|
Name |
Accession |
Description |
Interval |
E-value |
| OLF |
smart00284 |
Olfactomedin-like domains; |
210-460 |
2.26e-154 |
|
Olfactomedin-like domains;
Pssm-ID: 128580 Cd Length: 255 Bit Score: 438.50 E-value: 2.26e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 210 GKLTGISDPVTVKTSG-SRFGSWMTDPLAPEG-DNRVWYMDGY-HNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQV 286
Cdd:smart00284 1 GGLAGISKPVTLQTSWkGKSGAWMKDPLWNTTkKSLYWYMPLNtRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGTGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 287 VYNGSIYFNKFQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDESGLWAVYATNQNAGNIVVSRLDP 366
Cdd:smart00284 81 VYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 367 VSLQTLQTWNTSYPKRSAGEAFIICGTLYVTN-GYSGGTKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYA 445
Cdd:smart00284 161 ATLTIENTWITTYNKRSASNAFMICGILYVTRsLGSKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPNDRKLYA 240
|
250
....*....|....*
gi 17136143 446 WNNGHQILYNVTLFH 460
Cdd:smart00284 241 WNNGHLVHYDIALKP 255
|
|
| OLF |
pfam02191 |
Olfactomedin-like domain; |
212-458 |
1.40e-135 |
|
Olfactomedin-like domain;
Pssm-ID: 460482 Cd Length: 246 Bit Score: 390.36 E-value: 1.40e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 212 LTGISDPVTVKTSGSRFGSWMTDPLAPEgdNRVWYMDGYHNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQVVYNGS 291
Cdd:pfam02191 1 LVSVSKPVTVKLSGGKYGAWMKDPLPPS--DKIYVTDRGTSGNTLREYASLDDFKNGSPSKKYKLPYPWQGTGHVVYNGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 292 IYFNKFQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDESGLWAVYATNQNAGNIVVSRLDPVSLQT 371
Cdd:pfam02191 79 LYYNKYNSRNIVKYDLTTRTVAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLDPETLEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 372 LQTWNTSYPKRSAGEAFIICGTLYVTNGYSGG-TKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYAWNNGH 450
Cdd:pfam02191 159 EQTWNTSYPKRSAGNAFMVCGVLYAVRSVNTRrEEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLYAWDDGY 238
|
....*...
gi 17136143 451 QILYNVTL 458
Cdd:pfam02191 239 QVTYPVTF 246
|
|
| Noelin-1 |
pfam12308 |
Neurogenesis glycoprotein; This domain family is found in eukaryotes, and is approximately 100 ... |
38-134 |
9.29e-54 |
|
Neurogenesis glycoprotein; This domain family is found in eukaryotes, and is approximately 100 amino acids in length. The family is found in association with pfam02191. There are two conserved sequence motifs: SAQ and VQN. Noelin-1 is a glycoprotein which is secreted mainly by postmitotic neurogenic tissues in the developing central and peripheral nervous systems, first appearing after neural tube closure. It is likely that it forms large multimeric complexes.It has a divergent function in neurogenesis. In animal caps neuralized by expression of noggin, co-expression of Noelin-1 causes expression of neuronal differentiation markers several stages before neurogenesis normally occurs in this tissue. Finally, only secreted forms of the protein can activate sensory marker expression, while all forms of the protein can induce early neurogenesis.
Pssm-ID: 432468 [Multi-domain] Cd Length: 100 Bit Score: 175.35 E-value: 9.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 38 PEESWQVYSSAQDSEGRCICTVVAPQQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESK 117
Cdd:pfam12308 3 PEEGWQVYSSAQDPDGRCVCTVVAPAQDVCSRDPRSRQLRQLMEKVQNVSQSMEVLDLRTSRDLQYVRTTETLLKTLDSK 82
|
90
....*....|....*..
