|
Name |
Accession |
Description |
Interval |
E-value |
| OLF |
smart00284 |
Olfactomedin-like domains; |
200-450 |
7.00e-157 |
|
Olfactomedin-like domains;
Pssm-ID: 128580 Cd Length: 255 Bit Score: 444.28 E-value: 7.00e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 200 GKLTGISDPVTVKTSG-SRFGSWMTDPLAPEG-DNRVWYMDGY-HNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQV 276
Cdd:smart00284 1 GGLAGISKPVTLQTSWkGKSGAWMKDPLWNTTkKSLYWYMPLNtRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGTGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 277 VYNGSIYFNKFQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDENGLWAVYATNQNAGNIVISKLDP 356
Cdd:smart00284 81 VYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 357 VSLQILQTWNTSYPKRSAGEAFIICGTLYVTN-GYSGGTKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYA 435
Cdd:smart00284 161 ATLTIENTWITTYNKRSASNAFMICGILYVTRsLGSKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPNDRKLYA 240
|
250
....*....|....*
gi 84370353 436 WNNGHQTLYNVTLFH 450
Cdd:smart00284 241 WNNGHLVHYDIALKP 255
|
|
| OLF |
pfam02191 |
Olfactomedin-like domain; |
202-448 |
5.22e-137 |
|
Olfactomedin-like domain;
Pssm-ID: 460482 Cd Length: 246 Bit Score: 393.44 E-value: 5.22e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 202 LTGISDPVTVKTSGSRFGSWMTDPLAPEgdNRVWYMDGYHNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQVVYNGS 281
Cdd:pfam02191 1 LVSVSKPVTVKLSGGKYGAWMKDPLPPS--DKIYVTDRGTSGNTLREYASLDDFKNGSPSKKYKLPYPWQGTGHVVYNGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 282 IYFNKFQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDENGLWAVYATNQNAGNIVISKLDPVSLQI 361
Cdd:pfam02191 79 LYYNKYNSRNIVKYDLTTRTVAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLDPETLEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 362 LQTWNTSYPKRSAGEAFIICGTLYVTNGYSGG-TKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYAWNNGH 440
Cdd:pfam02191 159 EQTWNTSYPKRSAGNAFMVCGVLYAVRSVNTRrEEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLYAWDDGY 238
|
....*...
gi 84370353 441 QTLYNVTL 448
Cdd:pfam02191 239 QVTYPVTF 246
|
|
| Noelin-1 |
pfam12308 |
Neurogenesis glycoprotein; This domain family is found in eukaryotes, and is approximately 100 ... |
28-124 |
2.23e-53 |
|
Neurogenesis glycoprotein; This domain family is found in eukaryotes, and is approximately 100 amino acids in length. The family is found in association with pfam02191. There are two conserved sequence motifs: SAQ and VQN. Noelin-1 is a glycoprotein which is secreted mainly by postmitotic neurogenic tissues in the developing central and peripheral nervous systems, first appearing after neural tube closure. It is likely that it forms large multimeric complexes.It has a divergent function in neurogenesis. In animal caps neuralized by expression of noggin, co-expression of Noelin-1 causes expression of neuronal differentiation markers several stages before neurogenesis normally occurs in this tissue. Finally, only secreted forms of the protein can activate sensory marker expression, while all forms of the protein can induce early neurogenesis.
Pssm-ID: 432468 [Multi-domain] Cd Length: 100 Bit Score: 174.19 E-value: 2.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 28 PEESWQVYSSAQDSEGRCICTVVAPQQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLETK 107
Cdd:pfam12308 3 PEEGWQVYSSAQDPDGRCVCTVVAPAQDVCSRDPRSRQLRQLMEKVQNVSQSMEVLDLRTSRDLQYVRTTETLLKTLDSK 82
|
90
....*....|....*..
