|
Name |
Accession |
Description |
Interval |
E-value |
| OLF |
smart00284 |
Olfactomedin-like domains; |
200-450 |
2.43e-152 |
|
Olfactomedin-like domains;
Pssm-ID: 128580 Cd Length: 255 Bit Score: 432.72 E-value: 2.43e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 200 GKLTGISDPITIKTSG-SRFGSWMTDPLAPEG-ENKVWYMDSY-HNNRFVREYKSMADFMNTDNFTSHRLPHPWSGTGQV 276
Cdd:smart00284 1 GGLAGISKPVTLQTSWkGKSGAWMKDPLWNTTkKSLYWYMPLNtRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGTGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 277 VYNGSIYFNKYQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDENGLWAVYATNQNAGNIVISKLDP 356
Cdd:smart00284 81 VYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 357 NTLQSLQTWNTSYPKRSAGEAFIICGTLYVTN-GYSGGTKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYA 435
Cdd:smart00284 161 ATLTIENTWITTYNKRSASNAFMICGILYVTRsLGSKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPNDRKLYA 240
|
250
....*....|....*
gi 971422655 436 WNNGHQILYNVTLFH 450
Cdd:smart00284 241 WNNGHLVHYDIALKP 255
|
|
| OLF |
pfam02191 |
Olfactomedin-like domain; |
202-448 |
4.58e-138 |
|
Olfactomedin-like domain;
Pssm-ID: 460482 Cd Length: 246 Bit Score: 396.13 E-value: 4.58e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 202 LTGISDPITIKTSGSRFGSWMTDPLAPEgeNKVWYMDSYHNNRFVREYKSMADFMNTDNFTSHRLPHPWSGTGQVVYNGS 281
Cdd:pfam02191 1 LVSVSKPVTVKLSGGKYGAWMKDPLPPS--DKIYVTDRGTSGNTLREYASLDDFKNGSPSKKYKLPYPWQGTGHVVYNGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 282 IYFNKYQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDENGLWAVYATNQNAGNIVISKLDPNTLQS 361
Cdd:pfam02191 79 LYYNKYNSRNIVKYDLTTRTVAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLDPETLEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 362 LQTWNTSYPKRSAGEAFIICGTLYVTNGYSGG-TKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYAWNNGH 440
Cdd:pfam02191 159 EQTWNTSYPKRSAGNAFMVCGVLYAVRSVNTRrEEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLYAWDDGY 238
|
....*...
gi 971422655 441 QILYNVTL 448
Cdd:pfam02191 239 QVTYPVTF 246
|
|
| Noelin-1 |
pfam12308 |
Neurogenesis glycoprotein; This domain family is found in eukaryotes, and is approximately 100 ... |
28-124 |
2.82e-54 |
|
Neurogenesis glycoprotein; This domain family is found in eukaryotes, and is approximately 100 amino acids in length. The family is found in association with pfam02191. There are two conserved sequence motifs: SAQ and VQN. Noelin-1 is a glycoprotein which is secreted mainly by postmitotic neurogenic tissues in the developing central and peripheral nervous systems, first appearing after neural tube closure. It is likely that it forms large multimeric complexes.It has a divergent function in neurogenesis. In animal caps neuralized by expression of noggin, co-expression of Noelin-1 causes expression of neuronal differentiation markers several stages before neurogenesis normally occurs in this tissue. Finally, only secreted forms of the protein can activate sensory marker expression, while all forms of the protein can induce early neurogenesis.
Pssm-ID: 432468 [Multi-domain] Cd Length: 100 Bit Score: 176.51 E-value: 2.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 28 PEESWQVYSSAQDSEGRCICTVVAPQQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMRGLESK 107
Cdd:pfam12308 3 PEEGWQVYSSAQDPDGRCVCTVVAPAQDVCSRDPRSRQLRQLMEKVQNVSQSMEVLDLRTSRDLQYVRTTETLLKTLDSK 82
|
90
....*....|....*..