gi 17136143 118 FKQVEESHKQHLARQFK 134
Cdd:pfam12308 83 LKVAEANPQSLSARSFQ 99
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
74-200 |
2.31e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 74 KQLRQLLEKVQNMSQSIEVLDRR----TQRDLQyVEKMENQMKGLESKFKQVEEshkqhlarQFKAIKAKMDELRPLIPV 149
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELkeeiEELEKE-LESLEGSKRKLEEKIRELEE--------RIEELKKEIEELEEKVKE 284
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 17136143 150 LEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAYdydelQSRVSNLEERL 200
Cdd:PRK03918 285 LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL-----EEEINGIEERI 330
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
74-217 |
2.06e-06 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 50.24 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 74 KQLRQLLEKVQNMSQSIevldrRTQRDL--QYVEKMENQMKGLESKFKQVEE--SHKQHLA--RQFKAIKAKMDELRPLI 147
Cdd:pfam06160 121 EEVEELKDKYRELRKTL-----LANRFSygPAIDELEKQLAEIEEEFSQFEEltESGDYLEarEVLEKLEEETDALEELM 195
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 148 PVLEEYKADAKLVlqFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLACGKLTGISD 217
Cdd:pfam06160 196 EDIPPLYEELKTE--LPDQLEELKEGYREMEEEGYALEHLNVDKEIQQLEEQLEENLALLENLELDEAEE 263
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
70-202 |
2.11e-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: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 70 DARTKQLRQLLEK----VQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVE---ESHKQHL-----ARQFKAIK 137
Cdd:COG1579 16 DSELDRLEHRLKElpaeLAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEariKKYEEQLgnvrnNKEYEALQ 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17136143 138 AKMDELRPLIPVLEEykadakLVLQFKEEVQNLTSVLNELQEEIgaydyDELQSRVSNLEERLRA 202
Cdd:COG1579 96 KEIESLKRRISDLED------EILELMERIEELEEELAELEAEL-----AELEAELEEKKAELDE 149
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
70-200 |
1.32e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 70 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQ-------MKGLESKFKQVE------ESHKQHLARQFKAI 136
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqilrerLANLERQLEELEaqleelESKLDELAEELAEL 342
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17136143 137 KAKMDELRplipvlEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAY--DYDELQ-------SRVSNLEERL 200
Cdd:TIGR02168 343 EEKLEELK------EELESLEAELEELEAELEELESRLEELEEQLETLrsKVAQLElqiaslnNEIERLEARL 409
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
70-198 |
6.29e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 70 DARTKQLRQLLEKVQNMsqsievldRRTQRDLQYVEKMENQMKGLESKFKQ--VEESHKQhlARQFKAIKAKMDELRPLI 147
Cdd:PRK03918 472 EEKERKLRKELRELEKV--------LKKESELIKLKELAEQLKELEEKLKKynLEELEKK--AEEYEKLKEKLIKLKGEI 541
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 17136143 148 PVL-------EEYKADAKLVLQFKEEVQN-LTSVLNELqEEIGAYDYDELQSRVSNLEE 198
Cdd:PRK03918 542 KSLkkeleklEELKKKLAELEKKLDELEEeLAELLKEL-EELGFESVEELEERLKELEP 599
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
217-402 |
1.83e-04 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 43.08 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 217 DPVT--VKTSGSRFGSWMTDpLAPEGDNRVWYMDGYhNNRFVReyksmVDfMNTDNFTSHRLPHPWSGTGQVVY--NGSI 292
Cdd:COG4257 44 DPATgeFTEYPLGGGSGPHG-IAVDPDGNLWFTDNG-NNRIGR-----ID-PKTGEITTFALPGGGSNPHGIAFdpDGNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 293 YFNKFQSHIIIRFDLKTETILKTRSldYAGYNNMYhyawgghsdiDLMVDESGlwAVYATNQNAGNIVvsRLDP----VS 368
Cdd:COG4257 116 WFTDQGGNRIGRLDPATGEVTEFPL--PTGGAGPY----------GIAVDPDG--NLWVTDFGANAIG--RIDPdtgtLT 179
|
170 180 190
....*....|....*....|....*....|....*
gi 17136143 369 LQTLQTwNTSYPKR-SAGEAfiicGTLYVTNGYSG 402
Cdd:COG4257 180 EYALPT-PGAGPRGlAVDPD----GNLWVADTGSG 209
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
70-180 |
2.31e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 70 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVEESHKQhLARQFKAIKAKMDELRPLIPV 149
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE-LQSEIAEREEELKELEEQLES 161
|
90 100 110
....*....|....*....|....*....|.