gi 84370353 108 FKQVEESHKQHLARQFK 124
Cdd:pfam12308 83 LKVAEANPQSLSARSFQ 99
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
64-190 |
3.74e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 64 KQLRQLLEKVQNMSQSIEVLDRR----TQRDLQyVEKMENQMKGLETKFKQVEEshkqhlarQFKAIKAKMDELRPLIPV 139
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELkeeiEELEKE-LESLEGSKRKLEEKIRELEE--------RIEELKKEIEELEEKVKE 284
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 84370353 140 LEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAYdydelQSRVSNLEERL 190
Cdd:PRK03918 285 LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL-----EEEINGIEERI 330
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
60-192 |
3.62e-06 |
|
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: 48.00 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 60 DARTKQLRQLLEK----VQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLETKFKQVE---ESHKQHL-----ARQFKAIK 127
Cdd:COG1579 16 DSELDRLEHRLKElpaeLAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEariKKYEEQLgnvrnNKEYEALQ 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 84370353 128 AKMDELRPLIPVLEEykadakLVLQFKEEVQNLTSVLNELQEEIgaydyDELQSRVSNLEERLRA 192
Cdd:COG1579 96 KEIESLKRRISDLED------EILELMERIEELEEELAELEAEL-----AELEAELEEKKAELDE 149
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
64-207 |
5.08e-06 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 48.70 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 64 KQLRQLLEKVQNMSQSIevldrRTQRDL--QYVEKMENQMKGLETKFKQVEE--SHKQHLA--RQFKAIKAKMDELRPLI 137
Cdd:pfam06160 121 EEVEELKDKYRELRKTL-----LANRFSygPAIDELEKQLAEIEEEFSQFEEltESGDYLEarEVLEKLEEETDALEELM 195
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 138 PVLEEYKADAKLVlqFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLACGKLTGISD 207
Cdd:pfam06160 196 EDIPPLYEELKTE--LPDQLEELKEGYREMEEEGYALEHLNVDKEIQQLEEQLEENLALLENLELDEAEE 263
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
60-190 |
1.23e-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: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 60 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQ-------MKGLETKFKQVE------ESHKQHLARQFKAI 126
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqilrerLANLERQLEELEaqleelESKLDELAEELAEL 342
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 84370353 127 KAKMDELRplipvlEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAY--DYDELQ-------SRVSNLEERL 190
Cdd:TIGR02168 343 EEKLEELK------EELESLEAELEELEAELEELESRLEELEEQLETLrsKVAQLElqiaslnNEIERLEARL 409
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
207-392 |
2.09e-04 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 43.08 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 207 DPVT--VKTSGSRFGSWMTDpLAPEGDNRVWYMDGYhNNRFVReyksmVDfMNTDNFTSHRLPHPWSGTGQVVY--NGSI 282
Cdd:COG4257 44 DPATgeFTEYPLGGGSGPHG-IAVDPDGNLWFTDNG-NNRIGR-----ID-PKTGEITTFALPGGGSNPHGIAFdpDGNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 283 YFNKFQSHIIIRFDLKTETILKTRSldYAGYNNMYhyawgghsdiDLMVDENGlwAVYATNQNAGNIVisKLDPVSLQI- 361
Cdd:COG4257 116 WFTDQGGNRIGRLDPATGEVTEFPL--PTGGAGPY----------GIAVDPDG--NLWVTDFGANAIG--RIDPDTGTLt 179
|
170 180 190
....*....|....*....|....*....|....*
gi 84370353 362 ---LQTwNTSYPKR-SAGEAfiicGTLYVTNGYSG 392
Cdd:COG4257 180 eyaLPT-PGAGPRGlAVDPD----GNLWVADTGSG 209
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
60-188 |
2.48e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 60 DARTKQLRQLLEKVQNMsqsievldRRTQRDLQYVEKMENQMKGLETKFKQ--VEESHKQhlARQFKAIKAKMDELRPLI 137
Cdd:PRK03918 472 EEKERKLRKELRELEKV--------LKKESELIKLKELAEQLKELEEKLKKynLEELEKK--AEEYEKLKEKLIKLKGEI 541
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 84370353 138 PVL-------EEYKADAKLVLQFKEEVQN-LTSVLNELqEEIGAYDYDELQSRVSNLEE 188
Cdd:PRK03918 542 KSLkkeleklEELKKKLAELEKKLDELEEeLAELLKEL-EELGFESVEELEERLKELEP 599
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
60-170 |
6.26e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 60 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLETKFKQVEESHKQhLARQFKAIKAKMDELRPLIPV 139
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE-LQSEIAEREEELKELEEQLES 161
|
90 100 110
....*....|....*....|....*....|.
