|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
55-349 |
1.50e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 55 QLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELETEsw 134
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE-- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 135 nlkyqmlEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDIDSSSEMVEV 214
Cdd:COG1196 353 -------LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 215 LALETEELRRKVDGPRSESISDREDMHEEIEILKAKVAELMKEKEEMTDQLLATSVERGRSLIADTPSLADELAGGDSSQ 294
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1831508212 295 LLDALREQEICNQKLRVYINGILMRVIERHPEILEIGEEGILSKLTVRRRISVLA 349
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA 560
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
45-265 |
2.19e-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: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 45 ALNDFSSQMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSD------EKARGTE 118
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEisrleqQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 119 SMSRLKRE-KELETESWNLKYQM--LEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFR 195
Cdd:TIGR02168 310 RLANLERQlEELEAQLEELESKLdeLAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 196 KFKEEAQQ----------DIDSSSEMVEVLALETEELRRKVDGPRSESISDR-EDMHEEIEILKAKVAELMKEKEEMTDQ 264
Cdd:TIGR02168 390 QLELQIASlnneierleaRLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREE 469
|
.
gi 1831508212 265 L 265
Cdd:TIGR02168 470 L 470
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
55-303 |
2.51e-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: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 55 QLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELETESw 134
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 135 nlkyQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDIDSSSEMVEV 214
Cdd:COG1196 305 ----ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 215 LALETEELRRKVDGpRSESISDREDMHEEIEILKAKVAELMKEKEEMTDQLLATSVERGRSLIADTPSLADELAGGDSSQ 294
Cdd:COG1196 381 LEELAEELLEALRA-AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
....*....
gi 1831508212 295 LLDALREQE 303
Cdd:COG1196 460 ALLELLAEL 468
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
76-309 |
4.15e-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: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 76 ERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDekargTESMSRLKREKELETESWNLKYQMLEKDLISVKKDAERS 155
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEE-----LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 156 NEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDIDSSSEMVEVLALETEELRRKVDG-----PR 230
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERlesleRR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 231 SESISDR--------EDMHEEIEILKAKVAELMKEKEEMTDQL-----LATSVERGRSLIADTPSLADELAGGDSSQLLD 297
Cdd:TIGR02168 833 IAATERRledleeqiEELSEDIESLAAEIEELEELIEELESELeallnERASLEEALALLRSELEELSEELRELESKRSE 912
|
250
....*....|..
gi 1831508212 298 ALREQEICNQKL 309
Cdd:TIGR02168 913 LRRELEELREKL 924
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
43-288 |
4.26e-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: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 43 QDALNDFSSQMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSR 122
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 123 LKREKELETESwnlkyQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKF---KE 199
Cdd:COG1196 364 EEALLEAEAEL-----AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELeeeEE 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 200 EAQQDIDSSSEMVEVLALETEELRRKVDGPRSESISDREDMHEEIEILKAKVAELMKEKEEMTDQLLATSVERGRSLIAD 279
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
....*....
gi 1831508212 280 TPSLADELA 288
Cdd:COG1196 519 LRGLAGAVA 527
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
54-287 |
8.72e-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: 8.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 54 NQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLK--------- 124
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaeiaslers 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 125 -REKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQllvEGMEEERIQLERQFRKFKeEAQQ 203
Cdd:TIGR02169 310 iAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK---EELEDLRAELEEVDKEFA-ETRD 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 204 DIDSSSEMVEVLALETEELRRKVDGPRSESI---SDREDMHEEIEILKAKVAELMKEKEEMTDQlLATSVERGRSLIADT 280
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRELDRLQEELQrlsEELADLNAAIAGIEAKINELEEEKEDKALE-IKKQEWKLEQLAADL 464
|
....*..
