 428
Cdd:COG1196 280 ELELEEAQAEEYELLAELARleqdIARLEER-RRELEERLEELEEELAELEEELEEL---EEELEELEEELEEAEEELEE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 429 SQGLREEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLafqvEQVKRESELKLE 508
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL----EEELEELEEALA 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 509 EKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAAL-SRE 587
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLeGVK 511
|
250 260
....*....|....*....|
gi 733605517 588 QQRSSQEQGELQGRLAERVW 607
Cdd:COG1196 512 AALLLAGLRGLAGAVAVLIG 531
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
357-604 |
1.98e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.02 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 357 ESLKREVEMLRSELEKIKLEAQ---RYIAQLKSQVNALEGELEEQRKQ---KQKAlvdnEQLRHELAQLRAAQLEGERSQ 430
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEaaeKKKEEAKKKADAAKKKAEEKKKAdeaKKKA----EEDKKKADELKKAAAAKKKAD 1421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 431 GLREEAERKASATEARyNKLKEKHSelvhvhAELLRKNADTAKQLTVTQQSQEEvARVKEQLAFQVEQVKRESELK--LE 508
Cdd:PTZ00121 1422 EAKKKAEEKKKADEAK-KKAEEAKK------ADEAKKKAEEAKKAEEAKKKAEE-AKKADEAKKKAEEAKKADEAKkkAE 1493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 509 EKSDQLEKLKRELEAK--AGELARAQEALSHTEQSKSELSSRLDTLSAekdalsgAVRQREADLLAAQSLVRETEAALSR 586
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKkkADEAKKAEEAKKADEAKKAEEAKKADEAKK-------AEEKKKADELKKAEELKKAEEKKKA 1566
|
250
....*....|....*...
gi 733605517 587 EQQRSSQEQGELQGRLAE 604
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAE 1584
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
355-605 |
1.40e-12 |
|
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: 70.87 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 355 QIESLKREVEMLRSELEKIKLEAQryiaQLKSQVNALEGELEEQRKqKQKALVDNEQLR---------HELAQLRAAQLE 425
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEIS----ELEKRLEEIEQLLEELNK-KIKDLGEEEQLRvkekigeleAEIASLERSIAE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 426 GERSQglrEEAERKASATEARYNKLKEKHSELvhvHAELLRKNADTAkQLTVTQQSQEEVARVKEQLAFQVEQVKRESEL 505
Cdd:TIGR02169 313 KEREL---EDAEERLAKLEAEIDKLLAEIEEL---EREIEEERKRRD-KLTEEYAELKEELEDLRAELEEVDKEFAETRD 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 506 KLEEKSDQLEKLKRELE--------------AKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLL 571
Cdd:TIGR02169 386 ELKDYREKLEKLKREINelkreldrlqeelqRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
250 260 270
....*....|....*....|....*....|....
gi 733605517 572 AAQSLVRETEAALSREQQRSSQEQGELQGRLAER 605
Cdd:TIGR02169 466 KYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
367-598 |
1.13e-11 |
|
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: 68.16 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 367 RSELEKIKLEaqryIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRAAQLEGERS-QGLREEAERKASATEA 445
Cdd:TIGR02168 676 RREIEELEEK----IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDlARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 446 RYNKLKEKHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQL--------------------AFQVEQVKRESEL 505
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELkalrealdelraeltllneeAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 506 KLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAALS 585
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
250
....*....|...
gi 733605517 586 REQQRSSQEQGEL 598
Cdd:TIGR02168 912 ELRRELEELREKL 924
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
376-608 |
2.85e-11 |
|
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: 65.56 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 376 EAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRAAQLEGERSQglrEEAERKASATEARYNKLKEKHS 455
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL---AALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 456 ELVHVHAELLRKNADTAKQ----LTVTQQSQEEVAR-------VKEQLAFQVEQVKRESElKLEEKSDQLEKLKRELEAK 524
Cdd:COG4942 101 AQKEELAELLRALYRLGRQpplaLLLSPEDFLDAVRrlqylkyLAPARREQAEELRADLA-ELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 525 AGELARAQEALshtEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAALSREQQRS-SQEQGELQGRLA 603
Cdd:COG4942 180 LAELEEERAAL---EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTpAAGFAALKGKLP 256
|
....*
gi 733605517 604 ervWP 608
Cdd:COG4942 257 ---WP 258
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
342-590 |
4.02e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 342 GPPNGSVKDDRDLQIESLKREVEMLRSELEKI--KLEAQRYIAQLKSQVNALEGELE--EQRKQKQKALVDNEQLRHELA 417
Cdd:PRK02224 463 GSPHVETIEEDRERVEELEAELEDLEEEVEEVeeRLERAEDLVEAEDRIERLEERREdlEELIAERRETIEEKRERAEEL 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 418 QLRAAQLEGErSQGLREEAERKASATEARYNKLKEKHSELVHVHAELLRKNaDTAKQLTVTQQSQEEVARVKEQLAfQVE 497
Cdd:PRK02224 543 RERAAELEAE-AEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKRE-ALA 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 498 QVKRESELKLEEKSDQleklKRELEAKAGE--LARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQS 575
Cdd:PRK02224 620 ELNDERRERLAEKRER----KRELEAEFDEarIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
|
250
....*....|....*
gi 733605517 576 LvRETEAALSREQQR 590
Cdd:PRK02224 696 L-RERREALENRVEA 709
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
355-565 |
4.62e-11 |
|
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: 66.24 E-value: 4.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 355 QIESLKREVEMLRSELEKIKLEAQRYIAQL---KSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRA-AQLEGERSQ 430
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLAKLEAEIdklLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAeLEEVDKEFA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 431 GLREEA----ERKASATEARY----------NKLKEKHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQV 496
Cdd:TIGR02169 382 ETRDELkdyrEKLEKLKREINelkreldrlqEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 733605517 497 EQVKRESElKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQ 565
Cdd:TIGR02169 462 ADLSKYEQ-ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQ 529
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
375-605 |
8.23e-11 |
|
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: 65.46 E-value: 8.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 375 LEAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRAAQlegersqglrEEAERKASATEARYNKLKEKH 454
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL----------EELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 455 SELVHVHAELLRKNADTAKQLTVTQQSQEEVarvkEQLAFQVEQVKRESELKLEEKSDQLEKLKRELEAKAGELARAQEA 534
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEA----EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 733605517 535 LSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAA---LSREQQRSSQEQGELQGRLAER 605
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELieeLESELEALLNERASLEEALALL 892
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
355-561 |
8.52e-11 |
|
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: 65.08 E-value: 8.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 355 QIESLKREVEMLRSE---LEKIKLEAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRAAQLEGE-RSQ 430
Cdd:TIGR02168 296 EISRLEQQKQILRERlanLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELEsRLE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 431 GLREEAERKASATEARYNKLKEKHSELVHVHAELlrknADTAKQLTVTQQSQEEVARVKEQLAFQ-VEQVKRESELKLEE 509
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARL----ERLEDRRERLQQEIEELLKKLEEAELKeLQAELEELEEELEE 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 733605517 510 KSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSG 561
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
355-603 |
1.02e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 355 QIESLKREVEMLRSELEKIKL---EAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRAAQLEGERSqg 431
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLevsELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK-- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 432 lREEAERKASATEARYNKLKEKHSELvhvhAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRESELKLEEKS 511
Cdd:TIGR02168 332 -LDELAEELAELEEKLEELKEELESL----EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 512 DQLEKLKRELEAKAGELARAQEALShtEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAALsreQQRS 591
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL---DAAE 481
|
250
....*....|..
gi 733605517 592 SQEQgELQGRLA 603
Cdd:TIGR02168 482 RELA-QLQARLD 492
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
355-559 |
1.37e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.55 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 355 QIESLKREVEMLrselEKIKLEAQRYIAqlksqvnaLEGELEEQRKQKQKALVDNEQLRHELAQLRAAQLEGERsqglrE 434
Cdd:COG4913 243 ALEDAREQIELL----EPIRELAERYAA--------ARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL-----A 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 435 EAERKASATEARYNKLKEKHSELVHVHAEL-LRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRESELKLEEKSDQ 513
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL 385
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 733605517 514 LEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDAL 559
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
348-560 |
1.88e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.39 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 348 VKDDRDLQIESLKREVEMLR-SELEKIKLEAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQL-RAAQLE 425
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEaKKAEED 1673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 426 GERSQGLR--EEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKREs 503
Cdd:PTZ00121 1674 KKKAEEAKkaEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD- 1752
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 733605517 504 elklEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALS 560
Cdd:PTZ00121 1753 ----EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFD 1805
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
357-595 |
4.68e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.85 E-value: 4.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 357 ESLKREVEMLRSELEKIKLEAQRYIAQLKSQVNALEGELEEQRKQkqkalvdnEQLRHELAQLRAAQLEGERSQGLREEA 436
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA--------DEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 437 ERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTVTQQSQEevARVKEQLAfQVEQVKRESELKLEEKSDQLEK 516
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE--AKKADEAK-KAEEAKKADEAKKAEEKKKADE 1550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 517 LKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQ--READLLAAQSLVRETEAALSREQQRSSQE 594
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKlyEEEKKMKAEEAKKAEEAKIKAEELKKAEE 1630
|
.
gi 733605517 595 Q 595
Cdd:PTZ00121 1631 E 1631
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
433-605 |
6.25e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 6.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 433 REEAERKASATEA---------------------------RYNKLKE--KHSELVHVHAELLRKNADTAKQLTVTQQSQE 483
Cdd:COG1196 174 KEEAERKLEATEEnlerledilgelerqleplerqaekaeRYRELKEelKELEAELLLLKLRELEAELEELEAELEELEA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 484 EVARVKEQLAfQVEQVKRESELKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAV 563
Cdd:COG1196 254 ELEELEAELA-ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 733605517 564 RQREADLLAAQSLVRETEAALSREQQRSSQEQGELQGRLAER 605
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
376-604 |
1.04e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.61 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 376 EAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRaaqlegersqglrEEAERKASATEARYNKLKEkhs 455
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ-------------AEIAEAEAEIEERREELGE--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 456 elvhvHAELLRKNADTAKQLTVTQQSQ---------EEVARVKEQLAFQVEQVKRESElKLEEKSDQLEKLKRELEAKAG 526
Cdd:COG3883 91 -----RARALYRSGGSVSYLDVLLGSEsfsdfldrlSALSKIADADADLLEELKADKA-ELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 733605517 527 ELARAQEALshtEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAALSREQQRSSQEQGELQGRLAE 604
Cdd:COG3883 165 ELEAAKAEL---EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
355-548 |
1.30e-09 |
|
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: 60.55 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 355 QIESLKREVEMLRSELEKIK---LEAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELA-QLRAAQLEGER-- 428
Cdd:COG4942 42 ELAALKKEEKALLKQLAALErriAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAeLLRALYRLGRQpp 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 429 -----SQGLREEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLafqvEQVKRES 503
Cdd:COG4942 122 lalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL----EALKAER 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 733605517 504 ELKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSR 548
Cdd:COG4942 198 QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
357-594 |
1.63e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 357 ESLKREVEMLRSELEKIKLEAQRYIAQLKSQVNALEGELEEQRKQ----KQKALVDNEQLRHELAQLRAAQLEGERSQGL 432
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKaeeaKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 433 REEAERKASATEARYNKLKE-----KHSELVHVHAELLRKNADTAKQLTVTQQSQEEVaRVKEQLAFQVEQVKRESELKL 507
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKadeakKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK-KKADEAKKKAEEAKKADEAKK 1451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 508 E-EKSDQLEKLKR---------ELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEK--DALSGAVRQREADLLAAQS 575
Cdd:PTZ00121 1452 KaEEAKKAEEAKKkaeeakkadEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkaDEAKKAEEAKKADEAKKAE 1531
|
250
....*....|....*....
gi 733605517 576 LVRETEAALSREQQRSSQE 594
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADE 1550
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
357-597 |
1.91e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.93 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 357 ESLKREVEMLRSELEKIKLEAQRYIAQLKSQVNALEGELEEQRKQKQKA--LVDNEQLR--HELAQLRAAQLEGERSQGL 432
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAdeLKKAEELKkaEEKKKAEEAKKAEEDKNMA 1579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 433 REEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRESELKLEEKSD 512
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEN 1659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 513 QLEklKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAALSREQQRSS 592
Cdd:PTZ00121 1660 KIK--AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
....*
gi 733605517 593 QEQGE 597
Cdd:PTZ00121 1738 EAEED 1742
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
358-604 |
2.45e-09 |
|
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: 60.47 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 358 SLKREVEMLRSELEKIKLEaqryIAQLKSQVNALEGELEEQRkqkqkALVDNEQLRHELAQLRAAQLEGERSQgLREEAE 437
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRE----LSSLQSELRRIENRLDELS-----QELSDASRKIGEIEKEIEQLEQEEEK-LKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 438 RKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQltvtqqsQEEVARVKEQLAFQ-VEQVKRESElKLEEKSDQLEK 516
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL-------EEALNDLEARLSHSrIPEIQAELS-KLEEEVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 517 LKRELEAKAG----ELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAA---LSREQQ 589
Cdd:TIGR02169 813 RLREIEQKLNrltlEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRlgdLKKERD 892
|
250
....*....|....*
gi 733605517 590 RSSQEQGELQGRLAE 604
Cdd:TIGR02169 893 ELEAQLRELERKIEE 907
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
360-595 |
3.20e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 360 KREVEMLRSELEKIKLEAQRYIAQLKSQVNALEGELEEQRKQ------KQKALVDNEQLRHELAQLRAAQL------EGE 427
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKadelkkAAAAKKKADEAKKKAEEKKKADEakkkaeEAK 1444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 428 RSQGLREEAERKASATEARyNKLKEKHSelvhvhAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRESELKL 507
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAK-KKAEEAKK------ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK 1517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 508 EEKSDQLEKLKRELEA-------------KAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQ 574
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAkkadeakkaeekkKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597
|
250 260
....*....|....*....|.
