|
Name |
Accession |
Description |
Interval |
E-value |
| OLF |
smart00284 |
Olfactomedin-like domains; |
228-478 |
1.92e-156 |
|
Olfactomedin-like domains;
Pssm-ID: 128580 Cd Length: 255 Bit Score: 444.28 E-value: 1.92e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 228 GKLTGISDPVTVKTSG-SRFGSWMTDPLAPEG-DNRVWYMDGY-HNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQV 304
Cdd:smart00284 1 GGLAGISKPVTLQTSWkGKSGAWMKDPLWNTTkKSLYWYMPLNtRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGTGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 305 VYNGSIYFNKFQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDENGLWAVYATNQNAGNIVISKLDP 384
Cdd:smart00284 81 VYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 385 VSLQILQTWNTSYPKRSAGEAFIICGTLYVTN-GYSGGTKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYA 463
Cdd:smart00284 161 ATLTIENTWITTYNKRSASNAFMICGILYVTRsLGSKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPNDRKLYA 240
|
250
....*....|....*
gi 84370357 464 WNNGHQTLYNVTLFH 478
Cdd:smart00284 241 WNNGHLVHYDIALKP 255
|
|
| OLF |
pfam02191 |
Olfactomedin-like domain; |
230-476 |
8.21e-137 |
|
Olfactomedin-like domain;
Pssm-ID: 460482 Cd Length: 246 Bit Score: 394.21 E-value: 8.21e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 230 LTGISDPVTVKTSGSRFGSWMTDPLAPEgdNRVWYMDGYHNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQVVYNGS 309
Cdd:pfam02191 1 LVSVSKPVTVKLSGGKYGAWMKDPLPPS--DKIYVTDRGTSGNTLREYASLDDFKNGSPSKKYKLPYPWQGTGHVVYNGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 310 IYFNKFQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDENGLWAVYATNQNAGNIVISKLDPVSLQI 389
Cdd:pfam02191 79 LYYNKYNSRNIVKYDLTTRTVAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLDPETLEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 390 LQTWNTSYPKRSAGEAFIICGTLYVTNGYSGG-TKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYAWNNGH 468
Cdd:pfam02191 159 EQTWNTSYPKRSAGNAFMVCGVLYAVRSVNTRrEEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLYAWDDGY 238
|
....*...
gi 84370357 469 QTLYNVTL 476
Cdd:pfam02191 239 QVTYPVTF 246
|
|
| Noelin-1 |
pfam12308 |
Neurogenesis glycoprotein; This domain family is found in eukaryotes, and is approximately 100 ... |
56-152 |
1.71e-53 |
|
Neurogenesis glycoprotein; This domain family is found in eukaryotes, and is approximately 100 amino acids in length. The family is found in association with pfam02191. There are two conserved sequence motifs: SAQ and VQN. Noelin-1 is a glycoprotein which is secreted mainly by postmitotic neurogenic tissues in the developing central and peripheral nervous systems, first appearing after neural tube closure. It is likely that it forms large multimeric complexes.It has a divergent function in neurogenesis. In animal caps neuralized by expression of noggin, co-expression of Noelin-1 causes expression of neuronal differentiation markers several stages before neurogenesis normally occurs in this tissue. Finally, only secreted forms of the protein can activate sensory marker expression, while all forms of the protein can induce early neurogenesis.
Pssm-ID: 432468 [Multi-domain] Cd Length: 100 Bit Score: 174.97 E-value: 1.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 56 PEESWQVYSSAQDSEGRCICTVVAPQQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLETK 135
Cdd:pfam12308 3 PEEGWQVYSSAQDPDGRCVCTVVAPAQDVCSRDPRSRQLRQLMEKVQNVSQSMEVLDLRTSRDLQYVRTTETLLKTLDSK 82
|
90
....*....|....*..