gi 971422655 108 FKQVEESHKQHLARQFK 124
Cdd:pfam12308 83 LKVAEANPQSLSARSFQ 99
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
64-189 |
5.27e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 5.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 64 KQLRQLLEKVQNMSQSIEVLDRR----TQRDLQyVEKMENQMRGLESKFKQVEEshkqhlarQFKAIKAKMEELRPLIPV 139
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELkeeiEELEKE-LESLEGSKRKLEEKIRELEE--------RIEELKKEIEELEEKVKE 284
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 971422655 140 LEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAYDYE--ELQNRVSNLEER 189
Cdd:PRK03918 285 LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEinGIEERIKELEEK 336
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
53-198 |
1.01e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 53 QQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRR---TQRDLQYVEKMEnQMRGLESKFKQVEEsHKQHLARQFKAIKAK 129
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAEleeLREELEKLEKLL-QLLPLYQELEALEA-ELAELPERLEELEER 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 971422655 130 MEELRPLIPVLEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAYDYEELQNRVSNLEERLRACMQKLA 198
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
60-190 |
1.35e-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: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 60 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQ-------MRGLESKFKQVE------ESHKQHLARQFKAI 126
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqilrerLANLERQLEELEaqleelESKLDELAEELAEL 342
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 971422655 127 KAKMEELRplipvlEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAY---------DYEELQNRVSNLEERL 190
Cdd:TIGR02168 343 EEKLEELK------EELESLEAELEELEAELEELESRLEELEEQLETLrskvaqlelQIASLNNEIERLEARL 409
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
64-209 |
9.78e-05 |
|
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: 44.84 E-value: 9.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 64 KQLRQLLEKVQNMSQSIevldrRTQRDL--QYVEKMENQMRGLESKFKQVEE--SHKQHLA--RQFKAIKAKMEELRPLI 137
Cdd:pfam06160 121 EEVEELKDKYRELRKTL-----LANRFSygPAIDELEKQLAEIEEEFSQFEEltESGDYLEarEVLEKLEEETDALEELM 195
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 971422655 138 PVLEEYKADAKLVlqFKEEVQNLTSVLNELQEEIGAYDYEELQNRVSNLEERLRACMQKLACGKLTGISDPI 209
Cdd:pfam06160 196 EDIPPLYEELKTE--LPDQLEELKEGYREMEEEGYALEHLNVDKEIQQLEEQLEENLALLENLELDEAEEAL 265
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
64-158 |
7.48e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 64 KQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMRGLESKFKQVEESHKQHLAR-----QFKAIKAK---MEELRp 135
Cdd:PRK12704 86 KLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQElerisGLTAEEAKeilLEKVE- 164
|
90 100
....*....|....*....|....
gi 971422655 136 lipvlEEYKAD-AKLVLQFKEEVQ 158
Cdd:PRK12704 165 -----EEARHEaAVLIKEIEEEAK 183
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
60-170 |
8.22e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 8.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 60 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMRGLESKFKQVEESHKQhLARQFKAIKAKMEELRPLIPV 139
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE-LQSEIAEREEELKELEEQLES 161
|
90 100 110
....*....|....*....|....*....|.
gi 971422655 140 LEEYKADAKLVLQfKEEVQNLTSVLNELQEE 170
Cdd:COG4372 162 LQEELAALEQELQ-ALSEAEAEQALDELLKE 191
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
65-198 |
1.21e-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: 40.12 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 65 QLRQLLEKVQNMSQSIEVLDRRtqrdLQYVEKMENQMRGLESKFKQVEESHKQHLARQFKAIKAKMEELRPLipvLEeyk 144
Cdd:cd00176 34 SVEALLKKHEALEAELAAHEER----VEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQR---LE--- 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 971422655 145 aDAKLVLQFKEEVQNLTSVLNELQEEIGAYDY-------EELQNRVSNLEERLRACMQKLA 198
Cdd:cd00176 104 -EALDLQQFFRDADDLEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLK 163
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
226-358 |