gi 84370353 140 LEEYKADAKLVLQfKEEVQNLTSVLNELQEE 170
Cdd:COG4372 162 LQEELAALEQELQ-ALSEAEAEQALDELLKE 191
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| OLF |
smart00284 |
Olfactomedin-like domains; |
200-450 |
7.00e-157 |
|
Olfactomedin-like domains;
Pssm-ID: 128580 Cd Length: 255 Bit Score: 444.28 E-value: 7.00e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 200 GKLTGISDPVTVKTSG-SRFGSWMTDPLAPEG-DNRVWYMDGY-HNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQV 276
Cdd:smart00284 1 GGLAGISKPVTLQTSWkGKSGAWMKDPLWNTTkKSLYWYMPLNtRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGTGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 277 VYNGSIYFNKFQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDENGLWAVYATNQNAGNIVISKLDP 356
Cdd:smart00284 81 VYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 357 VSLQILQTWNTSYPKRSAGEAFIICGTLYVTN-GYSGGTKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYA 435
Cdd:smart00284 161 ATLTIENTWITTYNKRSASNAFMICGILYVTRsLGSKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPNDRKLYA 240
|
250
....*....|....*
gi 84370353 436 WNNGHQTLYNVTLFH 450
Cdd:smart00284 241 WNNGHLVHYDIALKP 255
|
|
| OLF |
pfam02191 |
Olfactomedin-like domain; |
202-448 |
5.22e-137 |
|
Olfactomedin-like domain;
Pssm-ID: 460482 Cd Length: 246 Bit Score: 393.44 E-value: 5.22e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 202 LTGISDPVTVKTSGSRFGSWMTDPLAPEgdNRVWYMDGYHNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQVVYNGS 281
Cdd:pfam02191 1 LVSVSKPVTVKLSGGKYGAWMKDPLPPS--DKIYVTDRGTSGNTLREYASLDDFKNGSPSKKYKLPYPWQGTGHVVYNGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 282 IYFNKFQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDENGLWAVYATNQNAGNIVISKLDPVSLQI 361
Cdd:pfam02191 79 LYYNKYNSRNIVKYDLTTRTVAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLDPETLEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 362 LQTWNTSYPKRSAGEAFIICGTLYVTNGYSGG-TKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYAWNNGH 440
Cdd:pfam02191 159 EQTWNTSYPKRSAGNAFMVCGVLYAVRSVNTRrEEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLYAWDDGY 238
|
....*...
gi 84370353 441 QTLYNVTL 448
Cdd:pfam02191 239 QVTYPVTF 246
|
|
| Noelin-1 |
pfam12308 |
Neurogenesis glycoprotein; This domain family is found in eukaryotes, and is approximately 100 ... |
28-124 |
2.23e-53 |
|
Neurogenesis glycoprotein; This domain family is found in eukaryotes, and is approximately 100 amino acids in length. The family is found in association with pfam02191. There are two conserved sequence motifs: SAQ and VQN. Noelin-1 is a glycoprotein which is secreted mainly by postmitotic neurogenic tissues in the developing central and peripheral nervous systems, first appearing after neural tube closure. It is likely that it forms large multimeric complexes.It has a divergent function in neurogenesis. In animal caps neuralized by expression of noggin, co-expression of Noelin-1 causes expression of neuronal differentiation markers several stages before neurogenesis normally occurs in this tissue. Finally, only secreted forms of the protein can activate sensory marker expression, while all forms of the protein can induce early neurogenesis.
