|
Name |
Accession |
Description |
Interval |
E-value |
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
1130-1207 |
1.25e-30 |
|
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.
Pssm-ID: 460543 Cd Length: 78 Bit Score: 115.77 E-value: 1.25e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217365688 1130 MSPELDTYGITKRVKEVLTDNNLGQRLFGETILGLTQGSVSDLLARPKPWHKLSLKGREpFVRMQLWLNDPNNVEKLM 1207
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERMEI 77
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
947-1015 |
8.34e-28 |
|
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.
Pssm-ID: 460543 Cd Length: 78 Bit Score: 107.68 E-value: 8.34e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217365688 947 MYQEVDTIELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLN 1015
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLS 68
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
556-632 |
2.12e-26 |
|
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.
Pssm-ID: 460543 Cd Length: 78 Bit Score: 103.83 E-value: 2.12e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217365688 556 EGEEMDTAEIARQVKEQLIKHNIGQRIFGHYVLGLSQGSVSEILARPKPWNKLTVRGKEpFHKMKQFLSDEQNILAL 632
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
|
|
| Homeodomain |
pfam00046 |
Homeodomain; |
1253-1309 |
1.59e-15 |
|
Homeodomain;
Pssm-ID: 459649 [Multi-domain] Cd Length: 57 Bit Score: 72.15 E-value: 1.59e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217365688 1253 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIRR 1309
Cdd:pfam00046 1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-375 |
2.46e-15 |
|
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: 82.03 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 107 DLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT----IKALKEKIREYEQTLKNQAETIALEkeQKLQND 182
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrqISALRKDLARLEAEVEQLEERIAQL--SKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 183 FAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDE----------ETTAKADEIEMIMTDLERANQ 252
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltllneEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 253 RAEVAQREAETLREQLSSANHSLqlaSQIQKAPDVAIEVLTrsSLEVELAAKEREIAQLVEDVQRLQASLTKLREnsasQ 332
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEI---EELEELIEELESELE--ALLNERASLEEALALLRSELEELSEELRELES----K 909
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2217365688 333 ISQLEQQLSAKNSTLKQLEEKLKG-QADYEEVKKELNILKSMEF 375
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGlEVRIDNLQERLSEEYSLTL 953
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
18-367 |
8.81e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 8.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 18 QQLQRELDATATVLANRQDESEQSRKRLIEQsrefkkntpedlrkqvapllksfqgEIDALSKRSKEAEAAFLNVYKRLi 97
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEA-------------------------ELEELEAELEELEAELAELEAEL- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 98 dvpdpvpaldlgQQLQLKVQRLhdieteNQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQ 177
Cdd:COG1196 270 ------------EELRLELEEL------ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 178 klQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEmimTDLERANQRAEVA 257
Cdd:COG1196 332 --LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR---AAAELAAQLEELE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 258 QREAETLREQLSSANHSLQLASQIQKApdvAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLE 337
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAEL---EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
330 340 350
....*....|....*....|....*....|
gi 2217365688 338 QQLSAKNSTLKQLEEKLKGQADYEEVKKEL 367
Cdd:COG1196 484 EELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
|
| homeodomain |
cd00086 |
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ... |
1253-1310 |
9.64e-13 |
|
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.
Pssm-ID: 238039 [Multi-domain] Cd Length: 59 Bit Score: 64.19 E-value: 9.64e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217365688 1253 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIRRE 1310
Cdd:cd00086 1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRS 58
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
111-427 |
1.40e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 111 QLQLKVQRLHDIETENQKLRETLEEYNKEFAEvknQEVTIKALKEKIREYEQTLKNQAETIalekeQKLQNDFAEKERKL 190
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEE---LEAELAELEAELEELRLELEELELEL-----EEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 191 QEtqmsttskLEEAEHKVQSLQTALEKTRTELfdlktkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS 270
Cdd:COG1196 298 AR--------LEQDIARLEERRRELEERLEEL-------EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 271 ANHSLQLASQIQKAPDVAIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLK 348
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEAlrAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217365688 349 QLEEKLKGQADYEEVKKELniLKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSDLSGSARRKGKDQP 427
Cdd:COG1196 443 ALEEAAEEEAELEEEEEAL--LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
82-406 |
3.15e-12 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 71.14 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 82 SKEAEAAFLNVYKRLIDVPDPVPALdlgQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT-----IKALKEK 156
Cdd:COG5185 221 LLEKAKEIINIEEALKGFQDPESEL---EDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANnlikqFENTKEK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 157 IREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYD-EETTA 235
Cdd:COG5185 298 IAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVElSKSSE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 236 KAD-----------EIEMIMTDLERANQRAE--------VAQREAETLREQLSSANHSLQLASQIQKA-------PDVAI 289
Cdd:COG5185 378 ELDsfkdtiestkeSLDEIPQNQRGYAQEILatledtlkAADRQIEELQRQIEQATSSNEEVSKLLNEliselnkVMREA 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 290 EVLTRSSLEVELAAKEREIAQ----LVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEvkk 365
Cdd:COG5185 458 DEESQSRLEEAYDEINRSVRSkkedLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARG--- 534
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2217365688 366 ELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENA 406
Cdd:COG5185 535 YAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQ 575
|
|
| HOX |
smart00389 |
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ... |
1253-1308 |
5.13e-12 |
|
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key developmental processes
Pssm-ID: 197696 [Multi-domain] Cd Length: 57 Bit Score: 62.27 E-value: 5.13e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217365688 1253 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIR 1308
Cdd:smart00389 2 RRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
58-355 |
1.85e-11 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 68.56 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 58 EDLRKQVAPLL---KSFQGEIDALSKRSKEAEAaflnvykrlIDVPDPVPALDLgQQLQLKVQRLHD----IETENQKLR 130
Cdd:pfam05622 17 HELDQQVSLLQeekNSLQQENKKLQERLDQLES---------GDDSGTPGGKKY-LLLQKQLEQLQEenfrLETARDDYR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 131 ETLEEYNKEFAE--VKNQEVT-----IKALKEKIREYEQTLK--NQAETIALEKEQKLQ--NDFAEKERKLQETQ---MS 196
Cdd:pfam05622 87 IKCEELEKEVLElqHRNEELTslaeeAQALKDEMDILRESSDkvKKLEATVETYKKKLEdlGDLRRQVKLLEERNaeyMQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 197 TTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLEranQRAEVAQREAETL---REQLSSANH 273
Cdd:pfam05622 167 RTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESK-KADKLEFEYKKLE---EKLEALQKEKERLiieRDTLRETNE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 274 SLQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRE----NSASQISQLEQQLSAKNSTLKQ 349
Cdd:pfam05622 243 ELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLgqegSYRERLTELQQLLEDANRRKNE 322
|
....*.
gi 2217365688 350 LEEKLK 355
Cdd:pfam05622 323 LETQNR 328
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
105-332 |
1.18e-10 |
|
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: 65.17 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 105 ALDLGQQLQLKVQRLH-DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIAL--EKEQKLQN 181
Cdd:COG4942 18 QADAAAEAEAELEQLQqEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEleKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 182 DFAEKERKLQET-----QMSTTSKLEEAEHKVQSLQTAlekTRTELFDLKTKYDEEttaKADEIEMIMTDLERANQRAEV 256
Cdd:COG4942 98 ELEAQKEELAELlralyRLGRQPPLALLLSPEDFLDAV---RRLQYLKYLAPARRE---QAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217365688 257 AQREAETLREQLSSANHSLQLASQIQKApdvaievlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQ 332
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQK--------LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
33-372 |
1.63e-10 |
|
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: 65.81 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 33 NRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQgEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPAL-----D 107
Cdd:TIGR04523 165 KKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLS-NLKKKIQKNKSLESQISELKKQNNQLKDNIEKKqqeinE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 108 LGQQLQLKVQRLHDIETENQKLRETLEEYNKEfaeVKNQEVTIKALKEKIreyeQTLKNQAETIALEKEQKLQNDFAE-- 185
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE---LEQNNKKIKELEKQL----NQLKSEISDLNNQKEQDWNKELKSel 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 186 --KERKLQETQmsttSKLEEAEHKVQSLQ---TALEKTRTELFDLKTKYDEETTAKADEIEmimtDLERANQRaevAQRE 260
Cdd:TIGR04523 317 knQEKKLEEIQ----NQISQNNKIISQLNeqiSQLKKELTNSESENSEKQRELEEKQNEIE----KLKKENQS---YKQE 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 261 AETLREQLSSANHSLQLASQIQKAPDVAIEvltrsSLEVELAAKEREIaqlvedvQRLQASLTKLrensASQISQLEQQL 340
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIK-----KLQQEKELLEKEI-------ERLKETIIKN----NSEIKDLTNQD 449
|
330 340 350
....*....|....*....|....*....|...
gi 2217365688 341 SAKNSTLKQLEEKLKGQADY-EEVKKELNILKS 372
Cdd:TIGR04523 450 SVKELIIKNLDNTRESLETQlKVLSRSINKIKQ 482
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
19-373 |
2.84e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 19 QLQRELDATATVLANRQDESEQsRKRLIEQSREFKKNTP-------EDLRKQvapLLKSFQGEIDALSKRSKEAEAAFLN 91
Cdd:PRK03918 402 EIEEEISKITARIGELKKEIKE-LKKAIEELKKAKGKCPvcgreltEEHRKE---LLEEYTAELKRIEKELKEIEEKERK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 92 VYKRLIDVpdpvpalDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtIKALKEKIREYEQTLKNQAETi 171
Cdd:PRK03918 478 LRKELREL-------EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEE--YEKLKEKLIKLKGEIKSLKKE- 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 172 aLEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQ-TALEKTRTELFDLKTKYDEETTAKADEIEmimtdLERA 250
Cdd:PRK03918 548 -LEKLEELKKKLAELEKKLDELE----EELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKE-----LERE 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 251 NQRAEVAQREAETLREQLSSANHSLQLASQiqkapdvAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQAsltklrensa 330
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLEELRK-------ELEELEKKYSEEEYEELREEYLELSRELAGLRA---------- 680
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2217365688 331 sQISQLEQQLSAKNSTLKQLEEKLKgqaDYEEVKKELNILKSM 373
Cdd:PRK03918 681 -ELEELEKRREEIKKTLEKLKEELE---EREKAKKELEKLEKA 719
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
123-410 |
6.29e-10 |
|
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: 64.31 E-value: 6.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 123 ETENqKLRET---LEEYNKEFAEVKNQEVTIKALKEKIREYeQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTS 199
Cdd:TIGR02168 176 ETER-KLERTrenLDRLEDILNELERQLKSLERQAEKAERY-KELKAELRELELALLVLRLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 200 KLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETT---AKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQ 276
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 277 LASQIQKAPDVAIEVLTRSSleVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKG 356
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEEL--ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER 411
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2217365688 357 QADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRI 410
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
127-351 |
1.68e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.63 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 127 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALekEQKLQNDFAEKERKLQETQM-STTSKLEEAE 205
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYL--RAALRLWFAQRRLELLEAELeELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 206 HKVQSLQTALEKTRTELFDLKTKYDEettAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQiqkap 285
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRG---NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE----- 380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217365688 286 dvaievltrsslevELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLE 351
Cdd:COG4913 381 --------------EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
110-283 |
1.79e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 110 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERK 189
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAE---LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 190 LQETQMSttskLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAK----ADEIEMIMTDLERANQRAEVAQREAETLR 265
Cdd:COG4717 151 LEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATEEElqdlAEELEELQQRLAELEEELEEAQEELEELE 226
|
170
....*....|....*...
gi 2217365688 266 EQLSSANHSLQLASQIQK 283
Cdd:COG4717 227 EELEQLENELEAAALEER 244
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
7-409 |
3.42e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 7 SMFQYWKRFDLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNtpedlrkqvapllksfQGEIDALSKRSKEAE 86
Cdd:COG4717 45 AMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL----------------QEELEELEEELEELE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 87 AAFLNVYKRLIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYnkefaevKNQEVTIKALKEKIREYEQTLKN 166
Cdd:COG4717 109 AELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL-------RELEEELEELEAELAELQEELEE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 167 QAETIALEKEQKLQnDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKtkyDEETTAKADEIEMIMT- 245
Cdd:COG4717 182 LLEQLSLATEEELQ-DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA---LEERLKEARLLLLIAAa 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 246 ----------DLERANQRAEVAQ-------REAETLREQLSSANHSLQLASQIQKAPDVAIEVLTR--SSLEVELAAKER 306
Cdd:COG4717 258 llallglggsLLSLILTIAGVLFlvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEEllAALGLPPDLSPE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 307 EIAQLVEDVQRLQASLTKLRE-NSASQISQLEQQLS-----AKNSTLKQLEEKLKGQADYEEVKKELNILKSmEFAPSEG 380
Cdd:COG4717 338 ELLELLDRIEELQELLREAEElEEELQLEELEQEIAallaeAGVEDEEELRAALEQAEEYQELKEELEELEE-QLEELLG 416
|
410 420
....*....|....*....|....*....
gi 2217365688 381 AGTQDAAKPLEVLLLEKNRSLQSENAALR 409
Cdd:COG4717 417 ELEELLEALDEEELEEELEELEEELEELE 445
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
36-355 |
4.19e-09 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 59.54 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 36 DESEQSRKRLIEQSREFKKNtpedlRKQVAPLLKSFQGEIDALSKRSKEaeaaFLNVYKRLIDVPDpvpalDLGQQLQ-L 114
Cdd:COG1340 11 EELEEKIEELREEIEELKEK-----RDELNEELKELAEKRDELNAQVKE----LREEAQELREKRD-----ELNEKVKeL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 115 KVQRLhDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLknQAETIALEKEQKLQNDFAEKERKLQETQ 194
Cdd:COG1340 77 KEERD-ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ--QTEVLSPEEEKELVEKIKELEKELEKAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 195 msttsKLEEAEHKVQSLQTALEKTRTELFDLKTKYdEETTAKADEIEMIMTDLeranqraevaQREAETLREQLSSANHs 274
Cdd:COG1340 154 -----KALEKNEKLKELRAELKELRKEAEEIHKKI-KELAEEAQELHEEMIEL----------YKEADELRKEADELHK- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 275 lqlasQIQKAPDVAIEVltrsslevelaakEREIAQLVEDVQRLQASLTKLRENSASqiSQLEQQLSAKNSTLKQLEEKL 354
Cdd:COG1340 217 -----EIVEAQEKADEL-------------HEEIIELQKELRELRKELKKLRKKQRA--LKREKEKEELEEKAEEIFEKL 276
|
.
gi 2217365688 355 K 355
Cdd:COG1340 277 K 277
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
16-370 |
4.32e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 16 DLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEidALSKRSKEAEaaflNVYKR 95
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE--ELEKKAEEYE----KLKEK 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 96 LIDVPdpvpaldlGQQLQLK--VQRLHDIETENQKLRETLEEYNKEFAEVKNQEV-----TIKALKEKIREYEQtlknqa 168
Cdd:PRK03918 534 LIKLK--------GEIKSLKkeLEKLEELKKKLAELEKKLDELEEELAELLKELEelgfeSVEELEERLKELEP------ 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 169 etiALEKEQKLQNDFAEKERKLQEtQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEiemIMTDLE 248
Cdd:PRK03918 600 ---FYNEYLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELRE---EYLELS 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 249 RANQRAEVAQREAETLREQLSSanhslqlasqiqkapdvAIEVLTRSSLEVELAAKERE-IAQLVEDVQRLQASLTK--- 324
Cdd:PRK03918 673 RELAGLRAELEELEKRREEIKK-----------------TLEKLKEELEEREKAKKELEkLEKALERVEELREKVKKyka 735
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2217365688 325 -LRENSASQISQLEQQLSAK-------NSTLKQLEEKLKGQADYEEVKKELNIL 370
Cdd:PRK03918 736 lLKERALSKVGEIASEIFEEltegkysGVRVKAEENKVKLFVVYQGKERPLTFL 789
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
128-436 |
5.15e-09 |
|
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: 61.24 E-value: 5.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 128 KLRETLEEYNKEFAEVKNQEVTIKALKEKIR----EYEQTLKN-QAETIALEKEQKLqndFAEKERKLQEtqmsttsKLE 202
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIEnrldELSQELSDaSRKIGEIEKEIEQ---LEQEEEKLKE-------RLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 203 EAEHKVQSLQTALEKTRTELFDLKTKYdEETTAKADEIEMIMTDLER--ANQRAEVAQREAETLREQLSSANHSLQlasq 280
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARI-EELEEDLHKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLR---- 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 281 iqkapdvaievltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAS----------QISQLEQQLSAKNSTLKQL 350
Cdd:TIGR02169 816 ---------------EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSiekeienlngKKEELEEELEELEAALRDL 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 351 EEKLKG-QADYEEVKKELNILKsmefapsEGAGTQDAAkplevllLEKNRSLQSE-NAALRISNSDLSGSARRKGKDQPE 428
Cdd:TIGR02169 881 ESRLGDlKKERDELEAQLRELE-------RKIEELEAQ-------IEKKRKRLSElKAKLEALEEELSEIEDPKGEDEEI 946
|
....*...