gi 1831508212 281 PSLADEL 287
Cdd:TIGR02169 465 SKYEQEL 471
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
72-267 |
1.56e-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: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 72 SLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELETeswnlkyqmLEKDLISVKKD 151
Cdd:pfam05667 280 LLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQREEELEE---------LQEQLEDLESS 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 152 AERSNEETKRIRNELEKTENKLEEaqllvegMEEERIQLERQFRKFK-------------EEAQQDIDSSSEMVEVLALE 218
Cdd:pfam05667 351 IQELEKEIKKLESSIKQVEEELEE-------LKEQNEELEKQYKVKKktldllpdaeeniAKLQALVDASAQRLVELAGQ 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1831508212 219 TEELR-------RKVDGPRSESISDREDMHEEIEILKAK---VAELMKEKEEMTDQLLA 267
Cdd:pfam05667 424 WEKHRvplieeyRALKEAKSNKEDESQRKLEEIKELREKikeVAEEAKQKEELYKQLVA 482
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
81-260 |
2.36e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 81 KTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESmSRLKREKELETESWNLKYQMLEKDLISVKKDAE--RSNEE 158
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE-ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkKAEEE 1631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 159 TKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFK------EEAQQDIDSSSEMVEVLALETEELRR--KVDGPR 230
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEedkkkaEEAKKAEEDEKKAAEALKKEAEEAKKaeELKKKE 1711
|
170 180 190
....*....|....*....|....*....|
gi 1831508212 231 SESISDREDMHEEIEILKAKVAELMKEKEE 260
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
65-265 |
4.66e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 65 ELEERNMSLSDERTRLKTENSVLKERMHNLEEQltdNEDRFKQLLSDEKARGTESMSRLKREKELETESWNLKYQMLEKD 144
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE---KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 145 LISVKKDAE----------RSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLErQFRKFKEEAQQDIDSSSEMVEV 214
Cdd:PTZ00121 1649 AEELKKAEEenkikaaeeaKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE-ELKKKEAEEKKKAEELKKAEEE 1727
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1831508212 215 LALETEELRRKVDGPRSESISDREDMHEeieilKAKVAELMKEKEEMTDQL 265
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEEAKKDEEE-----KKKIAHLKKEEEKKAEEI 1773
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
61-274 |
7.12e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 61 KRYSELEERNMSLSD-ERTRLKTENSV--LKERMHNLEEQLTDNEDRFKQLlsDEKARGTESMsrlkREKELETESWNLK 137
Cdd:PRK03918 228 KEVKELEELKEEIEElEKELESLEGSKrkLEEKIRELEERIEELKKEIEEL--EEKVKELKEL----KEKAEEYIKLSEF 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 138 YQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEaqllVEGMEEERIQLERQFRKFKEEAQQdidssSEMVEVLAL 217
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER----LEELKKKLKELEKRLEELEERHEL-----YEEAKAKKE 372
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1831508212 218 ETEELRRKVDGprsesisdredmhEEIEILKAKVAELMKEKEEMTDQLLATSVERGR 274
Cdd:PRK03918 373 ELERLKKRLTG-------------LTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
88-207 |
1.20e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 88 KERMHNLEEQLTDNEDRF--KQLLSDEKARGTESMSRL----KREKELETEswnlkYQMLEKDLISVKkDAERSNEETKR 161
Cdd:PRK04863 279 NERRVHLEEALELRRELYtsRRQLAAEQYRLVEMARELaelnEAESDLEQD-----YQAASDHLNLVQ-TALRQQEKIER 352
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1831508212 162 IRNELEKTENKLEEAQLLVEGMEEERIQLERQfrkfKEEAQQDIDS 207
Cdd:PRK04863 353 YQADLEELEERLEEQNEVVEEADEQQEENEAR----AEAAEEEVDE 394
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
61-206 |
1.27e-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: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 61 KRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKargtESMSRLKREKELETESWNLK-YQ 139
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE----EVEARIKKYEEQLGNVRNNKeYE 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831508212 140 MLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDID 206
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 ... |
294-330 |
1.29e-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: 41.94 E-value: 1.29e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1831508212 294 QLLDALREQEICNQKLRVYINGILMRVIERHPEILEI 330
Cdd:pfam09457 4 ELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEV 40
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
89-207 |
1.92e-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: 47.25 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 89 ERMHNLEEQLTDNEDRF--KQLLSDEKARGTESMSRLK----REKELETEswnlkYQMLEKDLISVKkDAERSNEETKRI 162
Cdd:COG3096 279 ERRELSERALELRRELFgaRRQLAEEQYRLVEMARELEelsaRESDLEQD-----YQAASDHLNLVQ-TALRQQEKIERY 352
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1831508212 163 RNELEKTENKLEEAQLLVEGMEEERIQLERQFrkfkEEAQQDIDS 207
