|
Name |
Accession |
Description |
Interval |
E-value |
| OLF |
smart00284 |
Olfactomedin-like domains; |
228-478 |
2.73e-154 |
|
Olfactomedin-like domains;
Pssm-ID: 128580 Cd Length: 255 Bit Score: 438.88 E-value: 2.73e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 228 GKLTGISDPVTVKTSG-SRFGSWMTDPLAPEG-DNRVWYMDGY-HNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQV 304
Cdd:smart00284 1 GGLAGISKPVTLQTSWkGKSGAWMKDPLWNTTkKSLYWYMPLNtRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGTGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 305 VYNGSIYFNKFQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDESGLWAVYATNQNAGNIVVSRLDP 384
Cdd:smart00284 81 VYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 385 VSLQTLQTWNTSYPKRSAGEAFIICGTLYVTN-GYSGGTKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYA 463
Cdd:smart00284 161 ATLTIENTWITTYNKRSASNAFMICGILYVTRsLGSKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPNDRKLYA 240
|
250
....*....|....*
gi 543871463 464 WNNGHQILYNVTLFH 478
Cdd:smart00284 241 WNNGHLVHYDIALKP 255
|
|
| OLF |
pfam02191 |
Olfactomedin-like domain; |
230-476 |
1.35e-135 |
|
Olfactomedin-like domain;
Pssm-ID: 460482 Cd Length: 246 Bit Score: 391.13 E-value: 1.35e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 230 LTGISDPVTVKTSGSRFGSWMTDPLAPEgdNRVWYMDGYHNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQVVYNGS 309
Cdd:pfam02191 1 LVSVSKPVTVKLSGGKYGAWMKDPLPPS--DKIYVTDRGTSGNTLREYASLDDFKNGSPSKKYKLPYPWQGTGHVVYNGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 310 IYFNKFQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDESGLWAVYATNQNAGNIVVSRLDPVSLQT 389
Cdd:pfam02191 79 LYYNKYNSRNIVKYDLTTRTVAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLDPETLEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 390 LQTWNTSYPKRSAGEAFIICGTLYVTNGYSGG-TKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYAWNNGH 468
Cdd:pfam02191 159 EQTWNTSYPKRSAGNAFMVCGVLYAVRSVNTRrEEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLYAWDDGY 238
|
....*...
gi 543871463 469 QILYNVTL 476
Cdd:pfam02191 239 QVTYPVTF 246
|
|
| Noelin-1 |
pfam12308 |
Neurogenesis glycoprotein; This domain family is found in eukaryotes, and is approximately 100 ... |
56-152 |
4.63e-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: 176.51 E-value: 4.63e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 56 PEESWQVYSSAQDSEGRCICTVVAPQQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESK 135
Cdd:pfam12308 3 PEEGWQVYSSAQDPDGRCVCTVVAPAQDVCSRDPRSRQLRQLMEKVQNVSQSMEVLDLRTSRDLQYVRTTETLLKTLDSK 82
|
90
....*....|....*..
gi 543871463 136 FKQVEESHKQHLARQFK 152
Cdd:pfam12308 83 LKVAEANPQSLSARSFQ 99
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
92-218 |
2.16e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 92 KQLRQLLEKVQNMSQSIEVLDRR----TQRDLQyVEKMENQMKGLESKFKQVEEshkqhlarQFKAIKAKMDELRPLIPV 167
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELkeeiEELEKE-LESLEGSKRKLEEKIRELEE--------RIEELKKEIEELEEKVKE 284
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 543871463 168 LEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAYdydelQSRVSNLEERL 218
Cdd:PRK03918 285 LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL-----EEEINGIEERI 330
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
92-235 |
9.50e-07 |
|
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: 51.39 E-value: 9.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 92 KQLRQLLEKVQNMSQSIevldrRTQRDL--QYVEKMENQMKGLESKFKQVEE--SHKQHLA--RQFKAIKAKMDELRPLI 165
Cdd:pfam06160 121 EEVEELKDKYRELRKTL-----LANRFSygPAIDELEKQLAEIEEEFSQFEEltESGDYLEarEVLEKLEEETDALEELM 195
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 166 PVLEEYKADAKLVlqFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLACGKLTGISD 235
Cdd:pfam06160 196 EDIPPLYEELKTE--LPDQLEELKEGYREMEEEGYALEHLNVDKEIQQLEEQLEENLALLENLELDEAEE 263
