|
Name |
Accession |
Description |
Interval |
E-value |
| OLF |
smart00284 |
Olfactomedin-like domains; |
201-451 |
3.82e-156 |
|
Olfactomedin-like domains;
Pssm-ID: 128580 Cd Length: 255 Bit Score: 442.73 E-value: 3.82e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 201 GKLTGISDPVTVKTSG-SRFGSWMTDPLAPEG-DNRVWYMDGY-HNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQV 277
Cdd:smart00284 1 GGLAGISKPVTLQTSWkGKSGAWMKDPLWNTTkKSLYWYMPLNtRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGTGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 278 VYNGSIYFNKFQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDESGLWAVYATNQNAGNIVVSRLDP 357
Cdd:smart00284 81 VYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 358 VSLQTLQTWNTSYPKRSAGEAFIICGTLYVTN-GYSGGTKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYA 436
Cdd:smart00284 161 ATLTIENTWITTYNKRSASNAFMICGILYVTRsLGSKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPNDRKLYA 240
|
250
....*....|....*
gi 543871461 437 WNNGHQILYNVTLFH 451
Cdd:smart00284 241 WNNGHLVHYDIALKP 255
|
|
| OLF |
pfam02191 |
Olfactomedin-like domain; |
203-449 |
7.26e-137 |
|
Olfactomedin-like domain;
Pssm-ID: 460482 Cd Length: 246 Bit Score: 393.05 E-value: 7.26e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 203 LTGISDPVTVKTSGSRFGSWMTDPLAPEgdNRVWYMDGYHNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQVVYNGS 282
Cdd:pfam02191 1 LVSVSKPVTVKLSGGKYGAWMKDPLPPS--DKIYVTDRGTSGNTLREYASLDDFKNGSPSKKYKLPYPWQGTGHVVYNGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 283 IYFNKFQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDESGLWAVYATNQNAGNIVVSRLDPVSLQT 362
Cdd:pfam02191 79 LYYNKYNSRNIVKYDLTTRTVAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLDPETLEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 363 LQTWNTSYPKRSAGEAFIICGTLYVTNGYSGG-TKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYAWNNGH 441
Cdd:pfam02191 159 EQTWNTSYPKRSAGNAFMVCGVLYAVRSVNTRrEEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLYAWDDGY 238
|
....*...
gi 543871461 442 QILYNVTL 449
Cdd:pfam02191 239 QVTYPVTF 246
|
|
| Noelin-1 |
pfam12308 |
Neurogenesis glycoprotein; This domain family is found in eukaryotes, and is approximately 100 ... |
29-125 |
7.70e-54 |
|
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: 175.35 E-value: 7.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 29 PEESWQVYSSAQDSEGRCICTVVAPQQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESK 108
Cdd:pfam12308 3 PEEGWQVYSSAQDPDGRCVCTVVAPAQDVCSRDPRSRQLRQLMEKVQNVSQSMEVLDLRTSRDLQYVRTTETLLKTLDSK 82
|
90
....*....|....*..