gi 733605517 575 SLVRETEAALSREQQRSSQEQ 595
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEA 1618
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
350-584 |
3.60e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.05 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 350 DDRDLQIESLKREVEMLRSELEKIKLEAQRYiAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRAAQLE-GER 428
Cdd:PRK02224 216 AELDEEIERYEEQREQARETRDEADEVLEEH-EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEElEEE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 429 SQGLREEAER---KASATEARYNKLKEKHSELvhvhAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRESEL 505
Cdd:PRK02224 295 RDDLLAEAGLddaDAEAVEARREELEDRDEEL----RDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELES 370
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 733605517 506 KLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAAL 584
Cdd:PRK02224 371 ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL 449
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
357-573 |
9.82e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 9.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 357 ESLKREVEMLRSELEKIKLEAQRYiAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRAAQLegersqglREEA 436
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEY-AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE--------LEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 437 ERKASATEARYNKLKEKHSELVHVHAELlrknadtakqltvtQQSQEEVARVKEQLAfqveqvkRESELKLEEKSDQLEK 516
Cdd:COG4717 138 EAELAELPERLEELEERLEELRELEEEL--------------EELEAELAELQEELE-------ELLEQLSLATEEELQD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 733605517 517 LKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAA 573
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL 253
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
355-594 |
1.77e-08 |
|
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: 57.77 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 355 QIESLKREVEMLRSELEKikleAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRAAQLEGERSqglre 434
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEK----LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR----- 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 435 EAERKASATEARYNKLKEKHSELVHVHAELLRK-NADTAKQLTVTQQSQEEVARV---KEQLAFQVEQV------KRESE 504
Cdd:TIGR02169 788 LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKlNRLTLEKEYLEKEIQELQEQRidlKEQIKSIEKEIenlngkKEELE 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 505 LKLEEKSDQLeklkRELEAKAGELARAQEALshtEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAAL 584
Cdd:TIGR02169 868 EELEELEAAL----RDLESRLGDLKKERDEL---EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK 940
|
250
....*....|
gi 733605517 585 SREQQRSSQE 594
Cdd:TIGR02169 941 GEDEEIPEEE 950
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
357-599 |
3.17e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 357 ESLKREVEMLRSELEKIKLEAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRAAQLEgERSQGLREEA 436
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAK-KKADEAKKAA 1506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 437 ERKASATEARYNKLKEKHSELVHvhAELLRKnADTAKQLTVTQQSQEevARVKEQLAfQVEQVKRESELKLEEKsDQLEK 516
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKK--AEEAKK-ADEAKKAEEKKKADE--LKKAEELK-KAEEKKKAEEAKKAEE-DKNMA 1579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 517 LKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAALSREQQRSSQEQG 596
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEN 1659
|
...
gi 733605517 597 ELQ 599
Cdd:PTZ00121 1660 KIK 1662
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
357-595 |
4.94e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 357 ESLKREVEMLRSELEKIKLEAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRhELAQLRAAQlEGERSQGLREEA 436
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKK-KADEAKKAE-EKKKADEAKKKA 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 437 ERKASATEARynklkeKHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAfqvEQVKRESELKLEEKSDQLEK 516
Cdd:PTZ00121 1312 EEAKKADEAK------KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA---EEKAEAAEKKKEEAKKKADA 1382
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 733605517 517 LKReleaKAGELARAQEALSHTEQSKSElSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAALSREQQRSSQEQ 595
Cdd:PTZ00121 1383 AKK----KAEEKKKADEAKKKAEEDKKK-ADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1456
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
355-574 |
5.09e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.18 E-value: 5.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 355 QIESLKREVEMLRSE--------------LEKIKLEAQRY---IAQLKSQVNALEGELEEQRKQKQ-------KALVDNE 410
Cdd:TIGR04523 343 QISQLKKELTNSESEnsekqreleekqneIEKLKKENQSYkqeIKNLESQINDLESKIQNQEKLNQqkdeqikKLQQEKE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 411 QLRHELAQLRA---------AQLEGERSQ---------GLREEAERKASATEARYNKLKekhSELVHVHAELLRKNADTA 472
Cdd:TIGR04523 423 LLEKEIERLKEtiiknnseiKDLTNQDSVkeliiknldNTRESLETQLKVLSRSINKIK---QNLEQKQKELKSKEKELK 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 473 KQLTVTQQSQEEVARVKEQLAFQVEQVKR-ESELKleEKSDQLEKLKRELEAKAGELARaqealSHTEQSKSELSSRLDT 551
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEKIEKlESEKK--EKESKISDLEDELNKDDFELKK-----ENLEKEIDEKNKEIEE 572
|
250 260
....*....|....*....|...
gi 733605517 552 LSAEKDALSGAvrQREADLLAAQ 574
Cdd:TIGR04523 573 LKQTQKSLKKK--QEEKQELIDQ 593
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
355-570 |
5.73e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 5.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 355 QIESLKREVEMLRSELEKIKL-EAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRAAQLE--GERSQG 431
Cdd:COG4913 263 RYAAARERLAELEYLRAALRLwFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGngGDRLEQ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 432 LREEAERKasatEARYNKLKEKHSELvhvhaellrknADTAKQLTVTQ-QSQEEVARVKEQLAFQVEQVKREselkLEEK 510
Cdd:COG4913 343 LEREIERL----ERELEERERRRARL-----------EALLAALGLPLpASAEEFAALRAEAAALLEALEEE----LEAL 403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 511 SDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLsaeKDALSGAVRQREADL 570
Cdd:COG4913 404 EEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL---RDALAEALGLDEAEL 460
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
376-604 |
6.46e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 376 EAQRYIAQLKSQVNALEgELEEQRKQKQKALVDNEQLRHELAQLRA--AQLEGERSQGLREEAERKASATEARYNKLKEK 453
Cdd:COG4913 239 RAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLwfAQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 454 HSELvhvhaellrknadtakqltvtqqsQEEVARVKEQLAfqveqvkreselklEEKSDQLEKLKRELEAKAGELARAQE 533
Cdd:COG4913 318 LDAL------------------------REELDELEAQIR--------------GNGGDRLEQLEREIERLERELEERER 359
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 733605517 534 ALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAALSREQQRSSQEQGELQGRLAE 604
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
381-600 |
1.00e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 381 IAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRAAQLEGERSQGLREE-AERKASATEARYNKLKEKHSELVH 459
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEkREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 460 VHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRESELKLEEK-----------SDQLEKLKRELEAKAGEL 528
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKigeleaeiaslERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 733605517 529 ARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAALSREQQRSSQEQGELQG 600
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK 396
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
382-530 |
1.55e-07 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 53.82 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 382 AQLKSQVNALEGELEEQRKQKQkalvdneQLRHELAQLRA----AQLEGERSQGLREEAERKASATEARYNKLKEKHSEL 457
Cdd:PRK09039 56 DRLNSQIAELADLLSLERQGNQ-------DLQDSVANLRAslsaAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSE 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 733605517 458 VHVHAELLRknadtakQLTVTQQsqeEVARVKEQLAfQVEQVKRESELKLEEKSDQLEKLKRELEA----KAGELAR 530
Cdd:PRK09039 129 KQVSARALA-------QVELLNQ---QIAALRRQLA-ALEAALDASEKRDRESQAKIADLGRRLNValaqRVQELNR 194
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
425-605 |
1.91e-07 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 53.53 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 425 EGERSQGLREEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQ---VKR 501
Cdd:pfam19220 42 ELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDktaQAE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 502 ESELKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETE 581
Cdd:pfam19220 122 ALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELE 201
|
170 180
....*....|....*....|....
gi 733605517 582 AALSREQQRSSQEQGELQGRLAER 605
Cdd:pfam19220 202 TQLDATRARLRALEGQLAAEQAER 225
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
377-583 |
3.28e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.89 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 377 AQRYIAQLKSQVNALEGELEEQRKQKQKAlvdnEQLRHELA--QLRAAQLEGERsqgLREEAERKASATEARYNKLKEKH 454
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQA----EELQQKQAaeQERLKQLEKER---LAAQEQKKQAEEAAKQAALKQKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 455 SElvhvhaellrknADTAKQLTVTQQSQEEVARVKEQLAFQVE---QVKRESELKLEEKSDQLEKLKRELEAKAGELARA 531
Cdd:PRK09510 134 AE------------EAAAKAAAAAKAKAEAEAKRAAAAAKKAAaeaKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKK 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 733605517 532 QEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAA 583
Cdd:PRK09510 202 KAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAA 253
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
356-573 |
4.04e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 356 IESLKREVEMLRSELEKIKlEAQRYIAQLKSQVNALEG----------ELEEQRKQKQKALVDNEQLRHELAQLRAAQLE 425
Cdd:PRK03918 216 LPELREELEKLEKEVKELE-ELKEEIEELEKELESLEGskrkleekirELEERIEELKKEIEELEEKVKELKELKEKAEE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 426 GERSQGLREEAERKASATEARYNKLKEKHSELVHVHAELLRKNadtaKQLTVTQQSQEEVARVKEQLafqveqvkRESEL 505
Cdd:PRK03918 295 YIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE----ERLEELKKKLKELEKRLEEL--------EERHE 362
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 733605517 506 KLEE---KSDQLEKLKRELEAKagELARAQEALSHTEQSKSELSSRLDTLSAEKdalsGAVRQREADLLAA 573
Cdd:PRK03918 363 LYEEakaKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARI----GELKKEIKELKKA 427
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
358-534 |
6.58e-07 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 52.31 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 358 SLKREVEMLRSELEKiKLEAQRYIAQLK---SQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRAAQLEGERSQGLRE 434
Cdd:pfam05262 178 SDKKVVEALREDNEK-GVNFRRDMTDLKereSQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 435 E--AERKASATEArynKLKEKHSELVHVHAELLRKNadtakqltvTQQSQEEVARVKEQLAFQVEQVKRESELKLEEKSd 512
Cdd:pfam05262 257 AknLPKPADTSSP---KEDKQVAENQKREIEKAQIE---------IKKNDEEALKAKDHKAFDLKQESKASEKEAEDKE- 323
|
170 180
....*....|....*....|..
gi 733605517 513 qlEKLKRELEAKAGELARAQEA 534
Cdd:pfam05262 324 --LEAQKKREPVAEDLQKTKPQ 343
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
360-597 |
8.37e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 8.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 360 KREVEMLRSELEKIKLEAQRYIAQLKsqvnalegELEEQRK--QKQKALVDNEQLRHELAQLRAAQLEGERSQGLREEAE 437
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAEELK--------KAEEKKKaeEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE 1604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 438 RKASATEARynklkekHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQL--AFQVEQVKRESEL-KLEEKSDQL 514
Cdd:PTZ00121 1605 KKMKAEEAK-------KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELkkAEEENKIKAAEEAkKAEEDKKKA 1677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 515 EKLKRELEAKagelARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAAlSREQQRSSQE 594
Cdd:PTZ00121 1678 EEAKKAEEDE----KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED-KKKAEEAKKD 1752
|
...
gi 733605517 595 QGE 597
Cdd:PTZ00121 1753 EEE 1755
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
346-605 |
1.01e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 346 GSVKDDRDLQIESLKR------EVEMLRSELEKIKLEAQRYIAQLKSQVNALEGELEEQRKQKQKAlvdnEQLRHELAQL 419
Cdd:PRK03918 168 GEVIKEIKRRIERLEKfikrteNIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL----EELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 420 RaaqLEGERSQGLREEAERKASATEARYNKLKEKHSELVHVHAEL--LRKNADT--------AKQLTVTQQSQEEVARVK 489
Cdd:PRK03918 244 E---KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELkeLKEKAEEyiklsefyEEYLDELREIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 490 EQLAFQVEQVKreselKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSeLSSRLDTLSAEKDALSgaVRQREAD 569
Cdd:PRK03918 321 EEINGIEERIK-----ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKA-KKEELERLKKRLTGLT--PEKLEKE 392
|
250 260 270
....*....|....*....|....*....|....*.
gi 733605517 570 LLAAQSLVRETEAALSREQQRssqeQGELQGRLAER 605
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITAR----IGELKKEIKEL 424
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
355-561 |
1.50e-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: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 355 QIESLKREVEMLR---SELEKIKLEAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRaAQLEGERSQg 431
Cdd:TIGR02168 324 QLEELESKLDELAeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE-LQIASLNNE- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 432 lREEAERKASATEARYNKLKEKHSELvhvhaellrknaDTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRESElKLEEKS 511
Cdd:TIGR02168 402 -IERLEARLERLEDRRERLQQEIEEL------------LKKLEEAELKELQAELEELEEELEELQEELERLEE-ALEELR 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 733605517 512 DQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSG 561
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
462-599 |
1.71e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.45 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 462 AELLRKNADTAKQLTvtQQSQEEVARVKEQLAFQVEQVK-----RESELKLEEKSDQLEKLKRELEAKAGELA------- 529
Cdd:PRK11281 82 TEQLKQQLAQAPAKL--RQAQAELEALKDDNDEETRETLstlslRQLESRLAQTLDQLQNAQNDLAEYNSQLVslqtqpe 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 530 RAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQR---EADLLAAQSLVRETEAA---------------LSREQQRS 591
Cdd:PRK11281 160 RAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLlqaEQALLNAQNDLQRKSLEgntqlqdllqkqrdyLTARIQRL 239
|
....*...
gi 733605517 592 SQEQGELQ 599
Cdd:PRK11281 240 EHQLQLLQ 247
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
346-590 |
1.86e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 346 GSVKDDRDLQIESLKREVEmlrselEKIKLEAQRYIAQLKSQVNALEGELEEQRKQKQKA----------LVDNEQLRHE 415
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIE------EKEEKDLHERLNGLESELAELDEEIERYEEQREQAretrdeadevLEEHEERREE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 416 LAQLRAaqlEGERSQGLREEAERKASATEARYNKLKEKHSELVHVHAELLRKNA-DTAKQLTVTQQsQEEVARVKEQLAF 494
Cdd:PRK02224 253 LETLEA---EIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlDDADAEAVEAR-REELEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 495 QVEQVK-------------RESELKLEEKSDQLEKLKRELEAkagELARAQEALSHTEQSKSELSSRLDTLSA------- 554
Cdd:PRK02224 329 RLEECRvaaqahneeaeslREDADDLEERAEELREEAAELES---ELEEAREAVEDRREEIEELEEEIEELRErfgdapv 405
|
250 260 270
....*....|....*....|....*....|....*.
gi 733605517 555 EKDALSGAVRQREADLLAAQSLVRETEAALSREQQR 590
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARER 441
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
381-604 |
2.40e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.72 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 381 IAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLR-----AAQLEGERSQGLREEAERKASATE--ARYNKLKEK 453
Cdd:COG3096 838 LAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNkllpqANLLADETLADRLEELREELDAAQeaQAFIQQHGK 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 454 HSELVHVHAELLRKNADTAKQLTV-TQQSQEEVARVKEQLAFQVEQVKR-------ESELKLEEKSDQLEKLKRELEAKA 525
Cdd:COG3096 918 ALAQLEPLVAVLQSDPEQFEQLQAdYLQAKEQQRRLKQQIFALSEVVQRrphfsyeDAVGLLGENSDLNEKLRARLEQAE 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 526 GELARAQEALshtEQSKSELSSRLDTLSAEKDALSGAV------RQREADL---------LAAQSLVRETEAALSREQQR 590
Cdd:COG3096 998 EARREAREQL---RQAQAQYSQYNQVLASLKSSRDAKQqtlqelEQELEELgvqadaeaeERARIRRDELHEELSQNRSR 1074
|
250 260
....*....|....*....|....