gi 17136143 150 LEEYKADAKLVLQfKEEVQNLTSVLNELQEE 180
Cdd:COG4372 162 LQEELAALEQELQ-ALSEAEAEQALDELLKE 191
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
75-208 |
5.49e-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: 38.20 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 75 QLRQLLEKVQNMSQSIEVLDRRtqrdLQYVEKMENQMKGLESKFKQVEESHKQHLARQFKAIKAKMDELRPLipvLEeyk 154
Cdd:cd00176 34 SVEALLKKHEALEAELAAHEER----VEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQR---LE--- 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17136143 155 aDAKLVLQFKEEVQNLTSVLNELQEEIGAYDYD-------ELQSRVSNLEERLRACMQKLA 208
Cdd:cd00176 104 -EALDLQQFFRDADDLEQWLEEKEAALASEDLGkdlesveELLKKHKELEEELEAHEPRLK 163
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| OLF |
smart00284 |
Olfactomedin-like domains; |
210-460 |
2.26e-154 |
|
Olfactomedin-like domains;
Pssm-ID: 128580 Cd Length: 255 Bit Score: 438.50 E-value: 2.26e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 210 GKLTGISDPVTVKTSG-SRFGSWMTDPLAPEG-DNRVWYMDGY-HNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQV 286
Cdd:smart00284 1 GGLAGISKPVTLQTSWkGKSGAWMKDPLWNTTkKSLYWYMPLNtRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGTGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 287 VYNGSIYFNKFQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDESGLWAVYATNQNAGNIVVSRLDP 366
Cdd:smart00284 81 VYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 367 VSLQTLQTWNTSYPKRSAGEAFIICGTLYVTN-GYSGGTKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYA 445
Cdd:smart00284 161 ATLTIENTWITTYNKRSASNAFMICGILYVTRsLGSKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPNDRKLYA 240
|
250
....*....|....*
gi 17136143 446 WNNGHQILYNVTLFH 460
Cdd:smart00284 241 WNNGHLVHYDIALKP 255
|
|
| OLF |
pfam02191 |
Olfactomedin-like domain; |
212-458 |
1.40e-135 |
|
Olfactomedin-like domain;
Pssm-ID: 460482 Cd Length: 246 Bit Score: 390.36 E-value: 1.40e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 212 LTGISDPVTVKTSGSRFGSWMTDPLAPEgdNRVWYMDGYHNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQVVYNGS 291
Cdd:pfam02191 1 LVSVSKPVTVKLSGGKYGAWMKDPLPPS--DKIYVTDRGTSGNTLREYASLDDFKNGSPSKKYKLPYPWQGTGHVVYNGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 292 IYFNKFQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDESGLWAVYATNQNAGNIVVSRLDPVSLQT 371
Cdd:pfam02191 79 LYYNKYNSRNIVKYDLTTRTVAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLDPETLEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 372 LQTWNTSYPKRSAGEAFIICGTLYVTNGYSGG-TKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYAWNNGH 450
Cdd:pfam02191 159 EQTWNTSYPKRSAGNAFMVCGVLYAVRSVNTRrEEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLYAWDDGY 238
|
....*...
gi 17136143 451 QILYNVTL 458
Cdd:pfam02191 239 QVTYPVTF 246
|
|
| Noelin-1 |
pfam12308 |
Neurogenesis glycoprotein; This domain family is found in eukaryotes, and is approximately 100 ... |
38-134 |
9.29e-54 |
|
Neurogenesis glycoprotein; This domain family is found in eukaryotes, and is approximately 100 amino acids in length. The family is found in association with pfam02191. There are two conserved sequence motifs: SAQ and VQN. Noelin-1 is a glycoprotein which is secreted mainly by postmitotic neurogenic tissues in the developing central and peripheral nervous systems, first appearing after neural tube closure. It is likely that it forms large multimeric complexes.It has a divergent function in neurogenesis. In animal caps neuralized by expression of noggin, co-expression of Noelin-1 causes expression of neuronal differentiation markers several stages before neurogenesis normally occurs in this tissue. Finally, only secreted forms of the protein can activate sensory marker expression, while all forms of the protein can induce early neurogenesis.