gi 543871461 109 FKQVEESHKQHLARQFK 125
Cdd:pfam12308 83 LKVAEANPQSLSARSFQ 99
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
65-191 |
3.92e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 65 KQLRQLLEKVQNMSQSIEVLDRR----TQRDLQyVEKMENQMKGLESKFKQVEEshkqhlarQFKAIKAKMDELRPLIPV 140
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELkeeiEELEKE-LESLEGSKRKLEEKIRELEE--------RIEELKKEIEELEEKVKE 284
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 543871461 141 LEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAYdydelQSRVSNLEERL 191
Cdd:PRK03918 285 LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL-----EEEINGIEERI 330
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
65-208 |
1.78e-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: 50.24 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 65 KQLRQLLEKVQNMSQSIevldrRTQRDL--QYVEKMENQMKGLESKFKQVEE--SHKQHLA--RQFKAIKAKMDELRPLI 138
Cdd:pfam06160 121 EEVEELKDKYRELRKTL-----LANRFSygPAIDELEKQLAEIEEEFSQFEEltESGDYLEarEVLEKLEEETDALEELM 195
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 139 PVLEEYKADAKLVlqFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLACGKLTGISD 208
Cdd:pfam06160 196 EDIPPLYEELKTE--LPDQLEELKEGYREMEEEGYALEHLNVDKEIQQLEEQLEENLALLENLELDEAEE 263
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
61-193 |
2.59e-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: 48.38 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 61 DARTKQLRQLLEK----VQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVE---ESHKQHL-----ARQFKAIK 128
Cdd:COG1579 16 DSELDRLEHRLKElpaeLAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEariKKYEEQLgnvrnNKEYEALQ 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543871461 129 AKMDELRPLIPVLEEykadakLVLQFKEEVQNLTSVLNELQEEIgaydyDELQSRVSNLEERLRA 193
Cdd:COG1579 96 KEIESLKRRISDLED------EILELMERIEELEEELAELEAEL-----AELEAELEEKKAELDE 149
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
61-191 |
1.64e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 61 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQ-------MKGLESKFKQVE------ESHKQHLARQFKAI 127
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqilrerLANLERQLEELEaqleelESKLDELAEELAEL 342
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543871461 128 KAKMDELRplipvlEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAY--DYDELQ-------SRVSNLEERL 191
Cdd:TIGR02168 343 EEKLEELK------EELESLEAELEELEAELEELESRLEELEEQLETLrsKVAQLElqiaslnNEIERLEARL 409
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
61-189 |
1.11e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 61 DARTKQLRQLLEKVQNMsqsievldRRTQRDLQYVEKMENQMKGLESKFKQ--VEESHKQhlARQFKAIKAKMDELRPLI 138
Cdd:PRK03918 472 EEKERKLRKELRELEKV--------LKKESELIKLKELAEQLKELEEKLKKynLEELEKK--AEEYEKLKEKLIKLKGEI 541
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 543871461 139 PVL-------EEYKADAKLVLQFKEEVQN-LTSVLNELqEEIGAYDYDELQSRVSNLEE 189
Cdd:PRK03918 542 KSLkkeleklEELKKKLAELEKKLDELEEeLAELLKEL-EELGFESVEELEERLKELEP 599
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
208-393 |
1.78e-04 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 43.08 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 208 DPVT--VKTSGSRFGSWMTDpLAPEGDNRVWYMDGYhNNRFVReyksmVDfMNTDNFTSHRLPHPWSGTGQVVY--NGSI 283
Cdd:COG4257 44 DPATgeFTEYPLGGGSGPHG-IAVDPDGNLWFTDNG-NNRIGR-----ID-PKTGEITTFALPGGGSNPHGIAFdpDGNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 284 YFNKFQSHIIIRFDLKTETILKTRSldYAGYNNMYhyawgghsdiDLMVDESGlwAVYATNQNAGNIVvsRLDP----VS 359
Cdd:COG4257 116 WFTDQGGNRIGRLDPATGEVTEFPL--PTGGAGPY----------GIAVDPDG--NLWVTDFGANAIG--RIDPdtgtLT 179
|
170 180 190
....*....|....*....|....*....|....*
gi 543871461 360 LQTLQTwNTSYPKR-SAGEAfiicGTLYVTNGYSG 393
Cdd:COG4257 180 EYALPT-PGAGPRGlAVDPD----GNLWVADTGSG 209
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
61-171 |
2.63e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 61 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVEESHKQhLARQFKAIKAKMDELRPLIPV 140
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE-LQSEIAEREEELKELEEQLES 161
|
90 100 110
....*....|....*....|....*....|.
