|
Name |
Accession |
Description |
Interval |
E-value |
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
166-396 |
6.29e-118 |
|
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
Pssm-ID: 318204 [Multi-domain] Cd Length: 234 Bit Score: 349.26 E-value: 6.29e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 166 VLREIAELICSLGSKEFSYNEIYDESSKENPFCTTIADMFARKFEQEQNQVE---INGQLSCQIKGLQENLKDRDNQISQ 242
Cdd:pfam15934 1 ILKEIADLICRLRSMEFSYNEIYTESSTENPFCAAIMDMFENKNEQEQQLKEftvQNQRLACQIDNLHETLKDRDHQIKQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 243 LQSMINSYSDFSENNRLKEEMHVLKQKNCDLSRQLRDLPSLLKNQENQSVELCTKYESLMASFEDQCQELKDAKRKAQSL 322
Cdd:pfam15934 81 LQSMITGYSDISENNRLKEEIHDLKQKNCVQARVVRKMGLELKGQEEQRVELCDKYESLLGSFEEQCQELKRANRRVQSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442627910 323 QTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQQKSAQLEMEKMRTLVRKMQSHLQLDDIRH 396
Cdd:pfam15934 161 QTRLSQVEKLQEELRTERKILREEVIALKEKDAKSNGRERALQDQLKCCQTEIEKSRTLIRNMQSHLQLEDAHH 234
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
138-517 |
6.11e-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: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 138 KYQRLDTESKKLEARIEsessvLQRNSDVLREIAELICSLG---SKEFSYNEIYDE-SSKEnpfcttiADMFARKFEQEQ 213
Cdd:TIGR02168 171 KERRKETERKLERTREN-----LDRLEDILNELERQLKSLErqaEKAERYKELKAElRELE-------LALLVLRLEELR 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 214 NQVEingQLSCQIKGLQENLKDRDNQISQLQSMINsysdfsennRLKEEMHVLKQKNCDLSRQLRDLPSLLKNQENQSVE 293
Cdd:TIGR02168 239 EELE---ELQEELKEAEEELEELTAELQELEEKLE---------ELRLEVSELEEEIEELQKELYALANEISRLEQQKQI 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 294 LCTKYESLMASFEDQCQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQ---QKS 370
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQletLRS 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 371 AQLEMEKMRTLVRKMQSHL--QLDDIRHResIQRMNETTESLREELRTISENCQQMQIRLNQQTEVNQQQEQIIDSFRKW 448
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLeaRLERLEDR--RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALE 464
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 449 K-DAQVRADEAMRLCAKRAEEHIHMLLDENRTLAEDYRNLFRDYKLLETEIKRVKQAVNCASSSaISCPP 517
Cdd:TIGR02168 465 ElREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL-ISVDE 533
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
110-374 |
5.46e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 110 DLDADAQMLEALRRRLLNLSQLNRELHGKYQRLDTESKKLEARIESEssvLQRNSDVLREIAELICSLGSKEFSYNEIYD 189
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL---EERRRELEERLEELEEELAELEEELEELEE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 190 EsskenpfcttIADMFARKFEQEQNQVEINGQLSCQIKGLQENLKDRDNQISQLQsminsySDFSENNRLKEEMHVLKQK 269
Cdd:COG1196 338 E----------LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE------ELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 270 NCDLSRQLRDLPSLLKNQENQSVELCTKYESLMASFEDQCQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVA 349
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
250 260
....*....|....*....|....*
gi 442627910 350 LKEKEAVSSGRERALQDQQKSAQLE 374
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYEGF 506
|
|
| F-BAR_PACSIN1 |
cd07680 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ... |
296-434 |
1.01e-04 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 1 or Syndapin I is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. It contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153364 [Multi-domain] Cd Length: 258 Bit Score: 44.27 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 296 TKYESLMASFEdQCQELKDAKRKAQSLQTRldQVEQLQDELRTERKILREEVVALKeKEAVSSGRERALQDQQKSAQLEM 375
Cdd:cd07680 102 AYHKQIMGGFK-ETKEAEDGFRKAQKPWAK--KMKELEAAKKAYHLACKEEKLAMT-REANSKAEQSVTPEQQKKLQDKV 177
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 376 EKMRTLVRKMQShlqlddiRHRESIQRMNETTESLREELRTISENCQQM-QIRLNQQTEV 434
Cdd:cd07680 178 DKCKQDVQKTQE-------KYEKVLDDVGKTTPQYMENMEQVFEQCQQFeEKRLVFLKEV 230
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
36-294 |
2.15e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 36 LNAELNDLLD-LHNKQEFQTIEIRRKRVSCFIEKLVSEREDTLKKLESIRSHLTILQSDLDQSCLISVDPESgpcdldad 114
Cdd:PRK05771 14 LKSYKDEVLEaLHELGVVHIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLE-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 115 aqmlEALRRRLLNLSQLNRE---LHGKYQRLDTESKKLEARIE---------SESSVLQRNSDVLREIAELicslgSKEF 182