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
88-220 |
2.23e-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: 48.77 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 88 DARTKQLRQLLEK----VQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVE---ESHKQHL-----ARQFKAIK 155
Cdd:COG1579 16 DSELDRLEHRLKElpaeLAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEariKKYEEQLgnvrnNKEYEALQ 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543871463 156 AKMDELRPLIPVLEEykadakLVLQFKEEVQNLTSVLNELQEEIgaydyDELQSRVSNLEERLRA 220
Cdd:COG1579 96 KEIESLKRRISDLED------EILELMERIEELEEELAELEAEL-----AELEAELEEKKAELDE 149
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
88-218 |
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: 48.13 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 88 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQ-------MKGLESKFKQVE------ESHKQHLARQFKAI 154
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqilrerLANLERQLEELEaqleelESKLDELAEELAEL 342
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543871463 155 KAKMDELRplipvlEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAY--DYDELQ-------SRVSNLEERL 218
Cdd:TIGR02168 343 EEKLEELK------EELESLEAELEELEAELEELESRLEELEEQLETLrsKVAQLElqiaslnNEIERLEARL 409
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
88-216 |
6.13e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 88 DARTKQLRQLLEKVQNMsqsievldRRTQRDLQYVEKMENQMKGLESKFKQ--VEESHKQhlARQFKAIKAKMDELRPLI 165
Cdd:PRK03918 472 EEKERKLRKELRELEKV--------LKKESELIKLKELAEQLKELEEKLKKynLEELEKK--AEEYEKLKEKLIKLKGEI 541
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 543871463 166 PVL-------EEYKADAKLVLQFKEEVQN-LTSVLNELqEEIGAYDYDELQSRVSNLEE 216
Cdd:PRK03918 542 KSLkkeleklEELKKKLAELEKKLDELEEeLAELLKEL-EELGFESVEELEERLKELEP 599
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
88-198 |
1.01e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 88 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVEESHKQhLARQFKAIKAKMDELRPLIPV 167
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE-LQSEIAEREEELKELEEQLES 161
|
90 100 110
....*....|....*....|....*....|.
gi 543871463 168 LEEYKADAKLVLQfKEEVQNLTSVLNELQEE 198
Cdd:COG4372 162 LQEELAALEQELQ-ALSEAEAEQALDELLKE 191
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
235-420 |
1.93e-04 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 43.08 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 235 DPVT--VKTSGSRFGSWMTDpLAPEGDNRVWYMDGYhNNRFVReyksmVDfMNTDNFTSHRLPHPWSGTGQVVY--NGSI 310
Cdd:COG4257 44 DPATgeFTEYPLGGGSGPHG-IAVDPDGNLWFTDNG-NNRIGR-----ID-PKTGEITTFALPGGGSNPHGIAFdpDGNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 311 YFNKFQSHIIIRFDLKTETILKTRSldYAGYNNMYhyawgghsdiDLMVDESGlwAVYATNQNAGNIVvsRLDP----VS 386
Cdd:COG4257 116 WFTDQGGNRIGRLDPATGEVTEFPL--PTGGAGPY----------GIAVDPDG--NLWVTDFGANAIG--RIDPdtgtLT 179
|
170 180 190
....*....|....*....|....*....|....*
gi 543871463 387 LQTLQTwNTSYPKR-SAGEAfiicGTLYVTNGYSG 420
Cdd:COG4257 180 EYALPT-PGAGPRGlAVDPD----GNLWVADTGSG 209
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
93-226 |
1.60e-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: 39.74 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 93 QLRQLLEKVQNMSQSIEVLDRRtqrdLQYVEKMENQMKGLESKFKQVEESHKQHLARQFKAIKAKMDELRPLipvLEeyk 172
Cdd:cd00176 34 SVEALLKKHEALEAELAAHEER----VEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQR---LE--- 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 543871463 173 aDAKLVLQFKEEVQNLTSVLNELQEEIGAYDYD-------ELQSRVSNLEERLRACMQKLA 226
Cdd:cd00176 104 -EALDLQQFFRDADDLEQWLEEKEAALASEDLGkdlesveELLKKHKELEEELEAHEPRLK 163
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| OLF |
smart00284 |
Olfactomedin-like domains; |
228-478 |
2.73e-154 |
|
Olfactomedin-like domains;
