|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
72-366 |
1.31e-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: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 72 QLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELETEsw 151
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE-- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 152 nlkyqmlEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDIDSSSEMVEV 231
Cdd:COG1196 353 -------LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 232 LALETEELRRKVDGPRSESISDREDMHEEIEILKAKVAELMKEKEEMTDQLLATSVERGRSLIADTPSLADELAGGDSSQ 311
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 17534411 312 LLDALREQEICNQKLRVYINGILMRVIERHPEILEIGEEGILSKLTVRRRISVLA 366
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA 560
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
62-282 |
2.23e-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: 53.52 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 62 ALNDFSSQMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSD------EKARGTE 135
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEisrleqQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 136 SMSRLKRE-KELETESWNLKYQM--LEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFR 212
Cdd:TIGR02168 310 RLANLERQlEELEAQLEELESKLdeLAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 213 KFKEEAQQ----------DIDSSSEMVEVLALETEELRRKVDGPRSESISDR-EDMHEEIEILKAKVAELMKEKEEMTDQ 281
Cdd:TIGR02168 390 QLELQIASlnneierleaRLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREE 469
|
.
gi 17534411 282 L 282
Cdd:TIGR02168 470 L 470
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
72-320 |
2.62e-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: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 72 QLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELETESw 151
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 152 nlkyQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDIDSSSEMVEV 231
Cdd:COG1196 305 ----ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 232 LALETEELRRKVDGpRSESISDREDMHEEIEILKAKVAELMKEKEEMTDQLLATSVERGRSLIADTPSLADELAGGDSSQ 311
Cdd:COG1196 381 LEELAEELLEALRA-AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
....*....
gi 17534411 312 LLDALREQE 320
Cdd:COG1196 460 ALLELLAEL 468
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
93-326 |
3.87e-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: 52.75 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 93 ERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDekargTESMSRLKREKELETESWNLKYQMLEKDLISVKKDAERS 172
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEE-----LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 173 NEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDIDSSSEMVEVLALETEELRRKVDG-----PR 247
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERlesleRR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 248 SESISDR--------EDMHEEIEILKAKVAELMKEKEEMTDQL-----LATSVERGRSLIADTPSLADELAGGDSSQLLD 314
Cdd:TIGR02168 833 IAATERRledleeqiEELSEDIESLAAEIEELEELIEELESELeallnERASLEEALALLRSELEELSEELRELESKRSE 912
|
250
....*....|..
gi 17534411 315 ALREQEICNQKL 326
Cdd:TIGR02168 913 LRRELEELREKL 924
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
60-305 |
4.29e-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: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 60 QDALNDFSSQMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSR 139
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 140 LKREKELETESwnlkyQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKF---KE 216
Cdd:COG1196 364 EEALLEAEAEL-----AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELeeeEE 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 217 EAQQDIDSSSEMVEVLALETEELRRKVDGPRSESISDREDMHEEIEILKAKVAELMKEKEEMTDQLLATSVERGRSLIAD 296
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
....*....
gi 17534411 297 TPSLADELA 305
Cdd:COG1196 519 LRGLAGAVA 527
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
71-304 |
9.31e-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: 51.61 E-value: 9.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 71 NQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLK--------- 141
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaeiaslers 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 142 -REKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQllvEGMEEERIQLERQFRKFKeEAQQ 220
Cdd:TIGR02169 310 iAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK---EELEDLRAELEEVDKEFA-ETRD 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 221 DIDSSSEMVEVLALETEELRRKVDGPRSESI---SDREDMHEEIEILKAKVAELMKEKEEMTDQlLATSVERGRSLIADT 297
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRELDRLQEELQrlsEELADLNAAIAGIEAKINELEEEKEDKALE-IKKQEWKLEQLAADL 464
|
....*..
