|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
69-363 |
1.24e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 69 QLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELETEsw 148
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE-- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 149 nlkyqmlEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDIDSSSEMVEV 228
Cdd:COG1196 353 -------LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 229 LALETEELRRKVDGPRSESISDREDMHEEIEILKAKVAELMKEKEEMTDQLLATSVERGRSLIADTPSLADELAGGDSSQ 308
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1831508208 309 LLDALREQEICNQKLRVYINGILMRVIERHPEILEIGEEGILSKLTVRRRISVLA 363
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA 560
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
59-279 |
1.67e-07 |
|
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: 53.91 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 59 ALNDFSSQMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSD------EKARGTE 132
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEisrleqQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 133 SMSRLKRE-KELETESWNLKYQM--LEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFR 209
Cdd:TIGR02168 310 RLANLERQlEELEAQLEELESKLdeLAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 210 KFKEEAQQ----------DIDSSSEMVEVLALETEELRRKVDGPRSESISDR-EDMHEEIEILKAKVAELMKEKEEMTDQ 278
Cdd:TIGR02168 390 QLELQIASlnneierleaRLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREE 469
|
.
gi 1831508208 279 L 279
Cdd:TIGR02168 470 L 470
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
69-317 |
2.26e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 69 QLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELETESw 148
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 149 nlkyQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDIDSSSEMVEV 228
Cdd:COG1196 305 ----ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 229 LALETEELRRKVDGpRSESISDREDMHEEIEILKAKVAELMKEKEEMTDQLLATSVERGRSLIADTPSLADELAGGDSSQ 308
Cdd:COG1196 381 LEELAEELLEALRA-AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
....*....
gi 1831508208 309 LLDALREQE 317
Cdd:COG1196 460 ALLELLAEL 468
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
90-323 |
3.30e-07 |
|
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: 53.14 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 90 ERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDekargTESMSRLKREKELETESWNLKYQMLEKDLISVKKDAERS 169
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEE-----LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 170 NEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDIDSSSEMVEVLALETEELRRKVDG-----PR 244
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERlesleRR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 245 SESISDR--------EDMHEEIEILKAKVAELMKEKEEMTDQL-----LATSVERGRSLIADTPSLADELAGGDSSQLLD 311
Cdd:TIGR02168 833 IAATERRledleeqiEELSEDIESLAAEIEELEELIEELESELeallnERASLEEALALLRSELEELSEELRELESKRSE 912
|
250
....*....|..
gi 1831508208 312 ALREQEICNQKL 323
Cdd:TIGR02168 913 LRRELEELREKL 924
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
57-302 |
4.10e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 57 QDALNDFSSQMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSR 136
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 137 LKREKELETESwnlkyQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKF---KE 213
Cdd:COG1196 364 EEALLEAEAEL-----AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELeeeEE 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 214 EAQQDIDSSSEMVEVLALETEELRRKVDGPRSESISDREDMHEEIEILKAKVAELMKEKEEMTDQLLATSVERGRSLIAD 293
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
....*....
gi 1831508208 294 TPSLADELA 302
Cdd:COG1196 519 LRGLAGAVA 527
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
68-301 |
7.36e-07 |
|
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: 51.99 E-value: 7.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 68 NQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLK--------- 138
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaeiaslers 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 139 -REKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQllvEGMEEERIQLERQFRKFKeEAQQ 217
Cdd:TIGR02169 310 iAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK---EELEDLRAELEEVDKEFA-ETRD 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 218 DIDSSSEMVEVLALETEELRRKVDGPRSESI---SDREDMHEEIEILKAKVAELMKEKEEMTDQlLATSVERGRSLIADT 294
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRELDRLQEELQrlsEELADLNAAIAGIEAKINELEEEKEDKALE-IKKQEWKLEQLAADL 464
|
....*..