Pssm-ID: 128580 Cd Length: 255 Bit Score: 438.88 E-value: 2.73e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 228 GKLTGISDPVTVKTSG-SRFGSWMTDPLAPEG-DNRVWYMDGY-HNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQV 304
Cdd:smart00284 1 GGLAGISKPVTLQTSWkGKSGAWMKDPLWNTTkKSLYWYMPLNtRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGTGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 305 VYNGSIYFNKFQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDESGLWAVYATNQNAGNIVVSRLDP 384
Cdd:smart00284 81 VYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 385 VSLQTLQTWNTSYPKRSAGEAFIICGTLYVTN-GYSGGTKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYA 463
Cdd:smart00284 161 ATLTIENTWITTYNKRSASNAFMICGILYVTRsLGSKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPNDRKLYA 240
|
250
....*....|....*
gi 543871463 464 WNNGHQILYNVTLFH 478
Cdd:smart00284 241 WNNGHLVHYDIALKP 255
|
|
| OLF |
pfam02191 |
Olfactomedin-like domain; |
230-476 |
1.35e-135 |
|
Olfactomedin-like domain;
Pssm-ID: 460482 Cd Length: 246 Bit Score: 391.13 E-value: 1.35e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 230 LTGISDPVTVKTSGSRFGSWMTDPLAPEgdNRVWYMDGYHNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQVVYNGS 309
Cdd:pfam02191 1 LVSVSKPVTVKLSGGKYGAWMKDPLPPS--DKIYVTDRGTSGNTLREYASLDDFKNGSPSKKYKLPYPWQGTGHVVYNGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 310 IYFNKFQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDESGLWAVYATNQNAGNIVVSRLDPVSLQT 389
Cdd:pfam02191 79 LYYNKYNSRNIVKYDLTTRTVAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLDPETLEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 390 LQTWNTSYPKRSAGEAFIICGTLYVTNGYSGG-TKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYAWNNGH 468
Cdd:pfam02191 159 EQTWNTSYPKRSAGNAFMVCGVLYAVRSVNTRrEEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLYAWDDGY 238
|
....*...
gi 543871463 469 QILYNVTL 476
Cdd:pfam02191 239 QVTYPVTF 246
|
|
| Noelin-1 |
pfam12308 |
Neurogenesis glycoprotein; This domain family is found in eukaryotes, and is approximately 100 ... |
56-152 |
4.63e-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: 176.51 E-value: 4.63e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 56 PEESWQVYSSAQDSEGRCICTVVAPQQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESK 135
Cdd:pfam12308 3 PEEGWQVYSSAQDPDGRCVCTVVAPAQDVCSRDPRSRQLRQLMEKVQNVSQSMEVLDLRTSRDLQYVRTTETLLKTLDSK 82
|
90
....*....|....*..
gi 543871463 136 FKQVEESHKQHLARQFK 152
Cdd:pfam12308 83 LKVAEANPQSLSARSFQ 99
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
92-218 |
2.16e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 92 KQLRQLLEKVQNMSQSIEVLDRR----TQRDLQyVEKMENQMKGLESKFKQVEEshkqhlarQFKAIKAKMDELRPLIPV 167
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELkeeiEELEKE-LESLEGSKRKLEEKIRELEE--------RIEELKKEIEELEEKVKE 284
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 543871463 168 LEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAYdydelQSRVSNLEERL 218
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 ... |
88-201 |
6.86e-07 |
|
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: 52.10 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 88 DARTKQLRQLLEKVQNmsqSIEVLDRRTQRDLQYVEKMENQMKGlESKFKQVEESHKQHLARQFKAIKAKMDEL------ 161
Cdd:pfam01576 888 EARIAQLEEELEEEQS---NTELLNDRLRKSTLQVEQLTTELAA-ERSTSQKSESARQQLERQNKELKAKLQEMegtvks 963
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 543871463 162 --RPLIPVLEeykadAKlVLQFKEEVQnltsvlNELQEEIGA 201
Cdd:pfam01576 964 kfKSSIAALE-----AK-IAQLEEQLE------QESRERQAA 993
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
92-235 |
9.50e-07 |
|
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: 51.39 E-value: 9.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 92 KQLRQLLEKVQNMSQSIevldrRTQRDL--QYVEKMENQMKGLESKFKQVEE--SHKQHLA--RQFKAIKAKMDELRPLI 165
Cdd:pfam06160 121 EEVEELKDKYRELRKTL-----LANRFSygPAIDELEKQLAEIEEEFSQFEEltESGDYLEarEVLEKLEEETDALEELM 195