gi 733605517 591 SSQ----------EQGELQGRLAE 604
Cdd:COG3096 1075 RSQlekqltrceaEMDSLQKRLRK 1098
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
349-557 |
2.86e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.40 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 349 KDDRDL--QIESLKREVEMLRSELEKIkleaQRYIAQLKSQVNALEGELEEQRKQKQKalvdNEQLRHELAQLRaaqleg 426
Cdd:TIGR04523 159 NKYNDLkkQKEELENELNLLEKEKLNI----QKNIDKIKNKLLKLELLLSNLKKKIQK----NKSLESQISELK------ 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 427 ERSQGLREEAERKASATEARYNKLKEKHSELVhvhaELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRE-SEL 505
Cdd:TIGR04523 225 KQNNQLKDNIEKKQQEINEKTTEISNTQTQLN----QLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEiSDL 300
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 733605517 506 KLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKD 557
Cdd:TIGR04523 301 NNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
349-604 |
3.08e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 50.36 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 349 KDDRDLQIESlkrevEMLRSELEKIKLEAQRYIAQLKSQVNALEGELEEQRKQKQKalvdneqlrhELAQLRAAQLEGER 428
Cdd:pfam02463 151 KPERRLEIEE-----EAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELK----------LKEQAKKALEYYQL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 429 SQGLREEAERkasATEARYNKLKEKHSELvhVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRESEL--- 505
Cdd:pfam02463 216 KEKLELEEEY---LLYLDYLKLNEERIDL--LQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEElkl 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 506 ---KLEEKSDQLEKLKRELEAKAGELARAQE---ALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRE 579
Cdd:pfam02463 291 lakEEEELKSELLKLERRKVDDEEKLKESEKekkKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQ 370
|
250 260
....*....|....*....|....*
gi 733605517 580 TEAALSREQQRSSQEQGELQGRLAE 604
Cdd:pfam02463 371 LEEELLAKKKLESERLSSAAKLKEE 395
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
348-565 |
3.62e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 348 VKDDRDLQIESLKREVEMLRSELEKIKLEAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRAAQLEGE 427
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 428 RSQGLREEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRESELKL 507
Cdd:COG1196 676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 733605517 508 EEKSDQLEKLKRELEAKAGELAR-------AQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQ 565
Cdd:COG1196 756 LPEPPDLEELERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDLEEARETLEEAIEE 820
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
357-577 |
3.83e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.34 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 357 ESLKREVEMLRSELEKIkLEAQRYIAQLKSQVNALEGELE--EQRKQKQKAL-VDNEQLRHELAQLRA-----AQLEGER 428
Cdd:COG3096 889 ETLADRLEELREELDAA-QEAQAFIQQHGKALAQLEPLVAvlQSDPEQFEQLqADYLQAKEQQRRLKQqifalSEVVQRR 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 429 SQGLREEAERKASATEARYNKLKEKHselvhVHAELLRKNADTAkqltvTQQSQEEVArvkeqlafQVEQVKRESELKLE 508
Cdd:COG3096 968 PHFSYEDAVGLLGENSDLNEKLRARL-----EQAEEARREAREQ-----LRQAQAQYS--------QYNQVLASLKSSRD 1029
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 509 EKSDQLEKLKRELE-------AKAGELARA-----QEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSL 576
Cdd:COG3096 1030 AKQQTLQELEQELEelgvqadAEAEERARIrrdelHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQ 1109
|
.
gi 733605517 577 V 577
Cdd:COG3096 1110 V 1110
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
355-567 |
3.85e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 355 QIESLKREVEMLRSELEKIKLEAQRYIAQLKSqVNALEGELEEQRKQKQKALVDNEQLRHELaqlraaqleGERSQGLRE 434
Cdd:PRK03918 519 ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK-LEELKKKLAELEKKLDELEEELAELLKEL---------EELGFESVE 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 435 EAERKASATEARYNKlkekHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAfqvEQVKRESELKLEEKSDQL 514
Cdd:PRK03918 589 ELEERLKELEPFYNE----YLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE---ELRKELEELEKKYSEEEY 661
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 733605517 515 EKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQRE 567
Cdd:PRK03918 662 EELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE 714
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
355-604 |
4.02e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 355 QIESLKREVEMLRSELEkiklEAQRYIAQLKSQVNALEG-----------------------ELEEQRKQKQKALVDNEQ 411
Cdd:COG4913 611 KLAALEAELAELEEELA----EAEERLEALEAELDALQErrealqrlaeyswdeidvasaerEIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 412 LRHELAQLRAAQLEGERSQGLREEAERKASATEARYNKLKEKHSElvhvhaelLRKNADTAKQLTVTQQSQEEVARVKEQ 491
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE--------LQDRLEAAEDLARLELRALLEERFAAA 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 492 LAFQVEQVKRESelkleeKSDQLEKLKRELEAKAGELARAQEAlsHTEQSKSELSsrldTLSAEKDALSGAVRQREAdlL 571
Cdd:COG4913 759 LGDAVERELREN------LEERIDALRARLNRAEEELERAMRA--FNREWPAETA----DLDADLESLPEYLALLDR--L 824
|
250 260 270
....*....|....*....|....*....|...
gi 733605517 572 AAQSLVRETEAALSREQQRSSQEQGELQGRLAE 604
Cdd:COG4913 825 EEDGLPEYEERFKELLNENSIEFVADLLSKLRR 857
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
438-599 |
4.14e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 438 RKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTV-TQQSQEEVARVKEQLAfQVEQVKRESELKLEEKSDQLEK 516
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEeLEQLREELEQAREELE-QLEEELEQARSELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 517 LKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAALSREQQRSSQEQG 596
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
...
gi 733605517 597 ELQ 599
Cdd:COG4372 165 ELA 167
|
|
| ANTH_N |
cd03564 |
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ... |
33-128 |
5.37e-06 |
|
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal Homology) domain family is composed of Adaptor Protein 180 (AP180), Clathrin Assembly Lymphoid Myeloid Leukemia protein (CALM), and similar proteins. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ANTH-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that the ANTH domain is a universal component of the machinery for clathrin-mediated membrane budding. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains.
Pssm-ID: 340767 Cd Length: 120 Bit Score: 45.73 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 33 ISISKAINTQEAPVKEKHARRIILGThhekgaftfwsYAIGLPLPSSSIL----------SW----KFCHVLHKVLRDGH 98
Cdd:cd03564 3 VAVVKATNHDEVPPKEKHVRKLLLAT-----------SNGGGRADVAYIVhalakrlhkkNWivvlKTLIVIHRLLREGS 71
|
90 100 110
....*....|....*....|....*....|
gi 733605517 99 PNVLHDCQRYRSNIREIgdlwGHLHDRYGQ 128
Cdd:cd03564 72 PSFLEELLRYSGHIFNL----SNFKDDSSP 97
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
357-605 |
5.59e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 357 ESLKREVEMLRSELEKIKLEAQRYIAQLKSQVNALEG-ELEEQRKQKQKALVDNEQLRHELAQLRAAQLEGE---RSQGL 432
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEArKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEeakKADEA 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 433 REEAERKASATEARYNKLKE--KHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVK-EQLAFQVEQVKRESEL--KL 507
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEakKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKaDAAKKKAEEKKKADEAkkKA 1400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 508 EEKSDQLEKLKR---------ELEAKAGELARAQEALSHTEQSK--SELSSRLDTLSAEKDALSGAVRQREADLLAAQSL 576
Cdd:PTZ00121 1401 EEDKKKADELKKaaaakkkadEAKKKAEEKKKADEAKKKAEEAKkaDEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE 1480
|
250 260
....*....|....*....|....*....
gi 733605517 577 VRETEAALSREQQRSSQEQGELQGRLAER 605
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKAAEAK 1509
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
354-601 |
5.70e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.79 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 354 LQIES-LKREVEMLRSELEKIKLEAQRYIAQLKSQVNALE---GELEEQRKQKQKALVD-NEQLRHELAQLRAAQLEger 428
Cdd:pfam01576 49 LQAETeLCAEAEEMRARLAARKQELEEILHELESRLEEEEersQQLQNEKKKMQQHIQDlEEQLDEEEAARQKLQLE--- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 429 sqglREEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTvtqqSQEEVARVKEQLAFQVEQVKRESE--LK 506
Cdd:pfam01576 126 ----KVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLA----EEEEKAKSLSKLKNKHEAMISDLEerLK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 507 LEEKSDQ-LEKLKRELEAKAGELaraQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAALS 585
Cdd:pfam01576 198 KEEKGRQeLEKAKRKLEGESTDL---QEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQIS 274
|
250 260
....*....|....*....|.
gi 733605517 586 R-----EQQRSSQEQGELQGR 601
Cdd:pfam01576 275 ElqedlESERAARNKAEKQRR 295
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
317-564 |
6.64e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 317 NLIEIS-TGPPAGEPVVVADLFDQTFgppngsVKDDRDLQIESLKREVEMLRSELEKIK---LEAQRYIAQLKSQVNALE 392
Cdd:COG3206 136 NVIEISyTSPDPELAAAVANALAEAY------LEQNLELRREEARKALEFLEEQLPELRkelEEAEAALEEFRQKNGLVD 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 393 geLEEQRKQKQKALVDNE----QLRHELAQLRA--AQLEGERSQGLREEAERKASATearYNKLKEKHSELVHVHAELLR 466
Cdd:COG3206 210 --LSEEAKLLLQQLSELEsqlaEARAELAEAEArlAALRAQLGSGPDALPELLQSPV---IQQLRAQLAELEAELAELSA 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 467 KNADT--------AKQLTVTQQSQEEVARVKEQLAFQVEQVKREsELKLEEKSDQLEKLKRELEAKAGELARAQEALSHT 538
Cdd:COG3206 285 RYTPNhpdvialrAQIAALRAQLQQEAQRILASLEAELEALQAR-EASLQAQLAQLEARLAELPELEAELRRLEREVEVA 363
|
250 260
....*....|....*....|....*.
gi 733605517 539 EQSKSELSSRLDTLSAEKDALSGAVR 564
Cdd:COG3206 364 RELYESLLQRLEEARLAEALTVGNVR 389
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
348-605 |
7.61e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 48.80 E-value: 7.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 348 VKDDRDLQIESLKREVEMLRsELEKIKLEAQRYIAQLKSQVNalegELEEQRKQKQKALVDNEQLR--HELAQLRAAQLE 425
Cdd:COG5185 259 VEQNTDLRLEKLGENAESSK-RLNENANNLIKQFENTKEKIA----EYTKSIDIKKATESLEEQLAaaEAEQELEESKRE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 426 GERS-QGLREEAERKASATEARYNKLKEKHSELVHVHAelLRKNADTAKQLTVTQQSQEE--------VARVKEQLAFQV 496
Cdd:COG5185 334 TETGiQNLTAEIEQGQESLTENLEAIKEEIENIVGEVE--LSKSSEELDSFKDTIESTKEsldeipqnQRGYAQEILATL 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 497 EQVKRESELKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQ-SKSELSSRLD--------TLSAEKDALSGAVRQRE 567
Cdd:COG5185 412 EDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMReADEESQSRLEeaydeinrSVRSKKEDLNEELTQIE 491
|
250 260 270
....*....|....*....|....*....|....*...
gi 733605517 568 ADLLAAQSLVRETEAALSREQQRSSQEQGELQGRLAER 605
Cdd:COG5185 492 SRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDF 529
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
413-605 |
7.79e-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: 49.28 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 413 RHE-LAQLRAAQLEGERSQGLREEAERK-------ASATEarynKLKEKHSELVHVHAELLrknadtAKQLtvtQQSQEE 484
Cdd:TIGR02168 174 RKEtERKLERTRENLDRLEDILNELERQlkslerqAEKAE----RYKELKAELRELELALL------VLRL---EELREE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 485 VARVKEQLAFQVEQVKR------ESELKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDA 558
Cdd:TIGR02168 241 LEELQEELKEAEEELEEltaelqELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 733605517 559 LSGAVRQREADLLAAQslvrETEAALSREQQRSSQEQGELQGRLAER 605
Cdd:TIGR02168 321 LEAQLEELESKLDELA----EELAELEEKLEELKEELESLEAELEEL 363
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
349-601 |
7.82e-06 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 48.87 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 349 KDDRDLQ--IESLKREVEMLRSELEKIKLEAQRyiaqLKSQVNALEGELEeqrkqKQKALVDNEQLRHELAQLRAAQLEg 426
Cdd:pfam05701 286 KTSTSIQaaLASAKKELEEVKANIEKAKDEVNC----LRVAAASLRSELE-----KEKAELASLRQREGMASIAVSSLE- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 427 ersqglrEEAERKASATEARYNKLKEKHSELVHVHAEL--LRKNADTAKQLtvTQQSQEEVARVKEqlafQVEQVKRES- 503
Cdd:pfam05701 356 -------AELNRTKSEIALVQAKEKEAREKMVELPKQLqqAAQEAEEAKSL--AQAAREELRKAKE----EAEQAKAAAs 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 504 --ELKLEEksdqlekLKRELEA-KAGE-LARA-----QEALSHTEQSKSELSSRLDTLSAEK-DALSGAVRQRE----AD 569
Cdd:pfam05701 423 tvESRLEA-------VLKEIEAaKASEkLALAaikalQESESSAESTNQEDSPRGVTLSLEEyYELSKRAHEAEelanKR 495
|
250 260 270
....*....|....*....|....*....|..
gi 733605517 570 LLAAQSLVRETEAALSREQQRSSQEQGELQGR 601
Cdd:pfam05701 496 VAEAVSQIEEAKESELRSLEKLEEVNREMEER 527
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
391-604 |
7.88e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.74 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 391 LEGELEEQRKQKqkalvdNEQLRHELAQLRAAQLEGERSQGLREEAERKASATEARYNKLK-------EKHSELVHVHAE 463
Cdd:pfam07888 32 LQNRLEECLQER------AELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKeelrqsrEKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 464 LLRKNADTAKQL-TVTQQSQEEVARVKE--QLAFQVEQVKRESELKLEEKSDQLEKLKRELEAKAGELARAQEALshtEQ 540
Cdd:pfam07888 106 LSASSEELSEEKdALLAQRAAHEARIREleEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKL---QQ 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 733605517 541 SKSELSSrldtLSAEKDALSGAVRQREADLLAAQSLV------------RETEAALSREQQRSSQEQGELQGRLAE 604
Cdd:pfam07888 183 TEEELRS----LSKEFQELRNSLAQRDTQVLQLQDTIttltqklttahrKEAENEALLEELRSLQERLNASERKVE 254
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
421-606 |
8.68e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 8.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 421 AAQLEGERSQglREEAERKASATEARYNKLKEKHSELvHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLafqvEQVK 500
Cdd:COG4913 609 RAKLAALEAE--LAELEEELAEAEERLEALEAELDAL-QERREALQRLAEYSWDEIDVASAEREIAELEAEL----ERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 501 RES-ELK-LEEKSDQLEKLKRELEAKAGELARAQEALshtEQSKSELSSRLDTLSAEKDALSGAVRQREADLLA---AQS 575
Cdd:COG4913 682 ASSdDLAaLEEQLEELEAELEELEEELDELKGEIGRL---EKELEQAEEELDELQDRLEAAEDLARLELRALLEerfAAA 758
|
170 180 190
....*....|....*....|....*....|.
gi 733605517 576 LVRETEAALSREQQRSSQEQGELQGRLAERV 606
Cdd:COG4913 759 LGDAVERELRENLEERIDALRARLNRAEEEL 789
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
355-603 |
9.52e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.96 E-value: 9.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 355 QIESLKREVEMLRSELEKIKLEAQRYIAQLKSQVNALEGELEEQRKQK----QKALVDNEQLRHELAQL----RAAQLEG 426
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERdqfsQESGNLDDQLQKLLADLhkreKELSLEK 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 427 ERSQGLREEAERKASATEARYNKLKEKHSELVHVHAELLRKNAD----TAKQLTVTQ---QSQEEVARVKEQLAFQVEQV 499
Cdd:pfam15921 398 EQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEcqgqMERQMAAIQgknESLEKVSSLTAQLESTKEML 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 500 KRESElKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDT-------LSAEKDALSGAvrQREADLLA 572
Cdd:pfam15921 478 RKVVE-ELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLklqelqhLKNEGDHLRNV--QTECEALK 554
|
250 260 270
....*....|....*....|....*....|.