gi 2217365688 429 SRRPGSLP 436
Cdd:TIGR02169 947 PEEELSLE 954
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
117-372 |
5.90e-09 |
|
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: 60.85 E-value: 5.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 117 QRLHDIETENQKLRETLEEYNKEfaevKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQ----- 191
Cdd:TIGR02169 184 ENIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEkltee 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 192 ---------------------------ETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLK---TKYDEETTAKADEIE 241
Cdd:TIGR02169 260 iselekrleeieqlleelnkkikdlgeEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEerlAKLEAEIDKLLAEIE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 242 MIMTDLERANQR-----AEVAQREAE--TLREQLSSANHSLQLASQIQKAPDVAIEVLTR---------SSLEVELAAKE 305
Cdd:TIGR02169 340 ELEREIEEERKRrdkltEEYAELKEEleDLRAELEEVDKEFAETRDELKDYREKLEKLKReinelkrelDRLQEELQRLS 419
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217365688 306 REIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLSAKNSTLKQLEEKL-KGQADYEEVKKELNILKS 372
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELeeeKEDKALEIKKQEWKLEQLAADLSKYEQELyDLKEEYDRVEKELSKLQR 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
15-316 |
1.18e-08 |
|
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: 60.07 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 15 FDLQQLQRELDATATVLANRQDESEQSRKRLIEQSREF--KKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAflnv 92
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELesKLDELAEELAELEEKLEELKEELESLEAELEELEAE---- 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 93 ykrlidvpdpvpaldlgqqlqlkvqrLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAETIA 172
Cdd:TIGR02168 367 --------------------------LEELESRLEELEEQLETLRSKVAQLELQ---IASLNNEIERLEARLERLEDRRE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 173 LEKEQKLQNDFAEKERKLQETQMSTTSK---LEEAEHKVQSLQTALEKTRTELFDLKTKYDeETTAKADEIEMIMTDLER 249
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAELKELQAELEELeeeLEELQEELERLEEALEELREELEEAEQALD-AAERELAQLQARLDSLER 496
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217365688 250 ANQRAEVAQREAETLREQLSSANHSLQLASQIqkapdvaIEVLTRSSLEVELAAKEREIAQLVEDVQ 316
Cdd:TIGR02168 497 LQENLEGFSEGVKALLKNQSGLSGILGVLSEL-------ISVDEGYEAAIEAALGGRLQAVVVENLN 556
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
172-368 |
2.16e-08 |
|
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: 56.47 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 172 ALEKEQKLQNDFAEKERKLQETQMsttsKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERAN 251
Cdd:COG1579 8 ALLDLQELDSELDRLEHRLKELPA----ELAELEDELAALEARLEAAKTELEDLEKEIKR----LELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 252 QRAEVA--QREAETLREQLSSanhslqLASQIQKAPDVAIEVLTRssleveLAAKEREIAQLVEDVQRLQASLTKLRENS 329
Cdd:COG1579 80 EQLGNVrnNKEYEALQKEIES------LKRRISDLEDEILELMER------IEELEEELAELEAELAELEAELEEKKAEL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2217365688 330 ASQISQLEQQLSAKNSTLKQLEEKLKGQ--ADYEEVKKELN 368
Cdd:COG1579 148 DEELAELEAELEELEAEREELAAKIPPEllALYERIRKRKN 188
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
18-371 |
2.95e-08 |
|
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: 58.49 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 18 QQLQRELDATATVLANRQDESEQSRKRLIEQsREFKKNTPEDLRKQVApllkSFQGEIDALsKRSKEAEAAFLNVYKRLI 97
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEIERLKET-IIKNNSEIKDLTNQDS----VKELIIKNL-DNTRESLETQLKVLSRSI 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 98 DVPDPvPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNqevTIKALKEKIREYEQTLKNQAETIaLEKEQ 177
Cdd:TIGR04523 478 NKIKQ-NLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE---KIEKLESEKKEKESKISDLEDEL-NKDDF 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 178 KLQNDFAEKErkLQETQmsttSKLEEAEHKvqslQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVA 257
Cdd:TIGR04523 553 ELKKENLEKE--IDEKN----KEIEELKQT----QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKA 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 258 QREAETLREQ----LSSANHSLQLASQIQKAPDVAIEVLTrsslevELAAKEREIAQLVEDVqrLQASLTKLRENSASQI 333
Cdd:TIGR04523 623 KKENEKLSSIikniKSKKNKLKQEVKQIKETIKEIRNKWP------EIIKKIKESKTKIDDI--IELMKDWLKELSLHYK 694
|
330 340 350
....*....|....*....|....*....|....*...
gi 2217365688 334 SQLEQQLsaKNSTLKQLEEKlkgqadYEEVKKELNILK 371
Cdd:TIGR04523 695 KYITRMI--RIKDLPKLEEK------YKEIEKELKKLD 724
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
25-358 |
3.85e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 25 DATATVLANRQDE----SEQSRKRLIEQ--SREFKKNTPEDLRKQVAPLlksfQGEIDALSKRSKEAEAAFLNVYKRLID 98
Cdd:PRK02224 306 DADAEAVEARREEledrDEELRDRLEECrvAAQAHNEEAESLREDADDL----EERAEELREEAAELESELEEAREAVED 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 99 VPDPVPALDlgQQLQLKVQRLHDIETEnqklRETLEEYNKEFAEVKNqevtikALKEKIREYEQTLKNQAETIAlEKEQK 178
Cdd:PRK02224 382 RREEIEELE--EEIEELRERFGDAPVD----LGNAEDFLEELREERD------ELREREAELEATLRTARERVE-EAEAL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 179 LQ-NDFAEKERKLQETQMSTTskLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAK--ADEIEMIMTDLERANQRAE 255
Cdd:PRK02224 449 LEaGKCPECGQPVEGSPHVET--IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaEDRIERLEERREDLEELIA 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 256 VAQREAETLREQLSSANHSLQ-LASQIQKAPDVAIEVLTRS-SLEVELAAKEREIAQLVEDVQRLQ--ASLTKLRENSAS 331
Cdd:PRK02224 527 ERRETIEEKRERAEELRERAAeLEAEAEEKREAAAEAEEEAeEAREEVAELNSKLAELKERIESLEriRTLLAAIADAED 606
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2217365688 332 QISQLEQQ--------------LSAKNSTLKQLEEKLKGQA 358
Cdd:PRK02224 607 EIERLREKrealaelnderrerLAEKRERKRELEAEFDEAR 647
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
17-353 |
4.71e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 17 LQQLQRELDATATVLANRQDESEQSRkrlIEQSREFKKNTPEDLRKQVAPLlKSFQGEIDALSKRSKEAEAAfLNVYKRL 96
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEA---LEAELAELPERLEELEERLEEL-RELEEELEELEAELAELQEE-LEELLEQ 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 97 IDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNqEVTIKALKEKIREYEQTL------------ 164
Cdd:COG4717 186 LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLLliaaallallgl 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 165 -------------------------------------KNQAETIALEKEQKLQNdfAEKERKLQETQMSTTSKLEEAE-- 205
Cdd:COG4717 265 ggsllsliltiagvlflvlgllallflllarekaslgKEAEELQALPALEELEE--EELEELLAALGLPPDLSPEELLel 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 206 -HKVQSLQTALEKTRTELFDLKTKYDEE------TTAKADEIEMIMTDLERANQRAEvAQREAETLREQLSSANHSLQLA 278
Cdd:COG4717 343 lDRIEELQELLREAEELEEELQLEELEQeiaallAEAGVEDEEELRAALEQAEEYQE-LKEELEELEEQLEELLGELEEL 421
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217365688 279 SQIQKAPDVAIEVltrSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAsqISQLEQQLSAKNSTLKQLEEK 353
Cdd:COG4717 422 LEALDEEELEEEL---EELEEELEELEEELEELREELAELEAELEQLEEDGE--LAELLQELEELKAELRELAEE 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
141-380 |
4.78e-08 |
|
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: 57.08 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 141 AEVKNQEVTIKALKEKIREYEQTLKNQAETI--ALEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQTALEKT 218
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEkaLLKQLAALERRIAALARRIRALE----QELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 219 RTELFDLKTKYDE-----ETTAKADEIEMIM--TDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAiev 291
Cdd:COG4942 96 RAELEAQKEELAEllralYRLGRQPPLALLLspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE--- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 292 ltRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRensaSQISQLEQQLSAKNSTLKQLEEKLKGQAdyEEVKKELNILK 371
Cdd:COG4942 173 --RAELEALLAELEEERAALEALKAERQKLLARLE----KELAELAAELAELQQEAEELEALIARLE--AEAAAAAERTP 244
|
....*....
gi 2217365688 372 SMEFAPSEG 380
Cdd:COG4942 245 AAGFAALKG 253
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
117-264 |
6.86e-08 |
|
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: 54.93 E-value: 6.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 117 QRLHDIETENQKLRETLEEYNKEF----AEVKNQEVTIKALKEKIREYEQTL---KNQAETIALEKEQklqnDFAEKERK 189
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELedleKEIKRLELEIEEVEARIKKYEEQLgnvRNNKEYEALQKEI----ESLKRRIS 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217365688 190 LQETqmsttsKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERAN-QRAEVAQREAETL 264
Cdd:COG1579 107 DLED------EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEaEREELAAKIPPEL 176
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
18-419 |
9.27e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 57.16 E-value: 9.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 18 QQLQRELDATATVLANRQDESEQSRKRLIEQSrefkkntpedlrkqvapllksfqGEIDALSKRSKEAEAAFLNVYKRLI 97
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVQAN-----------------------GELEKASREETFARTALKNARLDLR 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 98 DVpdpvpaLDLGQQLQLKVQRlhDIETENQKLRETLEEYNKEfaevknqevtIKALKEKIREYEQTLKNQAETIALEKEQ 177
Cdd:pfam12128 657 RL------FDEKQSEKDKKNK--ALAERKDSANERLNSLEAQ----------LKQLDKKHQAWLEEQKEQKREARTEKQA 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 178 KLQNdfAEKERKLQETQMSTTSKLEEAEHKVQslQTALEKTRTElfDLKTK-YDEETTAK-ADEIEMIMTDLERANQRAE 255
Cdd:pfam12128 719 YWQV--VEGALDAQLALLKAAIAARRSGAKAE--LKALETWYKR--DLASLgVDPDVIAKlKREIRTLERKIERIAVRRQ 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 256 VAQREAETLREQLSSANHSLQlasqiqkapdvaievltrssleVELAAKEREIAQLVEDVQRLQASlTKLRensasqISQ 335
Cdd:pfam12128 793 EVLRYFDWYQETWLQRRPRLA----------------------TQLSNIERAISELQQQLARLIAD-TKLR------RAK 843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 336 LEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSDL 415
Cdd:pfam12128 844 LEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIADH 923
|
....
gi 2217365688 416 SGSA 419
Cdd:pfam12128 924 SGSG 927
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
131-350 |
2.16e-07 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 52.99 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 131 ETLEEYNKEFAEVKN--QEVT------IKALKEKIREyeqtLKNQAEtialEKEQKLQNDFAEKERkLQEtqmsttsKLE 202
Cdd:pfam13851 1 ELMKNHEKAFNEIKNyyNDITrnnlelIKSLKEEIAE----LKKKEE----RNEKLMSEIQQENKR-LTE-------PLQ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 203 EAEHKVQSLQTAL---EKTRTELfdlktkydEETTAKADEIEMIMTDLERAN----QRAEVAQREAETLREQLSSANHSL 275
Cdd:pfam13851 65 KAQEEVEELRKQLenyEKDKQSL--------KNLKARLKVLEKELKDLKWEHevleQRFEKVERERDELYDKFEAAIQDV 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217365688 276 QlasqiQKApDVAIEVLTR--SSLEVELAAKEREIAQLvedvqrLQASltKLRENSASQISQ-LEQQLSAKNSTLKQL 350
Cdd:pfam13851 137 Q-----QKT-GLKNLLLEKklQALGETLEKKEAQLNEV------LAAA--NLDPDALQAVTEkLEDVLESKNQLIKDL 200
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
110-270 |
2.32e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 110 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERK 189
Cdd:COG4913 274 LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 190 LQETQmsttSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLS 269
Cdd:COG4913 354 LEERE----RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
.
gi 2217365688 270 S 270
Cdd:COG4913 430 S 430
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
119-414 |
2.50e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 55.83 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 119 LHDIETENQKLRETLEEYNKEFAevKNQEVTI--------KALKEKIREYEQTLKNqAETIALEKEQKLQNDFAEKERKL 190
Cdd:TIGR01612 988 LNDYEAKNNELIKYFNDLKANLG--KNKENMLyhqfdekeKATNDIEQKIEDANKN-IPNIEIAIHTSIYNIIDEIEKEI 1064
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 191 -QETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKydEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQls 269
Cdd:TIGR01612 1065 gKNIELLNKEILEEAEINITNFNEIKEKLKHYNFDDFGK--EENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKK-- 1140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 270 SANHSLQLASQIQKAPDVAIEVLTRSSLEvELAAKEREIAQLVEDVQRLQASLTKLrensASQISQLEQQLSA----KNS 345
Cdd:TIGR01612 1141 SENYIDEIKAQINDLEDVADKAISNDDPE-EIEKKIENIVTKIDKKKNIYDEIKKL----LNEIAEIEKDKTSleevKGI 1215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217365688 346 TL---KQLEEKLKGQADyEEVKKELNILKSMEfAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSD 414
Cdd:TIGR01612 1216 NLsygKNLGKLFLEKID-EEKKKSEHMIKAME-AYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDD 1285
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
58-250 |
4.44e-07 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 53.53 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 58 EDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfLNVYKRLIDVPDpvpaldlgQQLQLKVQRLHDI-ETENQKL-RETLEE 135
Cdd:cd22656 113 EEAKKTIKALLDDLLKEAKKYQDKAAKVVDK-LTDFENQTEKDQ--------TALETLEKALKDLlTDEGGAIaRKEIKD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 136 YNKEFAevKNQEVTIKALKEKIREYEQTLKNQAETIAleKEQKLQNDFaekerKLQETQM-STTSKLEEAEHKVQSLQTA 214
Cdd:cd22656 184 LQKELE--KLNEEYAAKLKAKIDELKALIADDEAKLA--AALRLIADL-----TAADTDLdNLLALIGPAIPALEKLQGA 254
|
170 180 190
....*....|....*....|....*....|....*.
gi 2217365688 215 LEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERA 250
Cdd:cd22656 255 WQAIATDLDSLKDLLEDDIS-KIPAAILAKLELEKA 289
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
151-353 |
4.49e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 54.64 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 151 KALKEKIREYEQTLKNQAETIALEKEQ-KLQNDFAEKERKL-----QETQMSTTSKLEEAE-HKVQ--SLQT-------- 213
Cdd:PHA02562 170 KLNKDKIRELNQQIQTLDMKIDHIQQQiKTYNKNIEEQRKKngeniARKQNKYDELVEEAKtIKAEieELTDellnlvmd 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 214 ------ALEKTRTELFDLKTKYdeETTAKadEIEMI---------MTDLERANQRaevaqreAETLREQLSSANHSL-QL 277
Cdd:PHA02562 250 iedpsaALNKLNTAAAKIKSKI--EQFQK--VIKMYekggvcptcTQQISEGPDR-------ITKIKDKLKELQHSLeKL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 278 ASQIQKAPDVAIEVLTRSS----LEVELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLSAKNSTLKQL 350
Cdd:PHA02562 319 DTAIDELEEIMDEFNEQSKklleLKNKISTNKQSLITLVDKAKKVKAAIEELqaeFVDNAEELAKLQDELDKIVKTKSEL 398
|
...
gi 2217365688 351 EEK 353
Cdd:PHA02562 399 VKE 401
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
96-373 |
4.50e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 96 LIDVPDPVPALDLGQQLQLKVQrlhDIETENQKLR---------ETLEEYNKEFAEVKNQEVTIKALKEKIreyeqTLKN 166
Cdd:COG3206 60 LVEPQSSDVLLSGLSSLSASDS---PLETQIEILKsrpvlervvDKLNLDEDPLGEEASREAAIERLRKNL-----TVEP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 167 QAETIAL---------EKEQKLQNDFAE------KERKLQETQMSTT---SKLEEAEHKVQSLQTALE--KTRTELFDLk 226
Cdd:COG3206 132 VKGSNVIeisytspdpELAAAVANALAEayleqnLELRREEARKALEfleEQLPELRKELEEAEAALEefRQKNGLVDL- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 227 tkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSanhSLQLASQIQKAPDVAIEVLTRSSLEVELA---- 302
Cdd:COG3206 211 ---SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS---GPDALPELLQSPVIQQLRAQLAELEAELAelsa 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 303 ----------AKEREIA----QLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKlkgQADYEEVKKELN 368
Cdd:COG3206 285 rytpnhpdviALRAQIAalraQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL---EAELRRLEREVE 361
|
....*
gi 2217365688 369 ILKSM 373
Cdd:COG3206 362 VAREL 366
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
17-354 |
6.31e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.46 E-value: 6.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 17 LQQLQRELDATATVLANRQDESEQSRKRLIEQSREfkkntpedLRKQVAPLLKSFQGEIDALSKRSKEAEA---AFLNVY 93
Cdd:pfam12128 260 LSHLHFGYKSDETLIASRQEERQETSAELNQLLRT--------LDDQWKEKRDELNGELSAADAAVAKDRSeleALEDQH 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 94 KRLIDVPDPVPALDLGQQLQLK-----VQRLHDIETENQklRETLEEYNKEFAEVKNQEVT----IKALKEKIREYEQTL 164
Cdd:pfam12128 332 GAFLDADIETAAADQEQLPSWQselenLEERLKALTGKH--QDVTAKYNRRRSKIKEQNNRdiagIKDKLAKIREARDRQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 165 KNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQ-TALEKTRTELFD-LKTKYDEETTAKADEIEM 242
Cdd:pfam12128 410 LAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATaTPELLLQLENFDeRIERAREEQEAANAEVER 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 243 IMTD--------------LERANQRAEVAQREAETLREQLSSANHSLqLASQIQKAPD--------VAIEVLTRSSLEVE 300
Cdd:pfam12128 490 LQSElrqarkrrdqaseaLRQASRRLEERQSALDELELQLFPQAGTL-LHFLRKEAPDweqsigkvISPELLHRTDLDPE 568
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217365688 301 L----AAKEREIAQLVEDVQRLQA-SLTKLRENSASQISQLEQQLSAKNSTLKQLEEKL 354
Cdd:pfam12128 569 VwdgsVGGELNLYGVKLDLKRIDVpEWAASEEELRERLDKAEEALQSAREKQAAAEEQL 627
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
151-422 |
7.69e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.21 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 151 KALKEKIREYEQTLKNQAETIALEK-EQKLQNDFAEKERKLQETQmsttsKLEEAEHKvqslqtalEKTRTELFDLKTKY 229
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLqELKLKEQAKKALEYYQLKE-----KLELEEEY--------LLYLDYLKLNEERI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 230 DEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKapDVAIEVLTRSSLEVELAAKEREIA 309
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAK--EEEELKSELLKLERRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 310 QLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSmefapSEGAGTQDAAKP 389
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK-----LESERLSSAAKL 392
|
250 260 270
....*....|....*....|....*....|...