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 166 PVLEEYKADAKLVlqFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLACGKLTGISD 235
Cdd:pfam06160 196 EDIPPLYEELKTE--LPDQLEELKEGYREMEEEGYALEHLNVDKEIQQLEEQLEENLALLENLELDEAEE 263
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
88-220 |
2.23e-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: 48.77 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 88 DARTKQLRQLLEK----VQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVE---ESHKQHL-----ARQFKAIK 155
Cdd:COG1579 16 DSELDRLEHRLKElpaeLAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEariKKYEEQLgnvrnNKEYEALQ 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543871463 156 AKMDELRPLIPVLEEykadakLVLQFKEEVQNLTSVLNELQEEIgaydyDELQSRVSNLEERLRA 220
Cdd:COG1579 96 KEIESLKRRISDLED------EILELMERIEELEEELAELEAEL-----AELEAELEEKKAELDE 149
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
81-226 |
2.41e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 81 QQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRR---TQRDLQYVEKMEnQMKGLESKFKQVEEsHKQHLARQFKAIKAK 157
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAEleeLREELEKLEKLL-QLLPLYQELEALEA-ELAELPERLEELEER 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 543871463 158 MDELRPLIPVLEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLA 226
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
57-225 |
3.10e-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: 49.72 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 57 EESWQVYSSAQDSEGRCICTVVAPQ-QTMCSRDARTKQLRQLLEKVQNMSQSI--EVLDRRTQRDL---QYVEKmENQMK 130
Cdd:pfam05483 179 EETRQVYMDLNNNIEKMILAFEELRvQAENARLEMHFKLKEDHEKIQHLEEEYkkEINDKEKQVSLlliQITEK-ENKMK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 131 GL-----ESKFK--QVEESHK-------------QHLARQFKAIKAKMDELRPLIPVLEE-YKADAKLVLQFKEEVQnlt 189
Cdd:pfam05483 258 DLtflleESRDKanQLEEKTKlqdenlkeliekkDHLTKELEDIKMSLQRSMSTQKALEEdLQIATKTICQLTEEKE--- 334
|
170 180 190
....*....|....*....|....*....|....*...
gi 543871463 190 SVLNELQEEIGAYDY--DELQSRVSNLEERLRACMQKL 225
Cdd:pfam05483 335 AQMEELNKAKAAHSFvvTEFEATTCSLEELLRTEQQRL 372
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
81-225 |
3.25e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 81 QQTMCSRDARTKQLRQLLEKVQNMSQSIEvldrRTQRDLQY----VEKMENQMKGLESKFKQVEESHKQhLARQFKAIKA 156
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELE----QLEEELEQarseLEQLEEELEELNEQLQAAQAELAQ-AQEELESLQE 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 543871463 157 KMDELRPLIpvlEEYKADAKlvlQFKEEVQNLTSVLNELQEEIGAYDY--DELQSRVSNLEERLRACMQKL 225
Cdd:COG4372 109 EAEELQEEL---EELQKERQ---DLEQQRKQLEAQIAELQSEIAEREEelKELEEQLESLQEELAALEQEL 173
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
86-219 |
1.18e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 86 SRDARTKQLRQLL-----EKV-QNMSQSIEVLDRRTQRDLQYVEKMENqmkgLESKFKQVEEShkqhLARQFKAIKAKMD 159
Cdd:PRK03918 143 SDESREKVVRQILglddyENAyKNLGEVIKEIKRRIERLEKFIKRTEN----IEELIKEKEKE----LEEVLREINEISS 214
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 160 ELRPLIPVLEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAydydeLQSRVSNLEERLR 219
Cdd:PRK03918 215 ELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRK-----LEEKIRELEERIE 269
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
88-218 |
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: 48.13 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 88 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQ-------MKGLESKFKQVE------ESHKQHLARQFKAI 154
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqilrerLANLERQLEELEaqleelESKLDELAEELAEL 342
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543871463 155 KAKMDELRplipvlEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAY--DYDELQ-------SRVSNLEERL 218
Cdd:TIGR02168 343 EEKLEELK------EELESLEAELEELEAELEELESRLEELEEQLETLrsKVAQLElqiaslnNEIERLEARL 409