Cdd:PRK05771 86 ----ELIKDVEEELEKIEKEikeLEEEISELENEIKELEQEIErlepwgnfdLDLSLLLGFKYVSVFVGTV-----PEDK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 183 sYNEIYDESSKENPFCT-------TIADMFARKFEQEQNQV-EINGQLSCQIKG---LQENLKDRDNQISQLQsminsys 251
Cdd:PRK05771 157 -LEELKLESDVENVEYIstdkgyvYVVVVVLKELSDEVEEElKKLGFERLELEEegtPSELIREIKEELEEIE------- 228
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 442627910 252 dfSENNRLKEEMHVLKQKNCDLSRQLRDLPSLLKNQENQSVEL 294
Cdd:PRK05771 229 --KERESLLEELKELAKKYLEELLALYEYLEIELERAEALSKF 269
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
312-492 |
6.36e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 312 LKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQQKSAQLEMEKMRTLvrkmQSHLQL 391
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLD----ASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 392 DDIRHResIQRMNETTESLREELRTISENCQQMQIRLNQ----QTEVNQQQEQIIDSFRKWKD-------AQVRADEAMR 460
Cdd:COG4913 688 AALEEQ--LEELEAELEELEEELDELKGEIGRLEKELEQaeeeLDELQDRLEAAEDLARLELRalleerfAAALGDAVER 765
|
170 180 190
....*....|....*....|....*....|..
gi 442627910 461 LCAKRAEEHIHMLLDENRTLAEDYRNLFRDYK 492
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEELERAMRAFN 797
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
66-417 |
6.43e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 66 IEKLVSERED----TLKKLESIRSHLTILQSDLDQsclisvdpesgpcdLDADAQMLEALRRRLLNLSQLNRELHGKYQR 141
Cdd:PRK03918 191 IEELIKEKEKeleeVLREINEISSELPELREELEK--------------LEKEVKELEELKEEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 142 LDTESKKLEARIESessvLQRNSDVLREIAELICSLGSKEFSYNEIYDesskenpfcttiadmFARKFEQEQNQVEIN-G 220
Cdd:PRK03918 257 LEEKIRELEERIEE----LKKEIEELEEKVKELKELKEKAEEYIKLSE---------------FYEEYLDELREIEKRlS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 221 QLSCQIKGLQENLKDRDNQISQLQSMINsysdfsENNRLKEEMHVLKQKncdlSRQLRDLPSLLKNQENQSVELCTKyes 300
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKK------KLKELEKRLEELEER----HELYEEAKAKKEELERLKKRLTGL--- 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 301 lmaSFEDQCQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQQKSAQLEmekmrt 380
Cdd:PRK03918 385 ---TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLE------ 455
|
330 340 350
....*....|....*....|....*....|....*..
gi 442627910 381 lvrkmQSHLQLDDIrhRESIQRMNETTESLREELRTI 417
Cdd:PRK03918 456 -----EYTAELKRI--EKELKEIEEKERKLRKELREL 485
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
306-505 |
4.25e-03 |
|
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: 40.11 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 306 EDQCQELKDAKRKAQSLQ-TRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQQKsaqlEMEKMRTlvrk 384
Cdd:pfam17380 356 EERKRELERIRQEEIAMEiSRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKV----EMEQIRA---- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 385 mqshlQLDDIRHREsIQRMNETTESLREELRTISENCQQMQIRLNQQTEVNQQQEQIIDsfrKWKDAQVRADEAMR-LCA 463
Cdd:pfam17380 428 -----EQEEARQRE-VRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELE---KEKRDRKRAEEQRRkILE 498
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 442627910 464 KRAEEHIHMLLDENRTlaedyrnlfrdYKLLETEIKRVKQAV 505
Cdd:pfam17380 499 KELEERKQAMIEEERK-----------RKLLEKEMEERQKAI 529
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
166-396 |
6.29e-118 |
|
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
Pssm-ID: 318204 [Multi-domain] Cd Length: 234 Bit Score: 349.26 E-value: 6.29e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 166 VLREIAELICSLGSKEFSYNEIYDESSKENPFCTTIADMFARKFEQEQNQVE---INGQLSCQIKGLQENLKDRDNQISQ 242
Cdd:pfam15934 1 ILKEIADLICRLRSMEFSYNEIYTESSTENPFCAAIMDMFENKNEQEQQLKEftvQNQRLACQIDNLHETLKDRDHQIKQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 243 LQSMINSYSDFSENNRLKEEMHVLKQKNCDLSRQLRDLPSLLKNQENQSVELCTKYESLMASFEDQCQELKDAKRKAQSL 322
Cdd:pfam15934 81 LQSMITGYSDISENNRLKEEIHDLKQKNCVQARVVRKMGLELKGQEEQRVELCDKYESLLGSFEEQCQELKRANRRVQSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442627910 323 QTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQQKSAQLEMEKMRTLVRKMQSHLQLDDIRH 396
Cdd:pfam15934 161 QTRLSQVEKLQEELRTERKILREEVIALKEKDAKSNGRERALQDQLKCCQTEIEKSRTLIRNMQSHLQLEDAHH 234
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
138-517 |
6.11e-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: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 138 KYQRLDTESKKLEARIEsessvLQRNSDVLREIAELICSLG---SKEFSYNEIYDE-SSKEnpfcttiADMFARKFEQEQ 213
Cdd:TIGR02168 171 KERRKETERKLERTREN-----LDRLEDILNELERQLKSLErqaEKAERYKELKAElRELE-------LALLVLRLEELR 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 214 NQVEingQLSCQIKGLQENLKDRDNQISQLQSMINsysdfsennRLKEEMHVLKQKNCDLSRQLRDLPSLLKNQENQSVE 293