gi 84370357 136 FKQVEESHKQHLARQFK 152
Cdd:pfam12308 83 LKVAEANPQSLSARSFQ 99
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
92-218 |
2.68e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 92 KQLRQLLEKVQNMSQSIEVLDRR----TQRDLQyVEKMENQMKGLETKFKQVEEshkqhlarQFKAIKAKMDELRPLIPV 167
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELkeeiEELEKE-LESLEGSKRKLEEKIRELEE--------RIEELKKEIEELEEKVKE 284
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 84370357 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 |
1.70e-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: 50.62 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 92 KQLRQLLEKVQNMSQSIevldrRTQRDL--QYVEKMENQMKGLETKFKQVEE--SHKQHLA--RQFKAIKAKMDELRPLI 165
Cdd:pfam06160 121 EEVEELKDKYRELRKTL-----LANRFSygPAIDELEKQLAEIEEEFSQFEEltESGDYLEarEVLEKLEEETDALEELM 195
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 166 PVLEEYKADAKLVlqFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLACGKLTGISD 235
Cdd:pfam06160 196 EDIPPLYEELKTE--LPDQLEELKEGYREMEEEGYALEHLNVDKEIQQLEEQLEENLALLENLELDEAEE 263
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
81-226 |
3.27e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 81 QQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRR---TQRDLQYVEKMEnQMKGLETKFKQVEEsHKQHLARQFKAIKAK 157
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAEleeLREELEKLEKLL-QLLPLYQELEALEA-ELAELPERLEELEER 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 84370357 158 MDELRPLIPVLEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLA 226
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
88-218 |
8.81e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 8.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 88 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQ-------MKGLETKFKQVE------ESHKQHLARQFKAI 154
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqilrerLANLERQLEELEaqleelESKLDELAEELAEL 342
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 84370357 155 KAKMDELRplipvlEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAY--DYDELQ-------SRVSNLEERL 218
Cdd:TIGR02168 343 EEKLEELK------EELESLEAELEELEAELEELESRLEELEEQLETLrsKVAQLElqiaslnNEIERLEARL 409
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
88-198 |
1.65e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 88 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLETKFKQVEESHKQhLARQFKAIKAKMDELRPLIPV 167
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE-LQSEIAEREEELKELEEQLES 161
|
90 100 110
....*....|....*....|....*....|.
gi 84370357 168 LEEYKADAKLVLQfKEEVQNLTSVLNELQEE 198
Cdd:COG4372 162 LQEELAALEQELQ-ALSEAEAEQALDELLKE 191
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
88-216 |
1.71e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 88 DARTKQLRQLLEKVQNMsqsievldRRTQRDLQYVEKMENQMKGLETKFKQ--VEESHKQhlARQFKAIKAKMDELRPLI 165
Cdd:PRK03918 472 EEKERKLRKELRELEKV--------LKKESELIKLKELAEQLKELEEKLKKynLEELEKK--AEEYEKLKEKLIKLKGEI 541
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 84370357 166 PVL-------EEYKADAKLVLQFKEEVQN-LTSVLNELqEEIGAYDYDELQSRVSNLEE 216
Cdd:PRK03918 542 KSLkkeleklEELKKKLAELEKKLDELEEeLAELLKEL-EELGFESVEELEERLKELEP 599
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
235-420 |
2.27e-04 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 43.08 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 235 DPVT--VKTSGSRFGSWMTDpLAPEGDNRVWYMDGYhNNRFVReyksmVDfMNTDNFTSHRLPHPWSGTGQVVY--NGSI 310
Cdd:COG4257 44 DPATgeFTEYPLGGGSGPHG-IAVDPDGNLWFTDNG-NNRIGR-----ID-PKTGEITTFALPGGGSNPHGIAFdpDGNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 311 YFNKFQSHIIIRFDLKTETILKTRSldYAGYNNMYhyawgghsdiDLMVDENGlwAVYATNQNAGNIVisKLDPVSLQI- 389
Cdd:COG4257 116 WFTDQGGNRIGRLDPATGEVTEFPL--PTGGAGPY----------GIAVDPDG--NLWVTDFGANAIG--RIDPDTGTLt 179
|
170 180 190
....*....|....*....|....*....|....*
gi 84370357 390 ---LQTwNTSYPKR-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 |