Cdd:COG3096 353 QEDLEELTERLEEQEEVVEEAAEQLAEAEARL----EAAEEEVDS 393
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
60-256 |
2.21e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 60 TKRYSELEERNMSLSDERTRLKTENSVLKE---RMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKRE-KELEteswn 135
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEERlKELE----- 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 136 lKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFK-EEAQQDIDSSSEMVEV 214
Cdd:PRK03918 599 -PFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAG 677
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1831508212 215 LALETEELRRKVDgprsESISDREDMHEEIEILKAKVAELMK 256
Cdd:PRK03918 678 LRAELEELEKRRE----EIKKTLEKLKEELEEREKAKKELEK 715
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
62-194 |
3.24e-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: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 62 RYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDnedrFKQLLSDEKARGTESmsrlkrekeletESWNLKYQML 141
Cdd:pfam12718 22 KVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKE----AKEKAEESEKLKTNN------------ENLTRKIQLL 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1831508212 142 EKDLisvkkdaERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQF 194
Cdd:pfam12718 86 EEEL-------EESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKY 131
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
52-289 |
5.33e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 52 QMNQLNSFTKRYSELEERNMSLSDERTRLK-----TENsvLKERMHNLEEQLTDNEDRFKQLlSDEKARGTESMSRLKRE 126
Cdd:PRK03918 153 QILGLDDYENAYKNLGEVIKEIKRRIERLEkfikrTEN--IEELIKEKEKELEEVLREINEI-SSELPELREELEKLEKE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 127 KElETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEE--ERIQLERQFRKFKEEAQQD 204
Cdd:PRK03918 230 VK-ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 205 IDSSSEMVEVLALETEELRRKvdgprsesISDREDMHEEIEILKAKVAELMKEKEEMTDQLLAtsVERGRSLIADTPSLA 284
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEER--------IKELEEKEERLEELKKKLKELEKRLEELEERHEL--YEEAKAKKEELERLK 378
|
....*
gi 1831508212 285 DELAG 289
Cdd:PRK03918 379 KRLTG 383
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
68-204 |
1.50e-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: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 68 ERNMSLSDERTRLKTENSVLKERMH---NLEEQLTDNEDRF-KQLLSDEKARGTESMSRLKREKELETESWNLKYQMLEK 143
Cdd:pfam15709 351 ERKRREQEEQRRLQQEQLERAEKMReelELEQQRRFEEIRLrKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRR 430
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831508212 144 DLISVK-----KDAERSNEETKRiRNELEktENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQD 204
Cdd:pfam15709 431 KLQELQrkkqqEEAERAEAEKQR-QKELE--MQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLE 493
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
80-310 |
1.58e-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: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 80 LKTENSVLKERMHNLEEQLTDNEDRFKQLL----------------SDEKARGTESMSRLKREKELETESWNLKYQMLEK 143
Cdd:pfam04849 92 LLKQNSVLTERNEALEEQLGSAREEILQLRhelskkddllqiysndAEESETESSCSTPLRRNESFSSLHGCVQLDALQE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 144 DLISVKKDAERSNEETKRIRNELEKTENKleEAQLLVEGMEEERiqlerqfrkfkeEAQQDIdssSEMVEVLALETEELR 223
Cdd:pfam04849 172 KLRGLEEENLKLRSEASHLKTETDTYEEK--EQQLMSDCVEQLS------------EANQQM---AELSEELARKMEENL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 224 RKvdgprsesisdredmHEEIEILKAKVAEL-------MKEKEEMTdQLLATSVERGRSLIADTPSLADELAggdssQLL 296
Cdd:pfam04849 235 RQ---------------QEEITSLLAQIVDLqhkckelGIENEELQ-QHLQASKEAQRQLTSELQELQDRYA-----ECL 293
|
250
....*....|....
gi 1831508212 297 DALREQEICNQKLR 310
Cdd:pfam04849 294 GMLHEAQEELKELR 307
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
104-310 |
1.71e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 104 RFKQLLSDEKARGTESMSRLKREKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGM 183
Cdd:COG1196 214 RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 184 EEERIQLERQfrkfKEEAQQDIDSSSEMVEVLALETEELRRKvdgprsesisdREDMHEEIEILKAKVAELMKEKEEMTD 263
Cdd:COG1196 294 LAELARLEQD----IARLEERRRELEERLEELEEELAELEEE-----------LEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1831508212 264 QLLATSVERGRSLIADTPSLADELAggDSSQLLDALREQEICNQKLR 310
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEE--LAEELLEALRAAAELAAQLE 403
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
52-227 |
2.62e-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: 43.57 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 52 QMNQLNSFTKRYSELEERNMS-LSDERTR-LKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKEL 129
Cdd:pfam17380 418 QKVEMEQIRAEQEEARQREVRrLEEERAReMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIL 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 130 ETESWNLKYQMLEkdlisvkkdaersnEETKR--IRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDIDS 207