Cdd:TIGR02168 239 EELE---ELQEELKEAEEELEELTAELQELEEKLE---------ELRLEVSELEEEIEELQKELYALANEISRLEQQKQI 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 294 LCTKYESLMASFEDQCQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQ---QKS 370
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQletLRS 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 371 AQLEMEKMRTLVRKMQSHL--QLDDIRHResIQRMNETTESLREELRTISENCQQMQIRLNQQTEVNQQQEQIIDSFRKW 448
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLeaRLERLEDR--RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALE 464
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 449 K-DAQVRADEAMRLCAKRAEEHIHMLLDENRTLAEDYRNLFRDYKLLETEIKRVKQAVNCASSSaISCPP 517
Cdd:TIGR02168 465 ElREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL-ISVDE 533
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
200-506 |
1.06e-06 |
|
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: 51.98 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 200 TIADMFARKFEQEQNQVEINGQ------LSCQIKGLQENLKDRDNQISQLQSMINSYSDfsENNRLKEEMHVLKQKNCDL 273
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELeekiaeLEKALAELRKELEELEEELEQLRKELEELSR--QISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 274 SRQLRDLPSLLKNQENQSVELCTKYESLMASFEDQCQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEV------ 347
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlrer 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 348 -------VALKEKEAVSSGRERA-LQDQQKSAQLEMEKMRTLVRKMQSHLQ-LDDIR--HRESIQRMNETTESLREELRT 416
Cdd:TIGR02168 826 leslerrIAATERRLEDLEEQIEeLSEDIESLAAEIEELEELIEELESELEaLLNERasLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 417 ISENCQQMqirlnqQTEVNQQQEQIIDSFRKWKDAQVRADEamrLCAKRAEEHIhMLLDEnrtLAEDYRNLFRDYKLLET 496
Cdd:TIGR02168 906 LESKRSEL------RRELEELREKLAQLELRLEGLEVRIDN---LQERLSEEYS-LTLEE---AEALENKIEDDEEEARR 972
|
330
....*....|
gi 442627910 497 EIKRVKQAVN 506
Cdd:TIGR02168 973 RLKRLENKIK 982
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
73-460 |
1.50e-06 |
|
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: 51.60 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 73 REDTLKKLESIRSHLTILQsDLdqsclisvdpesgpcdldadaqmLEALRRRLLNLsQLNRELHGKYQRLDTESKKLEAR 152
Cdd:TIGR02168 174 RKETERKLERTRENLDRLE-DI-----------------------LNELERQLKSL-ERQAEKAERYKELKAELRELELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 153 IesesSVLQrnsdvLREIAELICSLGSKEFSYNEIYDESSKEnpfcttiadmfARKFEQEQNQVE-INGQLSCQIKGLQE 231
Cdd:TIGR02168 229 L----LVLR-----LEELREELEELQEELKEAEEELEELTAE-----------LQELEEKLEELRlEVSELEEEIEELQK 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 232 NLKDRDNQISQLQSMInsysdfsenNRLKEEMHVLKQKNCDLSRQLRDLPSLLKNQENQSVELCTKYESLMASFEDQCQE 311
Cdd:TIGR02168 289 ELYALANEISRLEQQK---------QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 312 LKDAKRKAQSLqtrldqvEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQQKSAQLEMEKMRTLVRKMQSHLQL 391
Cdd:TIGR02168 360 LEELEAELEEL-------ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442627910 392 DDirhRESIQRMNETTESLREELRTISENCQQMQIRLNQQTEVNQQQEQIIDSFRKWKDAQVRADEAMR 460
Cdd:TIGR02168 433 AE---LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
110-374 |
5.46e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 110 DLDADAQMLEALRRRLLNLSQLNRELHGKYQRLDTESKKLEARIESEssvLQRNSDVLREIAELICSLGSKEFSYNEIYD 189
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL---EERRRELEERLEELEEELAELEEELEELEE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 190 EsskenpfcttIADMFARKFEQEQNQVEINGQLSCQIKGLQENLKDRDNQISQLQsminsySDFSENNRLKEEMHVLKQK 269
Cdd:COG1196 338 E----------LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE------ELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 270 NCDLSRQLRDLPSLLKNQENQSVELCTKYESLMASFEDQCQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVA 349
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
250 260
....*....|....*....|....*
gi 442627910 350 LKEKEAVSSGRERALQDQQKSAQLE 374
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYEGF 506
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
297-482 |
1.31e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 297 KYESLMASFEDQCQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQQKSAQLEME 376
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 377 KMRTLVRKMQSHLQLDDIRHRESIQRMNETTESLREELRTISENCQQMQIRLNQQTEVNQQQEQIIDSFRKWKDAQVRAD 456
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180
....*....|....*....|....*.