gi 733605517 573 AQSLVRETEAALSREQQRSSQEQGELQGRLA 603
Cdd:pfam15921 555 LQMAEKDKVIEILRQQIENMTQLVGQHGRTA 585
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
355-559 |
9.94e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.86 E-value: 9.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 355 QIESLKREVemlrSELEKIKLEAQRYIAQLKSQVNALEGELEEQR---KQKQKALVDNEQlrhELAQLRA--AQLEGERS 429
Cdd:TIGR04523 441 EIKDLTNQD----SVKELIIKNLDNTRESLETQLKVLSRSINKIKqnlEQKQKELKSKEK---ELKKLNEekKELEEKVK 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 430 QGLREEAERKaSATEARYNKLKEKHSELVHVHAELLRKNADTAKQL--TVTQQSQEEVARVK-EQLAFQVEQvkRESELK 506
Cdd:TIGR04523 514 DLTKKISSLK-EKIEKLESEKKEKESKISDLEDELNKDDFELKKENleKEIDEKNKEIEELKqTQKSLKKKQ--EEKQEL 590
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 733605517 507 LEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDAL 559
Cdd:TIGR04523 591 IDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
377-606 |
1.09e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 377 AQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRAAQLEGERSQG-------LREEAERKASAteARYNK 449
Cdd:PRK04863 440 AEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAwdvarelLRRLREQRHLA--EQLQQ 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 450 LKEKHSEL---VHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVK------RESELKLEEKSDQLEKLKRE 520
Cdd:PRK04863 518 LRMRLSELeqrLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSesvseaRERRMALRQQLEQLQARIQR 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 521 LEAKAGELARAQEALSH-TEQSKSELSSRLDTLSAEKDALsgaVRQREA----DLLAAQslVRETEAALSREQQRSSQEQ 595
Cdd:PRK04863 598 LAARAPAWLAAQDALARlREQSGEEFEDSQDVTEYMQQLL---ERERELtverDELAAR--KQALDEEIERLSQPGGSED 672
|
250
....*....|.
gi 733605517 596 GELQgRLAERV 606
Cdd:PRK04863 673 PRLN-ALAERF 682
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
355-533 |
1.19e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 355 QIESLKREVEMLRSELEKIKLEAQryiaQLKSQVNALEGELEEQRKQKQKAlvdNEQLRHELAQLRAAQLEGERSQGLRE 434
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELE----QLEEELEQARSELEQLEEELEEL---NEQLQAAQAELAQAQEELESLQEEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 435 EAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLtvtQQSQEEVARVKEQLAFQVEQVKRESELKLEEKSDQL 514
Cdd:COG4372 112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL---KELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170
....*....|....*....
gi 733605517 515 EKLKRELEAKAGELARAQE 533
Cdd:COG4372 189 LKEANRNAEKEEELAEAEK 207
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
325-566 |
1.39e-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: 47.53 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 325 PPAGEPVVVADLFD-----QTFGPPNGSVKDDRDLQIESLKREVEMLRSELEKIKLEAQRyIAQLKSQVNALEG--ELEE 397
Cdd:TIGR02794 31 PGGGAEIIQAVLVDpgavaQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQAR-QKELEQRAAAEKAakQAEQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 398 QRKQKQKALVDNEQLRHELAQLRAAQLEGERSQGLREEAERKASATearyNKLKEkhselvhvhAELLRKNADTAKQLTV 477
Cdd:TIGR02794 110 AAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEE----AKAKA---------AAEAKKKAEEAKKKAE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 478 TQQSQEEVARVK---EQLAFQVEQVKRESELKLEEKSDQLEKLKRELEA--KAGEL-ARAQEALSHTEQSKSELSSRLDT 551
Cdd:TIGR02794 177 AEAKAKAEAEAKakaEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAerKADEAeLGDIFGLASGSNAEKQGGARGAA 256
|
250
....*....|....*
gi 733605517 552 LSAEKDALSGAVRQR 566
Cdd:TIGR02794 257 AGSEVDKYAAIIQQA 271
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
359-597 |
1.85e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 359 LKREVEMLRSELEKIKLEAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRaAQLEGERSQglREEAER 438
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLE-EELEQARSE--LEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 439 KASATEaryNKLKEKHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAfQVEQVKRESELKLEEKSDQLEKLK 518
Cdd:COG4372 81 ELEELN---EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK-QLEAQIAELQSEIAEREEELKELE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 733605517 519 RELEAKAGELARAQEALShtEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAALSREQQRSSQEQGE 597
Cdd:COG4372 157 EQLESLQEELAALEQELQ--ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
350-605 |
2.03e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 350 DDRDLQIESLKREVEMLRSELEKIKL---EAQRYIAQLKSQVNAL---EGELEEQRKQKQKALVDNEQLRHELAQLRAAQ 423
Cdd:PRK02224 380 EDRREEIEELEEEIEELRERFGDAPVdlgNAEDFLEELREERDELrerEAELEATLRTARERVEEAEALLEAGKCPECGQ 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 424 -LEGERSQGLREEAERKASATEARYNKLKEKHSEL--VHVHAELLRKNADTAKQLtvtqqsQEEVARVKEQLAFQVEQVK 500
Cdd:PRK02224 460 pVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVeeRLERAEDLVEAEDRIERL------EERREDLEELIAERRETIE 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 501 RESElKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALsgavrqreADLLAAQSLVRET 580
Cdd:PRK02224 534 EKRE-RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL--------ERIRTLLAAIADA 604
|
250 260
....*....|....*....|....*...
gi 733605517 581 EAALSREQQRSSQEQ---GELQGRLAER 605
Cdd:PRK02224 605 EDEIERLREKREALAelnDERRERLAEK 632
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
350-536 |
2.03e-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: 47.74 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 350 DDRDLQIESLKREVEMLRSELEKIKLEAQRYIAQLKSQVNALEGELEEQRK--QKQKALVDNEQLRHELAQLRAAQLEgE 427
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeaANLRERLESLERRIAATERRLEDLE-E 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 428 RSQGLREEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTVTQQSQEEVArvkeqlafQVEQVKRESELKL 507
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR--------ELESKRSELRREL 917
|
170 180
....*....|....*....|....*....
gi 733605517 508 EEKSDQLEKLKRELEAKAGELARAQEALS 536
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRIDNLQERLS 946
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
355-575 |
2.05e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 47.38 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 355 QIESLKREVEMLRSELEKIKLEAQRYIAQLKSqvnaLEGELEEQRKQKQKALVDNEQLRHELAQLRAAQLEGERSQGLRE 434
Cdd:pfam05622 184 QLETYKRQVQELHGKLSEESKKADKLEFEYKK----LEEKLEALQKEKERLIIERDTLRETNEELRCAQLQQAELSQADA 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 435 EAERKAS-----ATEARYNKLKEKHSELVHVHAEL-LRKNADTAKQLTVTQQSQEEVARVKEQLAFQ---VEQVKRESEL 505
Cdd:pfam05622 260 LLSPSSDpgdnlAAEIMPAEIREKLIRLQHENKMLrLGQEGSYRERLTELQQLLEDANRRKNELETQnrlANQRILELQQ 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 506 KLEE----------KSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEK-DALSGAVRQREADLLAAQ 574
Cdd:pfam05622 340 QVEElqkalqeqgsKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKiDELQEALRKKDEDMKAME 419
|
.
gi 733605517 575 S 575
Cdd:pfam05622 420 E 420
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
354-577 |
2.18e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 354 LQIESLKREVEMLRSELEKIKlEAQRYIAQLKSQVNALEGELEEQRKQKQkalvDNEQLRHELAQLRAAQlegersqglR 433
Cdd:PRK04863 887 LADETLADRVEEIREQLDEAE-EAKRFVQQHGNALAQLEPIVSVLQSDPE----QFEQLKQDYQQAQQTQ---------R 952
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 434 EEAERKASATEARYNKLKEKHSELVhvhaELLRKNADTAKQLTVTQ-QSQEEVARVKEQLAFQVEQV----KRESELK-- 506
Cdd:PRK04863 953 DAKQQAFALTEVVQRRAHFSYEDAA----EMLAKNSDLNEKLRQRLeQAEQERTRAREQLRQAQAQLaqynQVLASLKss 1028
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 507 LEEKSDQLEKLKRELE-----AKAGELARA-------QEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQ 574
Cdd:PRK04863 1029 YDAKRQMLQELKQELQdlgvpADSGAEERArarrdelHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMR 1108
|
...
gi 733605517 575 SLV 577
Cdd:PRK04863 1109 EQV 1111
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
350-594 |
2.56e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.42 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 350 DDRDLQIESLKREVEMLRSELEKiKLEAQRYIAQLKSQ----VNALEGELEEQRkqkqkalvdnEQLRHELAQLRAAQLE 425
Cdd:pfam15921 422 DDRNMEVQRLEALLKAMKSECQG-QMERQMAAIQGKNEslekVSSLTAQLESTK----------EMLRKVVEELTAKKMT 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 426 GERSQ-------GLREEAERKASATEARYNKLKE----KHSELVHVHAE-------------LLRKNADTAKQLTVTQQS 481
Cdd:pfam15921 491 LESSErtvsdltASLQEKERAIEATNAEITKLRSrvdlKLQELQHLKNEgdhlrnvqteceaLKLQMAEKDKVIEILRQQ 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 482 QEEVARVKEQL-----AFQVEQVKRESEL---KLEEKSDQLEKLK-----RELEAKAGELARAQEALSHteqSKSELSSR 548
Cdd:pfam15921 571 IENMTQLVGQHgrtagAMQVEKAQLEKEIndrRLELQEFKILKDKkdakiRELEARVSDLELEKVKLVN---AGSERLRA 647
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 733605517 549 LDTLSAEKDALSGAVRQREADLlaaQSLVRETEaALSREQQRSSQE 594
Cdd:pfam15921 648 VKDIKQERDQLLNEVKTSRNEL---NSLSEDYE-VLKRNFRNKSEE 689
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
383-593 |
2.72e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.48 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 383 QLKSQVNALEGELEEQRKQKQKALVDNEQLRHEL-------------------------AQLRAAQLEGERSQGLREEA- 436
Cdd:pfam01576 746 QLVKQVRELEAELEDERKQRAQAVAAKKKLELDLkeleaqidaankgreeavkqlkklqAQMKDLQRELEEARASRDEIl 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 437 ------ERKASATEARYNKLKEKHSElvhvhAELLRKNADT---------AKQLTVTQQSQEEVARVKEQLAfQVEQVKR 501
Cdd:pfam01576 826 aqskesEKKLKNLEAELLQLQEDLAA-----SERARRQAQQerdeladeiASGASGKSALQDEKRRLEARIA-QLEEELE 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 502 ESELKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAA-QSLVRET 580
Cdd:pfam01576 900 EEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAAlEAKIAQL 979
|
250
....*....|....*.
gi 733605517 581 EAAL---SREQQRSSQ 593
Cdd:pfam01576 980 EEQLeqeSRERQAANK 995
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
357-560 |
2.81e-05 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 47.16 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 357 ESLKREVEMLRsELEKIK--LEAQRYIAQLKSQVNALEGELEEQRKQKQKAlvdnEQLRHELAQLRAAQlEGERSQGLRE 434
Cdd:PLN03229 531 LSLKYKLDMLN-EFSRAKalSEKKSKAEKLKAEINKKFKEVMDRPEIKEKM----EALKAEVASSGASS-GDELDDDLKE 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 435 EAERKASATEARY-NKLKEKHSELVHVHAellrKNADTAKQLTVtQQSQEEVARVKEQLAFQVEQVKRES-------ELK 506
Cdd:PLN03229 605 KVEKMKKEIELELaGVLKSMGLEVIGVTK----KNKDTAEQTPP-PNLQEKIESLNEEINKKIERVIRSSdlkskieLLK 679
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 733605517 507 LE----------EKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALS 560
Cdd:PLN03229 680 LEvakasktpdvTEKEKIEALEQQIKQKIAEALNSSELKEKFEELEAELAAARETAAESNGSLK 743
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
354-615 |
3.07e-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: 47.14 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 354 LQIESLKREVEMLRSELEKIKLEAQRYIAQLKSQVNALEGELEE------QRKQKQKALVDNEQLRHELAQLRAAQLEGE 427
Cdd:pfam12128 258 LRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEkrdelnGELSAADAAVAKDRSELEALEDQHGAFLDA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 428 RSQGLREEAERKASAtearynklkekHSELVHVHAELlrkNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRESE--- 504
Cdd:pfam12128 338 DIETAAADQEQLPSW-----------QSELENLEERL---KALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAkir 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 505 ----LKLEEKSDQLEKL------------------KRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGA 562
Cdd:pfam12128 404 eardRQLAVAEDDLQALeselreqleagklefneeEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAA 483
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 733605517 563 VRQREA---DLLAAQSLVRETEAALSREQQRSSQEQGELQgRLAERVWPPQMQQHH 615
Cdd:pfam12128 484 NAEVERlqsELRQARKRRDQASEALRQASRRLEERQSALD-ELELQLFPQAGTLLH 538
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
349-520 |
3.18e-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: 47.37 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 349 KDDRDLQIESLKREVEMLRSELEKIKLEAQRYIAQ---LKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRAA--Q 423
Cdd:TIGR02169 849 IKSIEKEIENLNGKKEELEEELEELEAALRDLESRlgdLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKleA 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 424 LEGERSQGLREEAERKA-SATEARYNKLKEKHSELvhvhAELLRKNADTakQLTVTQQSQEEVARVKEqLAFQVEQVKRE 502
Cdd:TIGR02169 929 LEEELSEIEDPKGEDEEiPEEELSLEDVQAELQRV----EEEIRALEPV--NMLAIQEYEEVLKRLDE-LKEKRAKLEEE 1001
|
170
....*....|....*...
gi 733605517 503 SElKLEEKSDQLEKLKRE 520
Cdd:TIGR02169 1002 RK-AILERIEEYEKKKRE 1018
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
355-599 |
3.41e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.81 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 355 QIESLKREVEMLRSELEKIKL---EAQRYIAQLKSQVNALEGELEEQRkQKQKALVDNEQLRHELAQLRAAQLEGERSQG 431
Cdd:pfam07888 81 RVAELKEELRQSREKHEELEEkykELSASSEELSEEKDALLAQRAAHE-ARIRELEEDIKTLTQRVLERETELERMKERA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 432 LREEAERKASATEAR--YNKLKEKHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLafqveqvkreselklee 509
Cdd:pfam07888 160 KKAGAQRKEEEAERKqlQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKL----------------- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 510 ksDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQreADLLAAQSLVRETEA--ALSRE 587
Cdd:pfam07888 223 --TTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQ--ARLQAAQLTLQLADAslALREG 298
|
250
....*....|..
gi 733605517 588 QQRSSQEQGELQ 599
Cdd:pfam07888 299 RARWAQERETLQ 310
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
353-604 |
3.54e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 353 DLQIESLKREVEmlrsELEKIKLEAQRYIAQLKSQVnaleGELEEQRKQKQKALVDNEQLRHElAQLRAAQLEGERSQGL 432
Cdd:PRK03918 383 GLTPEKLEKELE----ELEKAKEEIEEEISKITARI----GELKKEIKELKKAIEELKKAKGK-CPVCGRELTEEHRKEL 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 433 REEAERKASATEARYNKLKEKHSELVHVHAElLRKNADTAKQLTVTQQSQEEVARVKEQL-AFQVEQVKRESEL--KLEE 509
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRE-LEKVLKKESELIKLKELAEQLKELEEKLkKYNLEELEKKAEEyeKLKE 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 510 KSDQLEK----LKRELEAKAG---ELARAQEALSHTEQSKSELSSRLDTLSAEK-DALSGAVRQREA------DLLAAQS 575
Cdd:PRK03918 533 KLIKLKGeiksLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESvEELEERLKELEPfyneylELKDAEK 612
|
250 260
....*....|....*....|....*....
gi 733605517 576 LVRETEAALSREQQRSSQEQGELQGRLAE 604
Cdd:PRK03918 613 ELEREEKELKKLEEELDKAFEELAETEKR 641
|
|
| I_LWEQ |
pfam01608 |
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from ... |
446-590 |
3.55e-05 |
|
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from mouse talin and yeast Sla2p interact with F-actin. I/LWEQ domains can be placed into four major groups based on sequence similarity: (1) Metazoan talin; (2) Dictyostelium TalA/TalB and SLA110; (3) metazoan Hip1p; and (4) yeast Sla2p. The domain has four conserved blocks, the name of the domain is derived from the initial conserved amino acid of each of the four blocks.