Cdd:pfam17380 498 EKELEERKQAMIE--------------EERKRklLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE 563
|
170 180
....*....|....*....|
gi 1831508212 208 SSEMVEVLALETEELRRKVD 227
Cdd:pfam17380 564 ERSRLEAMEREREMMRQIVE 583
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
57-261 |
3.14e-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: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 57 NSFTKRYSELEERNMSLSDERTRLKTENsVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTEsmsrLKREKELETESWNL 136
Cdd:pfam17380 268 NEFLNQLLHIVQHQKAVSERQQQEKFEK-MEQERLRQEKEEKAREVERRRKLEEAEKARQAE----MDRQAAIYAEQERM 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 137 kyqmlekdlisvkkdAERSNEETKRIRNELEKTEN---KLEEAQLLVEGMEE-ERIQLERQ------------FRKFK-- 198
Cdd:pfam17380 343 ---------------AMERERELERIRQEERKRELeriRQEEIAMEISRMRElERLQMERQqknervrqeleaARKVKil 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831508212 199 -EEAQQDIDSSSEMVEVLALETEELR----RKVDGPRSESIS----DREDMHEEIEILKAKVAELMKEKEEM 261
Cdd:pfam17380 408 eEERQRKIQQQKVEMEQIRAEQEEARqrevRRLEEERAREMErvrlEEQERQQQVERLRQQEEERKRKKLEL 479
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
68-274 |
3.72e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 68 ERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESmsRLKREKELETESWNLKYQMLEKDLIS 147
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK--KKAEELKKAEEENKIKAAEEAKKAEE 1672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 148 VKKDAE--RSNEETKRIRNE-LEKTENKLEEAQLLVEGMEEERIQLErQFRKFKEEaqqdidsSSEMVEVLALETEELRR 224
Cdd:PTZ00121 1673 DKKKAEeaKKAEEDEKKAAEaLKKEAEEAKKAEELKKKEAEEKKKAE-ELKKAEEE-------NKIKAEEAKKEAEEDKK 1744
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1831508212 225 KVDGPRSESISDREDMHEEIEILKaKVAELMKEKEEMTDQLLATSVERGR 274
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 ... |
55-265 |
4.59e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 55 QLNSFTKRYSELEERnmslsdeRTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSdEKARGTESMSRLK---------R 125
Cdd:pfam01576 48 QLQAETELCAEAEEM-------RARLAARKQELEEILHELESRLEEEEERSQQLQN-EKKKMQQHIQDLEeqldeeeaaR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 126 EK-ELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEaqllvegmEEERIQLERQFRKFKEEAQQD 204
Cdd:pfam01576 120 QKlQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAE--------EEEKAKSLSKLKNKHEAMISD 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831508212 205 IDSSSEMVEVLALETEELRRKVDGPRSESISDREDMHEEIEILKAKVAelmKEKEEMTDQL 265
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 ... |
65-248 |
4.71e-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: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 65 ELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFK---QLLSDEKARGTESMSRLKREKELETESWNLKYQmL 141
Cdd:pfam01576 135 KLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKslsKLKNKHEAMISDLEERLKKEEKGRQELEKAKRK-L 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 142 EKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRkfkeEAQQDIdssSEMVEVLALETee 221
Cdd:pfam01576 214 EGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIR----ELEAQI---SELQEDLESER-- 284
|
170 180
....*....|....*....|....*..
gi 1831508212 222 lrrkvdGPRSESISDREDMHEEIEILK 248
Cdd:pfam01576 285 ------AARNKAEKQRRDLGEELEALK 305
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
137-250 |
5.00e-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: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 137 KYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDIDSSSEMVEVLA 216
Cdd:COG4026 129 EYNELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKRL 208
|
90 100 110
....*....|....*....|....*....|....
gi 1831508212 217 LETEELRRKVDGPRSESISDREDMHEEIEILKAK 250
Cdd:COG4026 209 LEVFSLEELWKELFPEELPEEDFIYFATENLKPG 242
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
87-265 |
5.10e-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: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 87 LKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNEL 166
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 167 EKTENKLEEAQLLVEGMEEERIQLERQFRKFKEE---AQQDIDSSSEMVEVLALETEELRRKVDGPRSESISDREDMHEE 243
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEEleeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180
....*....|....*....|..
gi 1831508212 244 IEILKAKVAELMKEKEEMTDQL 265
Cdd:COG1196 378 EEELEELAEELLEALRAAAELA 399
|
|
| PRK13169 |
PRK13169 |
DNA replication initiation control protein YabA; |
44-126 |
5.41e-04 |
|
DNA replication initiation control protein YabA;
Pssm-ID: 183876 Cd Length: 110 Bit Score: 39.46 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 44 DALNDFSSQMNQLnsfTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDrfkqllSDEKARGTESMSRL 123
Cdd:PRK13169 8 DALDDLEQNLGVL---LKELGALKKQLAELLEENTALRLENDKLRERLEELEAEEPAKEK------KKKEGEGKDNLARL 78
|
...