3.55e-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: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 93 QLRQLLEKVQNMSQSIEVLDRRtqrdLQYVEKMENQMKGLETKFKQVEESHKQHLARQFKAIKAKMDELRPLipvLEeyk 172
Cdd:cd00176 34 SVEALLKKHEALEAELAAHEER----VEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQR---LE--- 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 84370357 173 aDAKLVLQFKEEVQNLTSVLNELQEEIGAYDYD-------ELQSRVSNLEERLRACMQKLA 226
Cdd:cd00176 104 -EALDLQQFFRDADDLEQWLEEKEAALASEDLGkdlesveELLKKHKELEEELEAHEPRLK 163
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| OLF |
smart00284 |
Olfactomedin-like domains; |
228-478 |
1.92e-156 |
|
Olfactomedin-like domains;
Pssm-ID: 128580 Cd Length: 255 Bit Score: 444.28 E-value: 1.92e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 228 GKLTGISDPVTVKTSG-SRFGSWMTDPLAPEG-DNRVWYMDGY-HNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQV 304
Cdd:smart00284 1 GGLAGISKPVTLQTSWkGKSGAWMKDPLWNTTkKSLYWYMPLNtRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGTGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 305 VYNGSIYFNKFQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDENGLWAVYATNQNAGNIVISKLDP 384
Cdd:smart00284 81 VYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 385 VSLQILQTWNTSYPKRSAGEAFIICGTLYVTN-GYSGGTKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYA 463
Cdd:smart00284 161 ATLTIENTWITTYNKRSASNAFMICGILYVTRsLGSKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPNDRKLYA 240
|
250
....*....|....*
gi 84370357 464 WNNGHQTLYNVTLFH 478
Cdd:smart00284 241 WNNGHLVHYDIALKP 255
|
|
| OLF |
pfam02191 |
Olfactomedin-like domain; |
230-476 |
8.21e-137 |
|
Olfactomedin-like domain;
Pssm-ID: 460482 Cd Length: 246 Bit Score: 394.21 E-value: 8.21e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 230 LTGISDPVTVKTSGSRFGSWMTDPLAPEgdNRVWYMDGYHNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQVVYNGS 309
Cdd:pfam02191 1 LVSVSKPVTVKLSGGKYGAWMKDPLPPS--DKIYVTDRGTSGNTLREYASLDDFKNGSPSKKYKLPYPWQGTGHVVYNGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 310 IYFNKFQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDENGLWAVYATNQNAGNIVISKLDPVSLQI 389
Cdd:pfam02191 79 LYYNKYNSRNIVKYDLTTRTVAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLDPETLEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 390 LQTWNTSYPKRSAGEAFIICGTLYVTNGYSGG-TKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYAWNNGH 468
Cdd:pfam02191 159 EQTWNTSYPKRSAGNAFMVCGVLYAVRSVNTRrEEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLYAWDDGY 238
|
....*...
gi 84370357 469 QTLYNVTL 476
Cdd:pfam02191 239 QVTYPVTF 246
|
|
| Noelin-1 |
pfam12308 |
Neurogenesis glycoprotein; This domain family is found in eukaryotes, and is approximately 100 ... |
56-152 |
1.71e-53 |
|
Neurogenesis glycoprotein; This domain family is found in eukaryotes, and is approximately 100 amino acids in length. The family is found in association with pfam02191. There are two conserved sequence motifs: SAQ and VQN. Noelin-1 is a glycoprotein which is secreted mainly by postmitotic neurogenic tissues in the developing central and peripheral nervous systems, first appearing after neural tube closure. It is likely that it forms large multimeric complexes.It has a divergent function in neurogenesis. In animal caps neuralized by expression of noggin, co-expression of Noelin-1 causes expression of neuronal differentiation markers several stages before neurogenesis normally occurs in this tissue. Finally, only secreted forms of the protein can activate sensory marker expression, while all forms of the protein can induce early neurogenesis.
Pssm-ID: 432468 [Multi-domain] Cd Length: 100 Bit Score: 174.97 E-value: 1.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 56 PEESWQVYSSAQDSEGRCICTVVAPQQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLETK 135
Cdd:pfam12308 3 PEEGWQVYSSAQDPDGRCVCTVVAPAQDVCSRDPRSRQLRQLMEKVQNVSQSMEVLDLRTSRDLQYVRTTETLLKTLDSK 82
|
90
....*....|....*..