4.58e-03 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 38.85 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 226 LAPEGENKVWYMDSYHNN--RFVREyksmadfmnTDNFTSHRLPhPWSGTGQVVY--NGSIYFNKYQSHIIIRFDLKTET 301
Cdd:COG4257 22 VAVDPDGAVWFTDQGGGRigRLDPA---------TGEFTEYPLG-GGSGPHGIAVdpDGNLWFTDNGNNRIGRIDPKTGE 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 971422655 302 IlktRSLDYAGynnmyhyawGGHSDIDLMVDENGlwAVYATNQNAGniVISKLDPNT 358
Cdd:COG4257 92 I---TTFALPG---------GGSNPHGIAFDPDG--NLWFTDQGGN--RIGRLDPAT 132
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
22-181 |
9.81e-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: 38.49 E-value: 9.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 22 QVLPTNPEESWQVYSSAQDSEGRCICTvvapQQTMCSRDARTKQLRQLLEKVQNMSQSIEVLD--------RRTQRD--- 90
Cdd:TIGR00606 210 KYLKQYKEKACEIRDQITSKEAQLESS----REIVKSYENELDPLKNRLKEIEHNLSKIMKLDneikalksRKKQMEkdn 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 91 LQYVEKMENQMRGLESKFKQVEESHKqhlarqfKAIKAKMEELRPLIPVLEEYKADAKLVLQFKEEVQNLTSVL----NE 166
Cdd:TIGR00606 286 SELELKMEKVFQGTDEQLNDLYHNHQ-------RTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLqlqaDR 358
|
170
....*....|....*
gi 971422655 167 LQEEIGAYDYEELQN 181
Cdd:TIGR00606 359 HQEHIRARDSLIQSL 373
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| OLF |
smart00284 |
Olfactomedin-like domains; |
200-450 |
2.43e-152 |
|
Olfactomedin-like domains;
Pssm-ID: 128580 Cd Length: 255 Bit Score: 432.72 E-value: 2.43e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 200 GKLTGISDPITIKTSG-SRFGSWMTDPLAPEG-ENKVWYMDSY-HNNRFVREYKSMADFMNTDNFTSHRLPHPWSGTGQV 276
Cdd:smart00284 1 GGLAGISKPVTLQTSWkGKSGAWMKDPLWNTTkKSLYWYMPLNtRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGTGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 277 VYNGSIYFNKYQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDENGLWAVYATNQNAGNIVISKLDP 356
Cdd:smart00284 81 VYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 357 NTLQSLQTWNTSYPKRSAGEAFIICGTLYVTN-GYSGGTKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYA 435
Cdd:smart00284 161 ATLTIENTWITTYNKRSASNAFMICGILYVTRsLGSKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPNDRKLYA 240
|
250
....*....|....*
gi 971422655 436 WNNGHQILYNVTLFH 450
Cdd:smart00284 241 WNNGHLVHYDIALKP 255
|
|
| OLF |
pfam02191 |
Olfactomedin-like domain; |
202-448 |
4.58e-138 |
|
Olfactomedin-like domain;
Pssm-ID: 460482 Cd Length: 246 Bit Score: 396.13 E-value: 4.58e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 202 LTGISDPITIKTSGSRFGSWMTDPLAPEgeNKVWYMDSYHNNRFVREYKSMADFMNTDNFTSHRLPHPWSGTGQVVYNGS 281
Cdd:pfam02191 1 LVSVSKPVTVKLSGGKYGAWMKDPLPPS--DKIYVTDRGTSGNTLREYASLDDFKNGSPSKKYKLPYPWQGTGHVVYNGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 282 IYFNKYQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDENGLWAVYATNQNAGNIVISKLDPNTLQS 361
Cdd:pfam02191 79 LYYNKYNSRNIVKYDLTTRTVAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLDPETLEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 362 LQTWNTSYPKRSAGEAFIICGTLYVTNGYSGG-TKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYAWNNGH 440
Cdd:pfam02191 159 EQTWNTSYPKRSAGNAFMVCGVLYAVRSVNTRrEEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLYAWDDGY 238
|
....*...
gi 971422655 441 QILYNVTL 448
Cdd:pfam02191 239 QVTYPVTF 246
|
|
| Noelin-1 |
pfam12308 |
Neurogenesis glycoprotein; This domain family is found in eukaryotes, and is approximately 100 ... |
28-124 |
2.82e-54 |
|
Neurogenesis glycoprotein; This domain family is found in eukaryotes, and is approximately 100 amino acids in length. The family is found in association with pfam02191. There are two conserved sequence motifs: SAQ and VQN. Noelin-1 is a glycoprotein which is secreted mainly by postmitotic neurogenic tissues in the developing central and peripheral nervous systems, first appearing after neural tube closure. It is likely that it forms large multimeric complexes.It has a divergent function in neurogenesis. In animal caps neuralized by expression of noggin, co-expression of Noelin-1 causes expression of neuronal differentiation markers several stages before neurogenesis normally occurs in this tissue. Finally, only secreted forms of the protein can activate sensory marker expression, while all forms of the protein can induce early neurogenesis.