gi 2217365688 390 LEVLLLEKNRSLQSENAALRISNSDLSGSARRK 422
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEK 425
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
123-417 |
8.73e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.82 E-value: 8.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 123 ETENQKLRETLEEYNKEFAEVKNQEVTIKALK-EKIREYEQTLKNQAETIALEKEQklqNDFAEKERKLQETQMSTTSKL 201
Cdd:pfam02463 218 KLELEEEYLLYLDYLKLNEERIDLLQELLRDEqEEIESSKQEIEKEEEKLAQVLKE---NKEEEKEKKLQEEELKLLAKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 202 EEAEhkvqSLQTALEKTRTELFDLKTKYDEETTAKAD-EIEMIMTDLERAN--------QRAEVAQREAETLREQLSSAN 272
Cdd:pfam02463 295 EEEL----KSELLKLERRKVDDEEKLKESEKEKKKAEkELKKEKEEIEELEkelkeleiKREAEEEEEEELEKLQEKLEQ 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 273 HSLQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAS------QISQLEQQLSAKNST 346
Cdd:pfam02463 371 LEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELeileeeEESIELKQGKLTEEK 450
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217365688 347 LKQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSDLSG 417
Cdd:pfam02463 451 EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVG 521
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
232-412 |
1.04e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 232 ETTAKADEIEMIMTDLERANQRAEVAQREAETLR------EQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKE 305
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 306 REIAQLVEDVQRLQASLTKLRE-----------NSASQISQLEQQLSAKNSTLKQLEEKLK---------------GQAD 359
Cdd:COG4913 302 AELARLEAELERLEARLDALREeldeleaqirgNGGDRLEQLEREIERLERELEERERRRArleallaalglplpaSAEE 381
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217365688 360 YEEVKKELNILKsmEFAPSEGAGTQDAAKPLEVLLLEKNR---SLQSENAAL--RISN 412
Cdd:COG4913 382 FAALRAEAAALL--EALEEELEALEEALAEAEAALRDLRRelrELEAEIASLerRKSN 437
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
196-464 |
1.06e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 196 STTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL 275
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 276 QLASQIQKAPDV---------------AIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQ 338
Cdd:COG3883 96 YRSGGSVSYLDVllgsesfsdfldrlsALSKIADADADLleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 339 QLSAKNSTLKQLEEKLKgQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSDLSGS 418
Cdd:COG3883 176 QQAEQEALLAQLSAEEA-AAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2217365688 419 ARRKGKDQPESRRPGSLPAPPPSQLPRNPGEQASNTNGTHQFSPAG 464
Cdd:COG3883 255 AGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAAS 300
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
119-371 |
1.10e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 53.29 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 119 LHDIETENQKLRETLEEYNK---EFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQM 195
Cdd:pfam10174 201 LDQKEKENIHLREELHRRNQlqpDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVY 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 196 STTSKLeeAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKAD---EIEMIMTDLERANQRAEVAQREAETLREQLSSAN 272
Cdd:pfam10174 281 KSHSKF--MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDckqHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 273 HSLQ---------------LASQIQKAPDV------AIEVLTR--SSLEVELAAKEREIAQLVEDVQRLQASLTklreNS 329
Cdd:pfam10174 359 SFLNkktkqlqdlteekstLAGEIRDLKDMldvkerKINVLQKkiENLQEQLRDKDKQLAGLKERVKSLQTDSS----NT 434
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2217365688 330 ASQISQLEQQLSAKNSTLKQLEEK--LKGQADYEEV---KKELNILK 371
Cdd:pfam10174 435 DTALTTLEEALSEKERIIERLKEQreREDRERLEELeslKKENKDLK 481
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
16-374 |
1.37e-06 |
|
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: 53.19 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 16 DLQQLQRELDATATVLANRQDESEQSRKRLIEqsrefkKNTPEDLRKQVAPLLKSFQGeidalskrsKEAEAAFLnvykr 95
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVELEELKKILAE------DEKLLDEKKQFEKIAEELKG---------KEQELIFL----- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 96 lidvpdpvpaldlgqqLQLKVQRLHDIETENQKLRETLEEYNKEFAE---------VKNQEVTIKALKEKIREYEQTLKN 166
Cdd:pfam05483 445 ----------------LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDlktelekekLKNIELTAHCDKLLLENKELTQEA 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 167 QAETIALEKEQK-LQNDFAEKERKLQEtqmsttskLEEAEHKVQSLQTALEKTRTELF----DLKTKYDE-ETTAKADEI 240
Cdd:pfam05483 509 SDMTLELKKHQEdIINCKKQEERMLKQ--------IENLEEKEMNLRDELESVREEFIqkgdEVKCKLDKsEENARSIEY 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 241 EMImtdleRANQRAEVAQREAETLREQLSSANHSLQLASQIQKA---------PDVAIEVLTRSSLEVELAAKEREIAQL 311
Cdd:pfam05483 581 EVL-----KKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAlkkkgsaenKQLNAYEIKVNKLELELASAKQKFEEI 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 312 VEDVQRlQASLTKLRENS-----------ASQISQLEQQLSA----KNSTLKQLEEKLKGQAD--YEEVKKELNILKSME 374
Cdd:pfam05483 656 IDNYQK-EIEDKKISEEKlleevekakaiADEAVKLQKEIDKrcqhKIAEMVALMEKHKHQYDkiIEERDSELGLYKNKE 734
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
16-409 |
1.54e-06 |
|
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: 53.15 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 16 DLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPED---LRKQVAPL---LKSFQGEIDALSKRSKEAEAAF 89
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqlrVKEKIGELeaeIASLERSIAEKERELEDAEERL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 90 LNVYKRLIDVPDPVPALDlGQQLQLKVQRlHDIETENQKLREtleEYNKEFAEVKNQEVTIKALKEKIREYEQtlknqae 169
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELE-REIEEERKRR-DKLTEEYAELKE---ELEDLRAELEEVDKEFAETRDELKDYRE------- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 170 tiALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALektrtelfdlkTKYDEETTAKADEIEMIMTDLER 249
Cdd:TIGR02169 393 --KLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI-----------NELEEEKEDKALEIKKQEWKLEQ 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 250 ANQRAEVAQREAETLREQLssanhslqlaSQIQKapdvaievlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENS 329
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEY----------DRVEK---------ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASI 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 330 ASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGtqdaakPLEVLLLEKNRSLQSENAALR 409
Cdd:TIGR02169 521 QGVHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAG------RATFLPLNKMRDERRDLSILS 594
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
16-288 |
1.54e-06 |
|
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: 52.07 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 16 DLQQLQRELDAtatvLANRQDESEQSRKRLIEQsrefkkntpedlrkqvaplLKSFQGEIDALSKRSKEAEaaflnvykr 95
Cdd:COG4942 28 ELEQLQQEIAE----LEKELAALKKEEKALLKQ-------------------LAALERRIAALARRIRALE--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 96 lidvpdpvpaldlgQQLQLKVQRLHDIETENQKLRETLEEYNKEFAevknqEVTIKALKEKIREYEQTLKNQAETIALEK 175
Cdd:COG4942 76 --------------QELAALEAELAELEKEIAELRAELEAQKEELA-----ELLRALYRLGRQPPLALLLSPEDFLDAVR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 176 EQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAE 255
Cdd:COG4942 137 RLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
|
250 260 270
....*....|....*....|....*....|...
gi 2217365688 256 VAQREAETLREQLSSANHSLQLASQIQKAPDVA 288
Cdd:COG4942 217 ELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
117-317 |
1.78e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 117 QRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAETIALekeQKLQNDFAEKERKLQETQmS 196
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAE---LDALQERREALQRLAEYSWDEIDV---ASAEREIAELEAELERLD-A 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 197 TTSKLEEAEHKVQSLQTALEKTRTELFDLKTKY---DEETTAKADEIEMIMTDLERANQRAEVAQRE-AETLREQLSSAN 272
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIgrlEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALGDA 762
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2217365688 273 HSLQLASQIQKApdvaievltRSSLEVELAAKEREIAQLVEDVQR 317
Cdd:COG4913 763 VERELRENLEER---------IDALRARLNRAEEELERAMRAFNR 798
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
162-368 |
2.31e-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: 52.37 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 162 QTLKNQAETIALEKEQK-LQNDFAEKERKLQETQmSTTSKLEEAEHKVQSL----------------------------Q 212
Cdd:TIGR02168 671 SILERRREIEELEEKIEeLEEKIAELEKALAELR-KELEELEEELEQLRKEleelsrqisalrkdlarleaeveqleerI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 213 TALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQL--ASQIQKAPDVAIE 290
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlnEEAANLRERLESL 829
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217365688 291 VLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKlkgQADYEEVKKELN 368
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL---RSELEELSEELR 904
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
105-368 |
2.63e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 105 ALDLGQQLQLKVQRLHDIEtenqklrETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLknQAETIALEKEQKLQNDFA 184
Cdd:PRK04863 288 ALELRRELYTSRRQLAAEQ-------YRLVEMARELAELNEAESDLEQDYQAASDHLNLV--QTALRQQEKIERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 185 EKERKLQETQMST---TSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERANQ--------- 252
Cdd:PRK04863 359 ELEERLEEQNEVVeeaDEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQT-RAIQYQQAVQALERAKQlcglpdlta 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 253 -----RAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVelaakEREIAQlvedvQRLQASLTKLRE 327
Cdd:PRK04863 438 dnaedWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEV-----SRSEAW-----DVARELLRRLRE 507
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2217365688 328 --NSASQISQLEQQLSAknstlkqLEEKLKGQADYEEVKKELN 368
Cdd:PRK04863 508 qrHLAEQLQQLRMRLSE-------LEQRLRQQQRAERLLAEFC 543
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
36-374 |
3.01e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 36 DESEQSRKRLIEQSREFKKNTPEDLRKqvapllksfqgEIDALSKRSKEAEAAFLNVYKRLidvpdpvpaldlgQQLQLK 115
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGLTPEKLEK-----------ELEELEKAKEEIEEEISKITARI-------------GELKKE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 116 VQRLHD--IETENQKL------RETLEEYNKEF-----AEVKNQEVTIKALKEKIR-------EYEQTLKNQAETIALEK 175
Cdd:PRK03918 421 IKELKKaiEELKKAKGkcpvcgRELTEEHRKELleeytAELKRIEKELKEIEEKERklrkelrELEKVLKKESELIKLKE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 176 --------EQKLQNDFAEK-ERKLQE----------------TQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYD 230
Cdd:PRK03918 501 laeqlkelEEKLKKYNLEElEKKAEEyeklkekliklkgeikSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELE 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 231 EETTAKADEIEMIMTDLER----------ANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVE 300
Cdd:PRK03918 581 ELGFESVEELEERLKELEPfyneylelkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE 660
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217365688 301 LAAKEREIAQLVEDVQRLQA---SLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSME 374
Cdd:PRK03918 661 YEELREEYLELSRELAGLRAeleELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALL 737
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
37-372 |
3.06e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 37 ESEQSRKRLIEQSREFKKNtpEDLRKQVAPLLKSFQGEIDALSKRSKEAEaaflNVYKRLIDVpdpvpaldlGQQLQLKV 116
Cdd:PRK03918 142 ESDESREKVVRQILGLDDY--ENAYKNLGEVIKEIKRRIERLEKFIKRTE----NIEELIKEK---------EKELEEVL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 117 QRLHDIETENQKLRETLEEYNKEFAEV----------------------------KNQEVTIKALKEKIREYEQTLKNQA 168
Cdd:PRK03918 207 REINEISSELPELREELEKLEKEVKELeelkeeieelekeleslegskrkleekiRELEERIEELKKEIEELEEKVKELK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 169 ETIALEKE----QKLQNDFAEKERKLQETQMSTT----------SKLEEAEHKVQSLQTALEKTRTELFDLKTKYD--EE 232
Cdd:PRK03918 287 ELKEKAEEyiklSEFYEEYLDELREIEKRLSRLEeeingieeriKELEEKEERLEELKKKLKELEKRLEELEERHElyEE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 233 TTAKADEIEMIMTDL-----ERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKE-- 305
Cdd:PRK03918 367 AKAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRElt 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 306 ------------REIAQLVEDVQRLQASLTKLREN-------------------SASQISQLEQQLSAKNstLKQLEEKL 354
Cdd:PRK03918 447 eehrkelleeytAELKRIEKELKEIEEKERKLRKElrelekvlkkeseliklkeLAEQLKELEEKLKKYN--LEELEKKA 524
|
410
....*....|....*...