gi 84370357 136 FKQVEESHKQHLARQFK 152
Cdd:pfam12308 83 LKVAEANPQSLSARSFQ 99
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
92-218 |
2.68e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 92 KQLRQLLEKVQNMSQSIEVLDRR----TQRDLQyVEKMENQMKGLETKFKQVEEshkqhlarQFKAIKAKMDELRPLIPV 167
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELkeeiEELEKE-LESLEGSKRKLEEKIRELEE--------RIEELKKEIEELEEKVKE 284
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 84370357 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 |
8.08e-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: 51.71 E-value: 8.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 88 DARTKQLRQLLEKVQNmsqSIEVLDRRTQRDLQYVEKMENQMKGlETKFKQVEESHKQHLARQFKAIKAKMDEL------ 161
Cdd:pfam01576 888 EARIAQLEEELEEEQS---NTELLNDRLRKSTLQVEQLTTELAA-ERSTSQKSESARQQLERQNKELKAKLQEMegtvks 963
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 84370357 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 |
1.70e-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: 50.62 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 92 KQLRQLLEKVQNMSQSIevldrRTQRDL--QYVEKMENQMKGLETKFKQVEE--SHKQHLA--RQFKAIKAKMDELRPLI 165
Cdd:pfam06160 121 EEVEELKDKYRELRKTL-----LANRFSygPAIDELEKQLAEIEEEFSQFEEltESGDYLEarEVLEKLEEETDALEELM 195
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 166 PVLEEYKADAKLVlqFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLACGKLTGISD 235
Cdd:pfam06160 196 EDIPPLYEELKTE--LPDQLEELKEGYREMEEEGYALEHLNVDKEIQQLEEQLEENLALLENLELDEAEE 263
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
81-226 |
3.27e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 81 QQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRR---TQRDLQYVEKMEnQMKGLETKFKQVEEsHKQHLARQFKAIKAK 157
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAEleeLREELEKLEKLL-QLLPLYQELEALEA-ELAELPERLEELEER 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 84370357 158 MDELRPLIPVLEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLA 226
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
88-220 |
3.37e-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: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 88 DARTKQLRQLLEK----VQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLETKFKQVE---ESHKQHL-----ARQFKAIK 155
Cdd:COG1579 16 DSELDRLEHRLKElpaeLAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEariKKYEEQLgnvrnNKEYEALQ 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 84370357 156 AKMDELRPLIPVLEEykadakLVLQFKEEVQNLTSVLNELQEEIgaydyDELQSRVSNLEERLRA 220
Cdd:COG1579 96 KEIESLKRRISDLED------EILELMERIEELEEELAELEAEL-----AELEAELEEKKAELDE 149
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
81-225 |
4.39e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 81 QQTMCSRDARTKQLRQLLEKVQNMSQSIEvldrRTQRDLQY----VEKMENQMKGLETKFKQVEESHKQhLARQFKAIKA 156
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELE----QLEEELEQarseLEQLEEELEELNEQLQAAQAELAQ-AQEELESLQE 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 84370357 157 KMDELRPLIpvlEEYKADAKlvlQFKEEVQNLTSVLNELQEEIGAYDY--DELQSRVSNLEERLRACMQKL 225
Cdd:COG4372 109 EAEELQEEL---EELQKERQ---DLEQQRKQLEAQIAELQSEIAEREEelKELEEQLESLQEELAALEQEL 173
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
57-225 |
5.53e-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: 48.95 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 57 EESWQVYSSAQDSEGRCICTVVAPQ-QTMCSRDARTKQLRQLLEKVQNMSQSI--EVLDRRTQRDL---QYVEKmENQMK 130
Cdd:pfam05483 179 EETRQVYMDLNNNIEKMILAFEELRvQAENARLEMHFKLKEDHEKIQHLEEEYkkEINDKEKQVSLlliQITEK-ENKMK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 131 GL-------ETKFKQVEESHK-------------QHLARQFKAIKAKMDELRPLIPVLEE-YKADAKLVLQFKEEVQnlt 189
Cdd:pfam05483 258 DLtflleesRDKANQLEEKTKlqdenlkeliekkDHLTKELEDIKMSLQRSMSTQKALEEdLQIATKTICQLTEEKE--- 334
|
170 180 190
....*....|....*....|....*....|....*...