Pssm-ID: 432468 [Multi-domain] Cd Length: 100 Bit Score: 176.51 E-value: 2.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 28 PEESWQVYSSAQDSEGRCICTVVAPQQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMRGLESK 107
Cdd:pfam12308 3 PEEGWQVYSSAQDPDGRCVCTVVAPAQDVCSRDPRSRQLRQLMEKVQNVSQSMEVLDLRTSRDLQYVRTTETLLKTLDSK 82
|
90
....*....|....*..
gi 971422655 108 FKQVEESHKQHLARQFK 124
Cdd:pfam12308 83 LKVAEANPQSLSARSFQ 99
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
64-189 |
5.27e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 5.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 64 KQLRQLLEKVQNMSQSIEVLDRR----TQRDLQyVEKMENQMRGLESKFKQVEEshkqhlarQFKAIKAKMEELRPLIPV 139
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELkeeiEELEKE-LESLEGSKRKLEEKIRELEE--------RIEELKKEIEELEEKVKE 284
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 971422655 140 LEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAYDYE--ELQNRVSNLEER 189
Cdd:PRK03918 285 LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEinGIEERIKELEEK 336
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
53-198 |
1.01e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 53 QQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRR---TQRDLQYVEKMEnQMRGLESKFKQVEEsHKQHLARQFKAIKAK 129
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAEleeLREELEKLEKLL-QLLPLYQELEALEA-ELAELPERLEELEER 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 971422655 130 MEELRPLIPVLEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAYDYEELQNRVSNLEERLRACMQKLA 198
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
60-192 |
2.01e-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: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 60 DARTKQLRQLLEK----VQNMSQSIEVLDRRTQRDLQYVEKMENQMRGLESKFKQVE---ESHKQHL-----ARQFKAIK 127
Cdd:COG1579 16 DSELDRLEHRLKElpaeLAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEariKKYEEQLgnvrnNKEYEALQ 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 971422655 128 AKMEELRPLIPVLEEykadakLVLQFKEEVQNLTSVLNELQEEIgaydyEELQNRVSNLEERLRA 192
Cdd:COG1579 96 KEIESLKRRISDLED------EILELMERIEELEEELAELEAEL-----AELEAELEEKKAELDE 149
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
60-133 |
2.39e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.17 E-value: 2.39e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 971422655 60 DARTKQLRQLLEKVQNmsqSIEVLDRRTQRDLQYVEKMENQMRGlESKFKQVEESHKQHLARQFKAIKAKMEEL 133
Cdd:pfam01576 888 EARIAQLEEELEEEQS---NTELLNDRLRKSTLQVEQLTTELAA-ERSTSQKSESARQQLERQNKELKAKLQEM 957
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
60-190 |
1.35e-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: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 60 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQ-------MRGLESKFKQVE------ESHKQHLARQFKAI 126
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqilrerLANLERQLEELEaqleelESKLDELAEELAEL 342
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 971422655 127 KAKMEELRplipvlEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAY---------DYEELQNRVSNLEERL 190
Cdd:TIGR02168 343 EEKLEELK------EELESLEAELEELEAELEELESRLEELEEQLETLrskvaqlelQIASLNNEIERLEARL 409
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
66-197 |
1.36e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.59 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 66 LRQLLEKVQNMSQSIEVLDRrtQRDLqyvekMENQMRGLESKFKQVEESHKQHLARQFKAIKAKMEELRPLIPVLEEYKA 145
Cdd:PLN02939 245 LKAELIEVAETEERVFKLEK--ERSL-----LDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVE 317
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 971422655 146 DAKLVLQFKEEVQNLTSVLNELQEEIGAYDY-----EELQNRVSNLEERLRACMQKL 197
Cdd:PLN02939 318 KAALVLDQNQDLRDKVDKLEASLKEANVSKFssykvELLQQKLKLLEERLQASDHEI 374