gi 1831508208 295 PSLADEL 301
Cdd:TIGR02169 465 SKYEQEL 471
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
86-281 |
1.47e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 50.80 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 86 SLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELETeswnlkyqmLEKDLISVKKD 165
Cdd:pfam05667 280 LLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQREEELEE---------LQEQLEDLESS 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 166 AERSNEETKRIRNELEKTENKLEEaqllvegMEEERIQLERQFRKFK-------------EEAQQDIDSSSEMVEVLALE 232
Cdd:pfam05667 351 IQELEKEIKKLESSIKQVEEELEE-------LKEQNEELEKQYKVKKktldllpdaeeniAKLQALVDASAQRLVELAGQ 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1831508208 233 TEELR-------RKVDGPRSESISDREDMHEEIEILKAK---VAELMKEKEEMTDQLLA 281
Cdd:pfam05667 424 WEKHRvplieeyRALKEAKSNKEDESQRKLEEIKELREKikeVAEEAKQKEELYKQLVA 482
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
95-274 |
2.41e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 95 KTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESmSRLKREKELETESWNLKYQMLEKDLISVKKDAE--RSNEE 172
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE-ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkKAEEE 1631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 173 TKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFK------EEAQQDIDSSSEMVEVLALETEELRR--KVDGPR 244
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEedkkkaEEAKKAEEDEKKAAEALKKEAEEAKKaeELKKKE 1711
|
170 180 190
....*....|....*....|....*....|
gi 1831508208 245 SESISDREDMHEEIEILKAKVAELMKEKEE 274
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
79-279 |
4.58e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 79 ELEERNMSLSDERTRLKTENSVLKERMHNLEEQltdNEDRFKQLLSDEKARGTESMSRLKREKELETESWNLKYQMLEKD 158
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE---KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 159 LISVKKDAE----------RSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLErQFRKFKEEAQQDIDSSSEMVEV 228
Cdd:PTZ00121 1649 AEELKKAEEenkikaaeeaKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE-ELKKKEAEEKKKAEELKKAEEE 1727
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1831508208 229 LALETEELRRKVDGPRSESISDREDMHEeieilKAKVAELMKEKEEMTDQL 279
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEEAKKDEEE-----KKKIAHLKKEEEKKAEEI 1773
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
75-288 |
4.70e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 75 KRYSELEERNMSLSD-ERTRLKTENSV--LKERMHNLEEQLTDNEDRFKQLlsDEKARGTESMsrlkREKELETESWNLK 151
Cdd:PRK03918 228 KEVKELEELKEEIEElEKELESLEGSKrkLEEKIRELEERIEELKKEIEEL--EEKVKELKEL----KEKAEEYIKLSEF 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 152 YQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEaqllVEGMEEERIQLERQFRKFKEEAQQdidssSEMVEVLAL 231
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER----LEELKKKLKELEKRLEELEERHEL-----YEEAKAKKE 372
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1831508208 232 ETEELRRKVDGprsesisdredmhEEIEILKAKVAELMKEKEEMTDQLLATSVERGR 288
Cdd:PRK03918 373 ELERLKKRLTG-------------LTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
75-220 |
1.02e-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: 46.84 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 75 KRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKargtESMSRLKREKELETESWNLK-YQ 153
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE----EVEARIKKYEEQLGNVRNNKeYE 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831508208 154 MLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDID 220
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
102-221 |
1.10e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 102 KERMHNLEEQLTDNEDRF--KQLLSDEKARGTESMSRL----KREKELETEswnlkYQMLEKDLISVKkDAERSNEETKR 175
Cdd:PRK04863 279 NERRVHLEEALELRRELYtsRRQLAAEQYRLVEMARELaelnEAESDLEQD-----YQAASDHLNLVQ-TALRQQEKIER 352
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1831508208 176 IRNELEKTENKLEEAQLLVEGMEEERIQLERQfrkfKEEAQQDIDS 221
Cdd:PRK04863 353 YQADLEELEERLEEQNEVVEEADEQQEENEAR----AEAAEEEVDE 394
|
|
| RBD-FIP |
pfam09457 |
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of ... |
308-344 |
1.11e-05 |
|
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of Rab11-interacting proteins (FIPs). The Rab proteins constitute the largest family of small GTPases (>60 members in mammals). Among them Rab11 is a well characterized regulator of endocytic and recycling pathways. Rab11 associates with a broad range of post-Golgi organelles, including recycling endosomes.
Pssm-ID: 462805 [Multi-domain] Cd Length: 41 Bit Score: 42.33 E-value: 1.11e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1831508208 308 QLLDALREQEICNQKLRVYINGILMRVIERHPEILEI 344
Cdd:pfam09457 4 ELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEV 40
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
74-270 |
1.64e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 74 TKRYSELEERNMSLSDERTRLKTENSVLKE---RMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKRE-KELEteswn 149