gi 84370357 190 SVLNELQEEIGAYDY--DELQSRVSNLEERLRACMQKL 225
Cdd:pfam05483 335 AQMEELNKAKAAHSFvvTEFEATTCSLEELLRTEQQRL 372
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
92-225 |
8.43e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 8.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 92 KQLRQLLEkVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLETKFKQVEESHKQhLARQFKAIKAKMDELRPLIpvlEEY 171
Cdd:COG1579 4 EDLRALLD-LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED-LEKEIKRLELEIEEVEARI---KKY 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 84370357 172 KADAKLVLQFKEevqnltsvLNELQEEIgaydyDELQSRVSNLEERLRACMQKL 225
Cdd:COG1579 79 EEQLGNVRNNKE--------YEALQKEI-----ESLKRRISDLEDEILELMERI 119
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
88-218 |
8.81e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 8.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 88 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQ-------MKGLETKFKQVE------ESHKQHLARQFKAI 154
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqilrerLANLERQLEELEaqleelESKLDELAEELAEL 342
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 84370357 155 KAKMDELRplipvlEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAY--DYDELQ-------SRVSNLEERL 218
Cdd:TIGR02168 343 EEKLEELK------EELESLEAELEELEAELEELESRLEELEEQLETLrsKVAQLElqiaslnNEIERLEARL 409
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
86-219 |
1.45e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 86 SRDARTKQLRQLL-----EKV-QNMSQSIEVLDRRTQRDLQYVEKMENqmkgLETKFKQVEEShkqhLARQFKAIKAKMD 159
Cdd:PRK03918 143 SDESREKVVRQILglddyENAyKNLGEVIKEIKRRIERLEKFIKRTEN----IEELIKEKEKE----LEEVLREINEISS 214
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 160 ELRPLIPVLEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAydydeLQSRVSNLEERLR 219
Cdd:PRK03918 215 ELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRK-----LEEKIRELEERIE 269
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
88-226 |
3.35e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.37 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 88 DARTKQLRQLLEKVQNmsqsiEVLDRRTQrdlqY---VEKMENQMKGLETKFKQVEE-----------SHKQHLARQFKA 153
Cdd:PRK04778 139 REEVEQLKDLYRELRK-----SLLANRFS----FgpaLDELEKQLENLEEEFSQFVEltesgdyvearEILDQLEEELAA 209
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 84370357 154 IKAKMDELRPLIpvleeykadAKLVLQFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLA 226
Cdd:PRK04778 210 LEQIMEEIPELL---------KELQTELPDQLQELKAGYRELVEEGYHLDHLDIEKEIQDLKEQIDENLALLE 273
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
94-225 |
8.92e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.28 E-value: 8.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 94 LRQLLEKVQNMSQSIEVLDRrtQRDLqyvekMENQMKGLETKFKQVEESHKQHLARQFKAIKAKMDELRPLIPVLEEYKA 173
Cdd:PLN02939 245 LKAELIEVAETEERVFKLEK--ERSL-----LDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVE 317
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 84370357 174 DAKLVLQFKEEVQNLTSVLNELQEEIGAYDY-----DELQSRVSNLEERLRACMQKL 225
Cdd:PLN02939 318 KAALVLDQNQDLRDKVDKLEASLKEANVSKFssykvELLQQKLKLLEERLQASDHEI 374
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
87-225 |
9.92e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 9.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 87 RDARTKQLRQLLEKVQNMSQSIEVLDRRtqrdLQYVEKMENQMKGLETKFKQV-------EESHKqhlarQFKAIKAKMD 159
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEER----IKELEEKEERLEELKKKLKELekrleelEERHE-----LYEEAKAKKE 372
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 84370357 160 ELRPLIPVLEEYKADaklvlQFKEEVQNLTSVLNELQEEIgaydyDELQSRVSNLE---ERLRACMQKL 225
Cdd:PRK03918 373 ELERLKKRLTGLTPE-----KLEKELEELEKAKEEIEEEI-----SKITARIGELKkeiKELKKAIEEL 431
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
92-222 |
1.48e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.44 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 92 KQLRQLLEKVQNMSQSIEVLDrrtqrdlqyVEKMENQMKGLETK--------------FKQVEESHK------QHLARQF 151
Cdd:PRK04778 256 KEIQDLKEQIDENLALLEELD---------LDEAEEKNEEIQERidqlydilerevkaRKYVEKNSDtlpdflEHAKEQN 326
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 84370357 152 KAIKAKMDELRplipvlEEYK---ADAKLVLQFKEEVQNLTSVLNELQEEIGAYD--YDELQSRVSNLEERLRACM 222
Cdd:PRK04778 327 KELKEEIDRVK------QSYTlneSELESVRQLEKQLESLEKQYDEITERIAEQEiaYSELQEELEEILKQLEEIE 396
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
88-198 |
1.65e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 88 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLETKFKQVEESHKQhLARQFKAIKAKMDELRPLIPV 167
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE-LQSEIAEREEELKELEEQLES 161
|
90 100 110
....*....|....*....|....*....|.