gi 543871461 141 LEEYKADAKLVLQfKEEVQNLTSVLNELQEE 171
Cdd:COG4372 162 LQEELAALEQELQ-ALSEAEAEQALDELLKE 191
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
66-199 |
3.30e-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: 38.97 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 66 QLRQLLEKVQNMSQSIEVLDRRtqrdLQYVEKMENQMKGLESKFKQVEESHKQHLARQFKAIKAKMDELRPLipvLEeyk 145
Cdd:cd00176 34 SVEALLKKHEALEAELAAHEER----VEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQR---LE--- 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 543871461 146 aDAKLVLQFKEEVQNLTSVLNELQEEIGAYDYD-------ELQSRVSNLEERLRACMQKLA 199
Cdd:cd00176 104 -EALDLQQFFRDADDLEQWLEEKEAALASEDLGkdlesveELLKKHKELEEELEAHEPRLK 163
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| OLF |
smart00284 |
Olfactomedin-like domains; |
201-451 |
3.82e-156 |
|
Olfactomedin-like domains;
Pssm-ID: 128580 Cd Length: 255 Bit Score: 442.73 E-value: 3.82e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 201 GKLTGISDPVTVKTSG-SRFGSWMTDPLAPEG-DNRVWYMDGY-HNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQV 277
Cdd:smart00284 1 GGLAGISKPVTLQTSWkGKSGAWMKDPLWNTTkKSLYWYMPLNtRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGTGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 278 VYNGSIYFNKFQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDESGLWAVYATNQNAGNIVVSRLDP 357
Cdd:smart00284 81 VYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 358 VSLQTLQTWNTSYPKRSAGEAFIICGTLYVTN-GYSGGTKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYA 436
Cdd:smart00284 161 ATLTIENTWITTYNKRSASNAFMICGILYVTRsLGSKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPNDRKLYA 240
|
250
....*....|....*
gi 543871461 437 WNNGHQILYNVTLFH 451
Cdd:smart00284 241 WNNGHLVHYDIALKP 255
|
|
| OLF |
pfam02191 |
Olfactomedin-like domain; |
203-449 |
7.26e-137 |
|
Olfactomedin-like domain;
Pssm-ID: 460482 Cd Length: 246 Bit Score: 393.05 E-value: 7.26e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 203 LTGISDPVTVKTSGSRFGSWMTDPLAPEgdNRVWYMDGYHNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQVVYNGS 282
Cdd:pfam02191 1 LVSVSKPVTVKLSGGKYGAWMKDPLPPS--DKIYVTDRGTSGNTLREYASLDDFKNGSPSKKYKLPYPWQGTGHVVYNGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 283 IYFNKFQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDESGLWAVYATNQNAGNIVVSRLDPVSLQT 362
Cdd:pfam02191 79 LYYNKYNSRNIVKYDLTTRTVAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLDPETLEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 363 LQTWNTSYPKRSAGEAFIICGTLYVTNGYSGG-TKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYAWNNGH 441
Cdd:pfam02191 159 EQTWNTSYPKRSAGNAFMVCGVLYAVRSVNTRrEEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLYAWDDGY 238
|
....*...
gi 543871461 442 QILYNVTL 449
Cdd:pfam02191 239 QVTYPVTF 246
|
|
| Noelin-1 |
pfam12308 |
Neurogenesis glycoprotein; This domain family is found in eukaryotes, and is approximately 100 ... |
29-125 |
7.70e-54 |
|
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: 175.35 E-value: 7.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 29 PEESWQVYSSAQDSEGRCICTVVAPQQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESK 108
Cdd:pfam12308 3 PEEGWQVYSSAQDPDGRCVCTVVAPAQDVCSRDPRSRQLRQLMEKVQNVSQSMEVLDLRTSRDLQYVRTTETLLKTLDSK 82
|
90
....*....|....*..