gi 442627910 457 EAMRLCAKRAEEHIHMLLDENRTLAE 482
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLER 418
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
73-439 |
8.53e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 8.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 73 REDTLKKLESIRSHLTILQsDLdqsclisvdpesgpcdldadaqmLEALRRRLLNLS-QlnRELHGKYQRLDTESKKLEA 151
Cdd:COG1196 174 KEEAERKLEATEENLERLE-DI-----------------------LGELERQLEPLErQ--AEKAERYRELKEELKELEA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 152 riesESSVLQRNsDVLREIAELICSLGSKEFSYNEIYDESSKENpfcttiadmfaRKFEQEQNQVEingQLSCQIKGLQE 231
Cdd:COG1196 228 ----ELLLLKLR-ELEAELEELEAELEELEAELEELEAELAELE-----------AELEELRLELE---ELELELEEAQA 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 232 NLKDRDNQISQLQSMINSYSDfsENNRLKEEMHVLKQKNCDLSRQLRDLPSLLKNQENQSVELCTKYESLMASFEDQCQE 311
Cdd:COG1196 289 EEYELLAELARLEQDIARLEE--RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 312 LKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQQKSAQLEMEKMRTLVRKMQSHLQL 391
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 442627910 392 DDIRHRESIQRMNETTESLREELRTISENCQQMQIRLNQQTEVNQQQE 439
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| F-BAR_PACSIN1 |
cd07680 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ... |
296-434 |
1.01e-04 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 1 or Syndapin I is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. It contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153364 [Multi-domain] Cd Length: 258 Bit Score: 44.27 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 296 TKYESLMASFEdQCQELKDAKRKAQSLQTRldQVEQLQDELRTERKILREEVVALKeKEAVSSGRERALQDQQKSAQLEM 375
Cdd:cd07680 102 AYHKQIMGGFK-ETKEAEDGFRKAQKPWAK--KMKELEAAKKAYHLACKEEKLAMT-REANSKAEQSVTPEQQKKLQDKV 177
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 376 EKMRTLVRKMQShlqlddiRHRESIQRMNETTESLREELRTISENCQQM-QIRLNQQTEV 434
Cdd:cd07680 178 DKCKQDVQKTQE-------KYEKVLDDVGKTTPQYMENMEQVFEQCQQFeEKRLVFLKEV 230
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
36-294 |
2.15e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 36 LNAELNDLLD-LHNKQEFQTIEIRRKRVSCFIEKLVSEREDTLKKLESIRSHLTILQSDLDQSCLISVDPESgpcdldad 114
Cdd:PRK05771 14 LKSYKDEVLEaLHELGVVHIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLE-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 115 aqmlEALRRRLLNLSQLNRE---LHGKYQRLDTESKKLEARIE---------SESSVLQRNSDVLREIAELicslgSKEF 182
Cdd:PRK05771 86 ----ELIKDVEEELEKIEKEikeLEEEISELENEIKELEQEIErlepwgnfdLDLSLLLGFKYVSVFVGTV-----PEDK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 183 sYNEIYDESSKENPFCT-------TIADMFARKFEQEQNQV-EINGQLSCQIKG---LQENLKDRDNQISQLQsminsys 251
Cdd:PRK05771 157 -LEELKLESDVENVEYIstdkgyvYVVVVVLKELSDEVEEElKKLGFERLELEEegtPSELIREIKEELEEIE------- 228
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 442627910 252 dfSENNRLKEEMHVLKQKNCDLSRQLRDLPSLLKNQENQSVEL 294
Cdd:PRK05771 229 --KERESLLEELKELAKKYLEELLALYEYLEIELERAEALSKF 269
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
117-425 |
3.53e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 117 MLEALRRRLLNLsQLNRELHGKYQRLDTESKKLEARI---ESESSVLQRnSDVLREIAELICSLGSKEFSYNEIYDESSK 193