Pssm-ID: 432468 [Multi-domain] Cd Length: 100 Bit Score: 175.35 E-value: 9.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 38 PEESWQVYSSAQDSEGRCICTVVAPQQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESK 117
Cdd:pfam12308 3 PEEGWQVYSSAQDPDGRCVCTVVAPAQDVCSRDPRSRQLRQLMEKVQNVSQSMEVLDLRTSRDLQYVRTTETLLKTLDSK 82
|
90
....*....|....*..
gi 17136143 118 FKQVEESHKQHLARQFK 134
Cdd:pfam12308 83 LKVAEANPQSLSARSFQ 99
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
74-200 |
2.31e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 74 KQLRQLLEKVQNMSQSIEVLDRR----TQRDLQyVEKMENQMKGLESKFKQVEEshkqhlarQFKAIKAKMDELRPLIPV 149
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELkeeiEELEKE-LESLEGSKRKLEEKIRELEE--------RIEELKKEIEELEEKVKE 284
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 17136143 150 LEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAYdydelQSRVSNLEERL 200
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 ... |
70-143 |
1.99e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.56 E-value: 1.99e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17136143 70 DARTKQLRQLLEKVQNmsqSIEVLDRRTQRDLQYVEKMENQMKGlESKFKQVEESHKQHLARQFKAIKAKMDEL 143
Cdd:pfam01576 888 EARIAQLEEELEEEQS---NTELLNDRLRKSTLQVEQLTTELAA-ERSTSQKSESARQQLERQNKELKAKLQEM 957
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
74-217 |
2.06e-06 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 50.24 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 74 KQLRQLLEKVQNMSQSIevldrRTQRDL--QYVEKMENQMKGLESKFKQVEE--SHKQHLA--RQFKAIKAKMDELRPLI 147
Cdd:pfam06160 121 EEVEELKDKYRELRKTL-----LANRFSygPAIDELEKQLAEIEEEFSQFEEltESGDYLEarEVLEKLEEETDALEELM 195
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 148 PVLEEYKADAKLVlqFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLACGKLTGISD 217
Cdd:pfam06160 196 EDIPPLYEELKTE--LPDQLEELKEGYREMEEEGYALEHLNVDKEIQQLEEQLEENLALLENLELDEAEE 263
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
70-202 |
2.11e-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: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 70 DARTKQLRQLLEK----VQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVE---ESHKQHL-----ARQFKAIK 137
Cdd:COG1579 16 DSELDRLEHRLKElpaeLAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEariKKYEEQLgnvrnNKEYEALQ 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17136143 138 AKMDELRPLIPVLEEykadakLVLQFKEEVQNLTSVLNELQEEIgaydyDELQSRVSNLEERLRA 202
Cdd:COG1579 96 KEIESLKRRISDLED------EILELMERIEELEEELAELEAEL-----AELEAELEEKKAELDE 149
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
39-207 |
4.12e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.33 E-value: 4.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 39 EESWQVYSSAQDSEGRCICTVVAPQ-QTMCSRDARTKQLRQLLEKVQNMSQSI--EVLDRRTQRDL---QYVEKmENQMK 112
Cdd:pfam05483 179 EETRQVYMDLNNNIEKMILAFEELRvQAENARLEMHFKLKEDHEKIQHLEEEYkkEINDKEKQVSLlliQITEK-ENKMK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 113 GL-----ESKFK--QVEESHK-------------QHLARQFKAIKAKMDELRPLIPVLEE-YKADAKLVLQFKEEVQnlt 171
Cdd:pfam05483 258 DLtflleESRDKanQLEEKTKlqdenlkeliekkDHLTKELEDIKMSLQRSMSTQKALEEdLQIATKTICQLTEEKE--- 334
|
170 180 190
....*....|....*....|....*....|....*...