gi 543871461 109 FKQVEESHKQHLARQFK 125
Cdd:pfam12308 83 LKVAEANPQSLSARSFQ 99
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
65-191 |
3.92e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 65 KQLRQLLEKVQNMSQSIEVLDRR----TQRDLQyVEKMENQMKGLESKFKQVEEshkqhlarQFKAIKAKMDELRPLIPV 140
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELkeeiEELEKE-LESLEGSKRKLEEKIRELEE--------RIEELKKEIEELEEKVKE 284
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 543871461 141 LEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAYdydelQSRVSNLEERL 191
Cdd:PRK03918 285 LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL-----EEEINGIEERI 330
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
65-208 |
1.78e-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: 50.24 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 65 KQLRQLLEKVQNMSQSIevldrRTQRDL--QYVEKMENQMKGLESKFKQVEE--SHKQHLA--RQFKAIKAKMDELRPLI 138
Cdd:pfam06160 121 EEVEELKDKYRELRKTL-----LANRFSygPAIDELEKQLAEIEEEFSQFEEltESGDYLEarEVLEKLEEETDALEELM 195
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 139 PVLEEYKADAKLVlqFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLACGKLTGISD 208
Cdd:pfam06160 196 EDIPPLYEELKTE--LPDQLEELKEGYREMEEEGYALEHLNVDKEIQQLEEQLEENLALLENLELDEAEE 263
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
61-134 |
2.21e-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: 2.21e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 543871461 61 DARTKQLRQLLEKVQNmsqSIEVLDRRTQRDLQYVEKMENQMKGlESKFKQVEESHKQHLARQFKAIKAKMDEL 134
Cdd:pfam01576 888 EARIAQLEEELEEEQS---NTELLNDRLRKSTLQVEQLTTELAA-ERSTSQKSESARQQLERQNKELKAKLQEM 957
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
61-193 |
2.59e-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: 48.38 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 61 DARTKQLRQLLEK----VQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVE---ESHKQHL-----ARQFKAIK 128
Cdd:COG1579 16 DSELDRLEHRLKElpaeLAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEariKKYEEQLgnvrnNKEYEALQ 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543871461 129 AKMDELRPLIPVLEEykadakLVLQFKEEVQNLTSVLNELQEEIgaydyDELQSRVSNLEERLRA 193
Cdd:COG1579 96 KEIESLKRRISDLED------EILELMERIEELEEELAELEAEL-----AELEAELEEKKAELDE 149
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
30-198 |
4.02e-06 |
|
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: 49.33 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 30 EESWQVYSSAQDSEGRCICTVVAPQ-QTMCSRDARTKQLRQLLEKVQNMSQSI--EVLDRRTQRDL---QYVEKmENQMK 103
Cdd:pfam05483 179 EETRQVYMDLNNNIEKMILAFEELRvQAENARLEMHFKLKEDHEKIQHLEEEYkkEINDKEKQVSLlliQITEK-ENKMK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 104 GL-----ESKFK--QVEESHK-------------QHLARQFKAIKAKMDELRPLIPVLEE-YKADAKLVLQFKEEVQnlt 162
Cdd:pfam05483 258 DLtflleESRDKanQLEEKTKlqdenlkeliekkDHLTKELEDIKMSLQRSMSTQKALEEdLQIATKTICQLTEEKE--- 334
|
170 180 190
....*....|....*....|....*....|....*...