Cdd:TIGR02169 192 IIDEKRQQLERL-RREREKAERYQALLKEKREYEGYEllkEKEALERQK-EAIERQLASLEEELEKLTEEISELEKRLEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 194 ENPFCTTIADMFARKFEQEQNQVeingqlscqikglQENLKDRDNQISQLQSMINSYSDfsennRLKEEMHVLKQKNCDL 273
Cdd:TIGR02169 270 IEQLLEELNKKIKDLGEEEQLRV-------------KEKIGELEAEIASLERSIAEKER-----ELEDAEERLAKLEAEI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 274 SRQLRDLPSLLKNQENQSVELctkyESLMAsfedqcqELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEK 353
Cdd:TIGR02169 332 DKLLAEIEELEREIEEERKRR----DKLTE-------EYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442627910 354 EAVSSGRERALQDQQKSAQLEMEKMRT-LVRKMQSHLQLDdirhresiqrmnETTESLREELRTISENCQQMQ 425
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAaIAGIEAKINELE------------EEKEDKALEIKKQEWKLEQLA 461
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
266-482 |
4.61e-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: 42.83 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 266 LKQKNCDLSRQLRDLPSLLKNQENQSVELCTKYESLMASFEDQCQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILRE 345
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 346 EVVALKeKEAVSSGRERALQ---DQQKSAQLE--MEKMRTLVRKMQShlQLDDIrhRESIQRMNETTESLREELRTISEN 420
Cdd:COG4942 105 ELAELL-RALYRLGRQPPLAlllSPEDFLDAVrrLQYLKYLAPARRE--QAEEL--RADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442627910 421 CQQMQIRLNQQTEVNQQQEQIIDSFRKWKDAQVRADEAMRLCAKRAEEHIHMLLDENRTLAE 482
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
312-492 |
6.36e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 312 LKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQQKSAQLEMEKMRTLvrkmQSHLQL 391
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLD----ASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 392 DDIRHResIQRMNETTESLREELRTISENCQQMQIRLNQ----QTEVNQQQEQIIDSFRKWKD-------AQVRADEAMR 460
Cdd:COG4913 688 AALEEQ--LEELEAELEELEEELDELKGEIGRLEKELEQaeeeLDELQDRLEAAEDLARLELRalleerfAAALGDAVER 765
|
170 180 190
....*....|....*....|....*....|..
gi 442627910 461 LCAKRAEEHIHMLLDENRTLAEDYRNLFRDYK 492
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEELERAMRAFN 797
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
66-417 |
6.43e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 66 IEKLVSERED----TLKKLESIRSHLTILQSDLDQsclisvdpesgpcdLDADAQMLEALRRRLLNLSQLNRELHGKYQR 141
Cdd:PRK03918 191 IEELIKEKEKeleeVLREINEISSELPELREELEK--------------LEKEVKELEELKEEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 142 LDTESKKLEARIESessvLQRNSDVLREIAELICSLGSKEFSYNEIYDesskenpfcttiadmFARKFEQEQNQVEIN-G 220
Cdd:PRK03918 257 LEEKIRELEERIEE----LKKEIEELEEKVKELKELKEKAEEYIKLSE---------------FYEEYLDELREIEKRlS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 221 QLSCQIKGLQENLKDRDNQISQLQSMINsysdfsENNRLKEEMHVLKQKncdlSRQLRDLPSLLKNQENQSVELCTKyes 300
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKK------KLKELEKRLEELEER----HELYEEAKAKKEELERLKKRLTGL--- 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 301 lmaSFEDQCQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQQKSAQLEmekmrt 380
Cdd:PRK03918 385 ---TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLE------ 455
|
330 340 350
....*....|....*....|....*....|....*..