gi 1831508212 124 KRE 126
Cdd:PRK13169 79 YQE 81
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
124-265 |
6.10e-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: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 124 KREKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFrkfkEEAQQ 203
Cdd:TIGR02168 220 AELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL----YALAN 295
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831508212 204 DIDSSSEMVEVLALETEELRRK---VDGPRSESISDREDMHEEIEILKAKVAELMKEKEEMTDQL 265
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQleeLEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
50-236 |
6.30e-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: 41.67 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 50 SSQMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLsdekaRGTESMSRLKREKEL 129
Cdd:COG4942 51 KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL-----RALYRLGRQPPLALL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 130 -ETESWNLKYQMLE-------------KDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFR 195
Cdd:COG4942 126 lSPEDFLDAVRRLQylkylaparreqaEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE 205
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1831508212 196 KFKEEAQQDIDSSSEMVEVLALETEELRRKVDGPRSESISD 236
Cdd:COG4942 206 KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
153-260 |
7.53e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 153 ERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRK----FKEEAQQDIDSSSEMVEVLALETEELRRKVDG 228
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKlleeAEKEAQQAIKEAKKEADEIIKELRQLQKGGYA 602
|
90 100 110
....*....|....*....|....*....|....
gi 1831508212 229 P--RSESISDREDMHEEIEILKAKVAELMKEKEE 260
Cdd:PRK00409 603 SvkAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
87-304 |
7.56e-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: 7.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 87 LKERMHNLEEQLTDNEDRFKQLlsdEKARGTESMSRLKREKELETESWNLKYQMLEKDLisvkKDAERSNEETKRIRNEL 166
Cdd:COG4913 622 LEEELAEAEERLEALEAELDAL---QERREALQRLAEYSWDEIDVASAEREIAELEAEL----ERLDASSDDLAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 167 EKTENKLEEAQLLVEGMEEERIQLERQFRKFKEE---AQQDIDSSSEMVEV-LALETEELRRKVDGPRSESiSDREDMHE 242
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEEldeLQDRLEAAEDLARLeLRALLEERFAAALGDAVER-ELRENLEE 773
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831508212 243 EIEILKAKVAELMKEKEEMTDQLLATSVERGRSLIADTPSLADELAggdssqLLDALREQEI 304
Cdd:COG4913 774 RIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLA------LLDRLEEDGL 829
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
136-272 |
8.01e-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: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 136 LKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKE-----EAQQDIDSSSE 210
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArikkyEEQLGNVRNNK 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831508212 211 MVEVLALETEELRRKvdgprsesISDRED----MHEEIEILKAKVAELMKEKEEMTDQLLATSVER 272
Cdd:COG1579 90 EYEALQKEIESLKRR--------ISDLEDeileLMERIEELEEELAELEAELAELEAELEEKKAEL 147
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
55-221 |
8.82e-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: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 55 QLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERM-------HNLEEQLTDNEDR----FKQLLSDEKARGTESMSRL 123
Cdd:TIGR02169 731 EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIeeleedlHKLEEALNDLEARlshsRIPEIQAELSKLEEEVSRI 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 124 K---REKELETESWNLKYQMLEK---DLISVKKDAE-RSNEETKRIRN---ELEKTENKLEEAQLLVEGMEEERIQLERQ 193
Cdd:TIGR02169 811 EarlREIEQKLNRLTLEKEYLEKeiqELQEQRIDLKeQIKSIEKEIENlngKKEELEEELEELEAALRDLESRLGDLKKE 890
|
170 180 190
....*....|....*....|....*....|....
gi 1831508212 194 FRKFK------EEAQQDIDSSSEMVEVLALETEE 221
Cdd:TIGR02169 891 RDELEaqlrelERKIEELEAQIEKKRKRLSELKA 924
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
55-265 |
8.87e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 55 QLNSFTKRYSELEERnmsLSDERTRLKTENSVLKErmhnlEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKElETESW 134
Cdd:PRK03918 460 ELKRIEKELKEIEEK---ERKLRKELRELEKVLKK-----ESELIKLKELAEQLKELEEKLKKYNLEELEKKAE-EYEKL 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 135 NLKYQMLEKDLISVKKDAERSNEetkrIRNELEKTENKLEEAqllvegmEEERIQLERQFRKFKEEAQQDIDSSSEMVEV 214
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLEE----LKKKLAELEKKLDEL-------EEELAELLKELEELGFESVEELEERLKELEP 599
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1831508212 215 LALETEELRRKVDGPRSEsISDREDMHEEIEILKAKVAELMKEKEEMTDQL 265
Cdd:PRK03918 600 FYNEYLELKDAEKELERE-EKELKKLEEELDKAFEELAETEKRLEELRKEL 649
|
|
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
43-184 |
1.46e-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: 39.94 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 43 QDALNDFSSQMNQLNSFTKRYSELEERNmSLSDERTRLKTENSVLKERMHNLEEQLTDNE-------DRFKQLLS----- 110
Cdd:pfam15934 68 HETLKDRDHQIKQLQSMITGYSDISENN-RLKEEIHDLKQKNCVQARVVRKMGLELKGQEeqrvelcDKYESLLGsfeeq 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 111 -----DEKARGTESMSRL----KREKELETESwnlkyQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVE 181
Cdd:pfam15934 147 cqelkRANRRVQSLQTRLsqveKLQEELRTER-----KILREEVIALKEKDAKSNGRERALQDQLKCCQTEIEKSRTLIR 221
|
...