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
58-191 |
1.61e-05 |
|
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: 47.37 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 58 SRDARTKQL--RQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMRGLESKFKQVEESHK------QHLARQFKAIKAK 129
Cdd:TIGR02169 659 SRAPRGGILfsRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGeiekeiEQLEQEEEKLKER 738
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 130 MEELRPLIPVLEEYKADAKLVLQ-FKEEVQNLTSVLNELQEEIGA-YD------YEELQNRVSNLEERLR 191
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKeLEARIEELEEDLHKLEEALNDlEArlshsrIPEIQAELSKLEEEVS 808
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
53-197 |
2.40e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 53 QQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMRGLESKFKQVEESHKQhLARQFKAIKAKMEE 132
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQ-AQEELESLQEEAEE 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 971422655 133 LRPLIpvlEEYKADAKlvlQFKEEVQNLTSVLNELQEEIGAYDYE--ELQNRVSNLEERLRACMQKL 197
Cdd:COG4372 113 LQEEL---EELQKERQ---DLEQQRKQLEAQIAELQSEIAEREEElkELEEQLESLQEELAALEQEL 173
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
61-190 |
3.56e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 61 ARTKQLRQLLEKVQNMSQSIEVLdrrtQRDLQYVEKMENQMRGLESKFKQVEES----HKQHLARQFKAIKAKMEELRPL 136
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGEIKSL----KKELEKLEELKKKLAELEKKLDELEEElaelLKELEELGFESVEELEERLKEL 597
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 971422655 137 IPVLEEY------------------KADAKLVLQFKE------EVQNLTSVLNELQEEIGAYDYEELQNRVSNLEERL 190
Cdd:PRK03918 598 EPFYNEYlelkdaekelereekelkKLEEELDKAFEElaetekRLEELRKELEELEKKYSEEEYEELREEYLELSREL 675
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
58-191 |
4.09e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 58 SRDARTKQLRQLL-----EKV-QNMSQSIEVLDRRTQRDLQYVEKMENqmrgLESKFKQVEEShkqhLARQFKAIKAKME 131
Cdd:PRK03918 143 SDESREKVVRQILglddyENAyKNLGEVIKEIKRRIERLEKFIKRTEN----IEELIKEKEKE----LEEVLREINEISS 214
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 132 ELRPLIPVLEEYKADaklvlqfKEEVQNLTSVLNELQEEIgaydyEELQNRVSNLEERLR 191
Cdd:PRK03918 215 ELPELREELEKLEKE-------VKELEELKEEIEELEKEL-----ESLEGSKRKLEEKIR 262
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
64-198 |
4.89e-05 |
|
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: 44.53 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 64 KQLRQLLEkVQNMSQSIEVLDRRTQRDLQYVEKMENQMRGLESKFKQVEESHKQhLARQFKAIKAKMEELRPLIPVLE-- 141
Cdd:COG1579 4 EDLRALLD-LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED-LEKEIKRLELEIEEVEARIKKYEeq 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 971422655 142 --------EYKADAKLVLQFKEEVQNLTSVLNELQEEIgaydyEELQNRVSNLEERLRACMQKLA 198
Cdd:COG1579 82 lgnvrnnkEYEALQKEIESLKRRISDLEDEILELMERI-----EELEEELAELEAELAELEAELE 141
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
64-209 |
9.78e-05 |
|
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: 44.84 E-value: 9.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 64 KQLRQLLEKVQNMSQSIevldrRTQRDL--QYVEKMENQMRGLESKFKQVEE--SHKQHLA--RQFKAIKAKMEELRPLI 137
Cdd:pfam06160 121 EEVEELKDKYRELRKTL-----LANRFSygPAIDELEKQLAEIEEEFSQFEEltESGDYLEarEVLEKLEEETDALEELM 195
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 971422655 138 PVLEEYKADAKLVlqFKEEVQNLTSVLNELQEEIGAYDYEELQNRVSNLEERLRACMQKLACGKLTGISDPI 209
Cdd:pfam06160 196 EDIPPLYEELKTE--LPDQLEELKEGYREMEEEGYALEHLNVDKEIQQLEEQLEENLALLENLELDEAEEAL 265
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
65-198 |
1.54e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 65 QLRQLLEKVQNMSQSIEVLDRRTQRdlqYVEKMENQMRGLESKFKQVEEshkqhlarqfkaIKAKMEELRPLIPVLEEYK 144