gi 442627910 381 lvrkmQSHLQLDDIrhRESIQRMNETTESLREELRTI 417
Cdd:PRK03918 456 -----EYTAELKRI--EKELKEIEEKERKLRKELREL 485
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
292-457 |
7.30e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 7.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 292 VELCTKYESLMASFEDQcQELKDAkRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQ---- 367
Cdd:COG4913 258 RELAERYAAARERLAEL-EYLRAA-LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgn 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 368 --QKSAQLEME---KMRTLVRKMQSHLQLDdirhrESIQRMNETTESLREELRTISENCQQMQIRLNQQTEvnQQQEQII 442
Cdd:COG4913 336 ggDRLEQLEREierLERELEERERRRARLE-----ALLAALGLPLPASAEEFAALRAEAAALLEALEEELE--ALEEALA 408
|
170
....*....|....*
gi 442627910 443 DSFRKWKDAQVRADE 457
Cdd:COG4913 409 EAEAALRDLRRELRE 423
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
213-352 |
9.04e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 9.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 213 QNQVEINGQLSCQIKGLQENLKDRDNQISQLQSMINSYSDfsENNRLKEEMHVLKQKNCDLSRQLRDLPSLLKNQENQSV 292
Cdd:TIGR04523 303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNE--QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ 380
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 293 ELCTKYESLMASFEDQCQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKE 352
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS 440
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
30-458 |
1.27e-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: 42.03 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 30 SEMLRLLNAELNDLLDLHNKQEF----QTIEIRRKRVSCFIEK--LVSEREDTLKKLESIRSHLTILQSDLDQSCLISVD 103
Cdd:pfam15921 84 SHQVKDLQRRLNESNELHEKQKFylrqSVIDLQTKLQEMQMERdaMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKED 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 104 PesgpcdLDADAQMLEALRRRLLNLSQLNRELHGKYQRLDTESKKLEARIESESSVLQRN-----SDVLREIAELICSLG 178
Cdd:pfam15921 164 M------LEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSlgsaiSKILRELDTEISYLK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 179 SKEFSYNEIYDESSKENpfcttiADMFARKFEQEQNQVE-INGQLSCQIKGLQENLKDRDNQISQLQSMINSYSDFSENn 257
Cdd:pfam15921 238 GRIFPVEDQLEALKSES------QNKIELLLQQHQDRIEqLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARN- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 258 rlkeemhvlkqKNCDLSRQLRDLPSLLKNQENQSVELCTKYESLMASFEDQC----QELKDAKRK----AQSLQTRLDQV 329
Cdd:pfam15921 311 -----------QNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLvlanSELTEARTErdqfSQESGNLDDQL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 330 EQLQDELRTERKIL---REEVVALKEKEAVSSGRERALQDQQKSAQLEMEKMRTLVRKMQSHLQLDDIRHRESIQRMNET 406
Cdd:pfam15921 380 QKLLADLHKREKELsleKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNES 459
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 442627910 407 TE---SLREELRTISENCQQMQIRLNQQTEVNQQQEQIIDSFRKWKDAQVRADEA 458
Cdd:pfam15921 460 LEkvsSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEA 514
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
258-456 |
1.55e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 258 RLKEEMHVLKQKNCDLSRQLRDLPSLLknQENQSVELCTKYESLMASFEDQCQELKDAKRKAQSLQTRLDQVEQLQDELR 337
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERR--EALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELE 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 338 TERKILREEVVALKEKEAVSSGRERALQDQQKSAQLEMEKMRTLVRKmQSHLQLDDIRHRESI-QRMNETTESLREELRT 416
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL-ELRALLEERFAAALGdAVERELRENLEERIDA 777
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 442627910 417 isencqqmqirlnQQTEVNQQQEQIIDSF----RKWKDAQVRAD 456
Cdd:COG4913 778 -------------LRARLNRAEEELERAMrafnREWPAETADLD 808
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
275-441 |
2.27e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 275 RQLRDLPSLLKNQENQSVELCTKYESLmASFEDQCQELKDAKRKAQSLQTRLDQVEQLQD------ELRTERKILREEVV 348
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEEL-EELEEELEELEAELEELREELEKLEKLLQLLPlyqeleALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 349 ALKEKEAVSSGRERALQDQQKSAQLEMEKMRTLVRKMQSHLQLDDIRHRESIQRMNETTESLREELRTISENCQQMQIRL 428
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170
....*....|....*.
gi 442627910 429 NQ---QTEVNQQQEQI 441
Cdd:COG4717 230 EQlenELEAAALEERL 245
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
123-384 |
3.75e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 123 RRLLNLSQLNRelhgKYQRLDTESKKLEARIESESSVLQRNSDVLREIAELICSLGSKEFSYNEIydeSSKENPFCTTIA 202
Cdd:PRK03918 152 RQILGLDDYEN----AYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEI---SSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 203 DMFARKFEQEQNQVEINgQLSCQIKGLQENLKDRDNQISQLQSMINsysdfsennRLKEEMHVLKQKNCDLS-------- 274
Cdd:PRK03918 225 KLEKEVKELEELKEEIE-ELEKELESLEGSKRKLEEKIRELEERIE---------ELKKEIEELEEKVKELKelkekaee 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 275 -RQLRDLPSLLKNQENQSVELCTKYESLMASFEDQCQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEK 353
Cdd:PRK03918 295 yIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
250 260 270
....*....|....*....|....*....|.