gi 84370357 168 LEEYKADAKLVLQfKEEVQNLTSVLNELQEE 198
Cdd:COG4372 162 LQEELAALEQELQ-ALSEAEAEQALDELLKE 191
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
88-216 |
1.71e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 88 DARTKQLRQLLEKVQNMsqsievldRRTQRDLQYVEKMENQMKGLETKFKQ--VEESHKQhlARQFKAIKAKMDELRPLI 165
Cdd:PRK03918 472 EEKERKLRKELRELEKV--------LKKESELIKLKELAEQLKELEEKLKKynLEELEKK--AEEYEKLKEKLIKLKGEI 541
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 84370357 166 PVL-------EEYKADAKLVLQFKEEVQN-LTSVLNELqEEIGAYDYDELQSRVSNLEE 216
Cdd:PRK03918 542 KSLkkeleklEELKKKLAELEKKLDELEEeLAELLKEL-EELGFESVEELEERLKELEP 599
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
235-420 |
2.27e-04 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 43.08 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 235 DPVT--VKTSGSRFGSWMTDpLAPEGDNRVWYMDGYhNNRFVReyksmVDfMNTDNFTSHRLPHPWSGTGQVVY--NGSI 310
Cdd:COG4257 44 DPATgeFTEYPLGGGSGPHG-IAVDPDGNLWFTDNG-NNRIGR-----ID-PKTGEITTFALPGGGSNPHGIAFdpDGNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 311 YFNKFQSHIIIRFDLKTETILKTRSldYAGYNNMYhyawgghsdiDLMVDENGlwAVYATNQNAGNIVisKLDPVSLQI- 389
Cdd:COG4257 116 WFTDQGGNRIGRLDPATGEVTEFPL--PTGGAGPY----------GIAVDPDG--NLWVTDFGANAIG--RIDPDTGTLt 179
|
170 180 190
....*....|....*....|....*....|....*
gi 84370357 390 ---LQTwNTSYPKR-SAGEAfiicGTLYVTNGYSG 420
Cdd:COG4257 180 eyaLPT-PGAGPRGlAVDPD----GNLWVADTGSG 209
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
79-221 |
3.00e-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: 43.63 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 79 APQQTMCSRDARTKQlrQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLETKFKQvEESHKQHLARQFKAIKAKM 158
Cdd:pfam01576 57 AEAEEMRARLAARKQ--ELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE-EEAARQKLQLEKVTTEAKI 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 159 DELRPLIPVLEEykADAKLVLQFK---EEVQNLTSVLNElqEEIGAYDYDEL----QSRVSNLEERLRAC 221
Cdd:pfam01576 134 KKLEEDILLLED--QNSKLSKERKlleERISEFTSNLAE--EEEKAKSLSKLknkhEAMISDLEERLKKE 199
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
88-224 |
3.25e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 88 DARTKQLRQLLE---KVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLETKFKQVEESHKQHLARQFKAIKAKMDELRPL 164
Cdd:COG4913 671 AELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 165 ipvLEEYKADAKLVLQFKEEVQNLTSvlnelqeeigayDYDELQSRVSNLEERLRACMQK 224
Cdd:COG4913 751 ---LEERFAAALGDAVERELRENLEE------------RIDALRARLNRAEEELERAMRA 795
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
95-226 |
3.28e-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: 42.76 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 95 RQLLEKVQNMSQSIEVLDRRTQRDLQYVEK----MENQMKGLETKFKQVEESHKQHLARQfkaiKAKMDELR--PLIPVL 168
Cdd:pfam04108 20 RSLLEELVVLLAKIAFLRRGLSVQLANLEKvregLEKVLNELKKDFKQLLKDLDAALERL----EETLDKLRntPVEPAL 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 169 EEYKADAKLVLQF--KEEVQNLTSVLNELQEEIGAyDYDELQSRVSNLEERLRACMQKLA 226
Cdd:pfam04108 96 PPGEEKQKTLLDFidEDSVEILRDALKELIDELQA-AQESLDSDLKRFDDDLRDLQKELE 154
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
95-220 |
3.93e-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: 43.09 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 95 RQLLEKVQnmsqSIEVLDRRTQRDLQYVEKMENQMKGLETKFKQVEESHKQhLARQFKAIKAKMDELrplipvLEEYKAD 174
Cdd:TIGR04523 363 RELEEKQN----EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ-KDEQIKKLQQEKELL------EKEIERL 431
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 84370357 175 AKLVLQFKEEVQNLTSVLNELQEEigaydYDELQSRVSNLEERLRA 220