Pssm-ID: 432468 [Multi-domain] Cd Length: 100 Bit Score: 174.19 E-value: 2.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 28 PEESWQVYSSAQDSEGRCICTVVAPQQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLETK 107
Cdd:pfam12308 3 PEEGWQVYSSAQDPDGRCVCTVVAPAQDVCSRDPRSRQLRQLMEKVQNVSQSMEVLDLRTSRDLQYVRTTETLLKTLDSK 82
|
90
....*....|....*..
gi 84370353 108 FKQVEESHKQHLARQFK 124
Cdd:pfam12308 83 LKVAEANPQSLSARSFQ 99
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
64-190 |
3.74e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 64 KQLRQLLEKVQNMSQSIEVLDRR----TQRDLQyVEKMENQMKGLETKFKQVEEshkqhlarQFKAIKAKMDELRPLIPV 139
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELkeeiEELEKE-LESLEGSKRKLEEKIRELEE--------RIEELKKEIEELEEKVKE 284
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 84370353 140 LEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAYdydelQSRVSNLEERL 190
Cdd:PRK03918 285 LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL-----EEEINGIEERI 330
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
60-133 |
2.59e-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: 50.17 E-value: 2.59e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 84370353 60 DARTKQLRQLLEKVQNmsqSIEVLDRRTQRDLQYVEKMENQMKGlETKFKQVEESHKQHLARQFKAIKAKMDEL 133
Cdd:pfam01576 888 EARIAQLEEELEEEQS---NTELLNDRLRKSTLQVEQLTTELAA-ERSTSQKSESARQQLERQNKELKAKLQEM 957
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
60-192 |
3.62e-06 |
|
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: 48.00 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 60 DARTKQLRQLLEK----VQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLETKFKQVE---ESHKQHL-----ARQFKAIK 127
Cdd:COG1579 16 DSELDRLEHRLKElpaeLAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEariKKYEEQLgnvrnNKEYEALQ 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 84370353 128 AKMDELRPLIPVLEEykadakLVLQFKEEVQNLTSVLNELQEEIgaydyDELQSRVSNLEERLRA 192
Cdd:COG1579 96 KEIESLKRRISDLED------EILELMERIEELEEELAELEAEL-----AELEAELEEKKAELDE 149
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
64-207 |
5.08e-06 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 48.70 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 64 KQLRQLLEKVQNMSQSIevldrRTQRDL--QYVEKMENQMKGLETKFKQVEE--SHKQHLA--RQFKAIKAKMDELRPLI 137
Cdd:pfam06160 121 EEVEELKDKYRELRKTL-----LANRFSygPAIDELEKQLAEIEEEFSQFEEltESGDYLEarEVLEKLEEETDALEELM 195
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 138 PVLEEYKADAKLVlqFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLACGKLTGISD 207
Cdd:pfam06160 196 EDIPPLYEELKTE--LPDQLEELKEGYREMEEEGYALEHLNVDKEIQQLEEQLEENLALLENLELDEAEE 263
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
53-198 |
6.74e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 53 QQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRR---TQRDLQYVEKMEnQMKGLETKFKQVEEsHKQHLARQFKAIKAK 129
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAEleeLREELEKLEKLL-QLLPLYQELEALEA-ELAELPERLEELEER 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 84370353 130 MDELRPLIPVLEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLA 198
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
64-197 |
8.67e-06 |
|
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: 46.84 E-value: 8.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 64 KQLRQLLEkVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLETKFKQVEESHKQhLARQFKAIKAKMDELRPLIpvlEEY 143