gi 442627910 354 EAVSSGRERALQDQQKSAQLEMEKMRTLVRK 384
Cdd:PRK03918 375 ERLKKRLTGLTPEKLEKELEELEKAKEEIEE 405
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
61-440 |
3.85e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 61 RVSCFIEKLVSEREDTLKKLESIRSHLTILQSDLDQSclisvdpesgpcdldadAQMLEALRRRLLNLSQLNRELHGKYQ 140
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDA-----------------SRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 141 RLDTESKKLEARIESESSVLQrnsDVLREIAELICSLGSKEFSYNEIYDESSKEnpfcttiadmfarkfeqeqnqveing 220
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELK---ELEARIEELEEDLHKLEEALNDLEARLSHS-------------------------- 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 221 qlscQIKGLQENLKDRDNQISQLQSMINSYSdfSENNRLKEEMHVLKQKNCDLSRQLRDLpsllknqENQSVELCTKYES 300
Cdd:TIGR02169 792 ----RIPEIQAELSKLEEEVSRIEARLREIE--QKLNRLTLEKEYLEKEIQELQEQRIDL-------KEQIKSIEKEIEN 858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 301 LMASFEDQCQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVvalkekeavssgreralqdQQKSAQLEMEKMRT 380
Cdd:TIGR02169 859 LNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI-------------------EELEAQIEKKRKRL 919
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 381 LVRKMQSHLQLDDIRHRESIQRMNETTESLREELRTISENCQQMQIRLNQQTEVNQQQEQ 440
Cdd:TIGR02169 920 SELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQ 979
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
306-505 |
4.25e-03 |
|
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: 40.11 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 306 EDQCQELKDAKRKAQSLQ-TRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQQKsaqlEMEKMRTlvrk 384
Cdd:pfam17380 356 EERKRELERIRQEEIAMEiSRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKV----EMEQIRA---- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 385 mqshlQLDDIRHREsIQRMNETTESLREELRTISENCQQMQIRLNQQTEVNQQQEQIIDsfrKWKDAQVRADEAMR-LCA 463
Cdd:pfam17380 428 -----EQEEARQRE-VRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELE---KEKRDRKRAEEQRRkILE 498
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 442627910 464 KRAEEHIHMLLDENRTlaedyrnlfrdYKLLETEIKRVKQAV 505
Cdd:pfam17380 499 KELEERKQAMIEEERK-----------RKLLEKEMEERQKAI 529
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
217-490 |
5.43e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.61 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 217 EINGQLSCQIKGLQENLKDRDNQISQLQSMINSYSDFSENNRLKEemhvlKQKNCDLSRQLRDLPSLLKNQENQSVELCT 296
Cdd:PHA02562 167 EMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKN-----GENIARKQNKYDELVEEAKTIKAEIEELTD 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 297 KYESLMASFEDQCQELKDAKRKAQSLQTrldQVEQLQDELrterKILREEVVALKEKEAVSSGRERalqdqqksaqleME 376
Cdd:PHA02562 242 ELLNLVMDIEDPSAALNKLNTAAAKIKS---KIEQFQKVI----KMYEKGGVCPTCTQQISEGPDR------------IT 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 377 KMRTLVRKMQSHLQLDDIRHRESIQRMNETTEslreelrtisencQQMQIRLNqQTEVNQQQEQIIDSFRKWKDAQVRAD 456
Cdd:PHA02562 303 KIKDKLKELQHSLEKLDTAIDELEEIMDEFNE-------------QSKKLLEL-KNKISTNKQSLITLVDKAKKVKAAIE 368
|
250 260 270
....*....|....*....|....*....|....
gi 442627910 457 EAMRLCAKRAEEhIHMLLDENRTLAEDYRNLFRD 490
Cdd:PHA02562 369 ELQAEFVDNAEE-LAKLQDELDKIVKTKSELVKE 401
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
153-502 |
5.89e-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: 39.72 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 153 IESESSVLQ-----RNSDVLREIAEL---ICSLGSKEFSYNEIYDESSKENPFCTTIADMFARKFEQEQNQV-EINGQLS 223
Cdd:pfam15921 297 IQSQLEIIQeqarnQNSMYMRQLSDLestVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFsQESGNLD 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 224 CQIKGLQENLKDRDNQISQLQSMINSYSDFSENNRLKEEmhvlkqkncDLSRQLRDlpsllKNQENQsvelctKYESLMA 303
Cdd:pfam15921 377 DQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITID---------HLRRELDD-----RNMEVQ------RLEALLK 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 304 SFEDQCQELKDAKRKA-QSLQTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQQKSAQLE---MEKMR 379
Cdd:pfam15921 437 AMKSECQGQMERQMAAiQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKeraIEATN 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 380 TLVRKMQSHLqldDIRHRESIQRMNETteslrEELRTISENCQQMQIRLNQQTEVNQQQEQIIDSFRKWKDAQVRADEAM 459
Cdd:pfam15921 517 AEITKLRSRV---DLKLQELQHLKNEG-----DHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAM 588
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 442627910 460 RLCAKRAEEHIH---MLLDENRTLAEDYRNLFRDY--KLLETEIKRVK 502
Cdd:pfam15921 589 QVEKAQLEKEINdrrLELQEFKILKDKKDAKIRELeaRVSDLELEKVK 636
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
325-498 |
6.71e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 39.26 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 325 RLDQVEQLQDeLRTERKILREEVVALKEK-EAVSsgreralqdqqksaqlemEKMRTLVRKMQSHLQlddiRHRESIQRM 403
Cdd:pfam10168 570 KEQQLQELQS-LEEERKSLSERAEKLAEKyEEIK------------------DKQEKLMRRCKKVLQ----RLNSQLPVL 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 404 NETTESLREELRTISENCQQMQIRLNQQTE-VNQQQEQIIdsfrkwKDAQVRADEAMRLCAKRaEEHIHMLLDEnrtLAE 482
Cdd:pfam10168 627 SDAEREMKKELETINEQLKHLANAIKQAKKkMNYQRYQIA------KSQSIRKKSSLSLSEKQ-RKTIKEILKQ---LGS 696
|
170
....*....|....*.