gi 1831508212 182 GME 184
Cdd:pfam15934 222 NMQ 224
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
46-265 |
1.52e-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: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 46 LNDFSSQMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTdnedRFKQLLSDEKARGTESMSRLKR 125
Cdd:TIGR04523 144 LTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLL----KLELLLSNLKKKIQKNKSLESQ 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 126 EKELETESWNLKYQMLEKDLISVKKDAERSNEETK---------RIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRK 196
Cdd:TIGR04523 220 ISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQlnqlkdeqnKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD 299
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831508212 197 FKEEAQQDIdsSSEMVEVLALETEELrRKVDGPRSESISDREDMHEEIEILKAKVAELMKEKEEMTDQL 265
Cdd:TIGR04523 300 LNNQKEQDW--NKELKSELKNQEKKL-EEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
58-236 |
2.01e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.66 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 58 SFTKRYSELEERNMSLSDERTRLKTENSVLK---ERMHNLEEQLTDNEDRFKQLlsdeKARGTESMSRLKREKELETESW 134
Cdd:PLN02939 223 SLSKELDVLKEENMLLKDDIQFLKAELIEVAeteERVFKLEKERSLLDASLREL----ESKFIVAQEDVSKLSPLQYDCW 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 135 NLKYQMLEKDLISVKKDAERSN---EETKRIRNELEKTENKLEEAQL------LVEGMEEERIQLERQFRKFKEEAQQDI 205
Cdd:PLN02939 299 WEKVENLQDLLDRATNQVEKAAlvlDQNQDLRDKVDKLEASLKEANVskfssyKVELLQQKLKLLEERLQASDHEIHSYI 378
|
170 180 190
....*....|....*....|....*....|....*
gi 1831508212 206 ----DSSSEMVEVLALETEELRRKvdgPRSESISD 236
Cdd:PLN02939 379 qlyqESIKEFQDTLSKLKEESKKR---SLEHPADD 410
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
46-302 |
2.16e-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: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 46 LNDFSSQMNQLNS--------FTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLtdnedrfKQLLSDEKargt 117
Cdd:pfam15921 319 LSDLESTVSQLRSelreakrmYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL-------QKLLADLH---- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 118 esmsrlKREKELEteswnlkyqmLEKDLISVKKDAERSNEET-KRIRNELEKTENKLEEAQLLVEGMEEE-RIQLERQFR 195
Cdd:pfam15921 388 ------KREKELS----------LEKEQNKRLWDRDTGNSITiDHLRRELDDRNMEVQRLEALLKAMKSEcQGQMERQMA 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 196 KF--KEEAQQDIDSSSEMV----EVLALETEELR-RKVDGPRSE-SISD-REDMHEEIEILKAKVAELMKEKEEMTDQL- 265
Cdd:pfam15921 452 AIqgKNESLEKVSSLTAQLestkEMLRKVVEELTaKKMTLESSErTVSDlTASLQEKERAIEATNAEITKLRSRVDLKLq 531
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1831508212 266 ----LATSVERGRSLIADTPSLADELAGGDssQLLDALREQ 302
Cdd:pfam15921 532 elqhLKNEGDHLRNVQTECEALKLQMAEKD--KVIEILRQQ 570
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
61-260 |
2.39e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 61 KRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELEteswNLKYQM 140
Cdd:PTZ00121 1224 KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD----EAKKAE 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 141 LEKDLISVKKDAErsneETKRIRNELEKTENKLEEAQLLVEGMEEERIQLErqFRKFKEEAQQD-IDSSSEMVEVLALET 219
Cdd:PTZ00121 1300 EKKKADEAKKKAE----EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE--AAKAEAEAAADeAEAAEEKAEAAEKKK 1373
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1831508212 220 EELRRKVDG--PRSESISDREDMHEEIEILKAKVAELMKEKEE 260
Cdd:PTZ00121 1374 EEAKKKADAakKKAEEKKKADEAKKKAEEDKKKADELKKAAAA 1416
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
64-164 |
2.51e-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: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 64 SELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLS--DEKARGTESMSRLKREkeleteswnlkYQML 141
Cdd:COG2433 409 TEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSeeRREIRKDREISRLDRE-----------IERL 477
|
90 100
....*....|....*....|...