gi 17136143 172 SVLNELQEEIGAYDY--DELQSRVSNLEERLRACMQKL 207
Cdd:pfam05483 335 AQMEELNKAKAAHSFvvTEFEATTCSLEELLRTEQQRL 372
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
63-208 |
5.63e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 63 QQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRR---TQRDLQYVEKMEnQMKGLESKFKQVEEsHKQHLARQFKAIKAK 139
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAEleeLREELEKLEKLL-QLLPLYQELEALEA-ELAELPERLEELEER 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17136143 140 MDELRPLIPVLEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLA 208
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
63-207 |
1.19e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 63 QQTMCSRDARTKQLRQLLEKVQNMSQSIEvldrRTQRDLQY----VEKMENQMKGLESKFKQVEESHKQhLARQFKAIKA 138
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELE----QLEEELEQarseLEQLEEELEELNEQLQAAQAELAQ-AQEELESLQE 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17136143 139 KMDELRPLIpvlEEYKADAKlvlQFKEEVQNLTSVLNELQEEIGAYDY--DELQSRVSNLEERLRACMQKL 207
Cdd:COG4372 109 EAEELQEEL---EELQKERQ---DLEQQRKQLEAQIAELQSEIAEREEelKELEEQLESLQEELAALEQEL 173
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
68-201 |
1.23e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 68 SRDARTKQLRQLL-----EKV-QNMSQSIEVLDRRTQRDLQYVEKMENqmkgLESKFKQVEEShkqhLARQFKAIKAKMD 141
Cdd:PRK03918 143 SDESREKVVRQILglddyENAyKNLGEVIKEIKRRIERLEKFIKRTEN----IEELIKEKEKE----LEEVLREINEISS 214
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 142 ELRPLIPVLEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAydydeLQSRVSNLEERLR 201
Cdd:PRK03918 215 ELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRK-----LEEKIRELEERIE 269
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
70-200 |
1.32e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 70 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQ-------MKGLESKFKQVE------ESHKQHLARQFKAI 136
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqilrerLANLERQLEELEaqleelESKLDELAEELAEL 342
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17136143 137 KAKMDELRplipvlEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAY--DYDELQ-------SRVSNLEERL 200
Cdd:TIGR02168 343 EEKLEELK------EELESLEAELEELEAELEELESRLEELEEQLETLrsKVAQLElqiaslnNEIERLEARL 409
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
70-208 |
3.16e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.37 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 70 DARTKQLRQLLEKVQNmsqsiEVLDRRTQrdlqY---VEKMENQMKGLESKFKQVEE-----------SHKQHLARQFKA 135
Cdd:PRK04778 139 REEVEQLKDLYRELRK-----SLLANRFS----FgpaLDELEKQLENLEEEFSQFVEltesgdyvearEILDQLEEELAA 209
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17136143 136 IKAKMDELRPLIpvleeykadAKLVLQFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLA 208
Cdd:PRK04778 210 LEQIMEEIPELL---------KELQTELPDQLQELKAGYRELVEEGYHLDHLDIEKEIQDLKEQIDENLALLE 273
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
76-207 |
3.84e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.43 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 76 LRQLLEKVQNMSQSIEVLDRrtQRDLqyvekMENQMKGLESKFKQVEESHKQHLARQFKAIKAKMDELRPLIPVLEEYKA 155
Cdd:PLN02939 245 LKAELIEVAETEERVFKLEK--ERSL-----LDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVE 317
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 17136143 156 DAKLVLQFKEEVQNLTSVLNELQEEIGAYDY-----DELQSRVSNLEERLRACMQKL 207
Cdd:PLN02939 318 KAALVLDQNQDLRDKVDKLEASLKEANVSKFssykvELLQQKLKLLEERLQASDHEI 374
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
70-198 |
6.29e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 70 DARTKQLRQLLEKVQNMsqsievldRRTQRDLQYVEKMENQMKGLESKFKQ--VEESHKQhlARQFKAIKAKMDELRPLI 147