Cdd:COG1579 4 EDLRALLD-LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED-LEKEIKRLELEIEEVEARI---KKY 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 84370353 144 KADAKLVLQFKEevqnltsvLNELQEEIgaydyDELQSRVSNLEERLRACMQKL 197
Cdd:COG1579 79 EEQLGNVRNNKE--------YEALQKEI-----ESLKRRISDLEDEILELMERI 119
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
60-190 |
1.23e-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: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 60 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQ-------MKGLETKFKQVE------ESHKQHLARQFKAI 126
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqilrerLANLERQLEELEaqleelESKLDELAEELAEL 342
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 84370353 127 KAKMDELRplipvlEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAY--DYDELQ-------SRVSNLEERL 190
Cdd:TIGR02168 343 EEKLEELK------EELESLEAELEELEAELEELESRLEELEEQLETLrsKVAQLElqiaslnNEIERLEARL 409
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
29-197 |
1.82e-05 |
|
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: 47.41 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 29 EESWQVYSSAQDSEGRCICTVVAPQ-QTMCSRDARTKQLRQLLEKVQNMSQSI--EVLDRRTQRDL---QYVEKmENQMK 102
Cdd:pfam05483 179 EETRQVYMDLNNNIEKMILAFEELRvQAENARLEMHFKLKEDHEKIQHLEEEYkkEINDKEKQVSLlliQITEK-ENKMK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 103 GL-------ETKFKQVEESHK-------------QHLARQFKAIKAKMDELRPLIPVLEE-YKADAKLVLQFKEEVQnlt 161
Cdd:pfam05483 258 DLtflleesRDKANQLEEKTKlqdenlkeliekkDHLTKELEDIKMSLQRSMSTQKALEEdLQIATKTICQLTEEKE--- 334
|
170 180 190
....*....|....*....|....*....|....*...
gi 84370353 162 SVLNELQEEIGAYDY--DELQSRVSNLEERLRACMQKL 197
Cdd:pfam05483 335 AQMEELNKAKAAHSFvvTEFEATTCSLEELLRTEQQRL 372
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
58-191 |
2.01e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 58 SRDARTKQLRQLL-----EKV-QNMSQSIEVLDRRTQRDLQYVEKMENqmkgLETKFKQVEEShkqhLARQFKAIKAKMD 131
Cdd:PRK03918 143 SDESREKVVRQILglddyENAyKNLGEVIKEIKRRIERLEKFIKRTEN----IEELIKEKEKE----LEEVLREINEISS 214
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 132 ELRPLIPVLEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAydydeLQSRVSNLEERLR 191
Cdd:PRK03918 215 ELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRK-----LEEKIRELEERIE 269
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
53-197 |
3.69e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 53 QQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLETKFKQVEESHKQhLARQFKAIKAKMDE 132
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQ-AQEELESLQEEAEE 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84370353 133 LRPLIpvlEEYKADAKlvlQFKEEVQNLTSVLNELQEEIGAYDY--DELQSRVSNLEERLRACMQKL 197
Cdd:COG4372 113 LQEEL---EELQKERQ---DLEQQRKQLEAQIAELQSEIAEREEelKELEEQLESLQEELAALEQEL 173
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
60-198 |
8.95e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 8.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 60 DARTKQLRQLLEKVQNmsqsiEVLDRRTQrdlqY---VEKMENQMKGLETKFKQVEE-----------SHKQHLARQFKA 125
Cdd:PRK04778 139 REEVEQLKDLYRELRK-----SLLANRFS----FgpaLDELEKQLENLEEEFSQFVEltesgdyvearEILDQLEEELAA 209
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 84370353 126 IKAKMDELRPLIpvleeykadAKLVLQFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLA 198