gi 17534411 298 PSLADEL 304
Cdd:TIGR02169 465 SKYEQEL 471
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
89-284 |
1.77e-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: 50.41 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 89 SLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELETeswnlkyqmLEKDLISVKKD 168
Cdd:pfam05667 280 LLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQREEELEE---------LQEQLEDLESS 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 169 AERSNEETKRIRNELEKTENKLEEaqllvegMEEERIQLERQFRKFK-------------EEAQQDIDSSSEMVEVLALE 235
Cdd:pfam05667 351 IQELEKEIKKLESSIKQVEEELEE-------LKEQNEELEKQYKVKKktldllpdaeeniAKLQALVDASAQRLVELAGQ 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17534411 236 TEELR-------RKVDGPRSESISDREDMHEEIEILKAK---VAELMKEKEEMTDQLLA 284
Cdd:pfam05667 424 WEKHRvplieeyRALKEAKSNKEDESQRKLEEIKELREKikeVAEEAKQKEELYKQLVA 482
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
98-277 |
3.77e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 98 KTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESmSRLKREKELETESWNLKYQMLEKDLISVKKDAE--RSNEE 175
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE-ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkKAEEE 1631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 176 TKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFK------EEAQQDIDSSSEMVEVLALETEELRR--KVDGPR 247
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEedkkkaEEAKKAEEDEKKAAEALKKEAEEAKKaeELKKKE 1711
|
170 180 190
....*....|....*....|....*....|
gi 17534411 248 SESISDREDMHEEIEILKAKVAELMKEKEE 277
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
82-282 |
6.88e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 6.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 82 ELEERNMSLSDERTRLKTENSVLKERMHNLEEQltdNEDRFKQLLSDEKARGTESMSRLKREKELETESWNLKYQMLEKD 161
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE---KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 162 LISVKKDAE----------RSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLErQFRKFKEEAQQDIDSSSEMVEV 231
Cdd:PTZ00121 1649 AEELKKAEEenkikaaeeaKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE-ELKKKEAEEKKKAEELKKAEEE 1727
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17534411 232 LALETEELRRKVDGPRSESISDREDMHEeieilKAKVAELMKEKEEMTDQL 282
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEEAKKDEEE-----KKKIAHLKKEEEKKAEEI 1773
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
78-291 |
8.26e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 8.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 78 KRYSELEERNMSLSD-ERTRLKTENSV--LKERMHNLEEQLTDNEDRFKQLlsDEKARGTESMsrlkREKELETESWNLK 154
Cdd:PRK03918 228 KEVKELEELKEEIEElEKELESLEGSKrkLEEKIRELEERIEELKKEIEEL--EEKVKELKEL----KEKAEEYIKLSEF 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 155 YQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEaqllVEGMEEERIQLERQFRKFKEEAQQdidssSEMVEVLAL 234
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER----LEELKKKLKELEKRLEELEERHEL-----YEEAKAKKE 372
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17534411 235 ETEELRRKVDGprsesisdredmhEEIEILKAKVAELMKEKEEMTDQLLATSVERGR 291
Cdd:PRK03918 373 ELERLKKRLTG-------------LTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
105-224 |
1.11e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 105 KERMHNLEEQLTDNEDRF--KQLLSDEKARGTESMSRL----KREKELETEswnlkYQMLEKDLISVKkDAERSNEETKR 178
Cdd:PRK04863 279 NERRVHLEEALELRRELYtsRRQLAAEQYRLVEMARELaelnEAESDLEQD-----YQAASDHLNLVQ-TALRQQEKIER 352
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 17534411 179 IRNELEKTENKLEEAQLLVEGMEEERIQLERQfrkfKEEAQQDIDS 224
Cdd:PRK04863 353 YQADLEELEERLEEQNEVVEEADEQQEENEAR----AEAAEEEVDE 394
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
78-223 |
1.15e-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: 46.46 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 78 KRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKargtESMSRLKREKELETESWNLK-YQ 156
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE----EVEARIKKYEEQLGNVRNNKeYE 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17534411 157 MLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDID 223
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
|
| RBD-FIP |
pfam09457 |
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of ... |
311-347 |
1.16e-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: 1.16e-05
10 20 30
....*....|....*....|....*....|....*..