Cdd:PRK03918 472 EEKERKLRKELRELEKV--------LKKESELIKLKELAEQLKELEEKLKKynLEELEKK--AEEYEKLKEKLIKLKGEI 541
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 17136143 148 PVL-------EEYKADAKLVLQFKEEVQN-LTSVLNELqEEIGAYDYDELQSRVSNLEE 198
Cdd:PRK03918 542 KSLkkeleklEELKKKLAELEKKLDELEEeLAELLKEL-EELGFESVEELEERLKELEP 599
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
69-207 |
8.29e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 69 RDARTKQLRQLLEKVQNMSQSIEVLDRRtqrdLQYVEKMENQMKGLESKFKQV-------EESHKqhlarQFKAIKAKMD 141
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEER----IKELEEKEERLEELKKKLKELekrleelEERHE-----LYEEAKAKKE 372
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17136143 142 ELRPLIPVLEEYKADaklvlQFKEEVQNLTSVLNELQEEIgaydyDELQSRVSNLE---ERLRACMQKL 207
Cdd:PRK03918 373 ELERLKKRLTGLTPE-----KLEKELEELEKAKEEIEEEI-----SKITARIGELKkeiKELKKAIEEL 431
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
217-402 |
1.83e-04 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 43.08 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 217 DPVT--VKTSGSRFGSWMTDpLAPEGDNRVWYMDGYhNNRFVReyksmVDfMNTDNFTSHRLPHPWSGTGQVVY--NGSI 292
Cdd:COG4257 44 DPATgeFTEYPLGGGSGPHG-IAVDPDGNLWFTDNG-NNRIGR-----ID-PKTGEITTFALPGGGSNPHGIAFdpDGNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 293 YFNKFQSHIIIRFDLKTETILKTRSldYAGYNNMYhyawgghsdiDLMVDESGlwAVYATNQNAGNIVvsRLDP----VS 368
Cdd:COG4257 116 WFTDQGGNRIGRLDPATGEVTEFPL--PTGGAGPY----------GIAVDPDG--NLWVTDFGANAIG--RIDPdtgtLT 179
|
170 180 190
....*....|....*....|....*....|....*
gi 17136143 369 LQTLQTwNTSYPKR-SAGEAfiicGTLYVTNGYSG 402
Cdd:COG4257 180 EYALPT-PGAGPRGlAVDPD----GNLWVADTGSG 209
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
70-180 |
2.31e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 70 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVEESHKQhLARQFKAIKAKMDELRPLIPV 149
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE-LQSEIAEREEELKELEEQLES 161
|
90 100 110
....*....|....*....|....*....|.
gi 17136143 150 LEEYKADAKLVLQfKEEVQNLTSVLNELQEE 180
Cdd:COG4372 162 LQEELAALEQELQ-ALSEAEAEQALDELLKE 191
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
77-202 |
2.54e-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: 43.47 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 77 RQLLEKVQnmsqSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVEESHKQhLARQFKAIKAKMDELrplipvLEEYKAD 156
Cdd:TIGR04523 363 RELEEKQN----EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ-KDEQIKKLQQEKELL------EKEIERL 431
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 17136143 157 AKLVLQFKEEVQNLTSVLNELQEEigaydYDELQSRVSNLEERLRA 202
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELI-----IKNLDNTRESLETQLKV 472
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
68-208 |
2.56e-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: 43.52 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 68 SRDARTKQL--RQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKfkqVEESHKQHlarqfkaikakmDELRP 145
Cdd:TIGR02169 659 SRAPRGGILfsRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE---LSDASRKI------------GEIEK 723
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17136143 146 LIPVLEEYKAdaklvlQFKEEVQNLTSVLNELQEEIGAYD--YDELQSRVSNLEERLRACMQKLA 208
Cdd:TIGR02169 724 EIEQLEQEEE------KLKERLEELEEDLSSLEQEIENVKseLKELEARIEELEEDLHKLEEALN 782
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
74-204 |
2.84e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.29 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 74 KQLRQLLEKVQNMSQSIEVLDrrtqrdlqyVEKMENQMKGLESK--------------FKQVEESHK------QHLARQF 133
Cdd:PRK04778 256 KEIQDLKEQIDENLALLEELD---------LDEAEEKNEEIQERidqlydilerevkaRKYVEKNSDtlpdflEHAKEQN 326