Cdd:PRK04778 210 LEQIMEEIPELL---------KELQTELPDQLQELKAGYRELVEEGYHLDHLDIEKEIQDLKEQIDENLALLE 273
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
66-197 |
1.02e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.89 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 66 LRQLLEKVQNMSQSIEVLDRrtQRDLqyvekMENQMKGLETKFKQVEESHKQHLARQFKAIKAKMDELRPLIPVLEEYKA 145
Cdd:PLN02939 245 LKAELIEVAETEERVFKLEK--ERSL-----LDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVE 317
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 84370353 146 DAKLVLQFKEEVQNLTSVLNELQEEIGAYDY-----DELQSRVSNLEERLRACMQKL 197
Cdd:PLN02939 318 KAALVLDQNQDLRDKVDKLEASLKEANVSKFssykvELLQQKLKLLEERLQASDHEI 374
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
59-197 |
1.42e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 59 RDARTKQLRQLLEKVQNMSQSIEVLDRRtqrdLQYVEKMENQMKGLETKFKQV-------EESHKqhlarQFKAIKAKMD 131
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEER----IKELEEKEERLEELKKKLKELekrleelEERHE-----LYEEAKAKKE 372
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 84370353 132 ELRPLIPVLEEYKADaklvlQFKEEVQNLTSVLNELQEEIgaydyDELQSRVSNLE---ERLRACMQKL 197
Cdd:PRK03918 373 ELERLKKRLTGLTPE-----KLEKELEELEKAKEEIEEEI-----SKITARIGELKkeiKELKKAIEEL 431
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
207-392 |
2.09e-04 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 43.08 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 207 DPVT--VKTSGSRFGSWMTDpLAPEGDNRVWYMDGYhNNRFVReyksmVDfMNTDNFTSHRLPHPWSGTGQVVY--NGSI 282
Cdd:COG4257 44 DPATgeFTEYPLGGGSGPHG-IAVDPDGNLWFTDNG-NNRIGR-----ID-PKTGEITTFALPGGGSNPHGIAFdpDGNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 283 YFNKFQSHIIIRFDLKTETILKTRSldYAGYNNMYhyawgghsdiDLMVDENGlwAVYATNQNAGNIVisKLDPVSLQI- 361
Cdd:COG4257 116 WFTDQGGNRIGRLDPATGEVTEFPL--PTGGAGPY----------GIAVDPDG--NLWVTDFGANAIG--RIDPDTGTLt 179
|
170 180 190
....*....|....*....|....*....|....*
gi 84370353 362 ---LQTwNTSYPKR-SAGEAfiicGTLYVTNGYSG 392
Cdd:COG4257 180 eyaLPT-PGAGPRGlAVDPD----GNLWVADTGSG 209
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
60-188 |
2.48e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 60 DARTKQLRQLLEKVQNMsqsievldRRTQRDLQYVEKMENQMKGLETKFKQ--VEESHKQhlARQFKAIKAKMDELRPLI 137
Cdd:PRK03918 472 EEKERKLRKELRELEKV--------LKKESELIKLKELAEQLKELEEKLKKynLEELEKK--AEEYEKLKEKLIKLKGEI 541
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 84370353 138 PVL-------EEYKADAKLVLQFKEEVQN-LTSVLNELqEEIGAYDYDELQSRVSNLEE 188
Cdd:PRK03918 542 KSLkkeleklEELKKKLAELEKKLDELEEeLAELLKEL-EELGFESVEELEERLKELEP 599
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
60-196 |
3.07e-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: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 60 DARTKQLRQLLE---KVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLETKFKQVEESHKQHLARQFKAIKAKMDELRPL 136
Cdd:COG4913 671 AELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 137 ipvLEEYKADAKLVLQFKEEVQNLTSvlnelqeeigayDYDELQSRVSNLEERLRACMQK 196
Cdd:COG4913 751 ---LEERFAAALGDAVERELRENLEE------------RIDALRARLNRAEEELERAMRA 795
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
64-194 |
4.23e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.52 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 64 KQLRQLLEKVQNMSQSIEVLDrrtqrdlqyVEKMENQMKGLETK--------------FKQVEESHK------QHLARQF 123