gi 17534411 311 QLLDALREQEICNQKLRVYINGILMRVIERHPEILEI 347
Cdd:pfam09457 4 ELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEV 40
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
106-224 |
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 17534411 106 ERMHNLEEQLTDNEDRF--KQLLSDEKARGTESMSRLK----REKELETEswnlkYQMLEKDLISVKkDAERSNEETKRI 179
Cdd:COG3096 279 ERRELSERALELRRELFgaRRQLAEEQYRLVEMARELEelsaRESDLEQD-----YQAASDHLNLVQ-TALRQQEKIERY 352
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 17534411 180 RNELEKTENKLEEAQLLVEGMEEERIQLERQFrkfkEEAQQDIDS 224
Cdd:COG3096 353 QEDLEELTERLEEQEEVVEEAAEQLAEAEARL----EAAEEEVDS 393
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
77-273 |
2.60e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 77 TKRYSELEERNMSLSDERTRLKTENSVLKE---RMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKRE-KELEteswn 152
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEERlKELE----- 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 153 lKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFK-EEAQQDIDSSSEMVEV 231
Cdd:PRK03918 599 -PFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAG 677
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17534411 232 LALETEELRRKVDgprsESISDREDMHEEIEILKAKVAELMK 273
Cdd:PRK03918 678 LRAELEELEKRRE----EIKKTLEKLKEELEEREKAKKELEK 715
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
79-211 |
4.18e-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: 43.45 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 79 RYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDnedrFKQLLSDEKARGTESmsrlkrekeletESWNLKYQML 158
Cdd:pfam12718 22 KVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKE----AKEKAEESEKLKTNN------------ENLTRKIQLL 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 17534411 159 EKDLisvkkdaERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQF 211
Cdd:pfam12718 86 EEEL-------EESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKY 131
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
69-306 |
6.38e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 69 QMNQLNSFTKRYSELEERNMSLSDERTRLK-----TENsvLKERMHNLEEQLTDNEDRFKQLlSDEKARGTESMSRLKRE 143
Cdd:PRK03918 153 QILGLDDYENAYKNLGEVIKEIKRRIERLEkfikrTEN--IEELIKEKEKELEEVLREINEI-SSELPELREELEKLEKE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 144 KElETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEE--ERIQLERQFRKFKEEAQQD 221
Cdd:PRK03918 230 VK-ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 222 IDSSSEMVEVLALETEELRRKvdgprsesISDREDMHEEIEILKAKVAELMKEKEEMTDQLLAtsVERGRSLIADTPSLA 301
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEER--------IKELEEKEERLEELKKKLKELEKRLEELEERHEL--YEEAKAKKEELERLK 378
|
....*
gi 17534411 302 DELAG 306
Cdd:PRK03918 379 KRLTG 383
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
121-327 |
1.52e-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: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 121 RFKQLLSDEKARGTESMSRLKREKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGM 200
Cdd:COG1196 214 RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 201 EEERIQLERQfrkfKEEAQQDIDSSSEMVEVLALETEELRRKvdgprsesisdREDMHEEIEILKAKVAELMKEKEEMTD 280
Cdd:COG1196 294 LAELARLEQD----IARLEERRRELEERLEELEEELAELEEE-----------LEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17534411 281 QLLATSVERGRSLIADTPSLADELAggDSSQLLDALREQEICNQKLR 327
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEE--LAEELLEALRAAAELAAQLE 403
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
85-221 |
1.66e-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: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 85 ERNMSLSDERTRLKTENSVLKERMH---NLEEQLTDNEDRF-KQLLSDEKARGTESMSRLKREKELETESWNLKYQMLEK 160
Cdd:pfam15709 351 ERKRREQEEQRRLQQEQLERAEKMReelELEQQRRFEEIRLrKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRR 430
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17534411 161 DLISVK-----KDAERSNEETKRiRNELEktENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQD 221
Cdd:pfam15709 431 KLQELQrkkqqEEAERAEAEKQR-QKELE--MQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLE 493
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
97-327 |
1.80e-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: 43.48 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 97 LKTENSVLKERMHNLEEQLTDNEDRFKQLL----------------SDEKARGTESMSRLKREKELETESWNLKYQMLEK 160
Cdd:pfam04849 92 LLKQNSVLTERNEALEEQLGSAREEILQLRhelskkddllqiysndAEESETESSCSTPLRRNESFSSLHGCVQLDALQE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 161 DLISVKKDAERSNEETKRIRNELEKTENKleEAQLLVEGMEEERiqlerqfrkfkeEAQQDIdssSEMVEVLALETEELR 240
Cdd:pfam04849 172 KLRGLEEENLKLRSEASHLKTETDTYEEK--EQQLMSDCVEQLS------------EANQQM---AELSEELARKMEENL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 241 RKvdgprsesisdredmHEEIEILKAKVAEL-------MKEKEEMTdQLLATSVERGRSLIADTPSLADELAggdssQLL 313
Cdd:pfam04849 235 RQ---------------QEEITSLLAQIVDLqhkckelGIENEELQ-QHLQASKEAQRQLTSELQELQDRYA-----ECL 293
|
250
....*....|....