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEE---RIEELKKEIEELEEKVKELKE------------LKEKAEEYIKLSEFYEEYL 306
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 971422655 145 adaKLVLQFKEEVQNLTSVLNELQEEIGayDYEELQNRVSNLEERLRACMQKLA 198
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 ... |
51-193 |
2.47e-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: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 51 APQQTMCSRDARTKQlrQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMRGLESKFKQvEESHKQHLARQFKAIKAKM 130
Cdd:pfam01576 57 AEAEEMRARLAARKQ--ELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE-EEAARQKLQLEKVTTEAKI 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 131 EELRPLIPVLEEykADAKLVLQFK---EEVQNLTSVLNElqEEIGAYDYEELQNR----VSNLEERLRAC 193
Cdd:pfam01576 134 KKLEEDILLLED--QNSKLSKERKlleERISEFTSNLAE--EEEKAKSLSKLKNKheamISDLEERLKKE 199
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
60-196 |
3.26e-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: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 60 DARTKQLRQLLE---KVQNMSQSIEVLDRRTQRDLQYVEKMENQMRGLESKFKQVEESHKQHLARQFKAIKAKMEELRPL 136
Cdd:COG4913 671 AELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 137 ipvLEEYKADAKLVLQFKEEVQNLTSvlnelqeeigayDYEELQNRVSNLEERLRACMQK 196
Cdd:COG4913 751 ---LEERFAAALGDAVERELRENLEE------------RIDALRARLNRAEEELERAMRA 795
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
59-197 |
3.82e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 59 RDARTKQLRQLLEKVQNMSQSIEVLDRRtqrdLQYVEKMENQMRGLESKFKQVEE--SHKQHLARQFKAIKAKMEELRPL 136
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEER----IKELEEKEERLEELKKKLKELEKrlEELEERHELYEEAKAKKEELERL 377
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 971422655 137 IPVLEEYKADaklvlQFKEEVQNLTSVLNELQEEIgaydyEELQNRVSNLE---ERLRACMQKL 197
Cdd:PRK03918 378 KKRLTGLTPE-----KLEKELEELEKAKEEIEEEI-----SKITARIGELKkeiKELKKAIEEL 431
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
67-192 |
5.07e-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: 42.70 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 67 RQLLEKVQnmsqSIEVLDRRTQRDLQYVEKMENQMRGLESKFKQVEESHKQhLARQFKAIKAKMEELrplipvLEEYKAD 146
Cdd:TIGR04523 363 RELEEKQN----EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ-KDEQIKKLQQEKELL------EKEIERL 431
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 971422655 147 AKLVLQFKEEVQNLTSVLNELQEEigaydYEELQNRVSNLEERLRA 192
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELI-----IKNLDNTRESLETQLKV 472
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
64-158 |
7.48e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 64 KQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMRGLESKFKQVEESHKQHLAR-----QFKAIKAK---MEELRp 135
Cdd:PRK12704 86 KLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQElerisGLTAEEAKeilLEKVE- 164
|
90 100
....*....|....*....|....
gi 971422655 136 lipvlEEYKAD-AKLVLQFKEEVQ 158
Cdd:PRK12704 165 -----EEARHEaAVLIKEIEEEAK 183
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
60-170 |
8.22e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 8.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 60 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMRGLESKFKQVEESHKQhLARQFKAIKAKMEELRPLIPV 139
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE-LQSEIAEREEELKELEEQLES 161
|
90 100 110
....*....|....*....|....*....|.
gi 971422655 140 LEEYKADAKLVLQfKEEVQNLTSVLNELQEE 170
Cdd:COG4372 162 LQEELAALEQELQ-ALSEAEAEQALDELLKE 191
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
60-188 |
1.14e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 60 DARTKQLRQLLEKVQNMsqsievldRRTQRDLQYVEKMENQMRGLESKFKQ--VEESHKQhlARQFKAIKAKMEELRPLI 137