Pssm-ID: 460265 [Multi-domain] Cd Length: 149 Bit Score: 44.11 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 446 RYNKLKEKHSELVHVHAELLRKNADTAKQLtvtQQSQEEVARVKEQLAFQVEQVKRESELKLEEKSDQLEKLKRELEAka 525
Cdd:pfam01608 4 RWTEGLISAAKAVAAATNLLVEAADGVVQG---QGSEEELIVAAKEVAASTAQLVAASRVKADPNSKTQQRLEAASKA-- 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 733605517 526 geLARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREadLLAAQSLVRETEAALSREQQR 590
Cdd:pfam01608 79 --VTDATKNLVAAVKSAAELQEEEIEEEMDFSKLSLHQAKRQ--EMEAQVEILKLEKELEEARKK 139
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
416-604 |
3.71e-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: 46.30 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 416 LAQLRAAQLEGERSQGLREEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQ 495
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 496 VEQVKREselkLEEKSDQLEKLKRELEaKAGELARAQEALShtEQSKSELSSRLDTLSaekdALSGAVRQREADLLAAQS 575
Cdd:COG4942 92 IAELRAE----LEAQKEELAELLRALY-RLGRQPPLALLLS--PEDFLDAVRRLQYLK----YLAPARREQAEELRADLA 160
|
170 180
....*....|....*....|....*....
gi 733605517 576 LVRETEAALSREQQRSSQEQGELQGRLAE 604
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAA 189
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
401-606 |
3.89e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 401 QKQKALVDNEQLRHELAQLRAAQLEGERSqglREEAERKASATEARYNKLKEKHSELvhvhaellrknadtakqltvtqq 480
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRLKELPAE---LAELEDELAALEARLEAAKTELEDL----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 481 sQEEVARVKEQLAfQVEQVKRESELKLEEKSDQleklkRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALS 560
Cdd:COG1579 58 -EKEIKRLELEIE-EVEARIKKYEEQLGNVRNN-----KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 733605517 561 GAVRQREADLLAAQSLVRETEAALSREQQRSSQEQGELQGRLAERV 606
Cdd:COG1579 131 AELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPEL 176
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
410-595 |
5.52e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 46.27 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 410 EQLRHELAQLraaQLEGERSqglREEAERKASATEARYNKLKEKHSELvHVHAELLRKNADTAKQltvTQQSQEEVARVK 489
Cdd:pfam05557 12 SQLQNEKKQM---ELEHKRA---RIELEKKASALKRQLDRESDRNQEL-QKRIRLLEKREAEAEE---ALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 490 EQLAFQVEQVKRESELKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDtlsaEKDALSGAVRQREAD 569
Cdd:pfam05557 82 KKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLD----LLKAKASEAEQLRQN 157
|
170 180
....*....|....*....|....*..
gi 733605517 570 LLAAQSLVRETEAALSR-EQQRSSQEQ 595
Cdd:pfam05557 158 LEKQQSSLAEAEQRIKElEFEIQSQEQ 184
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
345-563 |
6.40e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 345 NGSVKDDRDLQ--IESLKREVEMLRSELEKIKLEAQRYIAQLKSQVNALEG-----ELEEQRKQKQKALVDN------EQ 411
Cdd:COG1196 550 NIVVEDDEVAAaaIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAvdlvaSDLREADARYYVLGDTllgrtlVA 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 412 LRHELAQLRAAQLEGER--SQGLREEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVK 489
Cdd:COG1196 630 ARLEAALRRAVTLAGRLreVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 733605517 490 EQLAFQVEQVKRESELKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALsGAV 563
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL-GPV 782
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
362-604 |
8.42e-05 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 45.67 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 362 EVEMLRSELEKIKLEAQRYIAQLKSQVNALEGELEEQRKQKQKAlvdNEQLRHELAQLRAAQleGERSQGLReeaeRKAS 441
Cdd:pfam15964 214 EDEKWRLELEKLKLLYEAKTEVLESQVKSLRKDLAESQKTCEDL---KERLKHKESLVAAST--SSRVGGLC----LKCA 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 442 ATEArynKLKEKHSElVHVHA-ELLRKNADTAKQLTVTQQSQEEVARVKEQLAF-QVEQVKRESELKLEEKSD---QLEK 516
Cdd:pfam15964 285 QHEA---VLAQTHTN-VHMQTiERLTKERDDLMSALVSVRSSLAEAQQRESSAYeQVKQAVQMTEEANFEKTKaliQCEQ 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 517 LKRELEAKAGELARaqealshteqsksELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAALSREQQRSSQEQG 596
Cdd:pfam15964 361 LKSELERQKERLEK-------------ELASQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKN 427
|
....*...
gi 733605517 597 ELQGRLAE 604
Cdd:pfam15964 428 SLVSQLEE 435
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
348-445 |
9.36e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 9.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 348 VKDDRDL--QIESLKREVEMLRSELEKIKLEAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRAAQLE 425
Cdd:COG3883 128 ADADADLleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
90 100
....*....|....*....|
gi 733605517 426 GERSQGLREEAERKASATEA 445
Cdd:COG3883 208 AEAAAAAAAAAAAAAAAAAA 227
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
403-606 |
1.17e-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: 45.33 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 403 QKALVDN-EQLRHELAQLRAAqlegERSQglrEEAERKASATEARYNKLKEKHSELVHVHAELlrknadtakqltvtqqs 481
Cdd:COG3096 507 QQALAQRlQQLRAQLAELEQR----LRQQ---QNAERLLEEFCQRIGQQLDAAEELEELLAEL----------------- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 482 QEEVARVKEQLAfqvEQVKRESELKLEEksDQLEKLKRELEAKAGELARAQEALSH-TEQSKSELSSRLDTLSAEKDALS 560
Cdd:COG3096 563 EAQLEELEEQAA---EAVEQRSELRQQL--EQLRARIKELAARAPAWLAAQDALERlREQSGEALADSQEVTAAMQQLLE 637
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 733605517 561 gavRQREA----DLLAAQSlvRETEAALSREQQRSSQEQGELQgRLAERV 606
Cdd:COG3096 638 ---REREAtverDELAARK--QALESQIERLSQPGGAEDPRLL-ALAERL 681
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
358-598 |
1.46e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.14 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 358 SLKREVEMLRSELEKIKLEAQRYIAQLKSqvnALEGELEEQRKQKQKALVDNEQLRHELAQLRAA----QLEGERSQGLR 433
Cdd:pfam00038 22 FLEQQNKLLETKISELRQKKGAEPSRLYS---LYEKEIEDLRRQLDTLTVERARLQLELDNLRLAaedfRQKYEDELNLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 434 EEAE------RK--ASAT------EARYNKLKEKHSELVHVH----AELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQ 495
Cdd:pfam00038 99 TSAEndlvglRKdlDEATlarvdlEAKIESLKEELAFLKKNHeeevRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 496 VEQVKRESELKLEEK-SDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREA----DL 570
Cdd:pfam00038 179 YEEIAAKNREEAEEWyQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEEryelQL 258
|
250 260 270
....*....|....*....|....*....|.
gi 733605517 571 LAAQSLVRETEAALSR---EQQRSSQEQGEL 598
Cdd:pfam00038 259 ADYQELISELEAELQEtrqEMARQLREYQEL 289
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
362-612 |
1.63e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.82 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 362 EVEMLRSELEKiklEAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQ----LRHELAQLRA-AQLEGERsqgLREEA 436
Cdd:NF041483 394 EAERIRREAEA---EADRLRGEAADQAEQLKGAAKDDTKEYRAKTVELQEearrLRGEAEQLRAeAVAEGER---IRGEA 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 437 ERKASATEARYNKLKEKHSELVHVHAELLRKNAdTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRESELKLEEKSDQLEK 516
Cdd:NF041483 468 RREAVQQIEEAARTAEELLTKAKADADELRSTA-TAESERVRTEAIERATTLRRQAEETLERTRAEAERLRAEAEEQAEE 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 517 LKRELEAKAGELAraQEALSHTEQSKSELSSRLDTLSAEKdalsgavrqrEADLLAAQSLVRETEAALSREQQRSSQEQG 596
Cdd:NF041483 547 VRAAAERAARELR--EETERAIAARQAEAAEELTRLHTEA----------EERLTAAEEALADARAEAERIRREAAEETE 614
|
250
....*....|....*.
gi 733605517 597 ELQGRLAERVWPPQMQ 612
Cdd:NF041483 615 RLRTEAAERIRTLQAQ 630
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
355-593 |
1.75e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 355 QIESLKR---EVEMLRSELEKIKLEAQ---RYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQ-LRAAQLEGE 427
Cdd:pfam01576 364 QLEQAKRnkaNLEKAKQALESENAELQaelRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEkLSKLQSELE 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 428 RSQGLREEAERKASateaRYNKLKEKHSELVHVHAELLRKnaDTAKQLTVT---QQSQEEVARVKEQLAFQVEQvKRESE 504
Cdd:pfam01576 444 SVSSLLNEAEGKNI----KLSKDVSSLESQLQDTQELLQE--ETRQKLNLStrlRQLEDERNSLQEQLEEEEEA-KRNVE 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 505 LKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGA---VRQREADLLAAQSLVRETE 581
Cdd:pfam01576 517 RQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTknrLQQELDDLLVDLDHQRQLV 596
|
250
....*....|..
gi 733605517 582 AALSREQQRSSQ 593
Cdd:pfam01576 597 SNLEKKQKKFDQ 608
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
390-606 |
2.21e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.30 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 390 ALEGELEEQRKQKQKALVDNEQLRHELAQLRAAQL-EGERSQgLREEAERKASAtearynklkEKHSELVHVHAELLRKN 468
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEELEAAALqPGEEEE-LEEERRRLSNA---------EKLREALQEALEALSGG 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 469 ADTA-KQLTVTQQSQEEVARVKEQLAFQVEQVkRESELKLEEKSDQLEKLKRELEAKAGELARAQEALS--HTEQSK--- 542
Cdd:COG0497 239 EGGAlDLLGQALRALERLAEYDPSLAELAERL-ESALIELEEAASELRRYLDSLEFDPERLEEVEERLAllRRLARKygv 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 733605517 543 --SELSSRLDTLSAEKDALSGAvrqrEADLLAAQSLVRETEAALSREQQRSSQEQGELQGRLAERV 606
Cdd:COG0497 318 tvEELLAYAEELRAELAELENS----DERLEELEAELAEAEAELLEAAEKLSAARKKAAKKLEKAV 379
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
362-573 |
2.30e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 362 EVEMLRSELEKIKLEAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRaaqlegersqglreeaerkas 441
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE--------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 442 ateARYNKLKEKHSelvhvhaellrkNADTAKQLTVTQQSQEEVARVKEQLafqvEQVKRESELKLEEKSDQLEKLKREL 521
Cdd:COG1579 73 ---ARIKKYEEQLG------------NVRNNKEYEALQKEIESLKRRISDL----EDEILELMERIEELEEELAELEAEL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 733605517 522 EAKAGELARAQEALshtEQSKSELSSRLDTLSAEKDALSGAVrqrEADLLAA 573
Cdd:COG1579 134 AELEAELEEKKAEL---DEELAELEAELEELEAEREELAAKI---PPELLAL 179
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
357-559 |
2.55e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 357 ESLKREVEMLRSEL----------------EKIKLEAQryIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLR 420
Cdd:pfam01576 853 ERARRQAQQERDELadeiasgasgksalqdEKRRLEAR--IAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAER 930
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 421 --AAQLEGERSQGLREEAERKASATEARyNKLKEKHSELVhvhAELLRKNADTAKQLTvtQQSQEEVARVK--------- 489
Cdd:pfam01576 931 stSQKSESARQQLERQNKELKAKLQEME-GTVKSKFKSSI---AALEAKIAQLEEQLE--QESRERQAANKlvrrtekkl 1004
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 733605517 490 EQLAFQVEQVKRESEL---KLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDAL 559
Cdd:pfam01576 1005 KEVLLQVEDERRHADQykdQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTL 1077
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
434-604 |
2.68e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 434 EEAERKASATEARYNKLKEKHSELVHVHAELlrknadtAKQLTVTQQSQEEVARVKEqlAFQVEQVKRESELKLEEKSDQ 513
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEEL-------EAELEELREELEKLEKLLQ--LLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 514 LEKLKRELEakagELARAQEALSHTEQSKSELSSRLDTLsaeKDALSGAVRQREADLLAAQSLVRETEAALSREQQRSSQ 593
Cdd:COG4717 148 LEELEERLE----ELRELEEELEELEAELAELQEELEEL---LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170
....*....|.