gi 17534411 314 DALREQEICNQKLR 327
Cdd:pfam04849 294 GMLHEAQEELKELR 307
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
69-244 |
3.59e-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: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 69 QMNQLNSFTKRYSELEERNMS-LSDERTR-LKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKEL 146
Cdd:pfam17380 418 QKVEMEQIRAEQEEARQREVRrLEEERAReMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIL 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 147 ETESWNLKYQMLEkdlisvkkdaersnEETKR--IRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDIDS 224
Cdd:pfam17380 498 EKELEERKQAMIE--------------EERKRklLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE 563
|
170 180
....*....|....*....|
gi 17534411 225 SSEMVEVLALETEELRRKVD 244
Cdd:pfam17380 564 ERSRLEAMEREREMMRQIVE 583
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
74-278 |
4.66e-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: 42.80 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 74 NSFTKRYSELEERNMSLSDERTRLKTENsVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTEsmsrLKREKELETESWNL 153
Cdd:pfam17380 268 NEFLNQLLHIVQHQKAVSERQQQEKFEK-MEQERLRQEKEEKAREVERRRKLEEAEKARQAE----MDRQAAIYAEQERM 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 154 kyqmlekdlisvkkdAERSNEETKRIRNELEKTEN---KLEEAQLLVEGMEE-ERIQLERQ------------FRKFK-- 215
Cdd:pfam17380 343 ---------------AMERERELERIRQEERKRELeriRQEEIAMEISRMRElERLQMERQqknervrqeleaARKVKil 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17534411 216 -EEAQQDIDSSSEMVEVLALETEELR----RKVDGPRSESIS----DREDMHEEIEILKAKVAELMKEKEEM 278
Cdd:pfam17380 408 eEERQRKIQQQKVEMEQIRAEQEEARqrevRRLEEERAREMErvrlEEQERQQQVERLRQQEEERKRKKLEL 479
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
104-282 |
4.86e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 104 LKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNEL 183
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 184 EKTENKLEEAQLLVEGMEEERIQLERQFRKFKEE---AQQDIDSSSEMVEVLALETEELRRKVDGPRSESISDREDMHEE 260
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEEleeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180
....*....|....*....|..
gi 17534411 261 IEILKAKVAELMKEKEEMTDQL 282
Cdd:COG1196 378 EEELEELAEELLEALRAAAELA 399
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
67-253 |
5.20e-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: 42.06 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 67 SSQMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLsdekaRGTESMSRLKREKEL 146
Cdd:COG4942 51 KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL-----RALYRLGRQPPLALL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 147 -ETESWNLKYQMLE-------------KDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFR 212
Cdd:COG4942 126 lSPEDFLDAVRRLQylkylaparreqaEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE 205
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17534411 213 KFKEEAQQDIDSSSEMVEVLALETEELRRKVDGPRSESISD 253
Cdd:COG4942 206 KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
154-267 |
5.27e-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: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 154 KYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDIDSSSEMVEVLA 233
Cdd:COG4026 129 EYNELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKRL 208
|
90 100 110
....*....|....*....|....*....|....
gi 17534411 234 LETEELRRKVDGPRSESISDREDMHEEIEILKAK 267
Cdd:COG4026 209 LEVFSLEELWKELFPEELPEEDFIYFATENLKPG 242
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
82-265 |
5.38e-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: 42.47 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 82 ELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFK---QLLSDEKARGTESMSRLKREKELETESWNLKYQmL 158
Cdd:pfam01576 135 KLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKslsKLKNKHEAMISDLEERLKKEEKGRQELEKAKRK-L 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 159 EKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRkfkeEAQQDIdssSEMVEVLALETee 238
Cdd:pfam01576 214 EGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIR----ELEAQI---SELQEDLESER-- 284
|
170 180
....*....|....*....|....*..
gi 17534411 239 lrrkvdGPRSESISDREDMHEEIEILK 265
Cdd:pfam01576 285 ------AARNKAEKQRRDLGEELEALK 305
|
|
| PRK13169 |
PRK13169 |
DNA replication initiation control protein YabA; |
61-143 |
5.59e-04 |
|
DNA replication initiation control protein YabA;
Pssm-ID: 183876 Cd Length: 110 Bit Score: 39.46 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 61 DALNDFSSQMNQLnsfTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDrfkqllSDEKARGTESMSRL 140
Cdd:PRK13169 8 DALDDLEQNLGVL---LKELGALKKQLAELLEENTALRLENDKLRERLEELEAEEPAKEK------KKKEGEGKDNLARL 78
|
...