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
88-226 |
1.66e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 47.14 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 88 DARTKQLRQLLEKVQNmsqsiEVLDRRTQrdlqY---VEKMENQMKGLESKFKQVEE-----------SHKQHLARQFKA 153
Cdd:PRK04778 139 REEVEQLKDLYRELRK-----SLLANRFS----FgpaLDELEKQLENLEEEFSQFVEltesgdyvearEILDQLEEELAA 209
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543871463 154 IKAKMDELRPLIpvleeykadAKLVLQFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLA 226
Cdd:PRK04778 210 LEQIMEEIPELL---------KELQTELPDQLQELKAGYRELVEEGYHLDHLDIEKEIQDLKEQIDENLALLE 273
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
94-225 |
3.21e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.82 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 94 LRQLLEKVQNMSQSIEVLDRrtQRDLqyvekMENQMKGLESKFKQVEESHKQHLARQFKAIKAKMDELRPLIPVLEEYKA 173
Cdd:PLN02939 245 LKAELIEVAETEERVFKLEK--ERSL-----LDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVE 317
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 543871463 174 DAKLVLQFKEEVQNLTSVLNELQEEIGAYDY-----DELQSRVSNLEERLRACMQKL 225
Cdd:PLN02939 318 KAALVLDQNQDLRDKVDKLEASLKEANVSKFssykvELLQQKLKLLEERLQASDHEI 374
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
88-216 |
6.13e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 88 DARTKQLRQLLEKVQNMsqsievldRRTQRDLQYVEKMENQMKGLESKFKQ--VEESHKQhlARQFKAIKAKMDELRPLI 165
Cdd:PRK03918 472 EEKERKLRKELRELEKV--------LKKESELIKLKELAEQLKELEEKLKKynLEELEKK--AEEYEKLKEKLIKLKGEI 541
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 543871463 166 PVL-------EEYKADAKLVLQFKEEVQN-LTSVLNELqEEIGAYDYDELQSRVSNLEE 216
Cdd:PRK03918 542 KSLkkeleklEELKKKLAELEKKLDELEEeLAELLKEL-EELGFESVEELEERLKELEP 599
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
87-225 |
8.14e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 8.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 87 RDARTKQLRQLLEKVQNMSQSIEVLDRRtqrdLQYVEKMENQMKGLESKFKQV-------EESHKqhlarQFKAIKAKMD 159
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEER----IKELEEKEERLEELKKKLKELekrleelEERHE-----LYEEAKAKKE 372
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 543871463 160 ELRPLIPVLEEYKADaklvlQFKEEVQNLTSVLNELQEEIgaydyDELQSRVSNLE---ERLRACMQKL 225
Cdd:PRK03918 373 ELERLKKRLTGLTPE-----KLEKELEELEKAKEEIEEEI-----SKITARIGELKkeiKELKKAIEEL 431
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
88-198 |
1.01e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 88 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVEESHKQhLARQFKAIKAKMDELRPLIPV 167
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE-LQSEIAEREEELKELEEQLES 161
|
90 100 110
....*....|....*....|....*....|.
gi 543871463 168 LEEYKADAKLVLQfKEEVQNLTSVLNELQEE 198
Cdd:COG4372 162 LQEELAALEQELQ-ALSEAEAEQALDELLKE 191
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
92-222 |
1.46e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.44 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 92 KQLRQLLEKVQNMSQSIEVLDrrtqrdlqyVEKMENQMKGLESK--------------FKQVEESHK------QHLARQF 151
Cdd:PRK04778 256 KEIQDLKEQIDENLALLEELD---------LDEAEEKNEEIQERidqlydilerevkaRKYVEKNSDtlpdflEHAKEQN 326
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 543871463 152 KAIKAKMDELRplipvlEEYK---ADAKLVLQFKEEVQNLTSVLNELQEEIGAYD--YDELQSRVSNLEERLRACM 222
Cdd:PRK04778 327 KELKEEIDRVK------QSYTlneSELESVRQLEKQLESLEKQYDEITERIAEQEiaYSELQEELEEILKQLEEIE 396
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
79-221 |
1.48e-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: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 79 APQQTMCSRDARTKQlrQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQvEESHKQHLARQFKAIKAKM 158