gi 733605517 594 EQGELQGRLAE 604
Cdd:COG4717 221 ELEELEEELEQ 231
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
374-600 |
3.30e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 374 KLEAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLR----------AAQ--LEGERSQ---GLREEAER 438
Cdd:pfam01576 259 KNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKteledtldttAAQqeLRSKREQevtELKKALEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 439 KASATEARYNKLKEKHSELVHVHAELL------------------RKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVK 500
Cdd:pfam01576 339 ETRSHEAQLQEMRQKHTQALEELTEQLeqakrnkanlekakqaleSENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 501 ---RESELKLEEKSDQLEKLKRELEAKAGELARA---------------------QEALSHTEQSKSELSSRLDTLSAEK 556
Cdd:pfam01576 419 arlSESERQRAELAEKLSKLQSELESVSSLLNEAegkniklskdvsslesqlqdtQELLQEETRQKLNLSTRLRQLEDER 498
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 733605517 557 DALSGAVRQREADLLAAQSLVRETEAALSREQQRSSQEQGELQG 600
Cdd:pfam01576 499 NSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA 542
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
435-594 |
3.94e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 435 EAERKASATEARYNKLKEKHSELV----HVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRESELKLEEK 510
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDakedNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAED 1138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 511 SDQLEKLKRELEAKAGELAR-AQEALSHTEQSKSELSSRLDtlsaekdALSGAVRQREADLLAAQSLVRETEAALSREQQ 589
Cdd:PTZ00121 1139 ARKAEEARKAEDAKRVEIARkAEDARKAEEARKAEDAKKAE-------AARKAEEVRKAEELRKAEDARKAEAARKAEEE 1211
|
....*
gi 733605517 590 RSSQE 594
Cdd:PTZ00121 1212 RKAEE 1216
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
395-548 |
4.31e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.07 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 395 LEEQRKQKQKALvdneQLRHELAQL--RAAQLEGERSQGLREEAERKASateaRYNKLKEKhselvhvhAELLRKNADTA 472
Cdd:pfam05262 183 VEALREDNEKGV----NFRRDMTDLkeRESQEDAKRAQQLKEELDKKQI----DADKAQQK--------ADFAQDNADKQ 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 473 KQlTVTQQSQEEV----------ARVKEQLAfqvEQVKRESELKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSK 542
Cdd:pfam05262 247 RD-EVRQKQQEAKnlpkpadtssPKEDKQVA---ENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDK 322
|
....*.
gi 733605517 543 SELSSR 548
Cdd:pfam05262 323 ELEAQK 328
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
355-604 |
4.53e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 355 QIESLKREVEMLRSELEKIKLEAQRY---------------------IAQLKSQVNALEGELEEQRKQKQKALVDNEQLR 413
Cdd:COG4913 339 RLEQLEREIERLERELEERERRRARLeallaalglplpasaeefaalRAEAAALLEALEEELEALEEALAEAEAALRDLR 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 414 HELAQLRA--AQLEGERS------QGLREEAERKASATEAR------YNKLKEKHSE----------------LV----- 458
Cdd:COG4913 419 RELRELEAeiASLERRKSniparlLALRDALAEALGLDEAElpfvgeLIEVRPEEERwrgaiervlggfaltlLVppehy 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 459 --------------HVHAELLRKNADTAKQLTVTQQS-------QEEVAR--VKEQLA--FQVEQVKRESELKLEEKS-- 511
Cdd:COG4913 499 aaalrwvnrlhlrgRLVYERVRTGLPDPERPRLDPDSlagkldfKPHPFRawLEAELGrrFDYVCVDSPEELRRHPRAit 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 512 --------------DQLEKLKRE----------LEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQRE 567
Cdd:COG4913 579 ragqvkgngtrhekDDRRRIRSRyvlgfdnrakLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW 658
|
330 340 350
....*....|....*....|....*....|....*....
gi 733605517 568 A--DLLAAQSLVRETEAALsREQQRSSQEQGELQGRLAE 604
Cdd:COG4913 659 DeiDVASAEREIAELEAEL-ERLDASSDDLAALEEQLEE 696
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
355-536 |
5.11e-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: 43.12 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 355 QIESLKREVEMLRS---ELEKIKLEAQRYIAQLKSQVNALEGELEEQRKQKqkalvdnEQLRHELAQLRAaqlegERSQG 431
Cdd:TIGR02168 359 ELEELEAELEELESrleELEEQLETLRSKVAQLELQIASLNNEIERLEARL-------ERLEDRRERLQQ-----EIEEL 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 432 LREEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRESElKLEEKS 511
Cdd:TIGR02168 427 LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE-NLEGFS 505
|
170 180
....*....|....*....|....*
gi 733605517 512 DQLEKLKRELEAKAGELARAQEALS 536
Cdd:TIGR02168 506 EGVKALLKNQSGLSGILGVLSELIS 530
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
352-594 |
5.72e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 352 RDLQIESLKREVEMLRSELEKIKlEAQRYIAQLKSQVNALEGE---LEEQRKQKQKALVDNEQLRHELAQLRAAQLEG-- 426
Cdd:TIGR00606 229 KEAQLESSREIVKSYENELDPLK-NRLKEIEHNLSKIMKLDNEikaLKSRKKQMEKDNSELELKMEKVFQGTDEQLNDly 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 427 ERSQGLREEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVE--------- 497
Cdd:TIGR00606 308 HNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfergpf 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 498 ---QVKRESELKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDT----LSAEKDALSGAVRQREA-- 568
Cdd:TIGR00606 388 serQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELkkeiLEKKQEELKFVIKELQQle 467
|
250 260 270
....*....|....*....|....*....|
gi 733605517 569 ----DLLAAQSLVRETEAALSREQQRSSQE 594
Cdd:TIGR00606 468 gssdRILELDQELRKAERELSKAEKNSLTE 497
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
352-602 |
6.05e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 352 RDLQIESLKREVEMLRSELEKIKLEAQRY--------------------------IAQLKSQVNALEGELEEQRKQKQKA 405
Cdd:PRK04863 784 REKRIEQLRAEREELAERYATLSFDVQKLqrlhqafsrfigshlavafeadpeaeLRQLNRRRVELERALADHESQEQQQ 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 406 LVDNEQLRHELAQLRAAQLE---------GERSQGLREEAER--KASATEARYNKLKEKHSELVHV------HAELLRKN 468
Cdd:PRK04863 864 RSQLEQAKEGLSALNRLLPRlnlladetlADRVEEIREQLDEaeEAKRFVQQHGNALAQLEPIVSVlqsdpeQFEQLKQD 943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 469 ADTAKQLTVTQQSQ----EEVARVKEQLAFQveqvkrESELKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSE 544
Cdd:PRK04863 944 YQQAQQTQRDAKQQafalTEVVQRRAHFSYE------DAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQ 1017
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 733605517 545 LSSRLDTLSAEKDALsgavRQREADLlaAQSLVRETEAALSREQQRSSQEQGELQGRL 602
Cdd:PRK04863 1018 YNQVLASLKSSYDAK----RQMLQEL--KQELQDLGVPADSGAEERARARRDELHARL 1069
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
460-605 |
6.06e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 460 VHAELLRKNADTAKQLTVTQQS--QEEVARVKEQLAFQVEQVKRESElKLEEKSDQLEKLKRELEAKAGELARAQEALSH 537
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEaaQAELDALQAELEELNEEYNELQA-ELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 538 -------------------TEQSKSELSSRLDTLS----AEKDALSgAVRQREADLLAAQSLVRETEAALSREQQRSSQE 594
Cdd:COG3883 91 raralyrsggsvsyldvllGSESFSDFLDRLSALSkiadADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170
....*....|.
gi 733605517 595 QGELQGRLAER 605
Cdd:COG3883 170 KAELEAQQAEQ 180
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
462-604 |
6.15e-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: 6.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 462 AELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRESELKleEKSDQLEKLKRELEAKagELARAQEALshtEQS 541
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA--ERYQALLKEKREYEGY--ELLKEKEAL---ERQ 238
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 733605517 542 KSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAALSREqqrSSQEQGELQGRLAE 604
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL---GEEEQLRVKEKIGE 298
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
357-541 |
6.43e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 357 ESLKREVEMLRSELEKIKLEAQRYIAQLKSQVNALEGE----LEEQRKQKQKALvdnEQLRHELAQ----LRAAQLEGER 428
Cdd:PRK00409 526 EELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEedklLEEAEKEAQQAI---KEAKKEADEiikeLRQLQKGGYA 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 429 SQGLREEAERKASATEArYNKLKEKHSELVHVHAELlrKNADTAKQLTVTQQSqeEVARVKEQLAFQVeqvkRESELKLE 508
Cdd:PRK00409 603 SVKAHELIEARKRLNKA-NEKKEKKKKKQKEKQEEL--KVGDEVKYLSLGQKG--EVLSIPDDKEAIV----QAGIMKMK 673
|
170 180 190
....*....|....*....|....*....|...
gi 733605517 509 EKSDQLEKLKRELEAKAGELARAQEALSHTEQS 541
Cdd:PRK00409 674 VPLSDLEKIQKPKKKKKKKPKTVKPKPRTVSLE 706
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
371-589 |
6.95e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 371 EKIKLEAQRYIAQLKSQVNALEG-ELEEQRKQKQ-KALVDNEQLRHELAQLRAAQLEGERSQGLREEAERKASATEaRYN 448
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEeELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE-IAA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 449 KLKEKHSElvhvHAELLRKNADTAKQLtvtQQSQEEVARVKEQLAFQVEQVKRESE-LKLEEKSDQLEKLKRELEAKAGE 527
Cdd:COG4717 375 LLAEAGVE----DEEELRAALEQAEEY---QELKEELEELEEQLEELLGELEELLEaLDEEELEEELEELEEELEELEEE 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 733605517 528 LARAQEALSHTEQSKSELSS--RLDTLSAEKDALSGAVRQREADLLA---AQSLVRETEAALSREQQ 589
Cdd:COG4717 448 LEELREELAELEAELEQLEEdgELAELLQELEELKAELRELAEEWAAlklALELLEEAREEYREERL 514
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
355-556 |
8.37e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 42.32 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 355 QIESLKREVEMLRSELEKIKLEAQRY-----IAQLKSQ----------VNALEGELEEQRKQKQKALVDNEQLRHELAQL 419
Cdd:pfam05701 71 ELESTKRLIEELKLNLERAQTEEAQAkqdseLAKLRVEemeqgiadeaSVAAKAQLEVAKARHAAAVAELKSVKEELESL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 420 R-----------AAQLEGERSQGLREEAERKASATEARYNKLKE--KHSELVHVHAELLRKNADTAKQLTVTQ------Q 480
Cdd:pfam05701 151 RkeyaslvserdIAIKRAEEAVSASKEIEKTVEELTIELIATKEslESAHAAHLEAEEHRIGAALAREQDKLNwekelkQ 230
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 733605517 481 SQEEVARVKEQLAfqveqVKRESELKLEEKSDQLEKLKRELEAKAgELARAQEALSHTEQSKSELSSRLDTLSAEK 556
Cdd:pfam05701 231 AEEELQRLNQQLL-----SAKDLKSKLETASALLLDLKAELAAYM-ESKLKEEADGEGNEKKTSTSIQAALASAKK 300
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
371-559 |
8.53e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.10 E-value: 8.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 371 EKIKLEAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQlrhelaQLRAAQLEGERSQglrEEAERKASATEARYNKL 450
Cdd:PRK09510 79 EQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQ------AEEAAKQAALKQK---QAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 451 KEKHSELvhvhAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQ-----VEQVKRESELKLEEKSDQLEKLKRELEAKA 525
Cdd:PRK09510 150 EAEAKRA----AAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEaaakaAAEAKKKAEAEAKKKAAAEAKKKAAAEAKA 225
|
170 180 190
....*....|....*....|....*....|....
gi 733605517 526 GELARAQEALSHTEQSKSELSSRLDTLSAEKDAL 559
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
362-553 |
8.58e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.67 E-value: 8.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 362 EVEMLRSELEKIKLEAQR-------YIAQLKSQ--------VNALEGELEEQRKQKQKALVDNEQLRHELAQLRA--AQL 424
Cdd:pfam09787 1 NLESAKQELADYKQKAARilqskekLIASLKEGsgvegldsSTALTLELEELRQERDLLREEIQKLRGQIQQLRTelQEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 425 EGERSQGLREEAERKASATEarynKLKEKHSELVHVHAELLRKnadtakqltvtqqsQEEVARVKEQLafqvEQVKRESE 504
Cdd:pfam09787 81 EAQQQEEAESSREQLQELEE----QLATERSARREAEAELERL--------------QEELRYLEEEL----RRSKATLQ 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 733605517 505 LKLEEKSDQLEKLKRELEAKagelaraqealSHTEQSKSELSSRLDTLS 553
Cdd:pfam09787 139 SRIKDREAEIEKLRNQLTSK-----------SQSSSSQSELENRLHQLT 176
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
378-531 |
8.82e-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: 42.63 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 378 QRYIAQLKSQVNALEGELEEQRKQKQKA--------------LVDNEQLRHELAQLRaAQLEgERSQGLREEAERkASAT 443
Cdd:COG3096 507 QQALAQRLQQLRAQLAELEQRLRQQQNAerlleefcqrigqqLDAAEELEELLAELE-AQLE-ELEEQAAEAVEQ-RSEL 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 444 EARYNKLKEKHSELvHVHAELLRKNADTAKQLtvTQQSQEEVARVKEQLAFQVEQVKRESELKLEEksDQLEKLKRELEA 523
Cdd:COG3096 584 RQQLEQLRARIKEL-AARAPAWLAAQDALERL--REQSGEALADSQEVTAAMQQLLEREREATVER--DELAARKQALES 658
|
....*...
gi 733605517 524 KAGELARA 531
Cdd:COG3096 659 QIERLSQP 666
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
394-525 |
8.95e-04 |
|
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: 42.25 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 394 ELEEQRKQKQKALVDNEQLRHELAQ----------LRAAQLEGERSQglREEAERK-ASATEARYNKLKEKHSELVHVHA 462
Cdd:pfam15709 356 EQEEQRRLQQEQLERAEKMREELELeqqrrfeeirLRKQRLEEERQR--QEEEERKqRLQLQAAQERARQQQEEFRRKLQ 433
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 733605517 463 ELLRKnadtaKQLTVTQQSQEEVARVKEQLAFQVEQVKRESELKLEEKSDQLEKlKRELEAKA 525
Cdd:pfam15709 434 ELQRK-----KQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQ-KQEAEEKA 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
349-565 |
1.01e-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: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 349 KDDRDLQIESLKREVEMLRSELEKIKLEAQryiaqlksqvnalegELEEQRKQKQKALvdnEQLRHELAQLRAAQleger 428
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELE---------------ALLNERASLEEAL---ALLRSELEELSEEL----- 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 429 sqglrEEAERKASATEARYNKLKEKHSELVhvhaelLRKNadtakQLTVTQQSQEEVARVKEQLAFQ-VEQVKRESELKL 507
Cdd:TIGR02168 904 -----RELESKRSELRRELEELREKLAQLE------LRLE-----GLEVRIDNLQERLSEEYSLTLEeAEALENKIEDDE 967
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 733605517 508 EEKSDQLEKLKRELEAKAGELARAQEALshteqskSELSSRLDTLSAEKDALSGAVRQ 565
Cdd:TIGR02168 968 EEARRRLKRLENKIKELGPVNLAAIEEY-------EELKERYDFLTAQKEDLTEAKET 1018
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
359-545 |
1.01e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 359 LKREVEMLRSELEKIKlEAQRYIAQLKSQVNALEGELEE-QRKQKQKALVDNEQLRHELAQLRAAQLEGERSQGLREEAE 437
Cdd:PRK03918 537 LKGEIKSLKKELEKLE-ELKKKLAELEKKLDELEEELAElLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELE 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 438 RKASATEARYNKLKEKHSELVHVHAEL--LRKNADTAKQLTvtqqSQEEVARVKEQLAFQVEQVKR-ESELK-LEEKSDQ 513
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLeeLRKELEELEKKY----SEEEYEELREEYLELSRELAGlRAELEeLEKRREE 691
|
170 180 190
....*....|....*....|....*....|..