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEERlKELE----- 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 150 lKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFK-EEAQQDIDSSSEMVEV 228
Cdd:PRK03918 599 -PFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAG 677
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1831508208 229 LALETEELRRKVDgprsESISDREDMHEEIEILKAKVAELMK 270
Cdd:PRK03918 678 LRAELEELEKRRE----EIKKTLEKLKEELEEREKAKKELEK 715
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
103-221 |
1.73e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.64 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 103 ERMHNLEEQLTDNEDRF--KQLLSDEKARGTESMSRLK----REKELETEswnlkYQMLEKDLISVKkDAERSNEETKRI 176
Cdd:COG3096 279 ERRELSERALELRRELFgaRRQLAEEQYRLVEMARELEelsaRESDLEQD-----YQAASDHLNLVQ-TALRQQEKIERY 352
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1831508208 177 RNELEKTENKLEEAQLLVEGMEEERIQLERQFrkfkEEAQQDIDS 221
Cdd:COG3096 353 QEDLEELTERLEEQEEVVEEAAEQLAEAEARL----EAAEEEVDS 393
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
76-208 |
2.88e-05 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 43.83 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 76 RYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDnedrFKQLLSDEKARGTESmsrlkrekeletESWNLKYQML 155
Cdd:pfam12718 22 KVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKE----AKEKAEESEKLKTNN------------ENLTRKIQLL 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1831508208 156 EKDLisvkkdaERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQF 208
Cdd:pfam12718 86 EEEL-------EESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKY 131
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
66-303 |
3.45e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 66 QMNQLNSFTKRYSELEERNMSLSDERTRLK-----TENsvLKERMHNLEEQLTDNEDRFKQLlSDEKARGTESMSRLKRE 140
Cdd:PRK03918 153 QILGLDDYENAYKNLGEVIKEIKRRIERLEkfikrTEN--IEELIKEKEKELEEVLREINEI-SSELPELREELEKLEKE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 141 KElETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEE--ERIQLERQFRKFKEEAQQD 218
Cdd:PRK03918 230 VK-ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 219 IDSSSEMVEVLALETEELRRKvdgprsesISDREDMHEEIEILKAKVAELMKEKEEMTDQLLAtsVERGRSLIADTPSLA 298
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEER--------IKELEEKEERLEELKKKLKELEKRLEELEERHEL--YEEAKAKKEELERLK 378
|
....*
gi 1831508208 299 DELAG 303
Cdd:PRK03918 379 KRLTG 383
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
118-324 |
1.32e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 118 RFKQLLSDEKARGTESMSRLKREKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGM 197
Cdd:COG1196 214 RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 198 EEERIQLERQfrkfKEEAQQDIDSSSEMVEVLALETEELRRKvdgprsesisdREDMHEEIEILKAKVAELMKEKEEMTD 277
Cdd:COG1196 294 LAELARLEQD----IARLEERRRELEERLEELEEELAELEEE-----------LEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1831508208 278 QLLATSVERGRSLIADTPSLADELAggDSSQLLDALREQEICNQKLR 324
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEE--LAEELLEALRAAAELAAQLE 403
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
94-324 |
1.37e-04 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 43.86 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 94 LKTENSVLKERMHNLEEQLTDNEDRFKQLL----------------SDEKARGTESMSRLKREKELETESWNLKYQMLEK 157
Cdd:pfam04849 92 LLKQNSVLTERNEALEEQLGSAREEILQLRhelskkddllqiysndAEESETESSCSTPLRRNESFSSLHGCVQLDALQE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 158 DLISVKKDAERSNEETKRIRNELEKTENKleEAQLLVEGMEEERiqlerqfrkfkeEAQQDIdssSEMVEVLALETEELR 237
Cdd:pfam04849 172 KLRGLEEENLKLRSEASHLKTETDTYEEK--EQQLMSDCVEQLS------------EANQQM---AELSEELARKMEENL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 238 RKvdgprsesisdredmHEEIEILKAKVAEL-------MKEKEEMTdQLLATSVERGRSLIADTPSLADELAggdssQLL 310
Cdd:pfam04849 235 RQ---------------QEEITSLLAQIVDLqhkckelGIENEELQ-QHLQASKEAQRQLTSELQELQDRYA-----ECL 293
|
250
....*....|....
gi 1831508208 311 DALREQEICNQKLR 324
Cdd:pfam04849 294 GMLHEAQEELKELR 307
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
82-218 |
1.62e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.17 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 82 ERNMSLSDERTRLKTENSVLKERMH---NLEEQLTDNEDRF-KQLLSDEKARGTESMSRLKREKELETESWNLKYQMLEK 157
Cdd:pfam15709 351 ERKRREQEEQRRLQQEQLERAEKMReelELEQQRRFEEIRLrKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRR 430
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831508208 158 DLISVK-----KDAERSNEETKRiRNELEktENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQD 218
Cdd:pfam15709 431 KLQELQrkkqqEEAERAEAEKQR-QKELE--MQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLE 493
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
66-241 |
2.87e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.57 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 66 QMNQLNSFTKRYSELEERNMS-LSDERTR-LKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKEL 143