Cdd:pfam01576 57 AEAEEMRARLAARKQ--ELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE-EEAARQKLQLEKVTTEAKI 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 159 DELRPLIPVLEEykADAKLVLQFK---EEVQNLTSVLNElqEEIGAYDYDEL----QSRVSNLEERLRAC 221
Cdd:pfam01576 134 KKLEEDILLLED--QNSKLSKERKlleERISEFTSNLAE--EEEKAKSLSKLknkhEAMISDLEERLKKE 199
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
235-420 |
1.93e-04 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 43.08 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 235 DPVT--VKTSGSRFGSWMTDpLAPEGDNRVWYMDGYhNNRFVReyksmVDfMNTDNFTSHRLPHPWSGTGQVVY--NGSI 310
Cdd:COG4257 44 DPATgeFTEYPLGGGSGPHG-IAVDPDGNLWFTDNG-NNRIGR-----ID-PKTGEITTFALPGGGSNPHGIAFdpDGNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 311 YFNKFQSHIIIRFDLKTETILKTRSldYAGYNNMYhyawgghsdiDLMVDESGlwAVYATNQNAGNIVvsRLDP----VS 386
Cdd:COG4257 116 WFTDQGGNRIGRLDPATGEVTEFPL--PTGGAGPY----------GIAVDPDG--NLWVTDFGANAIG--RIDPdtgtLT 179
|
170 180 190
....*....|....*....|....*....|....*
gi 543871463 387 LQTLQTwNTSYPKR-SAGEAfiicGTLYVTNGYSG 420
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 ... |
95-220 |
2.09e-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: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 95 RQLLEKVQnmsqSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVEESHKQhLARQFKAIKAKMDELrplipvLEEYKAD 174
Cdd:TIGR04523 363 RELEEKQN----EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ-KDEQIKKLQQEKELL------EKEIERL 431
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 543871463 175 AKLVLQFKEEVQNLTSVLNELQEEigaydYDELQSRVSNLEERLRA 220
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELI-----IKNLDNTRESLETQLKV 472
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
86-226 |
2.26e-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: 43.90 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 86 SRDARTKQL--RQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKfkqVEESHKQHlarqfkaikakmDELRP 163
Cdd:TIGR02169 659 SRAPRGGILfsRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE---LSDASRKI------------GEIEK 723
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543871463 164 LIPVLEEYKAdaklvlQFKEEVQNLTSVLNELQEEIGAYD--YDELQSRVSNLEERLRACMQKLA 226
Cdd:TIGR02169 724 EIEQLEQEEE------KLKERLEELEEDLSSLEQEIENVKseLKELEARIEELEEDLHKLEEALN 782
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
95-226 |
2.59e-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: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 95 RQLLEKVQNMSQSIEVLDRRTQRDLQYVEK----MENQMKGLESKFKQVEESHKQHLARQfkaiKAKMDELR--PLIPVL 168
Cdd:pfam04108 20 RSLLEELVVLLAKIAFLRRGLSVQLANLEKvregLEKVLNELKKDFKQLLKDLDAALERL----EETLDKLRntPVEPAL 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 169 EEYKADAKLVLQF--KEEVQNLTSVLNELQEEIGAyDYDELQSRVSNLEERLRACMQKLA 226
Cdd:pfam04108 96 PPGEEKQKTLLDFidEDSVEILRDALKELIDELQA-AQESLDSDLKRFDDDLRDLQKELE 154
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
88-224 |
2.81e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 88 DARTKQLRQLLE---KVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVEESHKQHLARQFKAIKAKMDELRPL 164
Cdd:COG4913 671 AELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 165 ipvLEEYKADAKLVLQFKEEVQNLTSvlnelqeeigayDYDELQSRVSNLEERLRACMQK 224
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 ... |
91-226 |
3.48e-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: 43.24 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 91 TKQLRQLLEKVQNmSQsiEVLDRRTQRDLQY---VEKMENQMKGLESKFKQVEES------HKQHLARQFKAIKAKMDEL 161
Cdd:pfam01576 460 SKDVSSLESQLQD-TQ--ELLQEETRQKLNLstrLRQLEDERNSLQEQLEEEEEAkrnverQLSTLQAQLSDMKKKLEED 536
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543871463 162 RPLIPVLEEYKADAK-----LVLQFKE---EVQNLTSVLNELQEEIG--AYDYDELQSRVSNLEERLRACMQKLA 226
Cdd:pfam01576 537 AGTLEALEEGKKRLQreleaLTQQLEEkaaAYDKLEKTKNRLQQELDdlLVDLDHQRQLVSNLEKKQKKFDQMLA 611
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
93-226 |