gi 733605517 514 LEKLKRELEAKAGELARAQEALSHTEQSKSEL 545
Cdd:PRK03918 692 IKKTLEKLKEELEEREKAKKELEKLEKALERV 723
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
361-605 |
1.06e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 361 REVEMLRSELEKIKLEAQRYIAQLKSQVNALEGE----LEEQRKQKQKALVdneQLRHELAQLRAAQLEGERSQGLREEA 436
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEAKKKAEDARKAEEARKAEdarkAEEARKAEDAKRV---EIARKAEDARKAEEARKAEDAKKAEA 1180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 437 ERKA----------SATEARYNKLKEKHSELVHvhAELLRKnADTAKQLTVTQQSQEevARVKEQLAFQVEQVKRESELK 506
Cdd:PTZ00121 1181 ARKAeevrkaeelrKAEDARKAEAARKAEEERK--AEEARK-AEDAKKAEAVKKAEE--AKKDAEEAKKAEEERNNEEIR 1255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 507 LEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAALSR 586
Cdd:PTZ00121 1256 KFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK 1335
|
250
....*....|....*....
gi 733605517 587 EQQRSSQEQGELQGRLAER 605
Cdd:PTZ00121 1336 KKAEEAKKAAEAAKAEAEA 1354
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
393-597 |
1.07e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 42.24 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 393 GELEEQRKQKQKAlvDNEQLRHELAQLRaaqLEgersqglREEAERKAsatearynKLKEKhselvhvhAELLRKNADTA 472
Cdd:PRK05035 436 AEIRAIEQEKKKA--EEAKARFEARQAR---LE-------REKAAREA--------RHKKA--------AEARAAKDKDA 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 473 kqltvtqqSQEEVARVKEQLAfQVEQVKRESELKLEEKSDQLEKLKRELEAKAGELARAQEAlSHTEQSKSELSSRLDTL 552
Cdd:PRK05035 488 --------VAAALARVKAKKA-AATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAA-AAADPKKAAVAAAIARA 557
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 733605517 553 SAEKDAL--SGAVRQREADLLAAQslvreTEAALSREQQRSSQEQGE 597
Cdd:PRK05035 558 KAKKAAQqaANAEAEEEVDPKKAA-----VAAAIARAKAKKAAQQAA 599
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
457-605 |
1.09e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 457 LVHVHAELLRKnadtakQLTVTQQSQEEVARVKEQLAFQVEQVKRESELKLEEKSDQLEKLKRELEAKAGELARAQEALS 536
Cdd:pfam07888 24 LVVPRAELLQN------RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 733605517 537 HTEQSKSELSSRLDTLSAEKDALSGA-------VRQREADLLAAQSLVRETEAALSREQQRSSQEQGELQGRLAER 605
Cdd:pfam07888 98 ELEEKYKELSASSEELSEEKDALLAQraahearIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAER 173
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
376-530 |
1.12e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 376 EAQRYIAQLKSQVNALEGELEEQRK-QKQKAlvdneqlrHELAQLRaaqlegERSQGLREEAERKASATEARYNKLKEKH 454
Cdd:PRK00409 506 EAKKLIGEDKEKLNELIASLEELEReLEQKA--------EEAEALL------KEAEKLKEELEEKKEKLQEEEDKLLEEA 571
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 733605517 455 SELVHVHAELLRKNADTAKQLTVTQQsQEEVARVKEQlafQVEQVKRESELKLEEKSDQLEKLKRELEA-KAGELAR 530
Cdd:PRK00409 572 EKEAQQAIKEAKKEADEIIKELRQLQ-KGGYASVKAH---ELIEARKRLNKANEKKEKKKKKQKEKQEElKVGDEVK 644
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
499-604 |
1.20e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 499 VKRESELKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSG---AVRQREADLLAAQS 575
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQeeeKLKERLEELEEDLS 747
|
90 100
....*....|....*....|....*....
gi 733605517 576 LVRETEAALSREQQRSSQEQGELQGRLAE 604
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHK 776
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
354-488 |
1.22e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 354 LQIESLKREVEMLRSELEKIKLEAQryiaqlksqvnALEGELEEQRKQKQKALVDNE-QLRHELAQLRAAQlegERSQGL 432
Cdd:COG0542 404 MEIDSKPEELDELERRLEQLEIEKE-----------ALKKEQDEASFERLAELRDELaELEEELEALKARW---EAEKEL 469
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 733605517 433 REEAERKASATEARYNKLKEKHSELVHVHAELlrKNADTAKQLTVTqqsQEEVARV 488
Cdd:COG0542 470 IEEIQELKEELEQRYGKIPELEKELAELEEEL--AELAPLLREEVT---EEDIAEV 520
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
375-531 |
1.23e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.78 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 375 LEAQ--RYIAQLKSQ----VNALEGELEEQRKQKQKalvdneqlrhelaQLRAAQLEGERSQGLREEAERKAsatearyn 448
Cdd:COG2268 186 LDALgrRKIAEIIRDariaEAEAERETEIAIAQANR-------------EAEEAELEQEREIETARIAEAEA-------- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 449 klkekhsELVHVHAELLRKnADTAKQLTvTQQSQEEVARVKEQLAFQVEQVKRESELKLEEKsdqlEKLKRELEAKAGEL 528
Cdd:COG2268 245 -------ELAKKKAEERRE-AETARAEA-EAAYEIAEANAEREVQRQLEIAEREREIELQEK----EAEREEAELEADVR 311
|
...
gi 733605517 529 ARA 531
Cdd:COG2268 312 KPA 314
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
397-573 |
1.29e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 40.51 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 397 EQRKQKQKALvdNEQLRHELAQLRAAQLEGERsqgLREEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLT 476
Cdd:cd00176 36 EALLKKHEAL--EAELAAHEERVEALNELGEQ---LIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 477 VTQQSQEEVARVKEQLAFQVEQVKRESELKLEEKSDQLEKLKRELEAKAGELARAQEAL-----SHTEQSKSELSSRLDT 551
Cdd:cd00176 111 FFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAeelleEGHPDADEEIEEKLEE 190
|
170 180
....*....|....*....|..
gi 733605517 552 LSAEKDALSGAVRQREADLLAA 573
Cdd:cd00176 191 LNERWEELLELAEERQKKLEEA 212
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
350-575 |
1.33e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 41.50 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 350 DDRDLqiESLKREVEMLRSELEKIKLEAQRyiaqlksqvNALEGELEEQRKQKQKALVDNEQLRHELAQLRAAQLEGERS 429
Cdd:PRK07735 3 PEKDL--EDLKKEAARRAKEEARKRLVAKH---------GAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 430 QGLREEAERKAS-ATEARYNKLKEKHSELVHVHAELLRKN-ADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKR----ES 503
Cdd:PRK07735 72 AALAKQKREGTEeVTEEEKAKAKAKAAAAAKAKAAALAKQkREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQkregTE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 733605517 504 ELKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQS 575
Cdd:PRK07735 152 EVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKA 223
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
376-604 |
1.54e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 376 EAQRYIAQLKSQvNALEGELEEQRKQKQKALVDNEQLRHELAQLRAAQLEGERSQGLREEAERKASATEARYNKLKEKHS 455
Cdd:COG1196 558 VAAAAIEYLKAA-KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 456 ELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRESELKLEEKSDQLEKLKRELEAKAGELARAQEAL 535
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 733605517 536 SHTEQSKSELSSRLDTLSAEKDALsgavrQREADLLAAQSLVRETEAALSREQQRssQEQGELQGRLAE 604
Cdd:COG1196 717 LEEELEEEALEEQLEAEREELLEE-----LLEEEELLEEEALEELPEPPDLEELE--RELERLEREIEA 778
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
364-559 |
1.73e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.63 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 364 EMLRSELEKI-KLEAQRYIAQLKSQVNAleGELEEQRKQKQKALVDNEQLRHELAQLRAAQLEGERSQGLREEaerkasa 442
Cdd:pfam05483 363 ELLRTEQQRLeKNEDQLKIITMELQKKS--SELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEE------- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 443 tearynkLKEKHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRESeLKLEEKSDQL----EKLK 518
Cdd:pfam05483 434 -------LKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKN-IELTAHCDKLllenKELT 505
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 733605517 519 RELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDAL 559
Cdd:pfam05483 506 QEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNL 546
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
366-600 |
1.83e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 366 LRSELEKIKleaqrYIAQLKSQVNALEGELEE-----QRKQKQKAlvDNEQLRHELAQ----LRAAQLEGERsqgLREEA 436
Cdd:PRK11281 41 VQAQLDALN-----KQKLLEAEDKLVQQDLEQtlallDKIDRQKE--ETEQLKQQLAQapakLRQAQAELEA---LKDDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 437 erkASATEARYNK--LKEKHSELVHVHAEL--LRKNADTAKQLTVTQQSQEEvaRVKEQLAfqvEQVKRESELKLEEKSD 512
Cdd:PRK11281 111 ---DEETRETLSTlsLRQLESRLAQTLDQLqnAQNDLAEYNSQLVSLQTQPE--RAQAALY---ANSQRLQQIRNLLKGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 513 QLEKlkRELEAKAGELARAQEAL--SHTEQSKSEL--SSRL-DTLSAEKDALSGAVRQREADLLAAQSLVRETEAALSRE 587
Cdd:PRK11281 183 KVGG--KALRPSQRVLLQAEQALlnAQNDLQRKSLegNTQLqDLLQKQRDYLTARIQRLEHQLQLLQEAINSKRLTLSEK 260
|
250
....*....|....*.
gi 733605517 588 ---QQRSSQEQGELQG 600
Cdd:PRK11281 261 tvqEAQSQDEAARIQA 276
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
399-596 |
1.98e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.35 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 399 RKQKQKALvdnEQLRHELAQLRA---AQLEGERSQG------LREEAERKASATEArynklkEKHSELVHVHAELLRKNA 469
Cdd:NF041483 519 RRQAEETL---ERTRAEAERLRAeaeEQAEEVRAAAeraareLREETERAIAARQA------EAAEELTRLHTEAEERLT 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 470 DTAKQLTvtqQSQEEVARVKEQLAFQVEQVKRESELKL----EEKSDQLEKLKRELEAKAGElARAQ----------EAL 535
Cdd:NF041483 590 AAEEALA---DARAEAERIRREAAEETERLRTEAAERIrtlqAQAEQEAERLRTEAAADASA-ARAEgenvavrlrsEAA 665
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 733605517 536 SHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQS-----LVRETEAALSREQQRSSQEQG 596
Cdd:NF041483 666 AEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAQeeaarRRREAEETLGSARAEADQERE 731
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
351-567 |
2.18e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.25 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 351 DRDLQIESLKREVEMLRSELEKIKLEAQRYIAQLKSQVNALEGELEEQRKQKQKalvdneQLRHELAQLRAAQLEGERSQ 430
Cdd:pfam05483 187 DLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEK------QVSLLLIQITEKENKMKDLT 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 431 GLREEAERKASATEARYN----KLKEKHSELVHVHAEL------LRKNADTAK--------------QLTVTQQSQ-EEV 485
Cdd:pfam05483 261 FLLEESRDKANQLEEKTKlqdeNLKELIEKKDHLTKELedikmsLQRSMSTQKaleedlqiatkticQLTEEKEAQmEEL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 486 ARVKEQLAFQV----------EQVKRESELKLEEKSDQLEKLKRELEAKAGELaraQEALSHTEQSKSELsSRLDTLSAE 555
Cdd:pfam05483 341 NKAKAAHSFVVtefeattcslEELLRTEQQRLEKNEDQLKIITMELQKKSSEL---EEMTKFKNNKEVEL-EELKKILAE 416
|
250
....*....|..
gi 733605517 556 KDALSGAVRQRE 567
Cdd:pfam05483 417 DEKLLDEKKQFE 428
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
357-470 |
2.35e-03 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 38.75 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 357 ESLKREVEMLRSELEKIKLEAQRYIAQLK---SQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRAAQLEgERSQGLR 433
Cdd:pfam09744 46 QEHNVELEELREDNEQLETQYEREKALRKraeEELEEIEDQWEQETKDLLSQVESLEEENRRLEADHVSRLE-EKEAELK 124
|
90 100 110
....*....|....*....|....*....|....*..
gi 733605517 434 EEaerkasatearYNKLKEKHSELVHVHAELLRKNAD 470
Cdd:pfam09744 125 KE-----------YSKLHERETEVLRKLKEVVDRQRD 150
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
475-570 |
2.41e-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: 40.52 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 475 LTVTQQSQEEVARVKEQLAFQVEQVKRESELKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSA 554
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90
....*....|....*.
gi 733605517 555 EKDALSGAVRQREADL 570
Cdd:COG4942 91 EIAELRAELEAQKEEL 106
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
382-606 |
2.78e-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: 40.72 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 382 AQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLraAQLEGERSQ---GLREEAERKASATEArynKLKEKHSELV 458
Cdd:TIGR00618 538 AQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSIL--TQCDNRSKEdipNLQNITVRLQDLTEK---LSEAEDMLAC 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 459 HVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQV----KRESELKLEEKSDQLEKLKR------ELEAKAGEL 528
Cdd:TIGR00618 613 EQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLtltqERVREHALSIRVLPKELLASrqlalqKMQSEKEQL 692
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 733605517 529 ARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAALSREQQRSSQEQGELQGRLAERV 606
Cdd:TIGR00618 693 TYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEV 770
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
352-595 |
2.84e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.81 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 352 RDLQIESLK-REVEMLRSELEKIKLEAQRYIAQLKSQVNALEG----ELEEQRKQKQ------KALVDN---EQL----R 413
Cdd:PRK10929 123 RQAQQEQDRaREISDSLSQLPQQQTEARRQLNEIERRLQTLGTpntpLAQAQLTALQaesaalKALVDElelAQLsannR 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 414 HELAQLRA-----------AQLEGERSQgLREEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTvtQQSQ 482
Cdd:PRK10929 203 QELARLRSelakkrsqqldAYLQALRNQ-LNSQRQREAERALESTELLAEQSGDLPKSIVAQFKINRELSQALN--QQAQ 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 483 E--EVARVKEQLAFQVEQVkRESELKLEEKSDQLEklkrelEAKA-GELARAQEAlSHTEQSKSElssRLDTLSAEKDal 559
Cdd:PRK10929 280 RmdLIASQQRQAASQTLQV-RQALNTLREQSQWLG------VSNAlGEALRAQVA-RLPEMPKPQ---QLDTEMAQLR-- 346
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 733605517 560 sgAVRQREADLLAAQSLVRETEAA----LSREQQRSSQEQ 595
Cdd:PRK10929 347 --VQRLRYEDLLNKQPQLRQIRQAdgqpLTAEQNRILDAQ 384
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
361-457 |
2.90e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 361 REVEMLRSELEKIKLEAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRA--AQLEG--ERSQGLREEA 436
Cdd:PRK09039 91 SAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRqlAALEAalDASEKRDRES 170
|
90 100
....*....|....*....|..