Cdd:PRK04778 256 KEIQDLKEQIDENLALLEELD---------LDEAEEKNEEIQERidqlydilerevkaRKYVEKNSDtlpdflEHAKEQN 326
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 84370353 124 KAIKAKMDELRplipvlEEYK---ADAKLVLQFKEEVQNLTSVLNELQEEIGAYD--YDELQSRVSNLEERLRACM 194
Cdd:PRK04778 327 KELKEEIDRVK------QSYTlneSELESVRQLEKQLESLEKQYDEITERIAEQEiaYSELQEELEEILKQLEEIE 396
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
67-198 |
4.96e-04 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 41.99 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 67 RQLLEKVQNMSQSIEVLDRRTQRDLQYVEK----MENQMKGLETKFKQVEESHKQHLARQfkaiKAKMDELR--PLIPVL 140
Cdd:pfam04108 20 RSLLEELVVLLAKIAFLRRGLSVQLANLEKvregLEKVLNELKKDFKQLLKDLDAALERL----EETLDKLRntPVEPAL 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 141 EEYKADAKLVLQF--KEEVQNLTSVLNELQEEIGAyDYDELQSRVSNLEERLRACMQKLA 198
Cdd:pfam04108 96 PPGEEKQKTLLDFidEDSVEILRDALKELIDELQA-AQESLDSDLKRFDDDLRDLQKELE 154
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
60-170 |
6.26e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 60 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLETKFKQVEESHKQhLARQFKAIKAKMDELRPLIPV 139
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE-LQSEIAEREEELKELEEQLES 161
|
90 100 110
....*....|....*....|....*....|.
gi 84370353 140 LEEYKADAKLVLQfKEEVQNLTSVLNELQEE 170
Cdd:COG4372 162 LQEELAALEQELQ-ALSEAEAEQALDELLKE 191
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
64-158 |
7.95e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 64 KQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLETKFKQVEESHKQHLAR-----QFKAIKAK---MDELRp 135
Cdd:PRK12704 86 KLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQElerisGLTAEEAKeilLEKVE- 164
|
90 100
....*....|....*....|....
gi 84370353 136 lipvlEEYKAD-AKLVLQFKEEVQ 158
Cdd:PRK12704 165 -----EEARHEaAVLIKEIEEEAK 183
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
58-198 |
8.03e-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: 41.98 E-value: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 58 SRDARTKQL--RQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLetkFKQVEESHKQHlarqfkaikakmDELRP 135
Cdd:TIGR02169 659 SRAPRGGILfsRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDEL---SQELSDASRKI------------GEIEK 723
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 84370353 136 LIPVLEEYKAdaklvlQFKEEVQNLTSVLNELQEEIGAYD--YDELQSRVSNLEERLRACMQKLA 198
Cdd:TIGR02169 724 EIEQLEQEEE------KLKERLEELEEDLSSLEQEIENVKseLKELEARIEELEEDLHKLEEALN 782
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
51-193 |
1.04e-03 |
|
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: 41.70 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 51 APQQTMCSRDARTKQlrQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLETKFKQvEESHKQHLARQFKAIKAKM 130
Cdd:pfam01576 57 AEAEEMRARLAARKQ--ELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE-EEAARQKLQLEKVTTEAKI 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 131 DELRPLIPVLEEykADAKLVLQFK---EEVQNLTSVLNElqEEIGAYDYDEL----QSRVSNLEERLRAC 193
Cdd:pfam01576 134 KKLEEDILLLED--QNSKLSKERKlleERISEFTSNLAE--EEEKAKSLSKLknkhEAMISDLEERLKKE 199
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
67-192 |
1.17e-03 |
|
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: 41.54 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 67 RQLLEKVQnmsqSIEVLDRRTQRDLQYVEKMENQMKGLETKFKQVEESHKQhLARQFKAIKAKMDELrplipvLEEYKAD 146