gi 543871461 163 SVLNELQEEIGAYDY--DELQSRVSNLEERLRACMQKL 198
Cdd:pfam05483 335 AQMEELNKAKAAHSFvvTEFEATTCSLEELLRTEQQRL 372
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
54-199 |
5.74e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 54 QQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMEnQMKGLESKFKQVE--ESHKQHLARQFKAIKAKM 131
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-KLLQLLPLYQELEalEAELAELPERLEELEERL 155
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 543871461 132 DELRPLIPVLEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLA 199
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
54-198 |
1.48e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 54 QQTMCSRDARTKQLRQLLEKVQNMSQSIEvldrRTQRDLQY----VEKMENQMKGLESKFKQVEESHKQhLARQFKAIKA 129
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELE----QLEEELEQarseLEQLEEELEELNEQLQAAQAELAQ-AQEELESLQE 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 543871461 130 KMDELRPLIpvlEEYKADAKlvlQFKEEVQNLTSVLNELQEEIGAYDY--DELQSRVSNLEERLRACMQKL 198
Cdd:COG4372 109 EAEELQEEL---EELQKERQ---DLEQQRKQLEAQIAELQSEIAEREEelKELEEQLESLQEELAALEQEL 173
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
61-191 |
1.64e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 61 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQ-------MKGLESKFKQVE------ESHKQHLARQFKAI 127
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqilrerLANLERQLEELEaqleelESKLDELAEELAEL 342
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543871461 128 KAKMDELRplipvlEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAY--DYDELQ-------SRVSNLEERL 191
Cdd:TIGR02168 343 EEKLEELK------EELESLEAELEELEAELEELESRLEELEEQLETLrsKVAQLElqiaslnNEIERLEARL 409
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
59-192 |
2.04e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 59 SRDARTKQLRQLL-----EKV-QNMSQSIEVLDRRTQRDLQYVEKMENqmkgLESKFKQVEEShkqhLARQFKAIKAKMD 132
Cdd:PRK03918 143 SDESREKVVRQILglddyENAyKNLGEVIKEIKRRIERLEKFIKRTEN----IEELIKEKEKE----LEEVLREINEISS 214
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 133 ELRPLIPVLEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAydydeLQSRVSNLEERLR 192
Cdd:PRK03918 215 ELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRK-----LEEKIRELEERIE 269
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
61-199 |
2.71e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.37 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 61 DARTKQLRQLLEKVQNmsqsiEVLDRRTQrdlqY---VEKMENQMKGLESKFKQVEE-----------SHKQHLARQFKA 126
Cdd:PRK04778 139 REEVEQLKDLYRELRK-----SLLANRFS----FgpaLDELEKQLENLEEEFSQFVEltesgdyvearEILDQLEEELAA 209
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543871461 127 IKAKMDELRPLIpvleeykadAKLVLQFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLA 199
Cdd:PRK04778 210 LEQIMEEIPELL---------KELQTELPDQLQELKAGYRELVEEGYHLDHLDIEKEIQDLKEQIDENLALLE 273
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
67-198 |
3.38e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.43 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 67 LRQLLEKVQNMSQSIEVLDRrtQRDLqyvekMENQMKGLESKFKQVEESHKQHLARQFKAIKAKMDELRPLIPVLEEYKA 146
Cdd:PLN02939 245 LKAELIEVAETEERVFKLEK--ERSL-----LDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVE 317
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 543871461 147 DAKLVLQFKEEVQNLTSVLNELQEEIGAYDY-----DELQSRVSNLEERLRACMQKL 198
Cdd:PLN02939 318 KAALVLDQNQDLRDKVDKLEASLKEANVSKFssykvELLQQKLKLLEERLQASDHEI 374
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
61-189 |
1.11e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 61 DARTKQLRQLLEKVQNMsqsievldRRTQRDLQYVEKMENQMKGLESKFKQ--VEESHKQhlARQFKAIKAKMDELRPLI 138
Cdd:PRK03918 472 EEKERKLRKELRELEKV--------LKKESELIKLKELAEQLKELEEKLKKynLEELEKK--AEEYEKLKEKLIKLKGEI 541