Cdd:pfam17380 418 QKVEMEQIRAEQEEARQREVRrLEEERAReMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIL 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 144 ETESWNLKYQMLEkdlisvkkdaersnEETKR--IRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDIDS 221
Cdd:pfam17380 498 EKELEERKQAMIE--------------EERKRklLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE 563
|
170 180
....*....|....*....|
gi 1831508208 222 SSEMVEVLALETEELRRKVD 241
Cdd:pfam17380 564 ERSRLEAMEREREMMRQIVE 583
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
71-275 |
3.62e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.19 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 71 NSFTKRYSELEERNMSLSDERTRLKTENsVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTEsmsrLKREKELETESWNL 150
Cdd:pfam17380 268 NEFLNQLLHIVQHQKAVSERQQQEKFEK-MEQERLRQEKEEKAREVERRRKLEEAEKARQAE----MDRQAAIYAEQERM 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 151 kyqmlekdlisvkkdAERSNEETKRIRNELEKTEN---KLEEAQLLVEGMEE-ERIQLERQ------------FRKFK-- 212
Cdd:pfam17380 343 ---------------AMERERELERIRQEERKRELeriRQEEIAMEISRMRElERLQMERQqknervrqeleaARKVKil 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831508208 213 -EEAQQDIDSSSEMVEVLALETEELR----RKVDGPRSESIS----DREDMHEEIEILKAKVAELMKEKEEM 275
Cdd:pfam17380 408 eEERQRKIQQQKVEMEQIRAEQEEARqrevRRLEEERAREMErvrlEEQERQQQVERLRQQEEERKRKKLEL 479
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
82-288 |
3.70e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 82 ERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESmsRLKREKELETESWNLKYQMLEKDLIS 161
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK--KKAEELKKAEEENKIKAAEEAKKAEE 1672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 162 VKKDAE--RSNEETKRIRNE-LEKTENKLEEAQLLVEGMEEERIQLErQFRKFKEEaqqdidsSSEMVEVLALETEELRR 238
Cdd:PTZ00121 1673 DKKKAEeaKKAEEDEKKAAEaLKKEAEEAKKAEELKKKEAEEKKKAE-ELKKAEEE-------NKIKAEEAKKEAEEDKK 1744
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1831508208 239 KVDGPRSESISDREDMHEEIEILKaKVAELMKEKEEMTDQLLATSVERGR 288
Cdd:PTZ00121 1745 KAEEAKKDEEEKKKIAHLKKEEEK-KAEEIRKEKEAVIEEELDEEDEKRR 1793
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
69-279 |
3.94e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 69 QLNSFTKRYSELEERnmslsdeRTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSdEKARGTESMSRLK---------R 139
Cdd:pfam01576 48 QLQAETELCAEAEEM-------RARLAARKQELEEILHELESRLEEEEERSQQLQN-EKKKMQQHIQDLEeqldeeeaaR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 140 EK-ELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEaqllvegmEEERIQLERQFRKFKEEAQQD 218
Cdd:pfam01576 120 QKlQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAE--------EEEKAKSLSKLKNKHEAMISD 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831508208 219 IDSSSEMVEVLALETEELRRKVDGPRSESISDREDMHEEIEILKAKVAelmKEKEEMTDQL 279
Cdd:pfam01576 192 LEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLA---KKEEELQAAL 249
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
79-262 |
4.15e-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: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 79 ELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFK---QLLSDEKARGTESMSRLKREKELETESWNLKYQmL 155
Cdd:pfam01576 135 KLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKslsKLKNKHEAMISDLEERLKKEEKGRQELEKAKRK-L 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 156 EKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRkfkeEAQQDIdssSEMVEVLALETee 235
Cdd:pfam01576 214 EGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIR----ELEAQI---SELQEDLESER-- 284
|
170 180
....*....|....*....|....*..
gi 1831508208 236 lrrkvdGPRSESISDREDMHEEIEILK 262
Cdd:pfam01576 285 ------AARNKAEKQRRDLGEELEALK 305
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
101-279 |
4.50e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 101 LKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNEL 180
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 181 EKTENKLEEAQLLVEGMEEERIQLERQFRKFKEE---AQQDIDSSSEMVEVLALETEELRRKVDGPRSESISDREDMHEE 257
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEEleeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180
....*....|....*....|..
gi 1831508208 258 IEILKAKVAELMKEKEEMTDQL 279
Cdd:COG1196 378 EEELEELAEELLEALRAAAELA 399
|
|
| PRK13169 |
PRK13169 |
DNA replication initiation control protein YabA; |
58-140 |
4.61e-04 |
|
DNA replication initiation control protein YabA;
Pssm-ID: 183876 Cd Length: 110 Bit Score: 39.46 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 58 DALNDFSSQMNQLnsfTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDrfkqllSDEKARGTESMSRL 137
Cdd:PRK13169 8 DALDDLEQNLGVL---LKELGALKKQLAELLEENTALRLENDKLRERLEELEAEEPAKEK------KKKEGEGKDNLARL 78
|
...
gi 1831508208 138 KRE 140
Cdd:PRK13169 79 YQE 81
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
151-264 |
4.77e-04 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 42.02 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 151 KYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDIDSSSEMVEVLA 230
Cdd:COG4026 129 EYNELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKRL 208
|
90 100 110
....*....|....*....|....*....|....