gi 2217365688 355 KgqaDYEEVKKELNILKS 372
Cdd:PRK03918 525 E---EYEKLKEKLIKLKG 539
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
16-359 |
3.85e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 16 DLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKntpedlrkqvapLLKSFQGEIDALSKRSKEAEAAflNVYKR 95
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQR------------LAEYSWDEIDVASAEREIAELE--AELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 96 LIDVPDpvpalDLgQQLQlkvQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAETIALEK 175
Cdd:COG4913 680 LDASSD-----DL-AALE---EQLEELEAELEELEEELDELKGEIGRLEKE---LEQAEEELDELQDRLEAAEDLARLEL 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 176 EQKLQNDFAEKERKLQETQMSttsklEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEiemIMTDLERANQ-RA 254
Cdd:COG4913 748 RALLEERFAAALGDAVERELR-----ENLEERIDALRARLNRAEEELERAMRAFNREWPAETAD---LDADLESLPEyLA 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 255 EVAQREAETL-------REQLSSANHS--LQLASQIQKAPDVAIEVLTR--SSLE---------VELAAKEREiaqlVED 314
Cdd:COG4913 820 LLDRLEEDGLpeyeerfKELLNENSIEfvADLLSKLRRAIREIKERIDPlnDSLKripfgpgryLRLEARPRP----DPE 895
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2217365688 315 VQRLQASLTKLRENSASQISQLEQqlsAKNSTLKQLEEKLKGQAD 359
Cdd:COG4913 896 VREFRQELRAVTSGASLFDEELSE---ARFAALKRLIERLRSEEE 937
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
125-412 |
3.93e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 51.90 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 125 ENQKLRETLE---EYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKL 201
Cdd:pfam02463 174 ALKKLIEETEnlaELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 202 EEAEhKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEmimTDLERANQRAEVAQREAETLREQLSSANHSLQLASQI 281
Cdd:pfam02463 254 ESSK-QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLA---KEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 282 QKAPDVAIE---------VLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKN------ST 346
Cdd:pfam02463 330 LKKEKEEIEelekelkelEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSeeekeaQL 409
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 347 LKQLEEKLKGQADYE---EVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSL-QSENAALRISN 412
Cdd:pfam02463 410 LLELARQLEDLLKEEkkeELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELkKSEDLLKETQL 479
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
11-361 |
4.58e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 51.62 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 11 YWKRFDLQQLQRELDATaTVLANRQDESEQSRKRLIE---QSREFK--KNTPEDLRKQVAPLLKSFQGEIDALSKrSKEA 85
Cdd:COG5022 851 FGRSLKAKKRFSLLKKE-TIYLQSAQRVELAERQLQElkiDVKSISslKLVNLELESEIIELKKSLSSDLIENLE-FKTE 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 86 EAAFLnvyKRLIDVPDPVPALDLGQQLQLKVQRLHdieTENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLK 165
Cdd:COG5022 929 LIARL---KKLLNNIDLEEGPSIEYVKLPELNKLH---EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELA 1002
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 166 N--------QAETIALEKEQK----LQND----FAEKERKLQETQMS---TTSKLEEAEHKVQSLQTALEKTRTELFDLK 226
Cdd:COG5022 1003 ElskqygalQESTKQLKELPVevaeLQSAskiiSSESTELSILKPLQklkGLLLLENNQLQARYKALKLRRENSLLDDKQ 1082
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 227 TKYDEETTAKADEIEmiMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQI-QKAPDVAIEVLTRSSLEVELaake 305
Cdd:COG5022 1083 LYQLESTENLLKTIN--VKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLsQLVNTLEPVFQKLSVLQLEL---- 1156
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217365688 306 rEIAQLVEDVQRLQAS--LTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYE 361
Cdd:COG5022 1157 -DGLFWEANLEALPSPppFAALSEKRLYQSALYDEKSKLSSSEVNDLKNELIALFSKI 1213
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
46-352 |
5.27e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 46 IEQSREFKKntpEDLRKQvaplLKSFQGEIDALSKRSKEAEAAfLNVYKRLIDVpdpvpaLDLGQQLQLKVQRLHDIETE 125
Cdd:COG3206 162 LEQNLELRR---EEARKA----LEFLEEQLPELRKELEEAEAA-LEEFRQKNGL------VDLSEEAKLLLQQLSELESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 126 NQKLRETLEEynkefaevknQEVTIKALKEKIREYEQTLKNQAETIALekeQKLQNDFAEKERKLQETQmsttSKLEEAE 205
Cdd:COG3206 228 LAEARAELAE----------AEARLAALRAQLGSGPDALPELLQSPVI---QQLRAQLAELEAELAELS----ARYTPNH 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 206 HKVQSLQTALEKTRTELfdlktkydeettakADEIEMIMTDLEranQRAEVAQREAETLREQLSsanhslQLASQIQKAP 285
Cdd:COG3206 291 PDVIALRAQIAALRAQL--------------QQEAQRILASLE---AELEALQAREASLQAQLA------QLEARLAELP 347
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217365688 286 dvaievltrsslevelaAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLSAKNSTLKQLEE 352
Cdd:COG3206 348 -----------------ELEAELRRLEREVEVARELYESLLQ----RLEEARLAEALTVGNVRVIDP 393
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
106-325 |
6.10e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.78 E-value: 6.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 106 LDLGQQlQLKVQRLHdIETENQKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKNQAETIalekeQKLQN 181
Cdd:PHA02562 190 IDHIQQ-QIKTYNKN-IEEQRKKNGENIARKQNKYDELVEEAKTIKAeieeLTDELLNLVMDIEDPSAAL-----NKLNT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 182 DFAEKERKLQ----ETQMST--------TSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETtakadeiemimtdlER 249
Cdd:PHA02562 263 AAAKIKSKIEqfqkVIKMYEkggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELE--------------EI 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217365688 250 ANQRAEvAQREAETLREQLSSANHSLQLASQIQKAPDVAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKL 325
Cdd:PHA02562 329 MDEFNE-QSKKLLELKNKISTNKQSLITLVDKAKKVKAAIE-----ELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
112-425 |
6.60e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.12 E-value: 6.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 112 LQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQ 191
Cdd:TIGR00618 589 LQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIR 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 192 ETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAkadeiemIMTDLERANQRAEVAQREAETLREQLSSA 271
Cdd:TIGR00618 669 VLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETH-------IEEYDREFNEIENASSSLGSDLAAREDAL 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 272 NHSLQLA-------------SQIQKAPDVAIEVLT-----------------RSSLEVELAAKEREIAQLVED------- 314
Cdd:TIGR00618 742 NQSLKELmhqartvlkarteAHFNNNEEVTAALQTgaelshlaaeiqffnrlREEDTHLLKTLEAEIGQEIPSdedilnl 821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 315 -----VQRLQASLTKLRENSASQIsQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKp 389
Cdd:TIGR00618 822 qcetlVQEEEQFLSRLEEKSATLG-EITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHE- 899
|
330 340 350
....*....|....*....|....*....|....*.
gi 2217365688 390 levLLLEKNRSLQSENAALRISNSDLSGSARRKGKD 425
Cdd:TIGR00618 900 ---ITLYANVRLANQSEGRFHGRYADSHVNARKYQG 932
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
18-237 |
7.47e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 7.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 18 QQLQRELDATATVLANRQDESEQSRKRLIEQS---REFKKNT----PEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFL 90
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEaalEEFRQKNglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 91 NVYKRLIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAET 170
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAALRAQLQQEAQRILASLEA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 171 ---IALEKEQKLQNDFAEKERKLQETQmSTTSKLEEAEHKVQSLQTALEktrtelfDLKTKYDEETTAKA 237
Cdd:COG3206 321 eleALQAREASLQAQLAQLEARLAELP-ELEAELRRLEREVEVARELYE-------SLLQRLEEARLAEA 382
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
109-374 |
8.46e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 8.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 109 GQQLQLKVQrlhdIE-TENQKLRETLEEYNKEFAEVKnqevtikalkEKIREYEQtlknQAETiALEKEQKLQNDFAEKE 187
Cdd:PRK02224 187 GSLDQLKAQ----IEeKEEKDLHERLNGLESELAELD----------EEIERYEE----QREQ-ARETRDEADEVLEEHE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 188 RKLQETQmsttsKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQ 267
Cdd:PRK02224 248 ERREELE-----TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 268 LSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKE-REIAQLVEDvqRLQASLTKLREnSASQISQLEQQLSAKNST 346
Cdd:PRK02224 323 DEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEElREEAAELES--ELEEAREAVED-RREEIEELEEEIEELRER 399
|
250 260
....*....|....*....|....*....
gi 2217365688 347 LKQLEEKLKGQADY-EEVKKELNILKSME 374
Cdd:PRK02224 400 FGDAPVDLGNAEDFlEELREERDELRERE 428
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
66-369 |
1.35e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.91 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 66 PLLKSFQGEIDALSKRsKEAEAAFLNVYKRLIDvpdpvpALDLGQQLQlkvqrlhDIETENQKLRETLEEYNKEFAEVKN 145
Cdd:PRK11281 36 PTEADVQAQLDALNKQ-KLLEAEDKLVQQDLEQ------TLALLDKID-------RQKEETEQLKQQLAQAPAKLRQAQA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 146 QevtIKALKEKIreyEQTLKNQAETIALEKeqkLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQTALEKTRTELFdl 225
Cdd:PRK11281 102 E---LEALKDDN---DEETRETLSTLSLRQ---LESRLAQTLDQLQNAQ----NDLAEYNSQLVSLQTQPERAQAALY-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 226 ktkydeettakadeiemimtdlerANQraevaQREAEtLREQLSS--ANHSLQLASQIQKapdvaievltrssLEVELAA 303
Cdd:PRK11281 167 ------------------------ANS-----QRLQQ-IRNLLKGgkVGGKALRPSQRVL-------------LQAEQAL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 304 KEREIA---QLVEDVQRLQASLTKLRENSASQISQLEQQL-------SAKNstLKQLEEKLKGQADYEE---------VK 364
Cdd:PRK11281 204 LNAQNDlqrKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLqllqeaiNSKR--LTLSEKTVQEAQSQDEaariqanplVA 281
|
....*
gi 2217365688 365 KELNI 369
Cdd:PRK11281 282 QELEI 286
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
17-408 |
1.68e-05 |
|
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: 49.73 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 17 LQQLQRELDATATVLANRQDESEQSRKRL------IEQSREFKKNTPEDLRKQVAPLLK---SFQG---EIDALSKRSKE 84
Cdd:pfam15921 119 LQEMQMERDAMADIRRRESQSQEDLRNQLqntvheLEAAKCLKEDMLEDSNTQIEQLRKmmlSHEGvlqEIRSILVDFEE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 85 AEAAflNVYKRliDVPDPVPALDLG-------QQLQLKVQ-----------RLHDIETENQKLRETLEEYNKEFAE--VK 144
Cdd:pfam15921 199 ASGK--KIYEH--DSMSTMHFRSLGsaiskilRELDTEISylkgrifpvedQLEALKSESQNKIELLLQQHQDRIEqlIS 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 145 NQEVTIKALKEKI---REYEQTLKNQAETIalEKEQKLQND-FAEKERKLQETQMSTTSKLEEA----EHKVQSLQTALE 216
Cdd:pfam15921 275 EHEVEITGLTEKAssaRSQANSIQSQLEII--QEQARNQNSmYMRQLSDLESTVSQLRSELREAkrmyEDKIEELEKQLV 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 217 KTRTELFDLKTKYDE---ETTAKADEIEMIMTDLERANQRAEVAQREAETLREQlssanhslqlasqiQKAPDVAIEVLT 293
Cdd:pfam15921 353 LANSELTEARTERDQfsqESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDR--------------DTGNSITIDHLR 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 294 RsslevELAAKEREiaqlvedVQRLQASLTKLRENSAsqiSQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKEL-NILKS 372
Cdd:pfam15921 419 R-----ELDDRNME-------VQRLEALLKAMKSECQ---GQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLrKVVEE 483
|
410 420 430
....*....|....*....|....*....|....*.
gi 2217365688 373 MEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAAL 408
Cdd:pfam15921 484 LTAKKMTLESSERTVSDLTASLQEKERAIEATNAEI 519
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
17-371 |
1.81e-05 |
|
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: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 17 LQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRL 96
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 97 IDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEynkefaevknqeVTIKALKEKIREYEQTLknqAETIALEKE 176
Cdd:COG1196 504 EGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEA------------ALAAALQNIVVEDDEVA---AAAIEYLKA 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 177 QKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEV 256
Cdd:COG1196 569 AKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 257 AQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQI--- 333
Cdd:COG1196 649 VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAlee 728
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2217365688 334 -------SQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILK 371
Cdd:COG1196 729 qleaereELLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
117-362 |
1.99e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 117 QRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEqtlknqaetialEKEQKLQNDFAEKERKLQETQMS 196
Cdd:PRK02224 314 ARREELEDRDEELRDRLEECRVAAQAHNEE---AESLREDADDLE------------ERAEELREEAAELESELEEAREA 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 197 TT---SKLEEAEHKVQSLQTALEKTRTELFDLKTkYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQ------ 267
Cdd:PRK02224 379 VEdrrEEIEELEEEIEELRERFGDAPVDLGNAED-FLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpec 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 268 ---LSSANHSLQLASQIQKAPDVAIEvltRSSLEVELAAKEREIAQLvEDVQRLQASLTKLRENSASQISQLEQQLSAKN 344
Cdd:PRK02224 458 gqpVEGSPHVETIEEDRERVEELEAE---LEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIE 533
|
250
....*....|....*...
gi 2217365688 345 STLKQLEEKLKGQADYEE 362
Cdd:PRK02224 534 EKRERAEELRERAAELEA 551
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
53-358 |
2.62e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.07 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 53 KKNTPEDLRKQVAPLLkSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPALDLGQQ-------LQLKVQRLH----- 120
Cdd:pfam12128 191 KEGKFRDVKSMIVAIL-EDDGVVPPKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQefntlesAELRLSHLHfgyks 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 121 ---DIETENQKLRETLEEYNKEFAEVKNQevtikaLKEKIREYEQTLKNQAETIALEKEQ---------KLQNDFAEKER 188
Cdd:pfam12128 270 detLIASRQEERQETSAELNQLLRTLDDQ------WKEKRDELNGELSAADAAVAKDRSElealedqhgAFLDADIETAA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 189 KLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETtakADEIEMIMTDLE-----RANQRAE---VAQRE 260
Cdd:pfam12128 344 ADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQN---NRDIAGIKDKLAkireaRDRQLAVaedDLQAL 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 261 AETLREQLSSANHSL-----QLASQI------QKAPDVAIEVLTRSSLEVELAAKEREIAQL----VEDVQRLQASLTKL 325
Cdd:pfam12128 421 ESELREQLEAGKLEFneeeyRLKSRLgelklrLNQATATPELLLQLENFDERIERAREEQEAanaeVERLQSELRQARKR 500
|
330 340 350
....*....|....*....|....*....|...
gi 2217365688 326 RENSASQISQLEQQLSAKNSTLKQLEEKLKGQA 358
Cdd:pfam12128 501 RDQASEALRQASRRLEERQSALDELELQLFPQA 533
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
21-366 |
3.04e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 21 QRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKqvAPLLKSFQGE---IDALSKRSKEAEAAflNVYKRLI 97
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK--ADELKKAAAAkkkADEAKKKAEEKKKA--DEAKKKA 1440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 98 DVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLE--EYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEK 175
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKkaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE 1520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 176 EQKLQN-DFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTElfdlKTKYDEETTAKADEIEMIMTDLE--RANQ 252
Cdd:PTZ00121 1521 AKKADEaKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE----EAKKAEEDKNMALRKAEEAKKAEeaRIEE 1596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 253 RAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQ 332
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK 1676
|
330 340 350
....*....|....*....|....*....|....
gi 2217365688 333 ISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKE 366
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
130-408 |
3.40e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.89 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 130 RETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKnqaetiALEK-EQKLQNDFAEKERKLQETQMSTTSKLEEAEHKV 208
Cdd:TIGR00606 237 REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIK------ALKSrKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNH 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 209 QSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQ---------REAETLREQLSSANHSLQLAS 279
Cdd:TIGR00606 311 QRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQehirardslIQSLATRLELDGFERGPFSER 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 280 QIQKAPDVAIEVLTR-----SSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKL 354
Cdd:TIGR00606 391 QIKNFHTLVIERQEDeaktaAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSS 470
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217365688 355 KG--QADYEEVKKELNILKSMEFAPSEGAGTQDAA-KPLEVLLLEKNRSLQSENAAL 408
Cdd:TIGR00606 471 DRilELDQELRKAERELSKAEKNSLTETLKKEVKSlQNEKADLDRKLRKLDQEMEQL 527
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
110-354 |
3.51e-05 |
|
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: 48.63 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 110 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVknqevtikaLKEKIREYEQTlknQAETIALEKEQKLQNDFAEKERK 189
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQL---------CEEKNALQEQL---QAETELCAEAEEMRARLAARKQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 190 LQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEE-------------TTAKADEIEMIMTDLERANQRaev 256
Cdd:pfam01576 73 LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEeaarqklqlekvtTEAKIKKLEEDILLLEDQNSK--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 257 AQREAETLREQLSsaNHSLQLASQIQKAPDVA----IEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSA-- 330
Cdd:pfam01576 150 LSKERKLLEERIS--EFTSNLAEEEEKAKSLSklknKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAel 227
|
250 260
....*....|....*....|....*
gi 2217365688 331 -SQISQLEQQLSAKNSTLKQLEEKL 354
Cdd:pfam01576 228 qAQIAELRAQLAKKEEELQAALARL 252
|
|
| COG5576 |
COG5576 |
Homeodomain-containing transcription factor [Transcription]; |
1253-1338 |
3.77e-05 |
|
Homeodomain-containing transcription factor [Transcription];
Pssm-ID: 227863 [Multi-domain] Cd Length: 156 Bit Score: 45.51 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 1253 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIRRelfieeiqagsQGQAGASDSPSA 1332
Cdd:COG5576 52 KSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKK-----------KRSGKVEQRPGE 120
|
....*.
gi 2217365688 1333 RSGRAA 1338
Cdd:COG5576 121 EEADLA 126
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
72-366 |
4.51e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 48.28 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 72 QGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPAL-----DLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ 146
Cdd:pfam10174 344 QTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLageirDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKER 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 147 evtIKALKEKIREYEQTLKNQAETIAlEKE---QKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELF 223
Cdd:pfam10174 424 ---VKSLQTDSSNTDTALTTLEEALS-EKEriiERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLI 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 224 DLKtkydEETTAKADEieMIMTDLERANQRAEVAQREAETLReqlssanhslqLASQIQKAPDVAIEVLTRSSLEVELAA 303
Cdd:pfam10174 500 DLK----EHASSLASS--GLKKDSKLKSLEIAVEQKKEECSK-----------LENQLKKAHNAEEAVRTNPEINDRIRL 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 304 KEREIAQLVEDVQRLQASLTKL------RENSAS----QISQLE---------QQLSAKNSTLKQLEEKLKGQADYEEVK 364
Cdd:pfam10174 563 LEQEVARYKEESGKAQAEVERLlgilreVENEKNdkdkKIAELEsltlrqmkeQNKKVANIKHGQQEMKKKGAQLLEEAR 642
|
..
gi 2217365688 365 KE 366
Cdd:pfam10174 643 RR 644
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
119-376 |
4.63e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 48.28 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 119 LHDIETENQKLRETL----EEYNKEFAEVKNQEVTIKALKEKIREYEQTL-KNQAETIALE-KEQKLQNDFAEKERKLQE 192
Cdd:pfam10174 249 IRDLEDEVQMLKTNGllhtEDREEEIKQMEVYKSHSKFMKNKIDQLKQELsKKESELLALQtKLETLTNQNSDCKQHIEV 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 193 TQMSTTSKLEEA---EHKVQSLQTALEKTRTeLFDLKTKY----DEETTAKADEIEMIMTDLERANQRAEVAQREAETLR 265
Cdd:pfam10174 329 LKESLTAKEQRAailQTEVDALRLRLEEKES-FLNKKTKQlqdlTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQ 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 266 EQLSSANhslqlaSQIQKAPDVAIEVLTRSS--------LEVELAAKEREIAQLVEDVQRLQ-------ASLTKLRENSA 330
Cdd:pfam10174 408 EQLRDKD------KQLAGLKERVKSLQTDSSntdtalttLEEALSEKERIIERLKEQREREDrerleelESLKKENKDLK 481
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2217365688 331 SQISQLEQQLSAKNSTLKQLEEKLKGQADyEEVKKElNILKSMEFA 376
Cdd:pfam10174 482 EKVSALQPELTEKESSLIDLKEHASSLAS-SGLKKD-SKLKSLEIA 525
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
141-385 |
6.37e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 6.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 141 AEVKNQEVTIKALKEKIREYEQTLKNQAETiALEKEQKLQNDFAEKERKLQETQM---STTSKLEEAEHKVQSLQTALEK 217
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRK-ALFELDKLQEELEQLREELEQAREeleQLEEELEQARSELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 218 TRTELfdlkTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEvltrsSL 297
Cdd:COG4372 85 LNEQL----QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK-----EL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 298 EVELAAKEREIAQLVEDVQRLqaSLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSMEFAP 377
Cdd:COG4372 156 EEQLESLQEELAALEQELQAL--SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
....*...