gi 17534411 141 KRE 143
Cdd:PRK13169 79 YQE 81
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
72-282 |
5.66e-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: 42.47 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 72 QLNSFTKRYSELEERnmslsdeRTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSdEKARGTESMSRLK---------R 142
Cdd:pfam01576 48 QLQAETELCAEAEEM-------RARLAARKQELEEILHELESRLEEEEERSQQLQN-EKKKMQQHIQDLEeqldeeeaaR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 143 EK-ELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEaqllvegmEEERIQLERQFRKFKEEAQQD 221
Cdd:pfam01576 120 QKlQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAE--------EEEKAKSLSKLKNKHEAMISD 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17534411 222 IDSSSEMVEVLALETEELRRKVDGPRSESISDREDMHEEIEILKAKVAelmKEKEEMTDQL 282
Cdd:pfam01576 192 LEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLA---KKEEELQAAL 249
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
85-291 |
6.09e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 85 ERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESmsRLKREKELETESWNLKYQMLEKDLIS 164
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK--KKAEELKKAEEENKIKAAEEAKKAEE 1672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 165 VKKDAE--RSNEETKRIRNE-LEKTENKLEEAQLLVEGMEEERIQLErQFRKFKEEAQQDidsssemVEVLALETEELRR 241
Cdd:PTZ00121 1673 DKKKAEeaKKAEEDEKKAAEaLKKEAEEAKKAEELKKKEAEEKKKAE-ELKKAEEENKIK-------AEEAKKEAEEDKK 1744
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17534411 242 KVDGPRSESISDREDMHEEIEILKaKVAELMKEKEEMTDQLLATSVERGR 291
Cdd:PTZ00121 1745 KAEEAKKDEEEKKKIAHLKKEEEK-KAEEIRKEKEAVIEEELDEEDEKRR 1793
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
141-282 |
6.23e-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: 42.35 E-value: 6.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 141 KREKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFrkfkEEAQQ 220
Cdd:TIGR02168 220 AELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL----YALAN 295
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17534411 221 DIDSSSEMVEVLALETEELRRK---VDGPRSESISDREDMHEEIEILKAKVAELMKEKEEMTDQL 282
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQleeLEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
104-321 |
7.21e-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: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 104 LKERMHNLEEQLTDNEDRFKQLlsdEKARGTESMSRLKREKELETESWNLKYQMLEKDLisvkKDAERSNEETKRIRNEL 183
Cdd:COG4913 622 LEEELAEAEERLEALEAELDAL---QERREALQRLAEYSWDEIDVASAEREIAELEAEL----ERLDASSDDLAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 184 EKTENKLEEAQLLVEGMEEERIQLERQFRKFKEE---AQQDIDSSSEMVEV-LALETEELRRKVDGPRSESiSDREDMHE 259
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEEldeLQDRLEAAEDLARLeLRALLEERFAAALGDAVER-ELRENLEE 773
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17534411 260 EIEILKAKVAELMKEKEEMTDQLLATSVERGRSLIADTPSLADELAggdssqLLDALREQEI 321
Cdd:COG4913 774 RIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLA------LLDRLEEDGL 829
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
153-289 |
7.34e-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: 41.06 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 153 LKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKE-----EAQQDIDSSSE 227
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArikkyEEQLGNVRNNK 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17534411 228 MVEVLALETEELRRKvdgprsesISDRED----MHEEIEILKAKVAELMKEKEEMTDQLLATSVER 289
Cdd:COG1579 90 EYEALQKEIESLKRR--------ISDLEDeileLMERIEELEEELAELEAELAELEAELEEKKAEL 147
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
170-277 |
7.96e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 7.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 170 ERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRK----FKEEAQQDIDSSSEMVEVLALETEELRRKVDG 245
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKlleeAEKEAQQAIKEAKKEADEIIKELRQLQKGGYA 602
|
90 100 110
....*....|....*....|....*....|....
gi 17534411 246 P--RSESISDREDMHEEIEILKAKVAELMKEKEE 277
Cdd:PRK00409 603 SvkAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
72-238 |
9.32e-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: 9.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 72 QLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERM-------HNLEEQLTDNEDR----FKQLLSDEKARGTESMSRL 140
Cdd:TIGR02169 731 EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIeeleedlHKLEEALNDLEARlshsRIPEIQAELSKLEEEVSRI 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 141 K---REKELETESWNLKYQMLEK---DLISVKKDAE-RSNEETKRIRN---ELEKTENKLEEAQLLVEGMEEERIQLERQ 210
Cdd:TIGR02169 811 EarlREIEQKLNRLTLEKEYLEKeiqELQEQRIDLKeQIKSIEKEIENlngKKEELEEELEELEAALRDLESRLGDLKKE 890
|
170 180 190
....*....|....*....|....*....|....
gi 17534411 211 FRKFK------EEAQQDIDSSSEMVEVLALETEE 238
Cdd:TIGR02169 891 RDELEaqlrelERKIEELEAQIEKKRKRLSELKA 924
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
72-282 |
1.06e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 72 QLNSFTKRYSELEERnmsLSDERTRLKTENSVLKErmhnlEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKElETESW 151
Cdd:PRK03918 460 ELKRIEKELKEIEEK---ERKLRKELRELEKVLKK-----ESELIKLKELAEQLKELEEKLKKYNLEELEKKAE-EYEKL 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 152 NLKYQMLEKDLISVKKDAERSNEetkrIRNELEKTENKLEEAqllvegmEEERIQLERQFRKFKEEAQQDIDSSSEMVEV 231
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLEE----LKKKLAELEKKLDEL-------EEELAELLKELEELGFESVEELEERLKELEP 599
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17534411 232 LALETEELRRKVDGPRSEsISDREDMHEEIEILKAKVAELMKEKEEMTDQL 282
Cdd:PRK03918 600 FYNEYLELKDAEKELERE-EKELKKLEEELDKAFEELAETEKRLEELRKEL 649
|
|
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
60-201 |
1.47e-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: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 60 QDALNDFSSQMNQLNSFTKRYSELEERNmSLSDERTRLKTENSVLKERMHNLEEQLTDNE-------DRFKQLLS----- 127
Cdd:pfam15934 68 HETLKDRDHQIKQLQSMITGYSDISENN-RLKEEIHDLKQKNCVQARVVRKMGLELKGQEeqrvelcDKYESLLGsfeeq 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 128 -----DEKARGTESMSRL----KREKELETESwnlkyQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVE 198
Cdd:pfam15934 147 cqelkRANRRVQSLQTRLsqveKLQEELRTER-----KILREEVIALKEKDAKSNGRERALQDQLKCCQTEIEKSRTLIR 221
|
...