gi 1831508208 231 LETEELRRKVDGPRSESISDREDMHEEIEILKAK 264
Cdd:COG4026 209 LEVFSLEELWKELFPEELPEEDFIYFATENLKPG 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
138-279 |
4.89e-04 |
|
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: 42.74 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 138 KREKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFrkfkEEAQQ 217
Cdd:TIGR02168 220 AELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL----YALAN 295
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831508208 218 DIDSSSEMVEVLALETEELRRK---VDGPRSESISDREDMHEEIEILKAKVAELMKEKEEMTDQL 279
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQleeLEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
64-250 |
4.93e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 64 SSQMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLsdekaRGTESMSRLKREKEL 143
Cdd:COG4942 51 KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL-----RALYRLGRQPPLALL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 144 -ETESWNLKYQMLE-------------KDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFR 209
Cdd:COG4942 126 lSPEDFLDAVRRLQylkylaparreqaEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE 205
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1831508208 210 KFKEEAQQDIDSSSEMVEVLALETEELRRKVDGPRSESISD 250
Cdd:COG4942 206 KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
150-286 |
6.30e-04 |
|
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: 41.45 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 150 LKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKE-----EAQQDIDSSSE 224
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArikkyEEQLGNVRNNK 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831508208 225 MVEVLALETEELRRKvdgprsesISDRED----MHEEIEILKAKVAELMKEKEEMTDQLLATSVER 286
Cdd:COG1579 90 EYEALQKEIESLKRR--------ISDLEDeileLMERIEELEEELAELEAELAELEAELEEKKAEL 147
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
157-274 |
6.36e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 157 KDLISvkKDAERSNE-----ETKRIR--NELEKTENKLEEAQLLVEGMEEERIQLERQFRK----FKEEAQQDIDSSSEM 225
Cdd:PRK00409 508 KKLIG--EDKEKLNEliaslEELEREleQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKlleeAEKEAQQAIKEAKKE 585
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1831508208 226 VEVLALETEELRRKVDGP--RSESISDREDMHEEIEILKAKVAELMKEKEE 274
Cdd:PRK00409 586 ADEIIKELRQLQKGGYASvkAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
69-279 |
6.47e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 69 QLNSFTKRYSELEERnmsLSDERTRLKTENSVLKErmhnlEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKElETESW 148
Cdd:PRK03918 460 ELKRIEKELKEIEEK---ERKLRKELRELEKVLKK-----ESELIKLKELAEQLKELEEKLKKYNLEELEKKAE-EYEKL 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 149 NLKYQMLEKDLISVKKDAERSNEetkrIRNELEKTENKLEEAqllvegmEEERIQLERQFRKFKEEAQQDIDSSSEMVEV 228
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLEE----LKKKLAELEKKLDEL-------EEELAELLKELEELGFESVEELEERLKELEP 599
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1831508208 229 LALETEELRRKVDGPRSEsISDREDMHEEIEILKAKVAELMKEKEEMTDQL 279
Cdd:PRK03918 600 FYNEYLELKDAEKELERE-EKELKKLEEELDKAFEELAETEKRLEELRKEL 649
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
101-318 |
7.39e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 7.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 101 LKERMHNLEEQLTDNEDRFKQLlsdEKARGTESMSRLKREKELETESWNLKYQMLEKDLisvkKDAERSNEETKRIRNEL 180
Cdd:COG4913 622 LEEELAEAEERLEALEAELDAL---QERREALQRLAEYSWDEIDVASAEREIAELEAEL----ERLDASSDDLAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 181 EKTENKLEEAQLLVEGMEEERIQLERQFRKFKEE---AQQDIDSSSEMVEV-LALETEELRRKVDGPRSESiSDREDMHE 256
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEEldeLQDRLEAAEDLARLeLRALLEERFAAALGDAVER-ELRENLEE 773
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831508208 257 EIEILKAKVAELMKEKEEMTDQLLATSVERGRSLIADTPSLADELAggdssqLLDALREQEI 318
Cdd:COG4913 774 RIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLA------LLDRLEEDGL 829
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
69-235 |
7.71e-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: 41.98 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 69 QLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERM-------HNLEEQLTDNEDR----FKQLLSDEKARGTESMSRL 137
Cdd:TIGR02169 731 EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIeeleedlHKLEEALNDLEARlshsRIPEIQAELSKLEEEVSRI 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 138 K---REKELETESWNLKYQMLEK---DLISVKKDAE-RSNEETKRIRN---ELEKTENKLEEAQLLVEGMEEERIQLERQ 207
Cdd:TIGR02169 811 EarlREIEQKLNRLTLEKEYLEKeiqELQEQRIDLKeQIKSIEKEIENlngKKEELEEELEELEAALRDLESRLGDLKKE 890
|
170 180 190
....*....|....*....|....*....|....
gi 1831508208 208 FRKFK------EEAQQDIDSSSEMVEVLALETEE 235
Cdd:TIGR02169 891 RDELEaqlrelERKIEELEAQIEKKRKRLSELKA 924
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
60-279 |
9.21e-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: 41.93 E-value: 9.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 60 LNDFSSQMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTdnedRFKQLLSDEKARGTESMSRLKR 139
Cdd:TIGR04523 144 LTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLL----KLELLLSNLKKKIQKNKSLESQ 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 140 EKELETESWNLKYQMLEKDLISVKKDAERSNEETK---------RIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRK 210
Cdd:TIGR04523 220 ISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQlnqlkdeqnKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD 299
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831508208 211 FKEEAQQDIdsSSEMVEVLALETEELrRKVDGPRSESISDREDMHEEIEILKAKVAELMKEKEEMTDQL 279
Cdd:TIGR04523 300 LNNQKEQDW--NKELKSELKNQEKKL-EEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
|
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
57-198 |
1.15e-03 |
|
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
Pssm-ID: 318204 [Multi-domain] Cd Length: 234 Bit Score: 40.33 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 57 QDALNDFSSQMNQLNSFTKRYSELEERNmSLSDERTRLKTENSVLKERMHNLEEQLTDNE-------DRFKQLLS----- 124
Cdd:pfam15934 68 HETLKDRDHQIKQLQSMITGYSDISENN-RLKEEIHDLKQKNCVQARVVRKMGLELKGQEeqrvelcDKYESLLGsfeeq 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 125 -----DEKARGTESMSRL----KREKELETESwnlkyQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVE 195
Cdd:pfam15934 147 cqelkRANRRVQSLQTRLsqveKLQEELRTER-----KILREEVIALKEKDAKSNGRERALQDQLKCCQTEIEKSRTLIR 221
|
...