4.14e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 93 QLRQLLEKVQNMSQSIEVLDRRTQRdlqYVEKMENQMKGLESKFKQVEEshkqhlarqfkaIKAKMDELRPLIPVLEEYK 172
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEE---RIEELKKEIEELEEKVKELKE------------LKEKAEEYIKLSEFYEEYL 306
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 543871463 173 adaKLVLQFKEEVQNLTSVLNELQEEIGayDYDELQSRVSNLEERLRACMQKLA 226
Cdd:PRK03918 307 ---DELREIEKRLSRLEEEINGIEERIK--ELEEKEERLEELKKKLKELEKRLE 355
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
92-216 |
5.28e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 92 KQLRQLLEKVQNMSQSIEVLDRRTQRD--LQYVeKMENqMKGLESKFKQVEESHKqhLARQFKAIKAKMDELRPLIPVLE 169
Cdd:COG4717 347 EELQELLREAEELEEELQLEELEQEIAalLAEA-GVED-EEELRAALEQAEEYQE--LKEELEELEEQLEELLGELEELL 422
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 543871463 170 EYKADAKL---VLQFKEEVQNLTSVLNELQEEIGaydydELQSRVSNLEE 216
Cdd:COG4717 423 EALDEEELeeeLEELEEELEELEEELEELREELA-----ELEAELEQLEE 467
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
92-186 |
7.17e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 92 KQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVEESHKQHLAR-----QFKAIKAK---MDELRp 163
Cdd:PRK12704 86 KLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQElerisGLTAEEAKeilLEKVE- 164
|
90 100
....*....|....*....|....
gi 543871463 164 lipvlEEYKAD-AKLVLQFKEEVQ 186
Cdd:PRK12704 165 -----EEARHEaAVLIKEIEEEAK 183
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
86-218 |
1.43e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 86 SRDARTKQLRQLLEKVQNMSQSIEVLdrRTQRDlqyveKMENQMKGLESKfkqveeshKQHLARQFKAIKAKMDELRpli 165
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEEL--KEKRD-----ELNEELKELAEK--------RDELNAQVKELREEAQELR--- 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543871463 166 pvlEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAY------------DYDELQSRVSNLEERL 218
Cdd:COG1340 64 ---EKRDELNEKVKELKEERDELNEKLNELREELDELrkelaelnkaggSIDKLRKEIERLEWRQ 125
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
93-226 |
1.60e-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: 39.74 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 93 QLRQLLEKVQNMSQSIEVLDRRtqrdLQYVEKMENQMKGLESKFKQVEESHKQHLARQFKAIKAKMDELRPLipvLEeyk 172
Cdd:cd00176 34 SVEALLKKHEALEAELAAHEER----VEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQR---LE--- 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 543871463 173 aDAKLVLQFKEEVQNLTSVLNELQEEIGAYDYD-------ELQSRVSNLEERLRACMQKLA 226
Cdd:cd00176 104 -EALDLQQFFRDADDLEQWLEEKEAALASEDLGkdlesveELLKKHKELEEELEAHEPRLK 163
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
89-218 |
1.80e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 89 ARTKQLRQLLEKVQNMSQSIEVLdrrtQRDLQYVEKMENQMKGLESKFKQVEES----HKQHLARQFKAIKAKMDELRPL 164
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGEIKSL----KKELEKLEELKKKLAELEKKLDELEEElaelLKELEELGFESVEELEERLKEL 597
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 543871463 165 IPVLEEY------------------KADAKLVLQFKE------EVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERL 218
Cdd:PRK03918 598 EPFYNEYlelkdaekelereekelkKLEEELDKAFEElaetekRLEELRKELEELEKKYSEEEYEELREEYLELSREL 675
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
84-224 |
2.55e-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: 40.42 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 84 MCSRDARTK-QLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKG--------LESKFKQVEE--SHKQHLARQFK 152
Cdd:TIGR00606 682 VCQRVFQTEaELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGlapgrqsiIDLKEKEIPElrNKLQKVNRDIQ 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 153 AIKAKMDE----LRPLIPVLEEYK---ADAKLVLQFKEEVQN----LTSVLNELQEEIGAYDYDELQSRVSNLEERLRAC 221
Cdd:TIGR00606 762 RLKNDIEEqetlLGTIMPEEESAKvclTDVTIMERFQMELKDverkIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTV 841
|
...