gi 17534411 199 GME 201
Cdd:pfam15934 222 NMQ 224
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
63-282 |
1.56e-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: 41.16 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 63 LNDFSSQMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTdnedRFKQLLSDEKARGTESMSRLKR 142
Cdd:TIGR04523 144 LTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLL----KLELLLSNLKKKIQKNKSLESQ 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 143 EKELETESWNLKYQMLEKDLISVKKDAERSNEETK---------RIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRK 213
Cdd:TIGR04523 220 ISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQlnqlkdeqnKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD 299
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17534411 214 FKEEAQQDIdsSSEMVEVLALETEELrRKVDGPRSESISDREDMHEEIEILKAKVAELMKEKEEMTDQL 282
Cdd:TIGR04523 300 LNNQKEQDW--NKELKSELKNQEKKL-EEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
75-253 |
2.18e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.66 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 75 SFTKRYSELEERNMSLSDERTRLKTENSVLK---ERMHNLEEQLTDNEDRFKQLlsdeKARGTESMSRLKREKELETESW 151
Cdd:PLN02939 223 SLSKELDVLKEENMLLKDDIQFLKAELIEVAeteERVFKLEKERSLLDASLREL----ESKFIVAQEDVSKLSPLQYDCW 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 152 NLKYQMLEKDLISVKKDAERSN---EETKRIRNELEKTENKLEEAQL------LVEGMEEERIQLERQFRKFKEEAQQDI 222
Cdd:PLN02939 299 WEKVENLQDLLDRATNQVEKAAlvlDQNQDLRDKVDKLEASLKEANVskfssyKVELLQQKLKLLEERLQASDHEIHSYI 378
|
170 180 190
....*....|....*....|....*....|....*
gi 17534411 223 ----DSSSEMVEVLALETEELRRKvdgPRSESISD 253
Cdd:PLN02939 379 qlyqESIKEFQDTLSKLKEESKKR---SLEHPADD 410
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
81-181 |
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 17534411 81 SELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLS--DEKARGTESMSRLKREkeleteswnlkYQML 158
Cdd:COG2433 409 TEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSeeRREIRKDREISRLDRE-----------IERL 477
|
90 100
....*....|....*....|...
gi 17534411 159 EKDLISVKKDAERSNEETKRIRN 181
Cdd:COG2433 478 ERELEEERERIEELKRKLERLKE 500
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
63-319 |
2.70e-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: 40.49 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 63 LNDFSSQMNQLNS--------FTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLtdnedrfKQLLSDEKargt 134
Cdd:pfam15921 319 LSDLESTVSQLRSelreakrmYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL-------QKLLADLH---- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 135 esmsrlKREKELEteswnlkyqmLEKDLISVKKDAERSNEET-KRIRNELEKTENKLEEAQLLVEGMEEE-RIQLERQFR 212
Cdd:pfam15921 388 ------KREKELS----------LEKEQNKRLWDRDTGNSITiDHLRRELDDRNMEVQRLEALLKAMKSEcQGQMERQMA 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 213 KF--KEEAQQDIDSSSEMV----EVLALETEELR-RKVDGPRSE-SISD-REDMHEEIEILKAKVAELMKEKEEMTDQL- 282
Cdd:pfam15921 452 AIqgKNESLEKVSSLTAQLestkEMLRKVVEELTaKKMTLESSErTVSDlTASLQEKERAIEATNAEITKLRSRVDLKLq 531
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 17534411 283 ----LATSVERGRSLIADTPSLADELAGGDssQLLDALREQ 319
Cdd:pfam15921 532 elqhLKNEGDHLRNVQTECEALKLQMAEKD--KVIEILRQQ 570
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
81-277 |
2.71e-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: 40.11 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 81 SELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQL--LSDEKARGTESMSRLKREKELETESWNLKYQML 158
Cdd:pfam05557 30 IELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQaeLNRLKKKYLEALNKKLNEKESQLADAREVISCL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 159 EKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQ-------------QDI--- 222
Cdd:pfam05557 110 KNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQrikelefeiqsqeQDSeiv 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17534411 223 -DSSSEMVEVLALETEELRRKVDGPR-SESISDREDMHEEIEILKAKVAELMKEKEE 277
Cdd:pfam05557 190 kNSKSELARIPELEKELERLREHNKHlNENIENKLLLKEEVEDLKRKLEREEKYREE 246
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
81-266 |
2.89e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 81 SELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELETESWNLK------ 154
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRdrleec 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 155 ---YQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEE---AQQDIDSSSEM 228
Cdd:PRK02224 334 rvaAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdAPVDLGNAEDF 413
|
170 180 190
....*....|....*....|....*....|....*...