Cdd:PRK03918 472 EEKERKLRKELRELEKV--------LKKESELIKLKELAEQLKELEEKLKKynLEELEKK--AEEYEKLKEKLIKLKGEI 541
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 971422655 138 PVL-------EEYKADAKLVLQFKEEVQN-LTSVLNELqEEIGAYDYEELQNRVSNLEE 188
Cdd:PRK03918 542 KSLkkeleklEELKKKLAELEKKLDELEEeLAELLKEL-EELGFESVEELEERLKELEP 599
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
65-198 |
1.21e-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: 40.12 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 65 QLRQLLEKVQNMSQSIEVLDRRtqrdLQYVEKMENQMRGLESKFKQVEESHKQHLARQFKAIKAKMEELRPLipvLEeyk 144
Cdd:cd00176 34 SVEALLKKHEALEAELAAHEER----VEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQR---LE--- 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 971422655 145 aDAKLVLQFKEEVQNLTSVLNELQEEIGAYDY-------EELQNRVSNLEERLRACMQKLA 198
Cdd:cd00176 104 -EALDLQQFFRDADDLEQWLEEKEAALASEDLgkdlesvEELLKKHKELEEELEAHEPRLK 163
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
66-198 |
1.41e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 66 LRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKmenQMRGLESKFKQVEEshkqhlarqfkaIKAKMEELRPLIPVLEEYKA 145
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEE---RIKELEEKEERLEE------------LKKKLKELEKRLEELEERHE 362
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 971422655 146 DAKLVLQFKEEVQNLTSVLNELQEEIGAYDYEELQNRVSNLEERLRACMQKLA 198
Cdd:PRK03918 363 LYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
60-198 |
1.42e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 60 DARTKQLRQLLEKVQNmsqsiEVLDRRTQrdlqY---VEKMENQMRGLESKFKQVEE-----------SHKQHLARQFKA 125
Cdd:PRK04778 139 REEVEQLKDLYRELRK-----SLLANRFS----FgpaLDELEKQLENLEEEFSQFVEltesgdyvearEILDQLEEELAA 209
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 971422655 126 IKAKMEELRPLIpvleeykadAKLVLQFKEEVQNLTSVLNELQEEigAYDYEELQ--NRVSNLEERLRACMQKLA 198
Cdd:PRK04778 210 LEQIMEEIPELL---------KELQTELPDQLQELKAGYRELVEE--GYHLDHLDieKEIQDLKEQIDENLALLE 273
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
64-194 |
1.55e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 64 KQLRQLLEKVQNMSQSIEVLDrrtqrdlqyVEKMENQMRGLESK--------------FKQVEESHK------QHLARQF 123
Cdd:PRK04778 256 KEIQDLKEQIDENLALLEELD---------LDEAEEKNEEIQERidqlydilerevkaRKYVEKNSDtlpdflEHAKEQN 326
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 971422655 124 KAIKAKMEELRplipvlEEYK---ADAKLVLQFKEEVQNLTSVLNELQEEIGAYD--YEELQNRVSNLEERLRACM 194
Cdd:PRK04778 327 KELKEEIDRVK------QSYTlneSELESVRQLEKQLESLEKQYDEITERIAEQEiaYSELQEELEEILKQLEEIE 396
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
85-188 |
1.98e-03 |
|
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: 40.81 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 85 RRTQRDLQYVEKME--NQMRGLESKFKQVEESHKQhLARQFKAIKAKMEELRPLIPVLEEYKADAklvlqfKEEVQNLTS 162
Cdd:TIGR02168 223 RELELALLVLRLEElrEELEELQEELKEAEEELEE-LTAELQELEEKLEELRLEVSELEEEIEEL------QKELYALAN 295
|
90 100
....*....|....*....|....*.
gi 971422655 163 VLNELQEEIGAYDyEELQNRVSNLEE 188
Cdd:TIGR02168 296 EISRLEQQKQILR-ERLANLERQLEE 320
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
56-196 |
2.04e-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: 40.80 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 56 MCSRDARTK-QLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMRG--------LESKFKQVEE--SHKQHLARQFK 124
Cdd:TIGR00606 682 VCQRVFQTEaELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGlapgrqsiIDLKEKEIPElrNKLQKVNRDIQ 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 125 AIKAKMEE----LRPLIPVLEEYK---ADAKLVLQFKEEVQN----LTSVLNELQEEIGAYDYEELQNRVSNLEERLRAC 193
Cdd:TIGR00606 762 RLKNDIEEqetlLGTIMPEEESAKvclTDVTIMERFQMELKDverkIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTV 841
|
...