gi 543871463 222 MQK 224
Cdd:TIGR00606 842 VSK 844
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
94-226 |
3.32e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 94 LRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKmenQMKGLESKFKQVEEshkqhLARQFKAIKAKMDELRPLIPVLEEyka 173
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEE---RIKELEEKEERLEE-----LKKKLKELEKRLEELEERHELYEE--- 366
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 543871463 174 daklVLQFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLA 226
Cdd:PRK03918 367 ----AKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
95-226 |
3.95e-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: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 95 RQLLEKVQNMSQSIEVLDRrTQRDlqyVEKMENQMKGLEskfkQVEESHkqhlaRQFKAIKAKMDELRPLIPVLEEYKAD 174
Cdd:COG4913 221 PDTFEAADALVEHFDDLER-AHEA---LEDAREQIELLE----PIRELA-----ERYAAARERLAELEYLRAALRLWFAQ 287
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 543871463 175 AKLVLQfKEEVQNLTSVLNELQEEIgaydyDELQSRVSNLEERLRACMQKLA 226
Cdd:COG4913 288 RRLELL-EAELEELRAELARLEAEL-----ERLEARLDALREELDELEAQIR 333
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
86-225 |
4.69e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.12 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 86 SRDARTKQLRQLLEKVQNmsqsiEVLDRRTQRDLqyVEKMenqmKGLESKFKQVEESHKQHlaRQFKAIKAKMDELRpli 165
Cdd:COG1340 110 SIDKLRKEIERLEWRQQT-----EVLSPEEEKEL--VEKI----KELEKELEKAKKALEKN--EKLKELRAELKELR--- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 166 pvleeykadaklvlqfkEEVQNLTSVLNELQEEIGAY-----------------------DYDELQSRVSNLEERLRACM 222
Cdd:COG1340 174 -----------------KEAEEIHKKIKELAEEAQELheemielykeadelrkeadelhkEIVEAQEKADELHEEIIELQ 236
|
...
gi 543871463 223 QKL 225
Cdd:COG1340 237 KEL 239
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
91-219 |
5.88e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 37.28 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 91 TKQLRQLLEKVQ-------NMSQSIEVLdrrtQRDLQYVEkmENQmkglESKFKQVEESHKQhlarqFKAIKAKMDELRP 163
Cdd:pfam10473 2 EKKQLHVLEKLKeserkadSLKDKVENL----ERELEMSE--ENQ----ELAILEAENSKAE-----VETLKAEIEEMAQ 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 543871463 164 LIPVLEeykadAKLVLqFKEEVQNLTSVLNELQEEIgaydyDELQSRVSNLEERLR 219
Cdd:pfam10473 67 NLRDLE-----LDLVT-LRSEKENLTKELQKKQERV-----SELESLNSSLENLLE 111
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
117-225 |
9.60e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.60 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 117 RDLQYVEKMENQMKGLESKFKQveESHKQHLARQFKAIKAKM-DELRPLIPVLEEYKADAKLVLQFKEEVQNLtsvLNEL 195
Cdd:COG4717 344 DRIEELQELLREAEELEEELQL--EELEQEIAALLAEAGVEDeEELRAALEQAEEYQELKEELEELEEQLEEL---LGEL 418
|
90 100 110
....*....|....*....|....*....|
gi 543871463 196 QEEIGAYDYDELQSRVSNLEERLRACMQKL 225
Cdd:COG4717 419 EELLEALDEEELEEELEELEEELEELEEEL 448
|
|
| FadA |
pfam09403 |
Adhesion protein FadA; FadA (Fusobacterium adhesin A) is an adhesin which forms two alpha ... |
119-216 |
9.95e-03 |
|
Adhesion protein FadA; FadA (Fusobacterium adhesin A) is an adhesin which forms two alpha helices that form an intra-molecular coiled-coil arrangement.
Pssm-ID: 430587 [Multi-domain] Cd Length: 99 Bit Score: 35.72 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543871463 119 LQYVEKMENQMKgleSKFKQVEESHKQHLARQfKAIKAKMDELRPLIPVLEEYKADAKlvlQFKEEVQNLTSVLNELQEE 198
Cdd:pfam09403 9 LQKLENKEEQRF---NKEKAKAEAAAADLAKN-YELKAEIEEKLAKLEADSDVRFYKD---EYKELLKKYKDLLKELEKE 81
|
90
....*....|....*...
gi 543871463 199 IgaydyDELQSRVSNLEE 216
Cdd:pfam09403 82 I-----KEEEKIIDNFEA 94
|
|
| |