gi 1831508208 196 GME 198
Cdd:pfam15934 222 NMQ 224
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
60-316 |
1.82e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 60 LNDFSSQMNQLNS--------FTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLtdnedrfKQLLSDEKargt 131
Cdd:pfam15921 319 LSDLESTVSQLRSelreakrmYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL-------QKLLADLH---- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 132 esmsrlKREKELEteswnlkyqmLEKDLISVKKDAERSNEET-KRIRNELEKTENKLEEAQLLVEGMEEE-RIQLERQFR 209
Cdd:pfam15921 388 ------KREKELS----------LEKEQNKRLWDRDTGNSITiDHLRRELDDRNMEVQRLEALLKAMKSEcQGQMERQMA 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 210 KF--KEEAQQDIDSSSEMV----EVLALETEELR-RKVDGPRSE-SISD-REDMHEEIEILKAKVAELMKEKEEMTDQL- 279
Cdd:pfam15921 452 AIqgKNESLEKVSSLTAQLestkEMLRKVVEELTaKKMTLESSErTVSDlTASLQEKERAIEATNAEITKLRSRVDLKLq 531
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1831508208 280 ----LATSVERGRSLIADTPSLADELAGGDssQLLDALREQ 316
Cdd:pfam15921 532 elqhLKNEGDHLRNVQTECEALKLQMAEKD--KVIEILRQQ 570
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
72-250 |
2.07e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.66 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 72 SFTKRYSELEERNMSLSDERTRLKTENSVLK---ERMHNLEEQLTDNEDRFKQLlsdeKARGTESMSRLKREKELETESW 148
Cdd:PLN02939 223 SLSKELDVLKEENMLLKDDIQFLKAELIEVAeteERVFKLEKERSLLDASLREL----ESKFIVAQEDVSKLSPLQYDCW 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 149 NLKYQMLEKDLISVKKDAERSN---EETKRIRNELEKTENKLEEAQL------LVEGMEEERIQLERQFRKFKEEAQQDI 219
Cdd:PLN02939 299 WEKVENLQDLLDRATNQVEKAAlvlDQNQDLRDKVDKLEASLKEANVskfssyKVELLQQKLKLLEERLQASDHEIHSYI 378
|
170 180 190
....*....|....*....|....*....|....*
gi 1831508208 220 ----DSSSEMVEVLALETEELRRKvdgPRSESISD 250
Cdd:PLN02939 379 qlyqESIKEFQDTLSKLKEESKKR---SLEHPADD 410
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
78-274 |
2.16e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.49 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 78 SELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQL--LSDEKARGTESMSRLKREKELETESWNLKYQML 155
Cdd:pfam05557 30 IELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQaeLNRLKKKYLEALNKKLNEKESQLADAREVISCL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 156 EKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQ-------------QDI--- 219
Cdd:pfam05557 110 KNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQrikelefeiqsqeQDSeiv 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1831508208 220 -DSSSEMVEVLALETEELRRKVDGPR-SESISDREDMHEEIEILKAKVAELMKEKEE 274
Cdd:pfam05557 190 kNSKSELARIPELEKELERLREHNKHlNENIENKLLLKEEVEDLKRKLEREEKYREE 246
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
75-274 |
2.48e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 75 KRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELEteswNLKYQM 154
Cdd:PTZ00121 1224 KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD----EAKKAE 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 155 LEKDLISVKKDAErsneETKRIRNELEKTENKLEEAQLLVEGMEEERIQLErqFRKFKEEAQQD-IDSSSEMVEVLALET 233
Cdd:PTZ00121 1300 EKKKADEAKKKAE----EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE--AAKAEAEAAADeAEAAEEKAEAAEKKK 1373
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1831508208 234 EELRRKVDG--PRSESISDREDMHEEIEILKAKVAELMKEKEE 274
Cdd:PTZ00121 1374 EEAKKKADAakKKAEEKKKADEAKKKAEEDKKKADELKKAAAA 1416
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
157-316 |
2.54e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 157 KDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFkeEAQQDIDSSSEMVEVLALETEEL 236
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL--PLYQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 237 RRKvdgprsesISDREDMHEEIEILKAKVAELMKEKEEMTDQLLATSVERGRSLIADTPSLADELAggDSSQLLDALREQ 316
Cdd:COG4717 152 EER--------LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLA--ELEEELEEAQEE 221
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
78-178 |
2.61e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 78 SELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLS--DEKARGTESMSRLKREkeleteswnlkYQML 155
Cdd:COG2433 409 TEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSeeRREIRKDREISRLDRE-----------IERL 477
|
90 100
....*....|....*....|...