gi 971422655 194 MQK 196
Cdd:TIGR00606 842 VSK 844
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
64-188 |
2.39e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 64 KQLRQLLEKVQNMSQSIEVLDRRTQRD--LQY--VEKMEnqmrGLESKFKQVEESHKqhLARQFKAIKAKMEELRPLIPV 139
Cdd:COG4717 347 EELQELLREAEELEEELQLEELEQEIAalLAEagVEDEE----ELRAALEQAEEYQE--LKEELEELEEQLEELLGELEE 420
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 971422655 140 LEEYKADAKL---VLQFKEEVQNLTSVLNELQEEIGaydyeELQNRVSNLEE 188
Cdd:COG4717 421 LLEALDEEELeeeLEELEEELEELEEELEELREELA-----ELEAELEQLEE 467
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
64-190 |
2.43e-03 |
|
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: 40.44 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 64 KQLRQLLEKVQNMSQSIEVLDRRtQRDLQY-VEKMENQMRGLESKFKQVE---ESHKQHLARQFKAIKAKMEELR---PL 136
Cdd:TIGR02169 861 GKKEELEEELEELEAALRDLESR-LGDLKKeRDELEAQLRELERKIEELEaqiEKKRKRLSELKAKLEALEEELSeieDP 939
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 971422655 137 IPVLEEYKADAKLVLQFKEEVQnltsvlnELQEEIGAY---------DYEELQNRVSNLEERL 190
Cdd:TIGR02169 940 KGEDEEIPEEELSLEDVQAELQ-------RVEEEIRALepvnmlaiqEYEEVLKRLDELKEKR 995
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
60-190 |
3.64e-03 |
|
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: 40.05 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 60 DARTKQLRQLLEKVQNMSQSIEVLDRRTQrdlqyVEKMENQMRGLESKFKQVEEShKQHLARQFKAIKAKMEELRPLIPV 139
Cdd:TIGR02169 764 EARIEELEEDLHKLEEALNDLEARLSHSR-----IPEIQAELSKLEEEVSRIEAR-LREIEQKLNRLTLEKEYLEKEIQE 837
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 971422655 140 LEEYKADAKL-VLQFKEEVQNLTSVLNELQEEIgaydyEELQNRVSNLEERL 190
Cdd:TIGR02169 838 LQEQRIDLKEqIKSIEKEIENLNGKKEELEEEL-----EELEAALRDLESRL 884
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
67-198 |
3.81e-03 |
|
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: 39.29 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 67 RQLLEKVQNMSQSIEVLDRRTQRDLQYVEK----MENQMRGLESKFKQVEESHKQHLARQfkaiKAKMEELR--PLIPVL 140
Cdd:pfam04108 20 RSLLEELVVLLAKIAFLRRGLSVQLANLEKvregLEKVLNELKKDFKQLLKDLDAALERL----EETLDKLRntPVEPAL 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 141 EEYKADAKLVLQF--KEEVQNLTSVLNELQEEIGAyDYEELQNRVSNLEERLRACMQKLA 198
Cdd:pfam04108 96 PPGEEKQKTLLDFidEDSVEILRDALKELIDELQA-AQESLDSDLKRFDDDLRDLQKELE 154
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
226-358 |
4.58e-03 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 38.85 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 226 LAPEGENKVWYMDSYHNN--RFVREyksmadfmnTDNFTSHRLPhPWSGTGQVVY--NGSIYFNKYQSHIIIRFDLKTET 301
Cdd:COG4257 22 VAVDPDGAVWFTDQGGGRigRLDPA---------TGEFTEYPLG-GGSGPHGIAVdpDGNLWFTDNGNNRIGRIDPKTGE 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 971422655 302 IlktRSLDYAGynnmyhyawGGHSDIDLMVDENGlwAVYATNQNAGniVISKLDPNT 358
Cdd:COG4257 92 I---TTFALPG---------GGSNPHGIAFDPDG--NLWFTDQGGN--RIGRLDPAT 132
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
89-197 |
6.58e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 89 RDLQYVEKMENQMRGLESKFKQveESHKQHLARQFKAIKAKMEE-LRPLIPVLEEYKADAKLVLQFKEEVQNLtsvLNEL 167
Cdd:COG4717 344 DRIEELQELLREAEELEEELQL--EELEQEIAALLAEAGVEDEEeLRAALEQAEEYQELKEELEELEEQLEEL---LGEL 418
|
90 100 110
....*....|....*....|....*....|
gi 971422655 168 QEEIGAYDYEELQNRVSNLEERLRACMQKL 197
Cdd:COG4717 419 EELLEALDEEELEEELEELEEELEELEEEL 448
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
22-181 |
9.81e-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: 38.49 E-value: 9.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 22 QVLPTNPEESWQVYSSAQDSEGRCICTvvapQQTMCSRDARTKQLRQLLEKVQNMSQSIEVLD--------RRTQRD--- 90
Cdd:TIGR00606 210 KYLKQYKEKACEIRDQITSKEAQLESS----REIVKSYENELDPLKNRLKEIEHNLSKIMKLDneikalksRKKQMEkdn 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971422655 91 LQYVEKMENQMRGLESKFKQVEESHKqhlarqfKAIKAKMEELRPLIPVLEEYKADAKLVLQFKEEVQNLTSVL----NE 166
Cdd:TIGR00606 286 SELELKMEKVFQGTDEQLNDLYHNHQ-------RTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLqlqaDR 358
|
170
....*....|....*
gi 971422655 167 LQEEIGAYDYEELQN 181
Cdd:TIGR00606 359 HQEHIRARDSLIQSL 373
|
|
| |