gi 1831508212 142 EKDLISVKKDAERSNEETKRIRN 164
Cdd:COG2433 478 ERELEEERERIEELKRKLERLKE 500
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
64-260 |
2.57e-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: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 64 SELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQL--LSDEKARGTESMSRLKREKELETESWNLKYQML 141
Cdd:pfam05557 30 IELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQaeLNRLKKKYLEALNKKLNEKESQLADAREVISCL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 142 EKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQ-------------QDI--- 205
Cdd:pfam05557 110 KNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQrikelefeiqsqeQDSeiv 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1831508212 206 -DSSSEMVEVLALETEELRRKVDGPR-SESISDREDMHEEIEILKAKVAELMKEKEE 260
Cdd:pfam05557 190 kNSKSELARIPELEKELERLREHNKHlNENIENKLLLKEEVEDLKRKLEREEKYREE 246
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
64-249 |
2.72e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 64 SELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELETESWNLK------ 137
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRdrleec 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 138 ---YQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEE---AQQDIDSSSEM 211
Cdd:PRK02224 334 rvaAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdAPVDLGNAEDF 413
|
170 180 190
....*....|....*....|....*....|....*...
gi 1831508212 212 VEVLALETEELRRKVDGPRSESISDREDMHEEIEILKA 249
Cdd:PRK02224 414 LEELREERDELREREAELEATLRTARERVEEAEALLEA 451
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
153-254 |
3.02e-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: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 153 ERSNEETKRIRNELEKTENKLEEAqllvegmeEERIQ-LERQFRKFKEEAQQDIDSSSEmVEVLALETEELRRKVdgprs 231
Cdd:COG2433 416 RRLEEQVERLEAEVEELEAELEEK--------DERIErLERELSEARSEERREIRKDRE-ISRLDREIERLEREL----- 481
|
90 100
....*....|....*....|...
gi 1831508212 232 esisdrEDMHEEIEILKAKVAEL 254
Cdd:COG2433 482 ------EEERERIEELKRKLERL 498
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
65-279 |
3.31e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 65 ELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFK--------QLLSDEKARGTESMSRLKREkELETESWNL 136
Cdd:PRK02224 409 NAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecgQPVEGSPHVETIEEDRERVE-ELEAELEDL 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 137 KYQMLE--------KDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLE---RQFRKFKEEAQQDI 205
Cdd:PRK02224 488 EEEVEEveerleraEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEaeaEEKREAAAEAEEEA 567
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831508212 206 DSSSEMVEVLALETEELRRKVDGPR--SESISDREDMHEEIEILKAKVAELmKEKEEMTDQLLATSVERGRSLIAD 279
Cdd:PRK02224 568 EEAREEVAELNSKLAELKERIESLEriRTLLAAIADAEDEIERLREKREAL-AELNDERRERLAEKRERKRELEAE 642
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
95-260 |
3.33e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 95 EEQLTDNEDRFKQLLSDEKAR-----------GTESMSRLKREKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIR 163
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEaeaikkealleAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 164 NELEKTENKLEEAQLLVEGMEEEriqLERqfrkfKEEAQQDidsssEMVEVLALETEELRRKVdgprsesisdREDMHEE 243
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEE---LEE-----LIEEQLQ-----ELERISGLTAEEAKEIL----------LEKVEEE 166
|
170
....*....|....*..