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 543871461 139 PVL-------EEYKADAKLVLQFKEEVQN-LTSVLNELqEEIGAYDYDELQSRVSNLEE 189
Cdd:PRK03918 542 KSLkkeleklEELKKKLAELEKKLDELEEeLAELLKEL-EELGFESVEELEERLKELEP 599
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
60-198 |
1.50e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 60 RDARTKQLRQLLEKVQNMSQSIEVLDRRtqrdLQYVEKMENQMKGLESKFKQV-------EESHKqhlarQFKAIKAKMD 132
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEER----IKELEEKEERLEELKKKLKELekrleelEERHE-----LYEEAKAKKE 372
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 543871461 133 ELRPLIPVLEEYKADaklvlQFKEEVQNLTSVLNELQEEIgaydyDELQSRVSNLE---ERLRACMQKL 198
Cdd:PRK03918 373 ELERLKKRLTGLTPE-----KLEKELEELEKAKEEIEEEI-----SKITARIGELKkeiKELKKAIEEL 431
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
208-393 |
1.78e-04 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 43.08 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 208 DPVT--VKTSGSRFGSWMTDpLAPEGDNRVWYMDGYhNNRFVReyksmVDfMNTDNFTSHRLPHPWSGTGQVVY--NGSI 283
Cdd:COG4257 44 DPATgeFTEYPLGGGSGPHG-IAVDPDGNLWFTDNG-NNRIGR-----ID-PKTGEITTFALPGGGSNPHGIAFdpDGNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 284 YFNKFQSHIIIRFDLKTETILKTRSldYAGYNNMYhyawgghsdiDLMVDESGlwAVYATNQNAGNIVvsRLDP----VS 359
Cdd:COG4257 116 WFTDQGGNRIGRLDPATGEVTEFPL--PTGGAGPY----------GIAVDPDG--NLWVTDFGANAIG--RIDPdtgtLT 179
|
170 180 190
....*....|....*....|....*....|....*
gi 543871461 360 LQTLQTwNTSYPKR-SAGEAfiicGTLYVTNGYSG 393
Cdd:COG4257 180 EYALPT-PGAGPRGlAVDPD----GNLWVADTGSG 209
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
68-193 |
1.82e-04 |
|
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: 43.86 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 68 RQLLEKVQnmsqSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVEESHKQhLARQFKAIKAKMDELrplipvLEEYKAD 147
Cdd:TIGR04523 363 RELEEKQN----EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ-KDEQIKKLQQEKELL------EKEIERL 431
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 543871461 148 AKLVLQFKEEVQNLTSVLNELQEEigaydYDELQSRVSNLEERLRA 193
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELI-----IKNLDNTRESLETQLKV 472
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
65-195 |
2.52e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.29 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 65 KQLRQLLEKVQNMSQSIEVLDrrtqrdlqyVEKMENQMKGLESK--------------FKQVEESHK------QHLARQF 124
Cdd:PRK04778 256 KEIQDLKEQIDENLALLEELD---------LDEAEEKNEEIQERidqlydilerevkaRKYVEKNSDtlpdflEHAKEQN 326
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 543871461 125 KAIKAKMDELRplipvlEEYK---ADAKLVLQFKEEVQNLTSVLNELQEEIGAYD--YDELQSRVSNLEERLRACM 195
Cdd:PRK04778 327 KELKEEIDRVK------QSYTlneSELESVRQLEKQLESLEKQYDEITERIAEQEiaYSELQEELEEILKQLEEIE 396
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
61-171 |
2.63e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 61 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVEESHKQhLARQFKAIKAKMDELRPLIPV 140
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE-LQSEIAEREEELKELEEQLES 161
|
90 100 110
....*....|....*....|....*....|.
gi 543871461 141 LEEYKADAKLVLQfKEEVQNLTSVLNELQEE 171
Cdd:COG4372 162 LQEELAALEQELQ-ALSEAEAEQALDELLKE 191
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
68-199 |
2.69e-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: 43.15 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 68 RQLLEKVQNMSQSIEVLDRRTQRDLQYVEK----MENQMKGLESKFKQVEESHKQHLARQfkaiKAKMDELR--PLIPVL 141
Cdd:pfam04108 20 RSLLEELVVLLAKIAFLRRGLSVQLANLEKvregLEKVLNELKKDFKQLLKDLDAALERL----EETLDKLRntPVEPAL 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 142 EEYKADAKLVLQF--KEEVQNLTSVLNELQEEIGAyDYDELQSRVSNLEERLRACMQKLA 199