gi 2217365688 378 SEGAGTQD 385
Cdd:COG4372 234 ALSALLDA 241
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
125-293 |
6.70e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 6.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 125 ENQKLRETLEEynkefaEVKNQEVTIKALKEKIREYEQTLKNQAETiaLEKeqklqndfaeKERKLQETQMSTTSKLEEA 204
Cdd:PRK12704 65 EIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLEL--LEK----------REEELEKKEKELEQKQQEL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 205 EHKVQSLQTALEKTRTELfdlktkydEETTA-KADEI-EMIMTDLErANQRAEVAQ--REAETLREQLSS--ANHSLQLA 278
Cdd:PRK12704 127 EKKEEELEELIEEQLQEL--------ERISGlTAEEAkEILLEKVE-EEARHEAAVliKEIEEEAKEEADkkAKEILAQA 197
|
170
....*....|....*.
gi 2217365688 279 sqIQK-APDVAIEVLT 293
Cdd:PRK12704 198 --IQRcAADHVAETTV 211
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
21-246 |
6.87e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 21 QRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEaaflnvykrlidvP 100
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE-------------E 1658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 101 DPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKnqAETIALEKEQKLQ 180
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK--AEEENKIKAEEAK 1736
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217365688 181 NDFAEKERKLQETQmsttsKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTD 246
Cdd:PTZ00121 1737 KEAEEDKKKAEEAK-----KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
118-227 |
7.92e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 46.55 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 118 RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAET---IALEKEQKLQNDFA---EKERKLQ 191
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQlkqLEDELEDCDPTELDrakEKLKKLL 217
|
90 100 110
....*....|....*....|....*....|....*.
gi 2217365688 192 ETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKT 227
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNT 253
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
221-371 |
8.05e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.16 E-value: 8.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 221 ELFD-LKTKYDEETTAKADEIEMIMTDLERANQRAEV--AQREAETLREQLSSANHSLQlasQIQKAPDVAIEVLTRSSL 297
Cdd:pfam06160 45 EKFEeWRKKWDDIVTKSLPDIEELLFEAEELNDKYRFkkAKKALDEIEELLDDIEEDIK---QILEELDELLESEEKNRE 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217365688 298 EVElaakereiaQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEkLKGQADYEEVKKELNILK 371
Cdd:pfam06160 122 EVE---------ELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSQFEE-LTESGDYLEAREVLEKLE 185
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
755-941 |
8.45e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 47.63 E-value: 8.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 755 STSPMPTVSSYPPLAISLKKPSAAPEAG--ASALPNPPALKKEAQDAPGLDPQGAADCAQGVLR--QVKNEVGRSGAWkd 830
Cdd:PHA03247 269 PETARGATGPPPPPEAAAPNGAAAPPDGvwGAALAGAPLALPAPPDPPPPAPAGDAEEEDDEDGamEVVSPLPRPRQH-- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 831 hwWSAVQPERRNAASSEEAKAEETGGgkekgsggsgggsqprAERSQLQGPSSSEYWKEWPSAESPYSQSSELSLTGASR 910
Cdd:PHA03247 347 --YPLGFPKRRRPTWTPPSSLEDLSA----------------GRHHPKRASLPTRKRRSARHAATPFARGPGGDDQTRPA 408
|
170 180 190
....*....|....*....|....*....|.
gi 2217365688 911 SETPQNSPLPSSPIVPMSKPTKPSVPPLTPE 941
Cdd:PHA03247 409 APVPASVPTPAPTPVPASAPPPPATPLPSAE 439
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
108-355 |
9.94e-05 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 46.61 E-value: 9.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 108 LGQQLQLkvqrLHDIETENQKLRETLEEYNKEfaevknqevTIKALKEKIREYEQTLKNQAETIAL------EKEQKLQN 181
Cdd:pfam04108 40 LSVQLAN----LEKVREGLEKVLNELKKDFKQ---------LLKDLDAALERLEETLDKLRNTPVEpalppgEEKQKTLL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 182 DFAEkERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKtKYDEETTAKADEIEMIMTDLERANQRAEvaqrEA 261
Cdd:pfam04108 107 DFID-EDSVEILRDALKELIDELQAAQESLDSDLKRFDDDLRDLQ-KELESLSSPSESISLIPTLLKELESLEE----EM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 262 ETLREQLssANH---SLQLASQIQKAPDVAIEVLTRSSLEV-----ELAAKEREIAQLVEDVQRLQASLTKLRENSAS-- 331
Cdd:pfam04108 181 ASLLESL--TNHydqCVTAVKLTEGGRAEMLEVLENDARELddvvpELQDRLDEMENNYERLQKLLEQKNSLIDELLSal 258
|
250 260
....*....|....*....|....*
gi 2217365688 332 -QISQLEQQLSAKNSTLKQLEEKLK 355
Cdd:pfam04108 259 qLIAEIQSRLPEYLAALKEFEERWE 283
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
109-353 |
1.07e-04 |
|
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: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 109 GQQLQLKVQRLH-DIETENQKLRE---TLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKNQaETIALEKEQKLQ 180
Cdd:COG3096 342 ALRQQEKIERYQeDLEELTERLEEqeeVVEEAAEQLAEAEARleaaEEEVDSLKSQLADYQQALDVQ-QTRAIQYQQAVQ 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 181 NdFAEKERKLQETQMSttskLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKA--DE----IEMIMTDLER--ANQ 252
Cdd:COG3096 421 A-LEKARALCGLPDLT----PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRqfEKayelVCKIAGEVERsqAWQ 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 253 RAE-----------VAQReAETLREQLSSANhslQLASQIQKAPDVAIEVLTRSSLEVELAAK-EREIAQLVEDVQRLQA 320
Cdd:COG3096 496 TARellrryrsqqaLAQR-LQQLRAQLAELE---QRLRQQQNAERLLEEFCQRIGQQLDAAEElEELLAELEAQLEELEE 571
|
250 260 270
....*....|....*....|....*....|...
gi 2217365688 321 SLTKLREnsasQISQLEQQLSAKNSTLKQLEEK 353
Cdd:COG3096 572 QAAEAVE----QRSELRQQLEQLRARIKELAAR 600
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
211-355 |
1.14e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 211 LQTALEKTRTELFDLKTKY-------DEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL-QLASQIQ 282
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTgiliaalSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELeQLEEELE 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217365688 283 KAPDVAIEVLT-RSSLEVELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLSAKNSTLKQLEEKLK 355
Cdd:COG4372 84 ELNEQLQAAQAeLAQAQEELESLQEEAEELQEELEELQKERQDLeqqRKQLEAQIAELQSEIAEREEELKELEEQLE 160
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
126-351 |
1.14e-04 |
|
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: 46.67 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 126 NQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQA-ETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEA 204
Cdd:pfam07111 58 SQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAmELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 205 EHK-VQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLE--RANQRAE--VAQREAETLREQLSSANHSLQlaS 279
Cdd:pfam07111 138 SQReLEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkRAGEAKQlaEAQKEAELLRKQLSKTQEELE--A 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 280 QIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQ---------ASLTKLRENSASQISQL-EQQLSAKNSTLKQ 349
Cdd:pfam07111 216 QVTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQedradlqatVELLQVRVQSLTHMLALqEEELTRKIQPSDS 295
|
..
gi 2217365688 350 LE 351
Cdd:pfam07111 296 LE 297
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
16-356 |
1.22e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 16 DLQQLQRELDATATVLANRQDESEQSRKRL------------IEQSREFKKNTPEDLRKQVApLLKSFQGEIDALSKRSK 83
Cdd:PRK04863 308 RLVEMARELAELNEAESDLEQDYQAASDHLnlvqtalrqqekIERYQADLEELEERLEEQNE-VVEEADEQQEENEARAE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 84 EAEAAFLNVYKRLIDVpdpVPALDLGQ----QLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtiKALKEKIRE 159
Cdd:PRK04863 387 AAEEEVDELKSQLADY---QQALDVQQtraiQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKE---QEATEELLS 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 160 YEQTLkNQAETIALEKEQKLQ-----NDFAEKERKlQETQMSTTSKLEEAEHKVQSLQTAlektRTELFDLKTKYDEETT 234
Cdd:PRK04863 461 LEQKL-SVAQAAHSQFEQAYQlvrkiAGEVSRSEA-WDVARELLRRLREQRHLAEQLQQL----RMRLSELEQRLRQQQR 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 235 AKA-------------DEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL-QLASQIQK----APD--VAIEVLTR 294
Cdd:PRK04863 535 AERllaefckrlgknlDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLeQLQARIQRlaarAPAwlAAQDALAR 614
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 295 SSLEVELAAKERE-IAQLVEDVQRLQASLTKLRENSASQISQLEQQLS-------AKNSTLKQLEEKLKG 356
Cdd:PRK04863 615 LREQSGEEFEDSQdVTEYMQQLLERERELTVERDELAARKQALDEEIErlsqpggSEDPRLNALAERFGG 684
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
60-266 |
1.33e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 60 LRKQVAPLLKSFQgEIDALSKRSKEAEAAFLNVYKR--LIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLR------- 130
Cdd:COG4717 293 LAREKASLGKEAE-ELQALPALEELEEEELEELLAAlgLPPDLSPEELLELLDRIEELQELLREAEELEEELQleeleqe 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 131 --ETLEEYN----KEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIaleKEQKLQNDFAEKERKLQETQMsttsKLEEA 204
Cdd:COG4717 372 iaALLAEAGvedeEELRAALEQAEEYQELKEELEELEEQLEELLGEL---EELLEALDEEELEEELEELEE----ELEEL 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217365688 205 EHKVQSLQTALEKTRTELFDLKTkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLRE 266
Cdd:COG4717 445 EEELEELREELAELEAELEQLEE--DGELAELLQELEELKAELRELAEEWAALKLALELLEE 504
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
122-351 |
2.13e-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: 45.94 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 122 IETENQKLRETLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKNQAE-------------TIALEKEQKLQNDFA 184
Cdd:pfam01576 690 LEQQVEEMKTQLEELEDELQATEDAklrlEVNMQALKAQFERDLQARDEQGEekrrqlvkqvrelEAELEDERKQRAQAV 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 185 EKERKLQ------ETQMSTTSK-LEEAEHKVQSLQTALEKTRTELFDLKTKYDE------ETTAKADEIEMIMTDLERAN 251
Cdd:pfam01576 770 AAKKKLEldlkelEAQIDAANKgREEAVKQLKKLQAQMKDLQRELEEARASRDEilaqskESEKKLKNLEAELLQLQEDL 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 252 QRAEVAQREAETLREQLssanhslqlasqiqkAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRE---N 328
Cdd:pfam01576 850 AASERARRQAQQERDEL---------------ADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDrlrK 914
|
250 260
....*....|....*....|...
gi 2217365688 329 SASQISQLEQQLSAKNSTLKQLE 351
Cdd:pfam01576 915 STLQVEQLTTELAAERSTSQKSE 937
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
199-464 |
2.79e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 199 SKLEEAEHKVQSLQTALEKTRTELFDLktkydeettakADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQL- 277
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDAL-----------QAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEEr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 278 ---------ASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLK 348
Cdd:COG3883 85 reelgerarALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 349 QLEEKLKG----QADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSDLSGSARRKGK 424
Cdd:COG3883 165 ELEAAKAEleaqQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2217365688 425 DQPESRRPGSLPAPPPSQLPRNPGEQASNTNGTHQFSPAG 464
Cdd:COG3883 245 SAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGG 284
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
23-371 |
3.00e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.81 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 23 ELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKqvaplLKSFQGEidalSKRSKEAEAA-------FLNVYKR 95
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLND-----LYHNHQR----TVREKERELVdcqreleKLNKERR 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 96 LIDVPDPVPALDLGqQLQLKVQRLH------DIETENQKLRETLEEYNKEF---AEVKN-QEVTIKALKEKIREYEQTLK 165
Cdd:TIGR00606 337 LLNQEKTELLVEQG-RLQLQADRHQehirarDSLIQSLATRLELDGFERGPfseRQIKNfHTLVIERQEDEAKTAAQLCA 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 166 NQAETIALEKEQ--KLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQT-------------ALEKTRTELFDL----- 225
Cdd:TIGR00606 416 DLQSKERLKQEQadEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQlegssdrileldqELRKAERELSKAeknsl 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 226 -KTKYDEETTAKADEIEMIMTdLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLT--------RSS 296
Cdd:TIGR00606 496 tETLKKEVKSLQNEKADLDRK-LRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTsllgyfpnKKQ 574
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217365688 297 LEVELAAKEREIAQLVEDVQRLQASLTKLRENSasqiSQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILK 371
Cdd:TIGR00606 575 LEDWLHSKSKEINQTRDRLAKLNKELASLEQNK----NHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLK 645
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
110-372 |
3.08e-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: 45.40 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 110 QQLQLKVQRL-HDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIReyeqTLKNQaETIALEKEQKLQND--FAEK 186
Cdd:TIGR04523 36 KQLEKKLKTIkNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIK----DLNDK-LKKNKDKINKLNSDlsKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 187 ERKLQETQMSTT----SKLEEAEHKVQSLQ----TALEKTRTELFDLKTKYDEETTakadEIEMIMTDLERANQRAEVAQ 258
Cdd:TIGR04523 111 EIKNDKEQKNKLevelNKLEKQKKENKKNIdkflTEIKKKEKELEKLNNKYNDLKK----QKEELENELNLLEKEKLNIQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 259 REAETLREQLSSANHSL-QLASQIQKAPDVAIEVL----TRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQI 333
Cdd:TIGR04523 187 KNIDKIKNKLLKLELLLsNLKKKIQKNKSLESQISelkkQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIK 266
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2217365688 334 SQLE---QQLSAKNSTLKQLEEKLKgqadyeEVKKELNILKS 372
Cdd:TIGR04523 267 KQLSekqKELEQNNKKIKELEKQLN------QLKSEISDLNN 302
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
32-277 |
3.28e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 45.13 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 32 ANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVpdpvpaldLGQQ 111
Cdd:pfam09731 231 VEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREIDQ--------LSKK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 112 LQ-LKVQRLHDIETENQKLRETL----EEYNKEFAEVKNQE-----VTIKALKEKIRE-YEQTLKNQAETIALEKEQKLQ 180
Cdd:pfam09731 303 LAeLKKREEKHIERALEKQKEELdklaEELSARLEEVRAADeaqlrLEFEREREEIREsYEEKLRTELERQAEAHEEHLK 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 181 NDFAEKERKLQETQMsttskleeaehkvQSLQTALEKTRtelfDLKTKYDEETTAKADEIEMIMT---DLERANQRAEVA 257
Cdd:pfam09731 383 DVLVEQEIELQREFL-------------QDIKEKVEEER----AGRLLKLNELLANLKGLEKATSshsEVEDENRKAQQL 445
|
250 260
....*....|....*....|
gi 2217365688 258 QREAETLREQLSSANHSLQL 277
Cdd:pfam09731 446 WLAVEALRSTLEDGSADSRP 465
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
13-374 |
3.83e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.42 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 13 KRFD-LQQLQRELDATATVLANRQDESE-----QSRKRLIEQSREFKKNTPEDLRKQVAPL------LKSFQGEIDALSK 80
Cdd:TIGR00606 173 QKFDeIFSATRYIKALETLRQVRQTQGQkvqehQMELKYLKQYKEKACEIRDQITSKEAQLessreiVKSYENELDPLKN 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 81 RSKEAEAAFLNVYKrlidVPDPVPALDlgqqlQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtikalKEKIREY 160
Cdd:TIGR00606 253 RLKEIEHNLSKIMK----LDNEIKALK-----SRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNH------QRTVREK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 161 EQTLKN-QAETIALEKEQKLQNdfaeKERKLQETQMSTTSkLEEAEHKVQSLQTALEK----TRTELFDLKTKYDEETTA 235
Cdd:TIGR00606 318 ERELVDcQRELEKLNKERRLLN----QEKTELLVEQGRLQ-LQADRHQEHIRARDSLIqslaTRLELDGFERGPFSERQI 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 236 K----------ADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEvLTRSSLEvELAAKE 305
Cdd:TIGR00606 393 KnfhtlvierqEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELK-FVIKELQ-QLEGSS 470
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217365688 306 REIAQLVEDVQRLQASLTKLRENSASQiSQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSME 374
Cdd:TIGR00606 471 DRILELDQELRKAERELSKAEKNSLTE-TLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQME 538
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
119-374 |
3.87e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 119 LHDIETENQKLRETLEEYNKEFAEVKNQEVtIKALKEKIREYEQTLKNQAETIALEKEQKlqNDFAEKERKLQETqMSTT 198
Cdd:PRK03918 141 LESDESREKVVRQILGLDDYENAYKNLGEV-IKEIKRRIERLEKFIKRTENIEELIKEKE--KELEEVLREINEI-SSEL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 199 SKLEEAEHKVQSLQTALEKTRTELFDLKtKYDEETTAKADEIEMIMTDLERanqRAEVAQREAETLREQlssanhslqlA 278
Cdd:PRK03918 217 PELREELEKLEKEVKELEELKEEIEELE-KELESLEGSKRKLEEKIRELEE---RIEELKKEIEELEEK----------V 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 279 SQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKlrensasQISQLEQQLSAKNSTLKQLEEKLKGQA 358
Cdd:PRK03918 283 KELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE-------RIKELEEKEERLEELKKKLKELEKRLE 355
|
250
....*....|....*.