gi 1831508212 244 ieiLKAKVAELMKEKEE 260
Cdd:PRK12704 167 ---ARHEAAVLIKEIEE 180
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
65-222 |
3.39e-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: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 65 ELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSRLKREKELETESWNLKYQMLEKD 144
Cdd:pfam07888 70 QWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831508212 145 LisvkkDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEEAQQDIDSSSEMVEVLALETEEL 222
Cdd:pfam07888 150 T-----ELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKL 222
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
143-302 |
3.53e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 143 KDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQfrkfkEEAQQDIDSSSEMVEVLALETEEL 222
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL-----LQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 223 RRKVdgprsESISDREDMHEEIEILKAKVAELMKEKEEMTDQLLATSVERGRSLIADTPSLADELAggDSSQLLDALREQ 302
Cdd:COG4717 149 EELE-----ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLA--ELEEELEEAQEE 221
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
75-265 |
4.18e-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: 39.70 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 75 DERTRLKTEN-SVLKERMHNLEEQLTDNEDRFKQLLSDEKAR------GTESMSRLKREKELETESWNLKYQM------- 140
Cdd:pfam05483 274 EEKTKLQDENlKELIEKKDHLTKELEDIKMSLQRSMSTQKALeedlqiATKTICQLTEEKEAQMEELNKAKAAhsfvvte 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 141 -------LEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEeerIQLErQFRKFKEEAQQDIDSSSEmVE 213
Cdd:pfam05483 354 feattcsLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKE---VELE-ELKKILAEDEKLLDEKKQ-FE 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1831508212 214 VLALETEELRRKVDGPRSESISDREDMHEEIEILKAKVAELMKEKEEMTDQL 265
Cdd:pfam05483 429 KIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL 480
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
121-254 |
4.92e-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: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 121 SRLKREKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEEERIQLERQFRKFKEE 200
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1831508212 201 AQQdidsSSEMVEVLALETEELRRKVDgprsESISDREDMHEEIEILKAKVAEL 254
Cdd:TIGR02169 739 LEE----LEEDLSSLEQEIENVKSELK----ELEARIEELEEDLHKLEEALNDL 784
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
89-265 |
6.10e-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: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 89 ERMHNLEEQLTDNEDRfkqlLSDEKARgTESMSRLKREKElETESWNL--KYQMLEKDLISVKKDAERSNEETKRIRNEL 166
Cdd:TIGR02169 187 ERLDLIIDEKRQQLER----LRREREK-AERYQALLKEKR-EYEGYELlkEKEALERQKEAIERQLASLEEELEKLTEEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 167 EKTENKLEEAQLLVEGM--------EEERIQLERQFRKFKEEAQQdIDSSSEMVEVLALETEELRRKVDGPRSESISDRE 238
Cdd:TIGR02169 261 SELEKRLEEIEQLLEELnkkikdlgEEEQLRVKEKIGELEAEIAS-LERSIAEKERELEDAEERLAKLEAEIDKLLAEIE 339
|
170 180
....*....|....*....|....*..
gi 1831508212 239 DMHEEIEILKAKVAELMKEKEEMTDQL 265
Cdd:TIGR02169 340 ELEREIEEERKRRDKLTEEYAELKEEL 366
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
118-226 |
6.91e-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: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 118 ESMSRLKREKELETESWNLKYQMLEKDLISVK-------KDAERSNEETKRIRNELEKTENKLEEAQLLVEGM------- 183
Cdd:pfam07111 151 EQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkrageaKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLrkyvgeq 230
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831508212 184 ----------EEERIQLERQFRKFKEEaQQDIDSSSEMVEV--------LALETEELRRKV 226
Cdd:pfam07111 231 vppevhsqtwELERQELLDTMQHLQED-RADLQATVELLQVrvqslthmLALQEEELTRKI 290
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
147-256 |
7.51e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 38.78 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 147 SVKKDAERSNEETKRIRNELEKTENKLEEAqllvEGMEEERIQLERQFRKFKEEAQQDIDSSSEmVEVLALETEELRRKV 226
Cdd:PRK04863 496 DVARELLRRLREQRHLAEQLQQLRMRLSEL----EQRLRQQQRAERLLAEFCKRLGKNLDDEDE-LEQLQEELEARLESL 570
|
90 100 110
....*....|....*....|....*....|
gi 1831508212 227 DGPRSESISDREDMHEEIEILKAKVAELMK 256
Cdd:PRK04863 571 SESVSEARERRMALRQQLEQLQARIQRLAA 600
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
43-227 |
7.75e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 38.84 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 43 QDALNDFSSQmNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEkargteSMSR 122
Cdd:COG3206 195 EAALEEFRQK-NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP------VIQQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 123 LKREkeleteswnlkYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKL-EEAQLLVEGMEEERIQLERQFRKFKEEA 201
Cdd:COG3206 268 LRAQ-----------LAELEAELAELSARYTPNHPDVIALRAQIAALRAQLqQEAQRILASLEAELEALQAREASLQAQL 336
|
170 180
....*....|....*....|....*.
gi 1831508212 202 QQDIDSSSEMVEVLAlETEELRRKVD 227
Cdd:COG3206 337 AQLEARLAELPELEA-ELRRLEREVE 361
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
43-211 |
7.96e-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: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 43 QDALNDFSSQMNQLNSFTKRYSELEERNMSLSDERTRLKTENSVLKERMHNLEEQLTDNEDRFKQLLSDEKARGTESMSR 122
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508212 123 LKREKELETESWNLKYQMLEKDLISVKKDAERSNEETKRIRNELEKTENKLEEAQLLVEGMEeeriQLERQFRKFKEEAQ 202
Cdd:TIGR02168 434 ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE----RLQENLEGFSEGVK 509
|
....*....
gi 1831508212 203 QDIDSSSEM 211
Cdd:TIGR02168 510 ALLKNQSGL 518
|
|
| |