Cdd:pfam04108 96 PPGEEKQKTLLDFidEDSVEILRDALKELIDELQA-AQESLDSDLKRFDDDLRDLQKELE 154
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
59-199 |
3.30e-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: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 59 SRDARTKQL--RQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKfkqVEESHKQHlarqfkaikakmDELRP 136
Cdd:TIGR02169 659 SRAPRGGILfsRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE---LSDASRKI------------GEIEK 723
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543871461 137 LIPVLEEYKAdaklvlQFKEEVQNLTSVLNELQEEIGAYD--YDELQSRVSNLEERLRACMQKLA 199
Cdd:TIGR02169 724 EIEQLEQEEE------KLKERLEELEEDLSSLEQEIENVKseLKELEARIEELEEDLHKLEEALN 782
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
61-197 |
3.62e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 61 DARTKQLRQLLE---KVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVEESHKQHLARQFKAIKAKMDELRPL 137
Cdd:COG4913 671 AELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 138 ipvLEEYKADAKLVLQFKEEVQNLTSvlnelqeeigayDYDELQSRVSNLEERLRACMQK 197
Cdd:COG4913 751 ---LEERFAAALGDAVERELRENLEE------------RIDALRARLNRAEEELERAMRA 795
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
52-194 |
5.11e-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: 42.85 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 52 APQQTMCSRDARTKQlrQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQvEESHKQHLARQFKAIKAKM 131
Cdd:pfam01576 57 AEAEEMRARLAARKQ--ELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE-EEAARQKLQLEKVTTEAKI 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 132 DELRPLIPVLEEykADAKLVLQFK---EEVQNLTSVLNElqEEIGAYDYDEL----QSRVSNLEERLRAC 194
Cdd:pfam01576 134 KKLEEDILLLED--QNSKLSKERKlleERISEFTSNLAE--EEEKAKSLSKLknkhEAMISDLEERLKKE 199
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
65-159 |
6.59e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 65 KQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVEESHKQHLAR-----QFKAIKAK---MDELRp 136
Cdd:PRK12704 86 KLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQElerisGLTAEEAKeilLEKVE- 164
|
90 100
....*....|....*....|....
gi 543871461 137 lipvlEEYKAD-AKLVLQFKEEVQ 159
Cdd:PRK12704 165 -----EEARHEaAVLIKEIEEEAK 183
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
66-199 |
6.76e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 66 QLRQLLEKVQNMSQSIEVLDRRTQRdlqYVEKMENQMKGLESKFKQVEEshkqhlarqfkaIKAKMDELRPLIPVLEEYK 145
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEE---RIEELKKEIEELEEKVKELKE------------LKEKAEEYIKLSEFYEEYL 306
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 543871461 146 adaKLVLQFKEEVQNLTSVLNELQEEIGayDYDELQSRVSNLEERLRACMQKLA 199
Cdd:PRK03918 307 ---DELREIEKRLSRLEEEINGIEERIK--ELEEKEERLEELKKKLKELEKRLE 355
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
64-199 |
1.21e-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: 41.31 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 64 TKQLRQLLEKVQNmSQsiEVLDRRTQRDLQY---VEKMENQMKGLESKFKQVEES------HKQHLARQFKAIKAKMDEL 134
Cdd:pfam01576 460 SKDVSSLESQLQD-TQ--ELLQEETRQKLNLstrLRQLEDERNSLQEQLEEEEEAkrnverQLSTLQAQLSDMKKKLEED 536
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543871461 135 RPLIPVLEEYKADAK-----LVLQFKE---EVQNLTSVLNELQEEIG--AYDYDELQSRVSNLEERLRACMQKLA 199
Cdd:pfam01576 537 AGTLEALEEGKKRLQreleaLTQQLEEkaaAYDKLEKTKNRLQQELDdlLVDLDHQRQLVSNLEKKQKKFDQMLA 611
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
65-189 |
1.36e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 65 KQLRQLLEKVQNMSQSIEVLDRRTQRD--LQYVeKMENqMKGLESKFKQVEESHKqhLARQFKAIKAKMDELRPLIPVLE 142
Cdd:COG4717 347 EELQELLREAEELEEELQLEELEQEIAalLAEA-GVED-EEELRAALEQAEEYQE--LKEELEELEEQLEELLGELEELL 422