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136143 134 KAIKAKMDELRplipvlEEYK---ADAKLVLQFKEEVQNLTSVLNELQEEIGAYD--YDELQSRVSNLEERLRACM 204
Cdd:PRK04778 327 KELKEEIDRVK------QSYTlneSELESVRQLEKQLESLEKQYDEITERIAEQEiaYSELQEELEEILKQLEEIE 396
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
70-206 |
3.40e-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: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 70 DARTKQLRQLLE---KVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVEESHKQHLARQFKAIKAKMDELRPL 146
Cdd:COG4913 671 AELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 147 ipvLEEYKADAKLVLQFKEEVQNLTSvlnelqeeigayDYDELQSRVSNLEERLRACMQK 206
Cdd:COG4913 751 ---LEERFAAALGDAVERELRENLEE------------RIDALRARLNRAEEELERAMRA 795
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
77-208 |
3.60e-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: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 77 RQLLEKVQNMSQSIEVLDRRTQRDLQYVEK----MENQMKGLESKFKQVEESHKQHLARQfkaiKAKMDELR--PLIPVL 150
Cdd:pfam04108 20 RSLLEELVVLLAKIAFLRRGLSVQLANLEKvregLEKVLNELKKDFKQLLKDLDAALERL----EETLDKLRntPVEPAL 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 151 EEYKADAKLVLQF--KEEVQNLTSVLNELQEEIGAyDYDELQSRVSNLEERLRACMQKLA 208
Cdd:pfam04108 96 PPGEEKQKTLLDFidEDSVEILRDALKELIDELQA-AQESLDSDLKRFDDDLRDLQKELE 154
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
75-208 |
4.23e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 75 QLRQLLEKVQNMSQSIEVLDRRTQRdlqYVEKMENQMKGLESKFKQVEEshkqhlarqfkaIKAKMDELRPLIPVLEEYK 154
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEE---RIEELKKEIEELEEKVKELKE------------LKEKAEEYIKLSEFYEEYL 306
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 17136143 155 adaKLVLQFKEEVQNLTSVLNELQEEIGayDYDELQSRVSNLEERLRACMQKLA 208
Cdd:PRK03918 307 ---DELREIEKRLSRLEEEINGIEERIK--ELEEKEERLEELKKKLKELEKRLE 355
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
61-203 |
4.59e-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: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 61 APQQTMCSRDARTKQlrQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQvEESHKQHLARQFKAIKAKM 140
Cdd:pfam01576 57 AEAEEMRARLAARKQ--ELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE-EEAARQKLQLEKVTTEAKI 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 141 DELRPLIPVLEEykADAKLVLQFK---EEVQNLTSVLNElqEEIGAYDYDEL----QSRVSNLEERLRAC 203
Cdd:pfam01576 134 KKLEEDILLLED--QNSKLSKERKlleERISEFTSNLAE--EEEKAKSLSKLknkhEAMISDLEERLKKE 199
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
74-168 |
6.78e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 74 KQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVEESHKQHLAR-----QFKAIKAK---MDELRp 145
Cdd:PRK12704 86 KLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQElerisGLTAEEAKeilLEKVE- 164
|
90 100
....*....|....*....|....
gi 17136143 146 lipvlEEYKAD-AKLVLQFKEEVQ 168
Cdd:PRK12704 165 -----EEARHEaAVLIKEIEEEAK 183
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
73-208 |
1.07e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 73 TKQLRQLLEKVQNmSQsiEVLDRRTQRDLQY---VEKMENQMKGLESKFKQVEES------HKQHLARQFKAIKAKMDEL 143
Cdd:pfam01576 460 SKDVSSLESQLQD-TQ--ELLQEETRQKLNLstrLRQLEDERNSLQEQLEEEEEAkrnverQLSTLQAQLSDMKKKLEED 536
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17136143 144 RPLIPVLEEYKADAK-----LVLQFKE---EVQNLTSVLNELQEEIG--AYDYDELQSRVSNLEERLRACMQKLA 208
Cdd:pfam01576 537 AGTLEALEEGKKRLQreleaLTQQLEEkaaAYDKLEKTKNRLQQELDdlLVDLDHQRQLVSNLEKKQKKFDQMLA 611
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
74-198 |
1.35e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 74 KQLRQLLEKVQNMSQSIEVLDRRTQRD--LQYVeKMENqMKGLESKFKQVEESHKqhLARQFKAIKAKMDELRPLIPVLE 151
Cdd:COG4717 347 EELQELLREAEELEEELQLEELEQEIAalLAEA-GVED-EEELRAALEQAEEYQE--LKEELEELEEQLEELLGELEELL 422