gi 1831508208 156 EKDLISVKKDAERSNEETKRIRN 178
Cdd:COG2433 478 ERELEEERERIEELKRKLERLKE 500
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
109-274 |
2.80e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 109 EEQLTDNEDRFKQLLSDEKAR-----------GTESMSRLKREKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIR 177
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEaeaikkealleAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 178 NELEKTENKLEEAQLLVEGMEEEriqLERqfrkfKEEAQQDidsssEMVEVLALETEELRRKVdgprsesisdREDMHEE 257
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEE---LEE-----LIEEQLQ-----ELERISGLTAEEAKEIL----------LEKVEEE 166
|
170
....*....|....*..
gi 1831508208 258 ieiLKAKVAELMKEKEE 274
Cdd:PRK12704 167 ---ARHEAAVLIKEIEE 180
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
78-263 |
2.82e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 78 SELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELETESWNLK------ 151
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRdrleec 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 152 ---YQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEE---AQQDIDSSSEM 225
Cdd:PRK02224 334 rvaAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdAPVDLGNAEDF 413
|
170 180 190
....*....|....*....|....*....|....*...
gi 1831508208 226 VEVLALETEELRRKVDGPRSESISDREDMHEEIEILKA 263
Cdd:PRK02224 414 LEELREERDELREREAELEATLRTARERVEEAEALLEA 451
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
167-268 |
3.15e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.84 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 167 ERSNEETKRIRNELEKTENKLEEAqllvegmeEERIQ-LERQFRKFKEEAQQDIDSSSEmVEVLALETEELRRKVdgprs 245
Cdd:COG2433 416 RRLEEQVERLEAEVEELEAELEEK--------DERIErLERELSEARSEERREIRKDRE-ISRLDREIERLEREL----- 481
|
90 100
....*....|....*....|...
gi 1831508208 246 esisdrEDMHEEIEILKAKVAEL 268
Cdd:COG2433 482 ------EEERERIEELKRKLERL 498
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
79-236 |
3.22e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.88 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 79 ELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELETESWNLKYQMLEKD 158
Cdd:pfam07888 70 QWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831508208 159 LisvkkDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDIDSSSEMVEVLALETEEL 236
Cdd:pfam07888 150 T-----ELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKL 222
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
89-279 |
3.29e-03 |
|
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: 40.09 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 89 DERTRLKTEN-SVLKERMHNLEEQLTDNEDRFKQLLSDEKAR------GTESMSRLKREKELETESWNLKYQM------- 154
Cdd:pfam05483 274 EEKTKLQDENlKELIEKKDHLTKELEDIKMSLQRSMSTQKALeedlqiATKTICQLTEEKEAQMEELNKAKAAhsfvvte 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 155 -------LEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEeerIQLErQFRKFKEEAQQDIDSSSEmVE 227
Cdd:pfam05483 354 feattcsLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKE---VELE-ELKKILAEDEKLLDEKKQ-FE 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1831508208 228 VLALETEELRRKVDGPRSESISDREDMHEEIEILKAKVAELMKEKEEMTDQL 279
Cdd:pfam05483 429 KIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL 480
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
79-293 |
3.32e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 79 ELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFK--------QLLSDEKARGTESMSRLKREkELETESWNL 150
Cdd:PRK02224 409 NAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecgQPVEGSPHVETIEEDRERVE-ELEAELEDL 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 151 KYQMLE--------KDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLE---RQFRKFKEEAQQDI 219
Cdd:PRK02224 488 EEEVEEveerleraEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEaeaEEKREAAAEAEEEA 567
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831508208 220 DSSSEMVEVLALETEELRRKVDGPR--SESISDREDMHEEIEILKAKVAELmKEKEEMTDQLLATSVERGRSLIAD 293
Cdd:PRK02224 568 EEAREEVAELNSKLAELKERIESLEriRTLLAAIADAEDEIERLREKREAL-AELNDERRERLAEKRERKRELEAE 642
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
135-268 |
4.44e-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: 39.67 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 135 SRLKREKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEE 214
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1831508208 215 AQQdidsSSEMVEVLALETEELRRKVDgprsESISDREDMHEEIEILKAKVAEL 268
Cdd:TIGR02169 739 LEE----LEEDLSSLEQEIENVKSELK----ELEARIEELEEDLHKLEEALNDL 784
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
103-279 |
5.05e-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: 39.67 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 103 ERMHNLEEQLTDNEDRfkqlLSDEKARgTESMSRLKREKElETESWNL--KYQMLEKDLISVKKDAERSNEETKRIRNEL 180
Cdd:TIGR02169 187 ERLDLIIDEKRQQLER----LRREREK-AERYQALLKEKR-EYEGYELlkEKEALERQKEAIERQLASLEEELEKLTEEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 181 EKTENKLEEAQLLVEGM--------EEERIQLERQFRKFKEEAQQdIDSSSEMVEVLALETEELRRKVDGPRSESISDRE 252
Cdd:TIGR02169 261 SELEKRLEEIEQLLEELnkkikdlgEEEQLRVKEKIGELEAEIAS-LERSIAEKERELEDAEERLAKLEAEIDKLLAEIE 339
|
170 180
....*....|....*....|....*..