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 543871461 143 EYKADAKL---VLQFKEEVQNLTSVLNELQEEIGaydydELQSRVSNLEE 189
Cdd:COG4717 423 EALDEEELeeeLEELEEELEELEEELEELREELA-----ELEAELEQLEE 467
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
62-191 |
2.97e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 62 ARTKQLRQLLEKVQNMSQSIEVLdrrtQRDLQYVEKMENQMKGLESKFKQVEES----HKQHLARQFKAIKAKMDELRPL 137
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGEIKSL----KKELEKLEELKKKLAELEKKLDELEEElaelLKELEELGFESVEELEERLKEL 597
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 543871461 138 IPVLEEY------------------KADAKLVLQFKE------EVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERL 191
Cdd:PRK03918 598 EPFYNEYlelkdaekelereekelkKLEEELDKAFEElaetekRLEELRKELEELEKKYSEEEYEELREEYLELSREL 675
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
66-199 |
3.30e-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: 38.97 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 66 QLRQLLEKVQNMSQSIEVLDRRtqrdLQYVEKMENQMKGLESKFKQVEESHKQHLARQFKAIKAKMDELRPLipvLEeyk 145
Cdd:cd00176 34 SVEALLKKHEALEAELAAHEER----VEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQR---LE--- 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 543871461 146 aDAKLVLQFKEEVQNLTSVLNELQEEIGAYDYD-------ELQSRVSNLEERLRACMQKLA 199
Cdd:cd00176 104 -EALDLQQFFRDADDLEQWLEEKEAALASEDLGkdlesveELLKKHKELEEELEAHEPRLK 163
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
67-199 |
5.16e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 67 LRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKmenQMKGLESKFKQVEEshkqhLARQFKAIKAKMDELRPLIPVLEEyka 146
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEE---RIKELEEKEERLEE-----LKKKLKELEKRLEELEERHELYEE--- 366
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 543871461 147 daklVLQFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLA 199
Cdd:PRK03918 367 ----AKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
59-191 |
5.27e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 38.74 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 59 SRDARTKQLRQLLEKVQNMSQSIEVLdrRTQRDlqyveKMENQMKGLESKfkqveeshKQHLARQFKAIKAKMDELRpli 138
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEEL--KEKRD-----ELNEELKELAEK--------RDELNAQVKELREEAQELR--- 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543871461 139 pvlEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAY------------DYDELQSRVSNLEERL 191
Cdd:COG1340 64 ---EKRDELNEKVKELKEERDELNEKLNELREELDELrkelaelnkaggSIDKLRKEIERLEWRQ 125
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
57-197 |
5.35e-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: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 57 MCSRDARTK-QLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKG--------LESKFKQVEE--SHKQHLARQFK 125
Cdd:TIGR00606 682 VCQRVFQTEaELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGlapgrqsiIDLKEKEIPElrNKLQKVNRDIQ 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 126 AIKAKMDE----LRPLIPVLEEYK---ADAKLVLQFKEEVQN----LTSVLNELQEEIGAYDYDELQSRVSNLEERLRAC 194
Cdd:TIGR00606 762 RLKNDIEEqetlLGTIMPEEESAKvclTDVTIMERFQMELKDverkIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTV 841
|
...
gi 543871461 195 MQK 197
Cdd:TIGR00606 842 VSK 844
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
68-199 |
5.49e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871461 68 RQLLEKVQNMSQSIEVLDRrTQRDlqyVEKMENQMKGLEskfkQVEESHkqhlaRQFKAIKAKMDELRPLIPVLEEYKAD 147
Cdd:COG4913 221 PDTFEAADALVEHFDDLER-AHEA---LEDAREQIELLE----PIRELA-----ERYAAARERLAELEYLRAALRLWFAQ 287
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 543871461 148 AKLVLQfKEEVQNLTSVLNELQEEIgaydyDELQSRVSNLEERLRACMQKLA 199
Cdd:COG4913 288 RRLELL-EAELEELRAELARLEAEL-----ERLEARLDALREELDELEAQIR 333
|
|
| |