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 17136143 152 EYKADAKL---VLQFKEEVQNLTSVLNELQEEIGaydydELQSRVSNLEE 198
Cdd:COG4717 423 EALDEEELeeeLEELEEELEELEEELEELREELA-----ELEAELEQLEE 467
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
71-200 |
1.83e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 71 ARTKQLRQLLEKVQNMSQSIEVLdrrtQRDLQYVEKMENQMKGLESKFKQVEES----HKQHLARQFKAIKAKMDELRPL 146
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGEIKSL----KKELEKLEELKKKLAELEKKLDELEEElaelLKELEELGFESVEELEERLKEL 597
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17136143 147 IPVLEEY------------------KADAKLVLQFKE------EVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERL 200
Cdd:PRK03918 598 EPFYNEYlelkdaekelereekelkKLEEELDKAFEElaetekRLEELRKELEELEKKYSEEEYEELREEYLELSREL 675
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
76-208 |
3.25e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 76 LRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKmenQMKGLESKFKQVEEshkqhLARQFKAIKAKMDELRPLIPVLEEyka 155
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEE---RIKELEEKEERLEE-----LKKKLKELEKRLEELEERHELYEE--- 366
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 17136143 156 daklVLQFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLA 208
Cdd:PRK03918 367 ----AKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
68-200 |
4.83e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 38.74 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 68 SRDARTKQLRQLLEKVQNMSQSIEVLdrRTQRDlqyveKMENQMKGLESKfkqveeshKQHLARQFKAIKAKMDELRpli 147
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEEL--KEKRD-----ELNEELKELAEK--------RDELNAQVKELREEAQELR--- 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17136143 148 pvlEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAY------------DYDELQSRVSNLEERL 200
Cdd:COG1340 64 ---EKRDELNEKVKELKEERDELNEKLNELREELDELrkelaelnkaggSIDKLRKEIERLEWRQ 125
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
77-208 |
5.18e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 77 RQLLEKVQNMSQSIEVLDRrTQRDlqyVEKMENQMKGLEskfkQVEESHkqhlaRQFKAIKAKMDELRPLIPVLEEYKAD 156
Cdd:COG4913 221 PDTFEAADALVEHFDDLER-AHEA---LEDAREQIELLE----PIRELA-----ERYAAARERLAELEYLRAALRLWFAQ 287
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 17136143 157 AKLVLQfKEEVQNLTSVLNELQEEIgaydyDELQSRVSNLEERLRACMQKLA 208
Cdd:COG4913 288 RRLELL-EAELEELRAELARLEAEL-----ERLEARLDALREELDELEAQIR 333
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
66-206 |
5.27e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.64 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 66 MCSRDARTK-QLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKG--------LESKFKQVEE--SHKQHLARQFK 134
Cdd:TIGR00606 682 VCQRVFQTEaELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGlapgrqsiIDLKEKEIPElrNKLQKVNRDIQ 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 135 AIKAKMDE----LRPLIPVLEEYK---ADAKLVLQFKEEVQN----LTSVLNELQEEIGAYDYDELQSRVSNLEERLRAC 203
Cdd:TIGR00606 762 RLKNDIEEqetlLGTIMPEEESAKvclTDVTIMERFQMELKDverkIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTV 841
|
...
gi 17136143 204 MQK 206
Cdd:TIGR00606 842 VSK 844
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
75-208 |
5.49e-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: 38.20 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136143 75 QLRQLLEKVQNMSQSIEVLDRRtqrdLQYVEKMENQMKGLESKFKQVEESHKQHLARQFKAIKAKMDELRPLipvLEeyk 154
Cdd:cd00176 34 SVEALLKKHEALEAELAAHEER----VEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQR---LE--- 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17136143 155 aDAKLVLQFKEEVQNLTSVLNELQEEIGAYDYD-------ELQSRVSNLEERLRACMQKLA 208
Cdd:cd00176 104 -EALDLQQFFRDADDLEQWLEEKEAALASEDLGkdlesveELLKKHKELEEELEAHEPRLK 163
|
|
| |