gi 2217365688 359 DYEEVKKELNILKSME 374
Cdd:PRK03918 356 ELEERHELYEEAKAKK 371
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
21-272 |
4.04e-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: 45.11 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 21 QRELDATATVLANRQD-----ESEQSRKRLIEQSREFKKNTPEDLRKQVAPL--LKSFQGEIDALSKR-SKEAEAAflnv 92
Cdd:pfam17380 326 QAEMDRQAAIYAEQERmamerERELERIRQEERKRELERIRQEEIAMEISRMreLERLQMERQQKNERvRQELEAA---- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 93 ykRLIDVPDPVPALDLGQQLQLKVQ-RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQaeTI 171
Cdd:pfam17380 402 --RKVKILEEERQRKIQQQKVEMEQiRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRK--KL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 172 ALEKEQKLQNDFAEKERKLQETQM-STTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYD-EETTAKADEIE-------- 241
Cdd:pfam17380 478 ELEKEKRDRKRAEEQRRKILEKELeERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREaEEERRKQQEMEerrriqeq 557
|
250 260 270
....*....|....*....|....*....|.
gi 2217365688 242 MIMTDLERAnqRAEVAQREAETLREQLSSAN 272
Cdd:pfam17380 558 MRKATEERS--RLEAMEREREMMRQIVESEK 586
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
67-367 |
4.58e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 67 LLKSFQGEIDALSKRSKEAEA-------------AFLNVYKRLIDVPDPVPAL-DLGQQLQLKVQRLHDIETENQKLRET 132
Cdd:PRK04863 787 RIEQLRAEREELAERYATLSFdvqklqrlhqafsRFIGSHLAVAFEADPEAELrQLNRRRVELERALADHESQEQQQRSQ 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 133 L----------------------EEYNKEFAEVKNQEVTIKALKEKIREYEQTLkNQAETIAlekeQKLQNDfaekerkl 190
Cdd:PRK04863 867 LeqakeglsalnrllprlnlladETLADRVEEIREQLDEAEEAKRFVQQHGNAL-AQLEPIV----SVLQSD-------- 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 191 qetqmstTSKLEEAEHKVQSLQTALEKTRTELFDLKT--------KYDEETTAKADEIEMImtdlERANQRAEVAQREAE 262
Cdd:PRK04863 934 -------PEQFEQLKQDYQQAQQTQRDAKQQAFALTEvvqrrahfSYEDAAEMLAKNSDLN----EKLRQRLEQAEQERT 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 263 TLREQLSSANHSLQLASQIQKAPDVAIEVL--TRSSLEVELA-----AKEREIAQLVEDVQRLQASLTklreNSASQISQ 335
Cdd:PRK04863 1003 RAREQLRQAQAQLAQYNQVLASLKSSYDAKrqMLQELKQELQdlgvpADSGAEERARARRDELHARLS----ANRSRRNQ 1078
|
330 340 350
....*....|....*....|....*....|...
gi 2217365688 336 LEQQLSAKNSTLKQLEEKL-KGQADYEEVKKEL 367
Cdd:PRK04863 1079 LEKQLTFCEAEMDNLTKKLrKLERDYHEMREQV 1111
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
49-367 |
6.79e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 49 SREFKKNtpEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDpvpALDLGQQLQLKVQRLHDIETENQK 128
Cdd:TIGR00618 183 LMEFAKK--KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLRE---ALQQTQQSHAYLTQKREAQEEQLK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 129 LRETLEEYNKEFAEVKNQEVTIKALKEKI---REYEQTLKNQAETIALEKE-----QKLQNDFAEKERKLQETQ--MSTT 198
Cdd:TIGR00618 258 KQQLLKQLRARIEELRAQEAVLEETQERInraRKAAPLAAHIKAVTQIEQQaqrihTELQSKMRSRAKLLMKRAahVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 199 SKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADE--IEMIMTDLERANQRAEVAQREAETLREQLSSAN--HS 274
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTqhIHTLQQQKTTLTQKLQSLCKELDILQREQATIDtrTS 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 275 LQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLREnsasqisqLEQQLSAKNSTLKQLEEKL 354
Cdd:TIGR00618 418 AFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKE--------REQQLQTKEQIHLQETRKK 489
|
330
....*....|...
gi 2217365688 355 KGQADYEEVKKEL 367
Cdd:TIGR00618 490 AVVLARLLELQEE 502
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
125-388 |
7.38e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 125 ENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIRE----YEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSK 200
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEvmklYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 201 LEEAEHKVQSLQtalektrtelfdlktKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQ 280
Cdd:PTZ00121 1642 EAEEKKKAEELK---------------KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 281 IQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTL-KQLEEKLKGQAD 359
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIrKEKEAVIEEELD 1786
|
250 260
....*....|....*....|....*....
gi 2217365688 360 YEEVKKELNILKSMEFAPSEGAGTQDAAK 388
Cdd:PTZ00121 1787 EEDEKRRMEVDKKIKDIFDNFANIIEGGK 1815
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
22-392 |
9.12e-04 |
|
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: 43.96 E-value: 9.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 22 RELDATATVLANRQDESEQSRKRLIEQSREFKK---------NTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAF--- 89
Cdd:pfam05557 51 QELQKRIRLLEKREAEAEEALREQAELNRLKKKylealnkklNEKESQLADAREVISCLKNELSELRRQIQRAELELqst 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 90 ---LNVYKRLIDVPDP--VPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKN--QEV----TIKALKEKIR 158
Cdd:pfam05557 131 nseLEELQERLDLLKAkaSEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNskSELaripELEKELERLR 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 159 EYEQTLKNQAETIALEKEQKlqndfAEKERKLqetqmsttSKLEEAEHKVQSLQTALEKTRTELfdlktkYDEETTAKAD 238
Cdd:pfam05557 211 EHNKHLNENIENKLLLKEEV-----EDLKRKL--------EREEKYREEAATLELEKEKLEQEL------QSWVKLAQDT 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 239 EIEMIMTDLERAnqRAEVAQREAETLREQLSSANHSlqlASQIQKA-PDVAIEVLTRSSLEVELAAKEREIAQLVEDVQR 317
Cdd:pfam05557 272 GLNLRSPEDLSR--RIEQLQQREIVLKEENSSLTSS---ARQLEKArRELEQELAQYLKKIEDLNKKLKRHKALVRRLQR 346
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217365688 318 LQASLTKLRENSASQISQLEQQLSAKNSTlKQLEEKLKGQADY-EEVKKELNILK-SMEFAPSEGAGTQDAAKPLEV 392
Cdd:pfam05557 347 RVLLLTKERDGYRAILESYDKELTMSNYS-PQLLERIEEAEDMtQKMQAHNEEMEaQLSVAEEELGGYKQQAQTLER 422
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
43-267 |
9.58e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 9.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 43 KRLIEQSREFKKNTPEDLRKqvapllksfqgeidalSKRSKEAEAAFLNVYKRLIDVPDPVPALDL--GQQLQLKVQRLH 120
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRK----------------AEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkAEEAKIKAEELK 1626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 121 DIETENQK---LRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMST 197
Cdd:PTZ00121 1627 KAEEEKKKveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217365688 198 TSKLEEAE-HKVQSLQTALEKTRTELFDLKTKyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQ 267
Cdd:PTZ00121 1707 LKKKEAEEkKKAEELKKAEEENKIKAEEAKKE-AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
63-228 |
9.69e-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: 42.60 E-value: 9.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 63 QVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLidvpdpvpaldlgQQLQLKVQRLhdiETENQKLRETLEEYNKEFAE 142
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTEL-------------EDLEKEIKRL---ELEIEEVEARIKKYEEQLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 143 VKNQ-EVT-----IKALKEKIREYEQTLKNqaetiALEKEQKLQNDFAEKERKLQETQmsttsklEEAEHKVQSLQTALE 216
Cdd:COG1579 85 VRNNkEYEalqkeIESLKRRISDLEDEILE-----LMERIEELEEELAELEAELAELE-------AELEEKKAELDEELA 152
|
170
....*....|..
gi 2217365688 217 KTRTELFDLKTK 228
Cdd:COG1579 153 ELEAELEELEAE 164
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
33-426 |
1.04e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 33 NRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEA----------EAAFLNVYKRLIDVPDP 102
Cdd:PTZ00121 1087 NRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDArkaeearkaeDAKRVEIARKAEDARKA 1166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 103 VPALDLGQQLQLKVQRLHDIETENQKLRETLE----EYNKEFAEVKNQEVTIKALKEK----IREYEQTLKNQAETIALE 174
Cdd:PTZ00121 1167 EEARKAEDAKKAEAARKAEEVRKAEELRKAEDarkaEAARKAEEERKAEEARKAEDAKkaeaVKKAEEAKKDAEEAKKAE 1246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 175 KEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTElfDLK----TKYDEETTAKADEIEmimtDLERA 250
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD--EAKkaeeKKKADEAKKKAEEAK----KADEA 1320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 251 NQRAEVAQREAETLREQlssanhslqlASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSA 330
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKK----------AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 331 SQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSMEfapsEGAGTQDAAKPLEVLLLEKNRSLQSENAALRI 410
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAD----EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKA 1466
|
410
....*....|....*.
gi 2217365688 411 SNSDLSGSARRKGKDQ 426
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEA 1482
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
28-355 |
1.09e-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: 43.35 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 28 ATVLANRQDESEQSRKRLIeQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVpdpvpald 107
Cdd:pfam07888 29 AELLQNRLEECLQERAELL-QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEEL-------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 108 lgQQLQLKVQRLHDIETENQklRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIalEKEQKLQNDFAEKE 187
Cdd:pfam07888 100 --EEKYKELSASSEELSEEK--DALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERA--KKAGAQRKEEEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 188 RKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLK----TKYDEETTA--KADEIEMIMTDLERANQRAEVAQREA 261
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQdtitTLTQKLTTAhrKEAENEALLEELRSLQERLNASERKV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 262 ETLREQLSSanhslqLASQiqkapdvaievltRSSLEVELAAKEREIAQLveDVQRLQASLtKLRENSAS---------Q 332
Cdd:pfam07888 254 EGLGEELSS------MAAQ-------------RDRTQAELHQARLQAAQL--TLQLADASL-ALREGRARwaqeretlqQ 311
|
330 340
....*....|....*....|....
gi 2217365688 333 ISQLEQQLSAK-NSTLKQLEEKLK 355
Cdd:pfam07888 312 SAEADKDRIEKlSAELQRLEERLQ 335
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
117-328 |
1.18e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 42.32 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 117 QRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKnQAETIALEKEQKL-----QNDFAEKERKLQ 191
Cdd:pfam00261 8 EELDEAEERLKEAMKKLEEAEKRAEKAEAE---VAALNRRIQLLEEELE-RTEERLAEALEKLeeaekAADESERGRKVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 192 ETqmsTTSKLEEaehKVQSLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERANQRAEVAQREAETLREQLSSA 271
Cdd:pfam00261 84 EN---RALKDEE---KMEILEAQLKEAKEIAEEADRKYEE----VARKLVVVEGDLERAEERAELAESKIVELEEELKVV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217365688 272 NHSLQ-LASQIQKAPD------VAIEVLTRSSLEVELAAK--EREIAQLVEDVQRLQASLTKLREN 328
Cdd:pfam00261 154 GNNLKsLEASEEKASEredkyeEQIRFLTEKLKEAETRAEfaERSVQKLEKEVDRLEDELEAEKEK 219
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
722-936 |
1.37e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.77 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 722 RREMEAQQAALDPA---------LKQAPLSQSDITILTPKLlSTSPMPTvssyPPLAISLKKPSAAPEAGASALPNPPAL 792
Cdd:PHA03247 2863 RRRPPSRSPAAKPAaparppvrrLARPAVSRSTESFALPPD-QPERPPQ----PQAPPPPQPQPQPPPPPQPQPPPPPPP 2937
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 793 KKEAQDAPGLDPQGAAdcaqgvlrqvknevGRSGAWKDHWWSAVQPERRNA--------ASSEEAKAEETGGGKEKGSGG 864
Cdd:PHA03247 2938 RPQPPLAPTTDPAGAG--------------EPSGAVPQPWLGALVPGRVAVprfrvpqpAPSREAPASSTPPLTGHSLSR 3003
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217365688 865 SGGGSQPRAERSQLQGPSSSEYWKEWPSAESPYSQSSELSLTGASRSETPQNSPLPSSPIVPMSKPTKPSVP 936
Cdd:PHA03247 3004 VSSWASSLALHEETDPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLEALDPLPPEPHDPFAHEPDPATP 3075
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
141-357 |
1.54e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 41.90 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 141 AEVKNQEVTIKALKEKIREYEQTLKNQAETialekeqklqNDFAEKERKLQEtqmsttsKLEEAEHKVQSLQTALEKTRT 220
Cdd:pfam12795 3 DELEKAKLDEAAKKKLLQDLQQALSLLDKI----------DASKQRAAAYQK-------ALDDAPAELRELRQELAALQA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 221 ELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA---------ETLREQLSSANHSLQLASQIQKAPDVAIEV 291
Cdd:pfam12795 66 KAEAAPKEILASLSLEELEQRLLQTSAQLQELQNQLAQLNSqlielqtrpERAQQQLSEARQRLQQIRNRLNGPAPPGEP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217365688 292 LT---RSSLEVELAAKEREIAQLvedvQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQ 357
Cdd:pfam12795 146 LSeaqRWALQAELAALKAQIDML----EQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQALQELLNEK 210
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
117-222 |
1.56e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 41.43 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 117 QRLHDIETENQKLRETLEE--------------YNKEFAEVKNQEVTIKALKEKIREyeqtLKNQAEtIALEKEQKLQND 182
Cdd:pfam13851 47 KLMSEIQQENKRLTEPLQKaqeeveelrkqlenYEKDKQSLKNLKARLKVLEKELKD----LKWEHE-VLEQRFEKVERE 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2217365688 183 FAEKERK----LQETQMSTTSKLEEAEHKVQSLQTALEKTRTEL 222
Cdd:pfam13851 122 RDELYDKfeaaIQDVQQKTGLKNLLLEKKLQALGETLEKKEAQL 165
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
697-965 |
1.60e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 43.15 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 697 EPAQPSSASGSGNSDDairsILQQARREMEAQQAALDPALKQAPLSQ---SDITILTPKLLSTSPMPTVSSYPPLAiSLK 773
Cdd:PRK10263 276 EEITYTARGVAADPDD----VLFSGNRATQPEYDEYDPLLNGAPITEpvaVAAAATTATQSWAAPVEPVTQTPPVA-SVD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 774 KPSAAPEAGASALPNPPAlkKEAQDAPglDPQGAADCAQGVLRQVknevgrsgAWKDHWWSAVQPERRNAASSEEAKAEE 853
Cdd:PRK10263 351 VPPAQPTVAWQPVPGPQT--GEPVIAP--APEGYPQQSQYAQPAV--------QYNEPLQQPVQPQQPYYAPAAEQPAQQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 854 TGGGKEKGSGGSGGGSQPRAER----SQLQGPSSSEYWKEWPSAEsPYSQSSELSLTGASRSETPQNSPLPSSPIVPMSK 929
Cdd:PRK10263 419 PYYAPAPEQPAQQPYYAPAPEQpvagNAWQAEEQQSTFAPQSTYQ-TEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVE 497
|
250 260 270
....*....|....*....|....*....|....*.
gi 2217365688 930 PTKPSVPPLtpeqyevYMYQEVDtiELTRQVKEKLA 965
Cdd:PRK10263 498 ETKPARPPL-------YYFEEVE--EKRAREREQLA 524
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
122-374 |
1.64e-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: 43.19 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 122 IETENQKLRETLEEYNKEFAEVKNQEVTIKAlkEKIRE-----YEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMS 196
Cdd:pfam17380 344 MERERELERIRQEERKRELERIRQEEIAMEI--SRMRElerlqMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVE 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 197 TTSKLEEAEHKVQSLQTALEKTRtelfdlktkydeettakADEIEMI-MTDLERANQRAEVAQREAETLREQLSSANhsl 275
Cdd:pfam17380 422 MEQIRAEQEEARQREVRRLEEER-----------------AREMERVrLEEQERQQQVERLRQQEEERKRKKLELEK--- 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 276 qlasqiQKAPDVAIEVLTRSSLEVELAAKEREIAQlvedVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQ--LEEK 353
Cdd:pfam17380 482 ------EKRDRKRAEEQRRKILEKELEERKQAMIE----EERKRKLLEKEMEERQKAIYEEERRREAEEERRKQqeMEER 551
|
250 260
....*....|....*....|.