gi 17534411 229 VEVLALETEELRRKVDGPRSESISDREDMHEEIEILKA 266
Cdd:PRK02224 414 LEELREERDELREREAELEATLRTARERVEEAEALLEA 451
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
170-271 |
3.13e-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: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 170 ERSNEETKRIRNELEKTENKLEEAqllvegmeEERIQ-LERQFRKFKEEAQQDIDSSSEmVEVLALETEELRRKVdgprs 248
Cdd:COG2433 416 RRLEEQVERLEAEVEELEAELEEK--------DERIErLERELSEARSEERREIRKDRE-ISRLDREIERLEREL----- 481
|
90 100
....*....|....*....|...
gi 17534411 249 esisdrEDMHEEIEILKAKVAEL 271
Cdd:COG2433 482 ------EEERERIEELKRKLERL 498
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
160-319 |
3.21e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 160 KDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFkeEAQQDIDSSSEMVEVLALETEEL 239
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL--PLYQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 240 RRKvdgprsesISDREDMHEEIEILKAKVAELMKEKEEMTDQLLATSVERGRSLIADTPSLADELAggDSSQLLDALREQ 319
Cdd:COG4717 152 EER--------LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLA--ELEEELEEAQEE 221
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
112-277 |
3.39e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 112 EEQLTDNEDRFKQLLSDEKAR-----------GTESMSRLKREKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIR 180
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEaeaikkealleAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 181 NELEKTENKLEEAQLLVEGMEEEriqLERqfrkfKEEAQQDidsssEMVEVLALETEELRRKVdgprsesisdREDMHEE 260
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEE---LEE-----LIEEQLQ-----ELERISGLTAEEAKEIL----------LEKVEEE 166
|
170
....*....|....*..
gi 17534411 261 ieiLKAKVAELMKEKEE 277
Cdd:PRK12704 167 ---ARHEAAVLIKEIEE 180
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
82-296 |
3.68e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 82 ELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFK--------QLLSDEKARGTESMSRLKREkELETESWNL 153
Cdd:PRK02224 409 NAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecgQPVEGSPHVETIEEDRERVE-ELEAELEDL 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 154 KYQMLE--------KDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLE---RQFRKFKEEAQQDI 222
Cdd:PRK02224 488 EEEVEEveerleraEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEaeaEEKREAAAEAEEEA 567
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17534411 223 DSSSEMVEVLALETEELRRKVDGPR--SESISDREDMHEEIEILKAKVAELmKEKEEMTDQLLATSVERGRSLIAD 296
Cdd:PRK02224 568 EEAREEVAELNSKLAELKERIESLEriRTLLAAIADAEDEIERLREKREAL-AELNDERRERLAEKRERKRELEAE 642
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
78-277 |
3.71e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 78 KRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELEteswNLKYQM 157
Cdd:PTZ00121 1224 KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD----EAKKAE 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 158 LEKDLISVKKDAErsneETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQfRKFKEEAQQDIDSSSEMVEVLALETE 237
Cdd:PTZ00121 1300 EKKKADEAKKKAE----EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAA-KAEAEAAADEAEAAEEKAEAAEKKKE 1374
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17534411 238 ELRRKVDG--PRSESISDREDMHEEIEILKAKVAELMKEKEE 277
Cdd:PTZ00121 1375 EAKKKADAakKKAEEKKKADEAKKKAEEDKKKADELKKAAAA 1416
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
82-239 |
3.76e-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: 39.49 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 82 ELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELETESWNLKYQMLEKD 161
Cdd:pfam07888 70 QWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17534411 162 LisvkkDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDIDSSSEMVEVLALETEEL 239
Cdd:pfam07888 150 T-----ELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKL 222
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
138-271 |
5.46e-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: 39.28 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 138 SRLKREKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEE 217
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 17534411 218 AQQdidsSSEMVEVLALETEELRRKVDgprsESISDREDMHEEIEILKAKVAEL 271
Cdd:TIGR02169 739 LEE----LEEDLSSLEQEIENVKSELK----ELEARIEELEEDLHKLEEALNDL 784
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
60-244 |
5.69e-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: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 60 QDALNDFSSQmNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEkargteSMSR 139
Cdd:COG3206 195 EAALEEFRQK-NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP------VIQQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 140 LKREkeleteswnlkYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKL-EEAQLLVEGMEEERIQLERQFRKFKEEA 218
Cdd:COG3206 268 LRAQ-----------LAELEAELAELSARYTPNHPDVIALRAQIAALRAQLqQEAQRILASLEAELEALQAREASLQAQL 336
|
170 180
....*....|....*....|....*.