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELI-----IKNLDNTRESLETQLKV 472
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
91-226 |
4.61e-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: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 91 TKQLRQLLEKVQNmSQsiEVLDRRTQRDLQY---VEKMENQMKGLETKFKQVEES------HKQHLARQFKAIKAKMDEL 161
Cdd:pfam01576 460 SKDVSSLESQLQD-TQ--ELLQEETRQKLNLstrLRQLEDERNSLQEQLEEEEEAkrnverQLSTLQAQLSDMKKKLEED 536
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 84370357 162 RPLIPVLEEYKADAK-----LVLQFKE---EVQNLTSVLNELQEEIG--AYDYDELQSRVSNLEERLRACMQKLA 226
Cdd:pfam01576 537 AGTLEALEEGKKRLQreleaLTQQLEEkaaAYDKLEKTKNRLQQELDdlLVDLDHQRQLVSNLEKKQKKFDQMLA 611
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
86-226 |
6.18e-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: 42.36 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 86 SRDARTKQL--RQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLetkFKQVEESHKQHlarqfkaikakmDELRP 163
Cdd:TIGR02169 659 SRAPRGGILfsRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDEL---SQELSDASRKI------------GEIEK 723
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 84370357 164 LIPVLEEYKAdaklvlQFKEEVQNLTSVLNELQEEIGAYD--YDELQSRVSNLEERLRACMQKLA 226
Cdd:TIGR02169 724 EIEQLEQEEE------KLKERLEELEEDLSSLEQEIENVKseLKELEARIEELEEDLHKLEEALN 782
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
92-186 |
8.68e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 92 KQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLETKFKQVEESHKQHLAR-----QFKAIKAK---MDELRp 163
Cdd:PRK12704 86 KLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQElerisGLTAEEAKeilLEKVE- 164
|
90 100
....*....|....*....|....
gi 84370357 164 lipvlEEYKAD-AKLVLQFKEEVQ 186
Cdd:PRK12704 165 -----EEARHEaAVLIKEIEEEAK 183
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
92-216 |
1.71e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 92 KQLRQLLEKVQNMSQSIEVLDRRTQRD--LQYVeKMENqMKGLETKFKQVEESHKqhLARQFKAIKAKMDELRPLIPVLE 169
Cdd:COG4717 347 EELQELLREAEELEEELQLEELEQEIAalLAEA-GVED-EEELRAALEQAEEYQE--LKEELEELEEQLEELLGELEELL 422
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 84370357 170 EYKADAKL---VLQFKEEVQNLTSVLNELQEEIGaydydELQSRVSNLEE 216
Cdd:COG4717 423 EALDEEELeeeLEELEEELEELEEELEELREELA-----ELEAELEQLEE 467
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
86-218 |
2.02e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 86 SRDARTKQLRQLLEKVQNMSQSIEVLdrRTQRDlqyveKMENQMKGL----ETKFKQVEEshkqhLARQFKAIKAKMDEL 161
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEEL--KEKRD-----ELNEELKELaekrDELNAQVKE-----LREEAQELREKRDEL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 84370357 162 rplipvLEEYKadaklvlQFKEEVQNLTSVLNELQEEIGAY------------DYDELQSRVSNLEERL 218
Cdd:COG1340 70 ------NEKVK-------ELKEERDELNEKLNELREELDELrkelaelnkaggSIDKLRKEIERLEWRQ 125
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
84-224 |
2.71e-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: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 84 MCSRDARTK-QLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKG--------LETKFKQVEE--SHKQHLARQFK 152
Cdd:TIGR00606 682 VCQRVFQTEaELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGlapgrqsiIDLKEKEIPElrNKLQKVNRDIQ 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 153 AIKAKMDE----LRPLIPVLEEYK---ADAKLVLQFKEEVQN----LTSVLNELQEEIGAYDYDELQSRVSNLEERLRAC 221
Cdd:TIGR00606 762 RLKNDIEEqetlLGTIMPEEESAKvclTDVTIMERFQMELKDverkIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTV 841
|
...