Cdd:TIGR04523 363 RELEEKQN----EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ-KDEQIKKLQQEKELL------EKEIERL 431
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 84370353 147 AKLVLQFKEEVQNLTSVLNELQEEigaydYDELQSRVSNLEERLRA 192
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELI-----IKNLDNTRESLETQLKV 472
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
63-198 |
1.65e-03 |
|
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: 40.93 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 63 TKQLRQLLEKVQNmSQsiEVLDRRTQRDLQY---VEKMENQMKGLETKFKQVEES------HKQHLARQFKAIKAKMDEL 133
Cdd:pfam01576 460 SKDVSSLESQLQD-TQ--ELLQEETRQKLNLstrLRQLEDERNSLQEQLEEEEEAkrnverQLSTLQAQLSDMKKKLEED 536
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 84370353 134 RPLIPVLEEYKADAK-----LVLQFKE---EVQNLTSVLNELQEEIG--AYDYDELQSRVSNLEERLRACMQKLA 198
Cdd:pfam01576 537 AGTLEALEEGKKRLQreleaLTQQLEEkaaAYDKLEKTKNRLQQELDdlLVDLDHQRQLVSNLEKKQKKFDQMLA 611
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
67-198 |
4.05e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 67 RQLLEKVQNMSQSIEVLDRrTQRDlqyVEKMENQMKGLEtkfkQVEESHkqhlaRQFKAIKAKMDELRPLIPVLEEYKAD 146
Cdd:COG4913 221 PDTFEAADALVEHFDDLER-AHEA---LEDAREQIELLE----PIRELA-----ERYAAARERLAELEYLRAALRLWFAQ 287
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 84370353 147 AKLVLQfKEEVQNLTSVLNELQEEIgaydyDELQSRVSNLEERLRACMQKLA 198
Cdd:COG4913 288 RRLELL-EAELEELRAELARLEAEL-----ERLEARLDALREELDELEAQIR 333
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
64-188 |
4.06e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 64 KQLRQLLEKVQNMSQSIEVLDRRTQRD--LQYVeKMENqMKGLETKFKQVEESHKqhLARQFKAIKAKMDELRPLIPVLE 141
Cdd:COG4717 347 EELQELLREAEELEEELQLEELEQEIAalLAEA-GVED-EEELRAALEQAEEYQE--LKEELEELEEQLEELLGELEELL 422
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 84370353 142 EYKADAKL---VLQFKEEVQNLTSVLNELQEEIGaydydELQSRVSNLEE 188
Cdd:COG4717 423 EALDEEELeeeLEELEEELEELEEELEELREELA-----ELEAELEQLEE 467
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
61-190 |
5.32e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 61 ARTKQLRQLLEKVQNMSQSIEVLdrrtQRDLQYVEKMENQMKGLETKFKQVEES----HKQHLARQFKAIKAKMDELRPL 136
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGEIKSL----KKELEKLEELKKKLAELEKKLDELEEElaelLKELEELGFESVEELEERLKEL 597
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 84370353 137 IPVLEEY------------------KADAKLVLQFKE------EVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERL 190
Cdd:PRK03918 598 EPFYNEYlelkdaekelereekelkKLEEELDKAFEElaetekRLEELRKELEELEKKYSEEEYEELREEYLELSREL 675
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
56-196 |
6.28e-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: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 56 MCSRDARTK-QLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKG--------LETKFKQVEE--SHKQHLARQFK 124
Cdd:TIGR00606 682 VCQRVFQTEaELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGlapgrqsiIDLKEKEIPElrNKLQKVNRDIQ 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370353 125 AIKAKMDE----LRPLIPVLEEYK---ADAKLVLQFKEEVQN----LTSVLNELQEEIGAYDYDELQSRVSNLEERLRAC 193
Cdd:TIGR00606 762 RLKNDIEEqetlLGTIMPEEESAKvclTDVTIMERFQMELKDverkIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTV 841
|
...
gi 84370353 194 MQK 196
Cdd:TIGR00606 842 VSK 844
|
|
| |