gi 1831508208 253 DMHEEIEILKAKVAELMKEKEEMTDQL 279
Cdd:TIGR02169 340 ELEREIEEERKRRDKLTEEYAELKEEL 366
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
79-274 |
5.68e-03 |
|
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: 39.23 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 79 ELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLlsdekARGTESMSRLKREKELETESWNLKYQMLEKD 158
Cdd:TIGR04523 416 KLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNL-----DNTRESLETQLKVLSRSINKIKQNLEQKQKE 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 159 LISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQD------------IDSSSEMV 226
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDdfelkkenlekeIDEKNKEI 570
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1831508208 227 EVLALETEELRRK---VDGPRSESISDREDMHEEIEILKAKVAELMKEKEE 274
Cdd:TIGR04523 571 EELKQTQKSLKKKqeeKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
132-240 |
5.77e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 39.35 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 132 ESMSRLKREKELETESWNLKYQMLEKDLISVK-------KDAERSNEETKRIRNELEKTENKLEEAQLLVEGM------- 197
Cdd:pfam07111 151 EQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkrageaKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLrkyvgeq 230
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831508208 198 ----------EEERIQLERQFRKFKEEaQQDIDSSSEMVEV--------LALETEELRRKV 240
Cdd:pfam07111 231 vppevhsqtwELERQELLDTMQHLQED-RADLQATVELLQVrvqslthmLALQEEELTRKI 290
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
63-200 |
6.19e-03 |
|
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: 39.23 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 63 FSSQMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRF--------KQLLSDEKARGTESM 134
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkddfelkKENLEKEIDEKNKEI 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 135 SRLKRE---------------KELETESWNLKYQMLEKD--LISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGM 197
Cdd:TIGR04523 571 EELKQTqkslkkkqeekqeliDQKEKEKKDLIKEIEEKEkkISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQI 650
|
...
gi 1831508208 198 EEE 200
Cdd:TIGR04523 651 KET 653
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
57-241 |
6.25e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.23 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 57 QDALNDFSSQmNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEkargteSMSR 136
Cdd:COG3206 195 EAALEEFRQK-NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP------VIQQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 137 LKREkeleteswnlkYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKL-EEAQLLVEGMEEERIQLERQFRKFKEEA 215
Cdd:COG3206 268 LRAQ-----------LAELEAELAELSARYTPNHPDVIALRAQIAALRAQLqQEAQRILASLEAELEALQAREASLQAQL 336
|
170 180
....*....|....*....|....*.
gi 1831508208 216 QQDIDSSSEMVEVLAlETEELRRKVD 241
Cdd:COG3206 337 AQLEARLAELPELEA-ELRRLEREVE 361
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
57-225 |
6.49e-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: 39.27 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 57 QDALNDFSSQMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSR 136
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 137 LKREKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEeeriQLERQFRKFKEEAQ 216
Cdd:TIGR02168 434 ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE----RLQENLEGFSEGVK 509
|
....*....
gi 1831508208 217 QDIDSSSEM 225
Cdd:TIGR02168 510 ALLKNQSGL 518
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
161-270 |
7.33e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.17 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 161 SVKKDAERSNEETKRIRNELEKTENKLEEAqllvEGMEEERIQLERQFRKFKEEAQQDIDSSSEmVEVLALETEELRRKV 240
Cdd:PRK04863 496 DVARELLRRLREQRHLAEQLQQLRMRLSEL----EQRLRQQQRAERLLAEFCKRLGKNLDDEDE-LEQLQEELEARLESL 570
|
90 100 110
....*....|....*....|....*....|
gi 1831508208 241 DGPRSESISDREDMHEEIEILKAKVAELMK 270
Cdd:PRK04863 571 SESVSEARERRMALRQQLEQLQARIQRLAA 600
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
75-301 |
9.48e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.51 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 75 KRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQL---------LSDEKARGTESMSRLKREKELET 145
Cdd:PRK03918 293 EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLeelkkklkeLEKRLEELEERHELYEEAKAKKE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 146 ESWNLKYQM-------LEKDLISVKKDAERSNEETKRI---RNELEKTENKLEEAQLLVEGM------------EEERIQ 203
Cdd:PRK03918 373 ELERLKKRLtgltpekLEKELEELEKAKEEIEEEISKItarIGELKKEIKELKKAIEELKKAkgkcpvcgreltEEHRKE 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 204 LERQFRKFKEEAQQDIDSSSEMVEVLALETEELRRKVDGPRseSISDREDMHEEIEILKAKVAELMKEKEEMTDQLLATS 283
Cdd:PRK03918 453 LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES--ELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKL 530
|
250
....*....|....*...
gi 1831508208 284 VERGRSLIADTPSLADEL 301
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKEL 548
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
151-279 |
9.99e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.27 E-value: 9.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508208 151 KYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFrkfkEEAQQDID---------- 220
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI----AEAEAEIEerreelgera 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831508208 221 -------SSSEMVEVL--------ALETEELRRKVDGPRSESISDREDMHEEIEILKAKVAELMKEKEEMTDQL 279
Cdd:COG3883 93 ralyrsgGSVSYLDVLlgsesfsdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
|
| |