gi 2217365688 354 LKGQADYEEVKKELNILKSME 374
Cdd:pfam17380 552 RRIQEQMRKATEERSRLEAME 572
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
125-273 |
1.76e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 41.41 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 125 ENQKLRETLEEynkefaEVKNQEVTIKALKEKIREYEQTLKNQAETIAlEKEQKLQndfaEKERKLQETQMSTTSKLEEA 204
Cdd:pfam12072 61 EIHKLRAEAER------ELKERRNELQRQERRLLQKEETLDRKDESLE-KKEESLE----KKEKELEAQQQQLEEKEEEL 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217365688 205 EHKVQSLQTALEK----TRTE----LFD-LKTKYDEETTAKADEIEmimtdlERANQRAEVAQREAETLREQLSSANH 273
Cdd:pfam12072 130 EELIEEQRQELERisglTSEEakeiLLDeVEEELRHEAAVMIKEIE------EEAKEEADKKAKEIIALAIQRCAADH 201
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
107-374 |
1.78e-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: 43.18 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 107 DLGQQLQ---------------------LKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLK 165
Cdd:pfam15921 500 DLTASLQekeraieatnaeitklrsrvdLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVG 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 166 NQAET---IALEKEQkLQNDFAEKERKLQETQM---STTSKLEEAEHKVQSLQtaLEKTR-----TELFDLKTKYDEETT 234
Cdd:pfam15921 580 QHGRTagaMQVEKAQ-LEKEINDRRLELQEFKIlkdKKDAKIRELEARVSDLE--LEKVKlvnagSERLRAVKDIKQERD 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 235 AKADEIEMIMTDLERANQRAEVAQR-------EAET----LREQLSSANHSLQLASQIQKAPDVAI--EVLTRSSLEVEL 301
Cdd:pfam15921 657 QLLNEVKTSRNELNSLSEDYEVLKRnfrnkseEMETttnkLKMQLKSAQSELEQTRNTLKSMEGSDghAMKVAMGMQKQI 736
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217365688 302 AAKEREIAQLVEDVQRLQASLTKLRENSASqISQLEQQLSAKNSTLKQLEEKLKGqadyeevkkELNILKSME 374
Cdd:pfam15921 737 TAKRGQIDALQSKIQFLEEAMTNANKEKHF-LKEEKNKLSQELSTVATEKNKMAG---------ELEVLRSQE 799
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
133-351 |
2.06e-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: 42.05 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 133 LEEYNKEFAEVKNQEVTIKALKEKIReyeQTLKNQA--ETIALEKEQKLQNDFAEKERKLQETQMsttskleeaehkvQS 210
Cdd:pfam09787 2 LESAKQELADYKQKAARILQSKEKLI---ASLKEGSgvEGLDSSTALTLELEELRQERDLLREEI-------------QK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 211 LQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLasqiqkapdvaie 290
Cdd:pfam09787 66 LRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRR------------- 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217365688 291 vlTRSSLEVELAAKEREIaqlvedvQRLQASLTkLRENSASQISQLEQQL------------------SAKNSTLKQLE 351
Cdd:pfam09787 133 --SKATLQSRIKDREAEI-------EKLRNQLT-SKSQSSSSQSELENRLhqltetliqkqtmlealsTEKNSLVLQLE 201
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1322-1395 |
2.07e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.85 E-value: 2.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217365688 1322 GQAGASDSPSARSGRAAPSSEGD-----SCDGVEATEGPGSADTEEPKSQGEAEREEVPRPAEQTEPPPSGTPGPDDAR 1395
Cdd:PHA03307 283 GPASSSSSPRERSPSPSPSSPGSgpapsSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPAD 361
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
17-232 |
2.10e-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: 42.75 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 17 LQQLQRELDATATVLA---------NRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPL---LKSFQGEIDALSKRSKE 84
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSriearlreiEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIekeIENLNGKKEELEEELEE 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 85 AEAAFLNVYKRLIDVPDPVpaLDLGQQLQLKVQRLHDIETENQKLRETLEEynkefaevknQEVTIKALKEKIREYEQTL 164
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKER--DELEAQLRELERKIEELEAQIEKKRKRLSE----------LKAKLEALEEELSEIEDPK 940
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217365688 165 KN----QAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQ---TALEKTRTELFDLKTKYDEE 232
Cdd:TIGR02169 941 GEdeeiPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKekrAKLEEERKAILERIEEYEKK 1015
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
16-356 |
2.13e-03 |
|
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: 43.02 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 16 DLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKkntpeDLRKQVApllkSFQGEIDALSKRSKEAEAAF--LNVY 93
Cdd:COG3096 355 DLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVD-----SLKSQLA----DYQQALDVQQTRAIQYQQAVqaLEKA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 94 KRLIDVPD--PVPALDLGQQLQLKVQRLHDIETEN-QKLR---ETLEEYNKEFA-------EVKNQEVTIKAlKEKIREY 160
Cdd:COG3096 426 RALCGLPDltPENAEDYLAAFRAKEQQATEEVLELeQKLSvadAARRQFEKAYElvckiagEVERSQAWQTA-RELLRRY 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 161 EQtLKNQAEtialeKEQKLQNDFAEKERKLQEtqmsttskleeaEHKVQSLQTALEKTrtelfdLKTKYDEettakADEI 240
Cdd:COG3096 505 RS-QQALAQ-----RLQQLRAQLAELEQRLRQ------------QQNAERLLEEFCQR------IGQQLDA-----AEEL 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 241 EMImtdLERANQRAEVAQREAETLREQLSSANHSL-QLASQI----QKAPD--VAIEVLTR----------SSLEV---- 299
Cdd:COG3096 556 EEL---LAELEAQLEELEEQAAEAVEQRSELRQQLeQLRARIkelaARAPAwlAAQDALERlreqsgealaDSQEVtaam 632
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217365688 300 -ELAAKEREIAQLVEDVQRLQASLtklrensASQISQLEQQLSAKNSTLKQLEEKLKG 356
Cdd:COG3096 633 qQLLEREREATVERDELAARKQAL-------ESQIERLSQPGGAEDPRLLALAERLGG 683
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
12-209 |
2.39e-03 |
|
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: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 12 WKRFDLQQLQRELDATATVLAN-------------RQDESEQSRKRLIEQSREFKKN--TPEDLRKQVAPLLKSFQGEID 76
Cdd:COG4913 658 WDEIDVASAEREIAELEAELERldassddlaaleeQLEELEAELEELEEELDELKGEigRLEKELEQAEEELDELQDRLE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 77 ALSKRSKEAEAAFLNvyKRLIDVPDPVPALDLGQQLQLKVQRLH-DIETENQKLRETLEEYNKEF-AEVKNQEVTIKALk 154
Cdd:COG4913 738 AAEDLARLELRALLE--ERFAAALGDAVERELRENLEERIDALRaRLNRAEEELERAMRAFNREWpAETADLDADLESL- 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217365688 155 ekiREYEQTLKNQAETIALEKEQKLqndfaeKERKLQETQMSTT---SKLEEAEHKVQ 209
Cdd:COG4913 815 ---PEYLALLDRLEEDGLPEYEERF------KELLNENSIEFVAdllSKLRRAIREIK 863
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
235-359 |
2.54e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 42.14 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 235 AKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQkapdvaievlTRSSLEVELAAKEREIAQLved 314
Cdd:COG3524 174 AREDAVRFAEEEVERAEERLRDAREALLAFRNRNGILDPEATAEALLQ----------LIATLEGQLAELEAELAAL--- 240
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2217365688 315 vqrlqasLTKLRENSAsQISQLEQQLSAKNSTLKQLEEKLKGQAD 359
Cdd:COG3524 241 -------RSYLSPNSP-QVRQLRRRIAALEKQIAAERARLTGASG 277
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
110-367 |
2.57e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 110 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIAlEKEQKLQNDFAEKERK 189
Cdd:COG4372 73 SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLE-AQIAELQSEIAEREEE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 190 LQETQmsttSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLS 269
Cdd:COG4372 152 LKELE----EQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 270 SANHSLQLASQIQKAPDVAIEVLTRsSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQ 349
Cdd:COG4372 228 EAKLGLALSALLDALELEEDKEELL-EEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAA 306
|
250
....*....|....*...
gi 2217365688 350 LEEKLKGQADYEEVKKEL 367
Cdd:COG4372 307 LSLIGALEDALLAALLEL 324
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
119-407 |
2.71e-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: 42.40 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 119 LHDIETENQK-LRETLEEYNKEFAEVKNQEVTIKAlkeKIREYEQTLKNQAETIALEKE--QKLQNDFAEKERKLQEtQM 195
Cdd:pfam05483 65 LKDSDFENSEgLSRLYSKLYKEAEKIKKWKVSIEA---ELKQKENKLQENRKIIEAQRKaiQELQFENEKVSLKLEE-EI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 196 STTSKLEEAEHKVQSLQTALEKT--RTELFDLKTKYDEETTAKA-----DEIEMIMTDLERANQRAEVAQREAE-TLREQ 267
Cdd:pfam05483 141 QENKDLIKENNATRHLCNLLKETcaRSAEKTKKYEYEREETRQVymdlnNNIEKMILAFEELRVQAENARLEMHfKLKED 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 268 LSSANHslqLASQIQKapdvaievltrsslevELAAKEREIA----QLVEDVQRLQaSLTKLRENSASQISQLEQQLSAK 343
Cdd:pfam05483 221 HEKIQH---LEEEYKK----------------EINDKEKQVSllliQITEKENKMK-DLTFLLEESRDKANQLEEKTKLQ 280
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217365688 344 NSTLKQLEEKLKG-QADYEEVKKELNilKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAA 407
Cdd:pfam05483 281 DENLKELIEKKDHlTKELEDIKMSLQ--RSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKA 343
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
54-371 |
2.72e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 54 KNTPEDLRKQVAPL------LKSFQGEIDALSK--------------RSKEAEAAFLNVYKRLIDVPDPVPAL----DLG 109
Cdd:PRK01156 172 KDVIDMLRAEISNIdyleekLKSSNLELENIKKqiaddekshsitlkEIERLSIEYNNAMDDYNNLKSALNELssleDMK 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 110 QQLQLKVQ----RLHDIETENQKLRETLEEYNK--EFAEVKNQEVTIKALKEK--IREYEQTLKNQAETIA--------L 173
Cdd:PRK01156 252 NRYESEIKtaesDLSMELEKNNYYKELEERHMKiiNDPVYKNRNYINDYFKYKndIENKKQILSNIDAEINkyhaiikkL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 174 EKEQKLQNDFAEKERKLQETQmSTTSKLEEAEHKVQSLQTALE----------KTRTELFDLKTKYDEETTAKADEI--- 240
Cdd:PRK01156 332 SVLQKDYNDYIKKKSRYDDLN-NQILELEGYEMDYNSYLKSIEslkkkieeysKNIERMSAFISEILKIQEIDPDAIkke 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 241 -EMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAP----DVAIEVLTR---------SSLEVELAAKER 306
Cdd:PRK01156 411 lNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPvcgtTLGEEKSNHiinhynekkSRLEEKIREIEI 490
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217365688 307 EIAQLVEDVQRLQASLTKLR-------ENSASQISQLEQQLSAKNSTLKQLEEKlkgQADYEEVKKELNILK 371
Cdd:PRK01156 491 EVKDIDEKIVDLKKRKEYLEseeinksINEYNKIESARADLEDIKIKINELKDK---HDKYEEIKNRYKSLK 559
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
17-354 |
3.01e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.13 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 17 LQQLQRELDATATVLANRQDESEQSRKRlIEQSREfkknTPEDLRKQVapLLKSFQ-GE-IDALSKRSKEAEAAFlNVYK 94
Cdd:PRK04778 114 LDLIEEDIEQILEELQELLESEEKNREE-VEQLKD----LYRELRKSL--LANRFSfGPaLDELEKQLENLEEEF-SQFV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 95 RLIDVPDPV-----------------------PAL------DLGQQL--------QLKVQ-----------RLHDIETEN 126
Cdd:PRK04778 186 ELTESGDYVeareildqleeelaaleqimeeiPELlkelqtELPDQLqelkagyrELVEEgyhldhldiekEIQDLKEQI 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 127 QKLRETLEEYNKEFAEVKNQEvtikaLKEKIRE-YEQtlknqaetiaLEKEQKLQNdfaekerklqetqmsttskleEAE 205
Cdd:PRK04778 266 DENLALLEELDLDEAEEKNEE-----IQERIDQlYDI----------LEREVKARK---------------------YVE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 206 HKVQSLQTALEKTRTELFDLKTKydeettakadeiemimtdLERANQRAEVAQREAETLR---EQLSSANHSLQLASQIQ 282
Cdd:PRK04778 310 KNSDTLPDFLEHAKEQNKELKEE------------------IDRVKQSYTLNESELESVRqleKQLESLEKQYDEITERI 371
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217365688 283 KAPDVAIevltrSSLEVELAAKEREIAQLVEDVQRLQASLTKLR--ENSASQ-ISQLEQQLsaknSTLKQLEEKL 354
Cdd:PRK04778 372 AEQEIAY-----SELQEELEEILKQLEEIEKEQEKLSEMLQGLRkdELEAREkLERYRNKL----HEIKRYLEKS 437
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1313-1402 |
3.04e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 42.20 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 1313 IEEIQAGSQGQAGASDSPSARSGRAAPSSEGDSCDGVEATEGPGSADTEEP-----KSQGEAEREEVPRPAEQTEPPPSG 1387
Cdd:PRK12678 55 IKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAApaaraAAAAAAEAASAPEAAQARERRERG 134
|
90
....*....|....*
gi 2217365688 1388 TPGPDDARDDDHEGG 1402
Cdd:PRK12678 135 EAARRGAARKAGEGG 149
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
174-428 |
3.55e-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: 42.04 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 174 EKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRtELFDLKTKYDEETTAKADEIEMIMTDLERANQR 253
Cdd:pfam05557 48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLN-EKESQLADAREVISCLKNELSELRRQIQRAELE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 254 AEVAQREAETLREQL----SSANHSLQLASQIQKAPDVAIEVLTR-SSLEVELAAKERE-------------IAQLVEDV 315
Cdd:pfam05557 127 LQSTNSELEELQERLdllkAKASEAEQLRQNLEKQQSSLAEAEQRiKELEFEIQSQEQDseivknskselarIPELEKEL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 316 QRLQASLTKLRENSASqISQLEQQLSAKNSTLKQlEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPleVLLL 395
Cdd:pfam05557 207 ERLREHNKHLNENIEN-KLLLKEEVEDLKRKLER-EEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSP--EDLS 282
|
250 260 270
....*....|....*....|....*....|...
gi 2217365688 396 EKNRSLQSENAALRISNSDLSGSARRKGKDQPE 428
Cdd:pfam05557 283 RRIEQLQQREIVLKEENSSLTSSARQLEKARRE 315
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
112-222 |
3.62e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 41.23 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 112 LQLKVQRLHDietENQKLRETLEEYNKEFAEVKNQEVTI-KALKEKIREYEQT---LKNQAETIALE-KEQKLQNDFAEK 186
Cdd:pfam15294 131 LHMEIERLKE---ENEKLKERLKTLESQATQALDEKSKLeKALKDLQKEQGAKkdvKSNLKEISDLEeKMAALKSDLEKT 207
|
90 100 110
....*....|....*....|....*....|....*.
gi 2217365688 187 ERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTEL 222
Cdd:pfam15294 208 LNASTALQKSLEEDLASTKHELLKVQEQLEMAEKEL 243
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
112-293 |
3.63e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 40.88 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 112 LQLKVQR---LHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQ---TLKNQAETIALEKEQ---KLQND 182
Cdd:pfam17078 20 LQLTVQSqnlLSKLEIAQQKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDqlsELKNSYEELTESNKQlkkRLENS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 183 FAEKERKLQETQMSTT-------SKLEEAEH---KVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQ 252
Cdd:pfam17078 100 SASETTLEAELERLQIqydalvdSQNEYKDHyqqEINTLQESLEDLKLENEKQLENYQQRISSNDKDIDTKLDSYNNKFK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2217365688 253 RAEVAQREAET-LREQLSSANHSLQLASQIQKAPDVAIEVLT 293
Cdd:pfam17078 180 NLDNIYVNKNNkLLTKLDSLAQLLDLPSWLNLYPESRNKILE 221
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
142-310 |
3.78e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 142 EVKNQEVTIKALKEKIREYEQTLknqaetiALEKEQKLQndfaekerkLQETQMSTTSKLEEAEHKVQSLQTALEKTRTE 221
Cdd:PRK09039 47 EISGKDSALDRLNSQIAELADLL-------SLERQGNQD---------LQDSVANLRASLSAAEAERSRLQALLAELAGA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 222 LFDLKTKyDEETTAKADEIEMIMtdlERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRsSLEVEL 301
Cdd:PRK09039 111 GAAAEGR-AGELAQELDSEKQVS---ARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGR-RLNVAL 185
|
....*....