gi 17534411 219 QQDIDSSSEMVEVLAlETEELRRKVD 244
Cdd:COG3206 337 AQLEARLAELPELEA-ELRRLEREVE 361
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
106-282 |
6.43e-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: 39.28 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 106 ERMHNLEEQLTDNEDRfkqlLSDEKARgTESMSRLKREKElETESWNL--KYQMLEKDLISVKKDAERSNEETKRIRNEL 183
Cdd:TIGR02169 187 ERLDLIIDEKRQQLER----LRREREK-AERYQALLKEKR-EYEGYELlkEKEALERQKEAIERQLASLEEELEKLTEEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 184 EKTENKLEEAQLLVEGM--------EEERIQLERQFRKFKEEAQQdIDSSSEMVEVLALETEELRRKVDGPRSESISDRE 255
Cdd:TIGR02169 261 SELEKRLEEIEQLLEELnkkikdlgEEEQLRVKEKIGELEAEIAS-LERSIAEKERELEDAEERLAKLEAEIDKLLAEIE 339
|
170 180
....*....|....*....|....*..
gi 17534411 256 DMHEEIEILKAKVAELMKEKEEMTDQL 282
Cdd:TIGR02169 340 ELEREIEEERKRRDKLTEEYAELKEEL 366
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
92-282 |
6.66e-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: 38.93 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 92 DERTRLKTEN-SVLKERMHNLEEQLTDNEDRFKQLLSDEKAR------GTESMSRLKREKELETESWNLKYQM------- 157
Cdd:pfam05483 274 EEKTKLQDENlKELIEKKDHLTKELEDIKMSLQRSMSTQKALeedlqiATKTICQLTEEKEAQMEELNKAKAAhsfvvte 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 158 -------LEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEeerIQLErQFRKFKEEAQQDIDSSSEmVE 230
Cdd:pfam05483 354 feattcsLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKE---VELE-ELKKILAEDEKLLDEKKQ-FE 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17534411 231 VLALETEELRRKVDGPRSESISDREDMHEEIEILKAKVAELMKEKEEMTDQL 282
Cdd:pfam05483 429 KIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL 480
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
164-273 |
7.39e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.17 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 164 SVKKDAERSNEETKRIRNELEKTENKLEEAqllvEGMEEERIQLERQFRKFKEEAQQDIDSSSEmVEVLALETEELRRKV 243
Cdd:PRK04863 496 DVARELLRRLREQRHLAEQLQQLRMRLSEL----EQRLRQQQRAERLLAEFCKRLGKNLDDEDE-LEQLQEELEARLESL 570
|
90 100 110
....*....|....*....|....*....|
gi 17534411 244 DGPRSESISDREDMHEEIEILKAKVAELMK 273
Cdd:PRK04863 571 SESVSEARERRMALRQQLEQLQARIQRLAA 600
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
60-228 |
7.45e-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: 38.88 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 60 QDALNDFSSQMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSR 139
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 140 LKREKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEeeriQLERQFRKFKEEAQ 219
Cdd:TIGR02168 434 ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE----RLQENLEGFSEGVK 509
|
....*....
gi 17534411 220 QDIDSSSEM 228
Cdd:TIGR02168 510 ALLKNQSGL 518
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
135-243 |
7.47e-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: 38.96 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534411 135 ESMSRLKREKELETESWNLKYQMLEKDLISVK-------KDAERSNEETKRIRNELEKTENKLEEAQLLVEGM------- 200
Cdd:pfam07111 151 EQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkrageaKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLrkyvgeq 230
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17534411 201 ----------EEERIQLERQFRKFKEEaQQDIDSSSEMVEV--------LALETEELRRKV 243
Cdd:pfam07111 231 vppevhsqtwELERQELLDTMQHLQED-RADLQATVELLQVrvqslthmLALQEEELTRKI 290
|
|
| |