gi 84370357 222 MQK 224
Cdd:TIGR00606 842 VSK 844
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
93-226 |
3.55e-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: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 93 QLRQLLEKVQNMSQSIEVLDRRtqrdLQYVEKMENQMKGLETKFKQVEESHKQHLARQFKAIKAKMDELRPLipvLEeyk 172
Cdd:cd00176 34 SVEALLKKHEALEAELAAHEER----VEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQR---LE--- 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 84370357 173 aDAKLVLQFKEEVQNLTSVLNELQEEIGAYDYD-------ELQSRVSNLEERLRACMQKLA 226
Cdd:cd00176 104 -EALDLQQFFRDADDLEQWLEEKEAALASEDLGkdlesveELLKKHKELEEELEAHEPRLK 163
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
86-225 |
3.66e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.51 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 86 SRDARTKQLRQLLEKVQNmsqsiEVLDRRTQRDLqyVEKMenqmKGLETKFKQVEESHKQHlaRQFKAIKAKMDELRpli 165
Cdd:COG1340 110 SIDKLRKEIERLEWRQQT-----EVLSPEEEKEL--VEKI----KELEKELEKAKKALEKN--EKLKELRAELKELR--- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 166 pvleeykadaklvlqfkEEVQNLTSVLNELQEEIGAY-----------------------DYDELQSRVSNLEERLRACM 222
Cdd:COG1340 174 -----------------KEAEEIHKKIKELAEEAQELheemielykeadelrkeadelhkEIVEAQEKADELHEEIIELQ 236
|
...
gi 84370357 223 QKL 225
Cdd:COG1340 237 KEL 239
|
|
| 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 84370357 95 RQLLEKVQNMSQSIEVLDRrTQRDlqyVEKMENQMKGLEtkfkQVEESHkqhlaRQFKAIKAKMDELRPLIPVLEEYKAD 174
Cdd:COG4913 221 PDTFEAADALVEHFDDLER-AHEA---LEDAREQIELLE----PIRELA-----ERYAAARERLAELEYLRAALRLWFAQ 287
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 84370357 175 AKLVLQfKEEVQNLTSVLNELQEEIgaydyDELQSRVSNLEERLRACMQKLA 226
Cdd:COG4913 288 RRLELL-EAELEELRAELARLEAEL-----ERLEARLDALREELDELEAQIR 333
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
89-218 |
3.97e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 89 ARTKQLRQLLEKVQNMSQSIEVLdrrtQRDLQYVEKMENQMKGLETKFKQVEES----HKQHLARQFKAIKAKMDELRPL 164
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGEIKSL----KKELEKLEELKKKLAELEKKLDELEEElaelLKELEELGFESVEELEERLKEL 597
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 84370357 165 IPVLEEY------------------KADAKLVLQFKE------EVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERL 218
Cdd:PRK03918 598 EPFYNEYlelkdaekelereekelkKLEEELDKAFEElaetekRLEELRKELEELEKKYSEEEYEELREEYLELSREL 675
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
91-219 |
5.05e-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: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84370357 91 TKQLRQLLEKVQ-------NMSQSIEVLdrrtQRDLQYVEKMENQMK-GLETKFKQVEEshkqhlarqfkaIKAKMDELR 162
Cdd:pfam10473 2 EKKQLHVLEKLKeserkadSLKDKVENL----ERELEMSEENQELAIlEAENSKAEVET------------LKAEIEEMA 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 84370357 163 PLIPVLEeykadAKLVLqFKEEVQNLTSVLNELQEEIgaydyDELQSRVSNLEERLR 219
Cdd:pfam10473 66 QNLRDLE-----LDLVT-LRSEKENLTKELQKKQERV-----SELESLNSSLENLLE 111
|
|
| |