gi 2217365688 302 AAKEREIAQ 310
Cdd:PRK09039 186 AQRVQELNR 194
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
29-342 |
3.84e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.96 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 29 TVLANRQDESEQSRKRLiEQSREFKknTPEDlrkqvAPLLKSFQGEIDALSKRSKEAEAAflNVYKRLIDvpdpvpaldl 108
Cdd:PRK10929 16 GAYAATAPDEKQITQEL-EQAKAAK--TPAQ-----AEIVEALQSALNWLEERKGSLERA--KQYQQVID---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 109 gqqlqlkvqrlhDIETENQKLRETLEEYNKEFAEVkNQEVTIKALKEKIREYEQTLKNQAETiaLEKEQKLQNDFAEKER 188
Cdd:PRK10929 76 ------------NFPKLSAELRQQLNNERDEPRSV-PPNMSTDALEQEILQVSSQLLEKSRQ--AQQEQDRAREISDSLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 189 KLQETQMSTTSKLEEAEHKVQSL--------QTALEKTRTELFDLKtkydeettAKADEIEMIMTDL----ERANQRAEV 256
Cdd:PRK10929 141 QLPQQQTEARRQLNEIERRLQTLgtpntplaQAQLTALQAESAALK--------ALVDELELAQLSAnnrqELARLRSEL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 257 AQREAETLREQLSSANHslQLASQIQKAPDVAIEvltrsslEVELAAKE---------------REIAQ-LVEDVQRLQA 320
Cdd:PRK10929 213 AKKRSQQLDAYLQALRN--QLNSQRQREAERALE-------STELLAEQsgdlpksivaqfkinRELSQaLNQQAQRMDL 283
|
330 340
....*....|....*....|..
gi 2217365688 321 SLTKLREnSASQISQLEQQLSA 342
Cdd:PRK10929 284 IASQQRQ-AASQTLQVRQALNT 304
|
|
| COG0610 |
COG0610 |
Type I site-specific restriction-modification system, R (restriction) subunit and related ... |
5-244 |
3.92e-03 |
|
Type I site-specific restriction-modification system, R (restriction) subunit and related helicases ... [Defense mechanisms];
Pssm-ID: 440375 [Multi-domain] Cd Length: 936 Bit Score: 41.78 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 5 VGSMFQYWKRFDLQQLQRELDATATVlANRQDESEQSRKRLIEQSREFKKntpedLRKQVAPLLKSFQGEIDALSKRSke 84
Cdd:COG0610 690 LRALFPEGVDFSAFDPTEKLEALDEA-VERFLGDEEARKEFKKLFKELSR-----LYNLLSPDDEFGDLELEKYRDDV-- 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 85 aeAAFLNVYKRLIDVPDPVPAldlgQQLQLKVQRLHD--IETENQKLRETLEE---YNKEFAE--------VKNQEVTIK 151
Cdd:COG0610 762 --SFYLALRAKLRKLGEKLDL----KEYEEKIRQLLDeaIDLERKEIKPRIKQnpvQYRKFSElleeiieeYNNGALDAD 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 152 ALKEKIREYEQTLKNQAETIA---LEKEQK-----LQNDFAEKERKLQETQMSTTSKlEEAEHKVQSLQTALEKTRTELF 223
Cdd:COG0610 836 EVLEELEELAKEVKEEEERAEeegLNEEELafydaLAENLGDEKLKELAKELDDLLK-KNVTVDWRKRESVRAKLRDAIK 914
|
250 260
....*....|....*....|.
gi 2217365688 224 DLKTKYDEETTAKAdeIEMIM 244
Cdd:COG0610 915 RLLRKYGYPKQDEA--VEEVY 933
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
297-368 |
4.59e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 297 LEVELAAKEREIAQLVEDVQRLQASLTKLRENS-------------------ASQISQLEQQ---LSAKNSTLKQLEEKL 354
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidvasaEREIAELEAElerLDASSDDLAALEEQL 694
|
90
....*....|....*
gi 2217365688 355 KG-QADYEEVKKELN 368
Cdd:COG4913 695 EElEAELEELEEELD 709
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
13-224 |
4.66e-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: 41.58 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 13 KRFDLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNT--PEDLRKQvaplLKSFQGEIDALSKRSKEAEAAFL 90
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEelIEELESE----LEALLNERASLEEALALLRSELE 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 91 NVYKRLIDVPDPVPALDlgQQLQLKVQRLHDIETENQKLRETL--------EEYNKEFAEVKNQEVTIKALKEKIREYEQ 162
Cdd:TIGR02168 898 ELSEELRELESKRSELR--RELEELREKLAQLELRLEGLEVRIdnlqerlsEEYSLTLEEAEALENKIEDDEEEARRRLK 975
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 163 TLKNQAETI------ALE--KEQKLQNDFAEKERKlqetqmsttsKLEEAEHKVQSLQTALEKTRTELFD 224
Cdd:TIGR02168 976 RLENKIKELgpvnlaAIEeyEELKERYDFLTAQKE----------DLTEAKETLEEAIEEIDREARERFK 1035
|
|
| iSH2_PIK3R2 |
cd12926 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
108-248 |
4.91e-03 |
|
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 2, PIK3R2, also called p85beta; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. p85beta, also called PIK3R2, contains N-terminal SH3 and GAP domains. It is expressed ubiquitously but at lower levels than p85alpha. Its expression is increased in breast and colon cancer, correlates with tumor progression, and enhanced invasion. During viral infection, the viral nonstructural (NS1) protein binds p85beta specifically, which leads to PI3K activation and the promotion of viral replication. Mice deficient with PIK3R2 develop normally and exhibit moderate metabolic and immunological defects.
Pssm-ID: 214019 [Multi-domain] Cd Length: 161 Bit Score: 39.29 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 108 LGQQLQLKVQRLHDIETENQKLretLEEYNKEFAEVKNQEVTIKALKEKIREYEQtlknQAETialekEQKLQNDFAEKE 187
Cdd:cd12926 6 VGAQLKVYHQQYQDKSREYDQL---YEEYTRTSQELQMKRTAIEAFNETIKIFEE----QGQT-----QEKCSKEYLERF 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217365688 188 RKlqetqmsttsklEEAEHKVQSLQTALEKTR---TELFDLKTKYDEETTAKAD---EIEMIMTDLE 248
Cdd:cd12926 74 RR------------EGNEKEMQRILLNSERLKsriAEIHESRTKLEQDLRAQASdnrEIDKRMNSLK 128
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
107-432 |
5.50e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 41.57 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 107 DLGQQLQ-LKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALkEKIREYEQTLKNQAETIALEKEQKLQNDFAE 185
Cdd:PTZ00108 1035 DLVKELKkLGYVRFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEEL-GAAVSYDYLLSMPIWSLTKEKVEKLNAELEK 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 186 KERKLQETQmSTTSK---LEEaehkVQSLQTALEKTRtelfdlktKYDEETTAKADEIEMIMTDLERANQR-------AE 255
Cdd:PTZ00108 1114 KEKELEKLK-NTTPKdmwLED----LDKFEEALEEQE--------EVEEKEIAKEQRLKSKTKGKASKLRKpklkkkeKK 1180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 256 VAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQ 335
Cdd:PTZ00108 1181 KKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEF 1260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 336 LEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSmeFAPSEGAGTQDA-AKPLEVLLLEKNRSLQSENAALRISNSD 414
Cdd:PTZ00108 1261 SSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESN--GGSKPSSPTKKKvKKRLEGSLAALKKKKKSEKKTARKKKSK 1338
|
330
....*....|....*...
gi 2217365688 415 lSGSARRKGKDQPESRRP 432
Cdd:PTZ00108 1339 -TRVKQASASQSSRLLRR 1355
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
127-270 |
5.58e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 40.64 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 127 QKLRETLEEYNKE-FAEVKNQEVTIKALKEKIREYEQTLknQAETIALEKE-----QKLQNDFAEKERK-LQETQMSTTS 199
Cdd:cd16269 149 EDREKLVEKYRQVpRKGVKAEEVLQEFLQSKEAEAEAIL--QADQALTEKEkeieaERAKAEAAEQERKlLEEQQRELEQ 226
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217365688 200 KLEEAEHkvqSLQTALEKtrtelfdLKTKYDEETTAKADEIEMIMTDLERANQR--AEVAQREAETLREQLSS 270
Cdd:cd16269 227 KLEDQER---SYEEHLRQ-------LKEKMEEERENLLKEQERALESKLKEQEAllEEGFKEQAELLQEEIRS 289
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
115-367 |
6.48e-03 |
|
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: 41.09 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 115 KVQRLH-----------------DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQ 177
Cdd:COG3096 810 KLQRLHqafsqfvgghlavafapDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADE 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 178 KLQNDFAEKERKLQETQMSTTS------KLEEAEHKVQSLQT------ALEKTRTELFDLKTKYDEETTA---------- 235
Cdd:COG3096 890 TLADRLEELREELDAAQEAQAFiqqhgkALAQLEPLVAVLQSdpeqfeQLQADYLQAKEQQRRLKQQIFAlsevvqrrph 969
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 236 --KADEIEMIM--TDL-ERANQRAEVAQREAETLREQLSSANHSLQLASQIQKApdvaievlTRSSLEV---ELAAKERE 307
Cdd:COG3096 970 fsYEDAVGLLGenSDLnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLAS--------LKSSRDAkqqTLQELEQE 1041
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217365688 308 IAQL------------VEDVQRLQASLTKLRensaSQISQLEQQLSAKNSTLKQLEEKL-KGQADYEEVKKEL 367
Cdd:COG3096 1042 LEELgvqadaeaeeraRIRRDELHEELSQNR----SRRSQLEKQLTRCEAEMDSLQKRLrKAERDYKQEREQV 1110
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
15-364 |
6.48e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 15 FDLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFkkntpEDLRKQvaplLKSFQGEIDALSKRSKEAEaaflnvyk 94
Cdd:COG4372 38 FELDKLQEELEQLREELEQAREELEQLEEELEQARSEL-----EQLEEE----LEELNEQLQAAQAELAQAQ-------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 95 rlidvpdpvpaldlgqqlqlkvQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtiKALKEKIREYEQTLKNQAETIale 174
Cdd:COG4372 101 ----------------------EELESLQEEAEELQEELEELQKERQDLEQQR---KQLEAQIAELQSEIAEREEEL--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 175 keQKLQNDFAEKERKLQETQMST-TSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQR 253
Cdd:COG4372 153 --KELEEQLESLQEELAALEQELqALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 254 AEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQI 333
Cdd:COG4372 231 LGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLI 310
|
330 340 350
....*....|....*....|....*....|.
gi 2217365688 334 SQLEQQLSAKNSTLKQLEEKLKGQADYEEVK 364
Cdd:COG4372 311 GALEDALLAALLELAKKLELALAILLAELAD 341
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
127-322 |
6.89e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.81 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 127 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETiALEK-EQKLQNDFAEKERKLQETQMSTTSKLEEAE 205
Cdd:COG1842 33 RDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARL-ALEKgREDLAREALERKAELEAQAEALEAQLAQLE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 206 HKVQSLQTALEKTRTELFDLKTKYDeetTAKAdeiemimtdleranqRAEVAQreaetLREQLSSANHSLQLAS------ 279
Cdd:COG1842 112 EQVEKLKEALRQLESKLEELKAKKD---TLKA---------------RAKAAK-----AQEKVNEALSGIDSDDatsale 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2217365688 280 -------QIQKAPDVAIEVLTRSSLEVELAAKEREIAqlVEDV-QRLQASL 322
Cdd:COG1842 169 rmeekieEMEARAEAAAELAAGDSLDDELAELEADSE--VEDElAALKAKM 217
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
115-431 |
7.43e-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: 40.88 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 115 KVQRLHDIETENQKLRETLEEYNKEFaevKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQ 194
Cdd:pfam17380 235 KMERRKESFNLAEDVTTMTPEYTVRY---NGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKARE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 195 MSTTSKLEEAEHKVQSL------------QTALEKTRT-ELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA 261
Cdd:pfam17380 312 VERRRKLEEAEKARQAEmdrqaaiyaeqeRMAMERERElERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKN 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 262 ETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVElAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLS 341
Cdd:pfam17380 392 ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQE-EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 342 AKNSTLKQLEEKLKGQADYEEVKKELnILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAAlRISNSDlsgsaRR 421
Cdd:pfam17380 471 ERKRKKLELEKEKRDRKRAEEQRRKI-LEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERR-REAEEE-----RR 543
|
330
....*....|
gi 2217365688 422 KGKDQPESRR 431
Cdd:pfam17380 544 KQQEMEERRR 553
|
|
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
126-409 |
7.73e-03 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 40.36 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 126 NQKLRETLEEYNKEFAEVKNQEVT--------IKALKEKIREYEQTLKNQAETIA---LEKEQKLQNDFAEKERklqetq 194
Cdd:pfam14915 1 NCMLQDEIAMLRLEIDTIKNQNQEkekkyledIEILKEKNDDLQKTLKLNEETLTktvFQYNGQLNVLKAENTM------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 195 msTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKadeiemimTDLERANQRaevAQREAETLREQLSSanhs 274
Cdd:pfam14915 75 --LNSKLENEKQNKERLETEVESYRSRLAAAIQDHEQSQTSK--------RDLELAFQR---ERDEWLRLQDKMNF---- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 275 lqlasqiqkapDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASltkLRENSaSQISQLEQQLSAKNSTLKQLEEKL 354
Cdd:pfam14915 138 -----------DVSNLRDENEILSQQLSKAESKANSLENELHRTRDA---LREKT-LLLESVQRDLSQAQCQKKELEHMY 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2217365688 355 kgQADYEEVKKELNILKSMEfapsegagtqdaakplevlllEKNRSLQSENAALR 409
Cdd:pfam14915 203 --QNEQDKVNKYIGKQESLE---------------------ERLAQLQSENMLLR 234
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
17-365 |
7.93e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 17 LQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDlrkQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRL 96
Cdd:TIGR00606 739 IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEE---ESAKVCLTDVTIMERFQMELKDVERKIAQQAAKL 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 97 IDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREyeqtlknqaetiALEKE 176
Cdd:TIGR00606 816 QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGT------------NLQRR 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 177 QKLQNDFAEKERKLQETqmstTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMI----------MTD 246
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSL----IREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIkekvknihgyMKD 959
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 247 LERANQraEVAQREAETLREQLSSANHSLQLASQIQK---------APDVAIEVLTRSSLEVELAAKEREiAQLVEDVQR 317
Cdd:TIGR00606 960 IENKIQ--DGKDDYLKQKETELNTVNAQLEECEKHQEkinedmrlmRQDIDTQKIQERWLQDNLTLRKRE-NELKEVEEE 1036
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2217365688 318 LQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKG-QADYEEVKK 365
Cdd:TIGR00606 1037 LKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGrQKGYEKEIK 1085
|
|
| Homeobox_KN |
pfam05920 |
Homeobox KN domain; This is a homeobox transcription factor KN domain conserved from fungi to ... |
1272-1306 |
8.79e-03 |
|
Homeobox KN domain; This is a homeobox transcription factor KN domain conserved from fungi to human and plants. They were first identified as TALE homeobox genes in eukaryotes, (including KNOX and MEIS genes). They have been recently classified.
Pssm-ID: 428673 Cd Length: 39 Bit Score: 35.57 E-value: 8.79e-03
10 20 30
....*....|....*....|....*....|....*
gi 2217365688 1272 QQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSR 1306
Cdd:pfam05920 5 LHNPYPSEEEKAELAKETGLSRKQISNWFINARRR 39
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
107-354 |
9.16e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.90 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 107 DLGQQLQLKVQRLHDI-ETENQKLRETLEEYNKEFAevkNQEVTIKALKEKIREYEQtlKNQAEtiaLEKEQKLQNDFAE 185
Cdd:pfam00038 36 ELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERA---RLQLELDNLRLAAEDFRQ--KYEDE---LNLRTSAENDLVG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 186 KERKLQETQMSTTskleEAEHKVQSLQTalektrtELFDLKTKYDEETTAKADEIEMIMTDLE-RANQRAEVAQREAEtL 264
Cdd:pfam00038 108 LRKDLDEATLARV----DLEAKIESLKE-------ELAFLKKNHEEEVRELQAQVSDTQVNVEmDAARKLDLTSALAE-I 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 265 REQLSS-ANHSLQLASQ--IQKAPDVAIEVlTRSSLEVElAAKErEIAQLVEDVQRLQASLTKLRENSAS---QISQLEQ 338
Cdd:pfam00038 176 RAQYEEiAAKNREEAEEwyQSKLEELQQAA-ARNGDALR-SAKE-EITELRRTIQSLEIELQSLKKQKASlerQLAETEE 252
|
250 260
....*....|....*....|
gi 2217365688 339 QLSAK----NSTLKQLEEKL 354
Cdd:pfam00038 253 RYELQladyQELISELEAEL 272
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
234-368 |
9.49e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 234 TAKADEIEmimtdlERANQRAEVAQREAETLREQLSsanhsLQLASQIQKApdvaievltRSSLEVELAAKEREIAQLVE 313
Cdd:PRK12704 30 EAKIKEAE------EEAKRILEEAKKEAEAIKKEAL-----LEAKEEIHKL---------RNEFEKELRERRNELQKLEK 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217365688 314 DVQRLQASLtklrENSASQISQLEQQLSAKNSTLKQLEEKLKG-QADYEEVKKELN 368
Cdd:PRK12704 90 RLLQKEENL----DRKLELLEKREEELEKKEKELEQKQQELEKkEEELEELIEEQL 141
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
110-212 |
9.95e-03 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 37.56 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365688 110 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREyeqtlkNQAETIALE-KEQKLQNDFAEKER 188
Cdd:pfam18595 19 RELQAKIDALQVVEKDLRSCIKLLEEIEAELAKLEEAKKKLKELRDALEE------KEIELRELErREERLQRQLENAQE 92
|
90 100
....*....|....*....|....
gi 2217365688 189 KLQETQMSTTSKLEEAEHKVQSLQ 212
Cdd:pfam18595 93 KLERLREQAEEKREAAQARLEELR 116
|
|
| |