gi 733605517 437 ERKASATEARYN-KLKEKHSEL 457
Cdd:PRK09039 171 QAKIADLGRRLNvALAQRVQEL 192
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
482-602 |
3.20e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.00 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 482 QEEVARVKEQLAFQVEQVKRESELK--LEEKSDQLEKLKRELEA-KAGELARAQEALSHTEQSKSELSSRLDTLSAEKDA 558
Cdd:smart00787 157 KEDYKLLMKELELLNSIKPKLRDRKdaLEEELRQLKQLEDELEDcDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQE 236
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 733605517 559 LSGAVRQREADLLAAQSLVRETEAALSREQQRSSQEQGELQGRL 602
Cdd:smart00787 237 LESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKLKEQL 280
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
355-501 |
3.54e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 355 QIESLKREVEMLRSELEKIKLEaqryIAQLKSQVNAL-------EGELEEQR------KQKQKALVDNEQLR---HELAQ 418
Cdd:COG1579 25 RLKELPAELAELEDELAALEAR----LEAAKTELEDLekeikrlELEIEEVEarikkyEEQLGNVRNNKEYEalqKEIES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 419 LRAAQLEGE----RSQGLREEAERKASATEARYNKLKEkhsELVHVHAELLRKNADTAKQL-TVTQQSQEEVARVKEQLA 493
Cdd:COG1579 101 LKRRISDLEdeilELMERIEELEEELAELEAELAELEA---ELEEKKAELDEELAELEAELeELEAEREELAAKIPPELL 177
|
....*...
gi 733605517 494 FQVEQVKR 501
Cdd:COG1579 178 ALYERIRK 185
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
373-567 |
4.23e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.08 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 373 IKLEAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHEL-AQLRAAQLEGERSQGLREEAERKASATEARYNKLK 451
Cdd:PRK12705 22 VVLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERnQQRQEARREREELQREEERLVQKEEQLDARAEKLD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 452 EKHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRESELKlEEKSDQLEKLKRELEAKAGELAR- 530
Cdd:PRK12705 102 NLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELE-EEKAQRVKKIEEEADLEAERKAQn 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 733605517 531 --AQEALSHTEQSKSELSsrLDTLSAEKDALSGAVRQRE 567
Cdd:PRK12705 181 ilAQAMQRIASETASDLS--VSVVPIPSDAMKGRIIGRE 217
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
346-453 |
4.52e-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: 39.75 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 346 GSVKDDRDLQIESLKR---EVEMLRSELEKIKLEAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLR-- 420
Cdd:COG4942 142 KYLAPARREQAEELRAdlaELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQqe 221
|
90 100 110
....*....|....*....|....*....|...
gi 733605517 421 AAQLEGERSQGLREEAERKASATEARYNKLKEK 453
Cdd:COG4942 222 AEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
393-555 |
4.79e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 40.12 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 393 GELEEQRKQKQKALVDNEQLRHELAQLRAAQLEgersQGLREEAERKASATEARYNKLKEKHSELVHVH---AELLRKNA 469
Cdd:pfam07111 59 QALSQQAELISRQLQELRRLEEEVRLLRETSLQ----QKMRLEAQAMELDALAVAEKAGQAEAEGLRAAlagAEMVRKNL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 470 DTAKQltvtqQSQEEVARVKEQLAFQVEQVKRESELKLEEKSDQLEKLKRELEAK-AGELARAQEALSHTEQSKSELSSR 548
Cdd:pfam07111 135 EEGSQ-----RELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKrAGEAKQLAEAQKEAELLRKQLSKT 209
|
....*..
gi 733605517 549 LDTLSAE 555
Cdd:pfam07111 210 QEELEAQ 216
|
|
| PRK13428 |
PRK13428 |
F0F1 ATP synthase subunit delta; Provisional |
419-606 |
5.36e-03 |
|
F0F1 ATP synthase subunit delta; Provisional
Pssm-ID: 184048 [Multi-domain] Cd Length: 445 Bit Score: 39.72 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 419 LRAAQLEGERSQ--GLREEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTvtQQSQEEVARVKEQLAFQV 496
Cdd:PRK13428 29 LMAARQDTVRQQlaESATAADRLAEADQAHTKAVEDAKAEAARVVEEAREDAERIAEQLR--AQADAEAERIKVQGARQV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 497 E----QVKRESELKL-EEKSDQLEKLKR------------------ELEAKAGELARAQEALSHTEQSKS-----ELSSR 548
Cdd:PRK13428 107 QllraQLTRQLRLELgHESVRQAGELVRnhvadpaqqsatvdrfldELDAMAPSTADVDYPLLAKMRSASrralaSLVDR 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 549 LDTL--SAEKDALSGAvrqreADLLAAQSLVRETEAALSREQQRSSqEQGELQGRLAERV 606
Cdd:PRK13428 187 FDSVaaDLDNQALTTL-----ADELVSVAKLLDREPVLTKHLTEPA-EDAAPKIRLVERL 240
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
352-520 |
6.44e-03 |
|
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: 39.55 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 352 RDLQIESLKREVEMlRSELEkikLEAQRYIAQLKSQVNALEGELEEQRKQKQKalvdnEQLRHELAQLRAAQLEGERSQG 431
Cdd:pfam15709 361 RRLQQEQLERAEKM-REELE---LEQQRRFEEIRLRKQRLEEERQRQEEEERK-----QRLQLQAAQERARQQQEEFRRK 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 432 LREEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQ--LTVTQQSQEEVARVKEQLAFQVEQVKRESELKLEE 509
Cdd:pfam15709 432 LQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEerLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEE 511
|
170
....*....|.
gi 733605517 510 KSDQLEKLKRE 520
Cdd:pfam15709 512 AMKQAQEQARQ 522
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
434-607 |
6.92e-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: 39.57 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 434 EEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTVTQQSQeevarvkeqlafQVEQVKRESELKLEEKSDQ 513
Cdd:TIGR00618 190 KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQT------------QQSHAYLTQKREAQEEQLK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 514 LEKLKRELEAKAGELaRAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAALSREQQRSSQ 593
Cdd:TIGR00618 258 KQQLLKQLRARIEEL-RAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ 336
|
170
....*....|....
gi 733605517 594 EQGELQGRLAERVW 607
Cdd:TIGR00618 337 QSSIEEQRRLLQTL 350
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
495-567 |
7.22e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 39.66 E-value: 7.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 733605517 495 QVEQVKRESELKLEE----KSDQLEKLKRELEAKAgelaraqealshteqskSELSSRLDTLSAEKDALSGAVRQRE 567
Cdd:pfam05911 60 QLRNVKEEQEQKIHDvvlkKTKEWEKIKAELEAKL-----------------VETEQELLRAAAENDALSRSLQERE 119
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
352-559 |
7.23e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 352 RDLQIESLKREVEMLRSELEKIkleaqryIAQLKSQVNALEG--------------------------ELEEQRKQKQKA 405
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKE-------IKELKKAIEELKKakgkcpvcgrelteehrkelleeytaELKRIEKELKEI 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 406 LVDNEQLRHELAQLRAAQLEGERSQGLREEAER--------------KASATEARYNKLKEKHSEL---VHVHAELLRKN 468
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKKESELIKLKELAEQlkeleeklkkynleELEKKAEEYEKLKEKLIKLkgeIKSLKKELEKL 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 469 ADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRESELKLEEKSDQLEKL----------KRELEAKAGELARAQEALSHT 538
Cdd:PRK03918 552 EELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFyneylelkdaEKELEREEKELKKLEEELDKA 631
|
250 260
....*....|....*....|.
gi 733605517 539 EQSKSELSSRLDTLSAEKDAL 559
Cdd:PRK03918 632 FEELAETEKRLEELRKELEEL 652
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
339-458 |
7.75e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 37.60 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 339 QTFGPPNGSVKDDRDLQIESLKREVEMLRSELEkiklEAQRYIAQLKSQVNALEGELEEQRK---QKQKALvdnEQLRHE 415
Cdd:pfam08614 35 PSTSSSKLSKASPQSASIQSLEQLLAQLREELA----ELYRSRGELAQRLVDLNEELQELEKklrEDERRL---AALEAE 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 733605517 416 LAQL------RAAQLEGER--SQGLREEAER---KASATEARYNKLKEKHSELV 458
Cdd:pfam08614 108 RAQLeeklkdREEELREKRklNQDLQDELVAlqlQLNMAEEKLRKLEKENRELV 161
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
355-599 |
8.38e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.26 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 355 QIESLKREVEMLRSELEKI--KLEAQRYIAQLKsqvnalEGELEEQRKQKQKALVDNEQLRHELAQLRAAQLEGERSQGL 432
Cdd:TIGR00606 710 KLKSTESELKKKEKRRDEMlgLAPGRQSIIDLK------EKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEES 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 433 REEAERKASATEARYNKLKEKHSELVHVHAELLRKNADtakqLTVTQQSQEevarvKEQLAFQVEQVKRESELKLEEKSD 512
Cdd:TIGR00606 784 AKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLD----RTVQQVNQE-----KQEKQHELDTVVSKIELNRKLIQD 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 513 QLEKLKrELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQ-READLLAAQSL---VRETEAALSREQ 588
Cdd:TIGR00606 855 QQEQIQ-HLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDaKEQDSPLETFLekdQQEKEELISSKE 933
|
250
....*....|.
gi 733605517 589 QRSSQEQGELQ 599
Cdd:TIGR00606 934 TSNKKAQDKVN 944
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
345-592 |
8.70e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 39.32 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 345 NGSVKDDRDL-QIESLKREVEMLRSELEKIKLEAQRYIAQL-----KSQVNALEGELEEQRKQKQKALVDN------EQL 412
Cdd:pfam05483 524 NCKKQEERMLkQIENLEEKEMNLRDELESVREEFIQKGDEVkckldKSEENARSIEYEVLKKEKQMKILENkcnnlkKQI 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 413 RHELAQLRAAQLEGERSQGLREEAERKASATEARYNKL-------KEKHSELVHVHAELLRKNADTAKQLtvTQQSQEEV 485
Cdd:pfam05483 604 ENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLelelasaKQKFEEIIDNYQKEIEDKKISEEKL--LEEVEKAK 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 486 ARVKEQLAFQVEQVKReSELKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDT-LSAEKDALSGAVR 564
Cdd:pfam05483 682 AIADEAVKLQKEIDKR-CQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIeLSNIKAELLSLKK 760
|
250 260
....*....|....*....|....*...
gi 733605517 565 QREADllaaqslvRETEAALSREQQRSS 592
Cdd:pfam05483 761 QLEIE--------KEEKEKLKMEAKENT 780
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
359-556 |
8.80e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 38.12 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 359 LKREVEMLRSELEKikleAQRYIAQLKSQVNALEGELEEQRKQKQKalvdneqlRHELAQlraAQLEGERSQGLREEAER 438
Cdd:pfam04012 27 LEQAIRDMQSELVK----ARQALAQTIARQKQLERRLEQQTEQAKK--------LEEKAQ---AALTKGNEELAREALAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 439 KASATearyNKLKEKHSEL--VHVHAELLRKN-ADTAKQLTVTQQSQEEVArVKEQLAFQVEQVKRES-ELKLEEKSDQL 514
Cdd:pfam04012 92 KKSLE----KQAEALETQLaqQRSAVEQLRKQlAALETKIQQLKAKKNLLK-ARLKAAKAQEAVQTSLgSLSTSSATDSF 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 733605517 515 EKLK-----RELEAKA-GELARAQEALSHTEQSKSELSSRLDTLSAEK 556
Cdd:pfam04012 167 ERIEekieeREARADAaAELASAVDLDAKLEQAGIQMEVSEDVLARLK 214
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
511-605 |
9.07e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.73 E-value: 9.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 511 SDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAALSREQQR 590
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90
....*....|....*
gi 733605517 591 SSQEQGELQGRLAER 605
Cdd:COG4372 110 AEELQEELEELQKER 124
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
474-604 |
9.29e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.23 E-value: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 474 QLTVTQQSQEEVARVKEQLA-----FQVEQVKRESELKLEEKSDQLEKLKRELEAKAGELA--RAQEALSHTEQSKSELS 546
Cdd:COG3206 139 EISYTSPDPELAAAVANALAeayleQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLL 218
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 733605517 547 SRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAALSREQQrsSQEQGELQGRLAE 604
Cdd:COG3206 219 QQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ--SPVIQQLRAQLAE 274
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
355-523 |
9.86e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 9.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 355 QIESLKREVEMLRSELEKIKLEAQRY-----IAQLKSQVNALEGELEEQRKQKQkalvDNEQLRHELAQLRAAQLEGERS 429
Cdd:COG4717 103 ELEELEAELEELREELEKLEKLLQLLplyqeLEALEAELAELPERLEELEERLE----ELRELEEELEELEAELAELQEE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 430 qgLREEAERKASATEARYNKLKEKHSElvhvhaelLRKNADTAKQLtvTQQSQEEVARVKEQLAfqveqvKRESELKLEE 509
Cdd:COG4717 179 --LEELLEQLSLATEEELQDLAEELEE--------LQQRLAELEEE--LEEAQEELEELEEELE------QLENELEAAA 240
|
170
....*....|....
gi 733605517 510 KSDQLEKLKRELEA 523
Cdd:COG4717 241 LEERLKEARLLLLI 254
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
349-542 |
9.89e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.99 E-value: 9.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 349 KDDRDLQIESLKREVEMLRselEKIKLEAQRYIAQLKSqvnalegELEEQRKQKQKALVDNEQlrhELAQlraaqleger 428
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIK---KEALLEAKEEIHKLRN-------EFEKELRERRNELQKLEK---RLLQ---------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 429 sqglREEA-ERKASATEARYNKLKEKHSELVHVHAELlrknadtakqltvtQQSQEEVARVKEQlafQVEQVKRESELKL 507
Cdd:PRK12704 94 ----KEENlDRKLELLEKREEELEKKEKELEQKQQEL--------------EKKEEELEELIEE---QLQELERISGLTA 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 733605517 508 EE-KSDQLEKLKRELEAKAGELARAQEALSHTEQSK 542
Cdd:PRK12704 153 EEaKEILLEKVEEEARHEAAVLIKEIEEEAKEEADK 188
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
511-595 |
9.96e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 38.41 E-value: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 511 SDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSA-------EKDALSGAVRQREADLLAAQSLVRETEAA 583
Cdd:PRK09039 45 SREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRAslsaaeaERSRLQALLAELAGAGAAAEGRAGELAQE 124
|
90
....*....|..
gi 733605517 584 LSREQQRSSQEQ 595
Cdd:PRK09039 125 LDSEKQVSARAL 136
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
483-580 |
9.98e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 38.91 E-value: 9.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733605517 483 EEVARVKEQLAFQVEQVKRESELKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGA 562
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKE 493
|
90
....*....|....*...
gi 733605517 563 VRQREADLLAAQSLVRET 580
Cdd:COG0542 494 LAELEEELAELAPLLREE 511
|
|
| |