gi 442627910 483 DYRNLFRDYKLLETEI 498
Cdd:pfam10168 697 EIDELIKQVKDINKHV 712
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
97-363 |
7.32e-03 |
|
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: 38.98 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 97 SCLISVDPESGPCDLDADAQMLEALRRRLLNLSQLNRELHGKYQRLDTESKKLEARIESESSVLQRNSDVLREIAElics 176
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 177 lgskefsyneiydesskenpfctTIADMFARKFEQEQNQVEINGQLSCQIKGLQENlkdrdNQISQLQSMINSySDFSEN 256
Cdd:COG4942 84 -----------------------ELAELEKEIAELRAELEAQKEELAELLRALYRL-----GRQPPLALLLSP-EDFLDA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 257 NR----LKEEMHVLKQKNCDLSRQLRDLPSLLKNQENQSVELctkyESLMASFEDQCQELKDAKRKAQSLQTRLDQVEQL 332
Cdd:COG4942 135 VRrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAEL----EALLAELEEERAALEALKAERQKLLARLEKELAE 210
|
250 260 270
....*....|....*....|....*....|....*
gi 442627910 333 Q----DELRTERKILREEVVALKEKEAVSSGRERA 363
Cdd:COG4942 211 LaaelAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
227-516 |
8.30e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 227 KGLQENLKDRDNQISQLQSMINSYSDFSEnnRLKEEMHVLKQKNCDLSRQLRDLPSLLKNQENQSVELcTKYESLMASFE 306
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEE--LIKEKEKELEEVLREINEISSELPELREELEKLEKEV-KELEELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 307 DQCQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKE--KEAVSSGRERALQDQQKSAQLEMEKMRTLVRk 384
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRLE- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 385 mqshlqlddiRHRESIQRMNETTESLREELRTISENCQQMQIRLnqqtevnqqqEQIIDSFRKWKDAQVRADEAMRLCAK 464
Cdd:PRK03918 321 ----------EEINGIEERIKELEEKEERLEELKKKLKELEKRL----------EELEERHELYEEAKAKKEELERLKKR 380
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 442627910 465 RA-------EEHIHMLLDENRTLAEDYRNLFRDYKLLETEIKRVKQAVNCASSSAISCP 516
Cdd:PRK03918 381 LTgltpeklEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCP 439
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
334-441 |
8.39e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 38.59 E-value: 8.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 334 DELRTERKILREEVVALKEKeaVSSGRERaLQDQQKSAQLEMEKMRTLVRKMQSHLQLDDIRHRES---IQRMNETTESL 410
Cdd:pfam09787 50 EELRQERDLLREEIQKLRGQ--IQQLRTE-LQELEAQQQEEAESSREQLQELEEQLATERSARREAeaeLERLQEELRYL 126
|
90 100 110
....*....|....*....|....*....|.
gi 442627910 411 REELRTiSENCQQMQIRlNQQTEVNQQQEQI 441
Cdd:pfam09787 127 EEELRR-SKATLQSRIK-DREAEIEKLRNQL 155
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
273-419 |
9.36e-03 |
|
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: 37.98 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627910 273 LSRQLRDLPSLLKNQENQSVELCTKYESLMASFEDQCQELKDAKRKAQSLQTRLDQVEQLQDELRTER--KILREEVVAL 350
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEALQKEIESL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442627910 351 KEKEAVSSGRERALQDQQKSAQLEMEKMRTLVRKMQSHLQLDDIRHRESIQRMNETTESLREELRTISE 419
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| |
