|
Name |
Accession |
Description |
Interval |
E-value |
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
1106-1183 |
9.94e-31 |
|
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: 116.15 E-value: 9.94e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 601983272 1106 MSPELDTYGITKRVKEVLTDNNLGQRLFGETILGLTQGSVSDLLARPKPWHKLSLKGREpFVRMQLWLNDPNNVEKLM 1183
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERMEI 77
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
923-991 |
6.82e-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: 108.06 E-value: 6.82e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 601983272 923 MYQEVDTIELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLN 991
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 |
2.96e-27 |
|
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: 106.14 E-value: 2.96e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 601983272 556 EGEEIDTAEIARQVKEQLIKHNIGQRIFGHYVLGLSQGSVSEILARPKPWNKLTVRGKEpFHKMKQFLSDEQNILAL 632
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
|
|
| Homeodomain |
pfam00046 |
Homeodomain; |
1229-1285 |
5.15e-16 |
|
Homeodomain;
Pssm-ID: 459649 [Multi-domain] Cd Length: 57 Bit Score: 73.30 E-value: 5.15e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 601983272 1229 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRR 1285
Cdd:pfam00046 1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-375 |
2.09e-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: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 107 DVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT----IKALKEKIREYEQtlKSQAETIALEKEQKLQND 182
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrqISALRKDLARLEA--EVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 183 FAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDE----------ETTAKADEIEMIMTDLERANQ 252
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltllneEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 253 RAEVAQREAETLREQLSSANHSLqlaSQIQKAPDVAIEVLTrsSLEVELAAKEREIAQLVEDVQRLQASLTKLREnsasQ 332
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEI---EELEELIEELESELE--ALLNERASLEEALALLRSELEELSEELRELES----K 909
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 601983272 333 ISQLEQQLNAKNSTLKQLEEKLKG-QADYEEVKKELNTLKSMEF 375
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGlEVRIDNLQERLSEEYSLTL 953
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
18-367 |
1.33e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.13 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 18 QQLQRELDATATVLANRQDESEQSRKRLIEQsrefkkntpedlrkqvapllksfqgEIDALSKRSKEAEAAFltvykrli 97
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEA-------------------------ELEELEAELEELEAEL-------- 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 98 dvpdpvpaldvgQQLEIKVQRLHD-IETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKE 176
Cdd:COG1196 263 ------------AELEAELEELRLeLEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 177 QklQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEmimTDLERANQRAEV 256
Cdd:COG1196 331 E--LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR---AAAELAAQLEEL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 257 AQREAETLREQLSSANHSLQLASQIQKApdvAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQL 336
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAEL---EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
330 340 350
....*....|....*....|....*....|.
gi 601983272 337 EQQLNAKNSTLKQLEEKLKGQADYEEVKKEL 367
Cdd:COG1196 483 LEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
|
| homeodomain |
cd00086 |
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ... |
1229-1286 |
1.82e-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: 66.11 E-value: 1.82e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 601983272 1229 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRRE 1286
Cdd:cd00086 1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRS 58
|
|
| HOX |
smart00389 |
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ... |
1229-1284 |
1.04e-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: 64.19 E-value: 1.04e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 601983272 1229 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIR 1284
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 |
1.28e-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: 68.95 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 58 EDLRKQVAPLL---KSFQGEIDALSKRSKEAEAafltvykrlIDVPDPVPA---LDVGQQLEIKVQRLHDIETENQKLRE 131
Cdd:pfam05622 17 HELDQQVSLLQeekNSLQQENKKLQERLDQLES---------GDDSGTPGGkkyLLLQKQLEQLQEENFRLETARDDYRI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 132 TLEEYNKEFAE--VKNQEVT-----IKALK----------EKIREYEQTLKSQaetialekEQKLQ--NDFAEKERKLQE 192
Cdd:pfam05622 88 KCEELEKEVLElqHRNEELTslaeeAQALKdemdilressDKVKKLEATVETY--------KKKLEdlGDLRRQVKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 193 TQ---MSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLEranQRAEVAQREAETL---RE 266
Cdd:pfam05622 160 RNaeyMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESK-KADKLEFEYKKLE---EKLEALQKEKERLiieRD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 267 QLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRE----NSASQISQLEQQLNA 342
Cdd:pfam05622 236 TLRETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLgqegSYRERLTELQQLLED 315
|
330
....*....|...
gi 601983272 343 KNSTLKQLEEKLK 355
Cdd:pfam05622 316 ANRRKNELETQNR 328
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
123-409 |
1.76e-11 |
|
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: 69.32 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 123 ETENqKLRET---LEEYNKEFAEVKNQEVTIKALKEKIREYeQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTS 199
Cdd:TIGR02168 176 ETER-KLERTrenLDRLEDILNELERQLKSLERQAEKAERY-KELKAELRELELALLVLRLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 200 KLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETT---AKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQ 276
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 277 LASQIQKAPDVAIEVLTRSSleVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKG 356
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEEL--ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER 411
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 601983272 357 QAD-----YEEVKKELNTLKSMEFApsEGAGTQDSTKPLEVLLLEKNRSLQSENATLR 409
Cdd:TIGR02168 412 LEDrrerlQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEALEELR 467
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
19-373 |
3.90e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.17 E-value: 3.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 19 QLQRELDATATVLANRQDESEQsRKRLIEQSREFKKNTP-------EDLRKQvapLLKSFQGEIDALSKRSKEAEAAFLT 91
Cdd:PRK03918 402 EIEEEISKITARIGELKKEIKE-LKKAIEELKKAKGKCPvcgreltEEHRKE---LLEEYTAELKRIEKELKEIEEKERK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 92 VYKRLIDVpdpvpalDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtIKALKEKIREYEQTLKSQAETi 171
Cdd:PRK03918 478 LRKELREL-------EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEE--YEKLKEKLIKLKGEIKSLKKE- 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 172 aLEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQ-TALEKTRTELFDLKTKYDEETTAKADEIEmimtdLERA 250
Cdd:PRK03918 548 -LEKLEELKKKLAELEKKLDELE----EELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKE-----LERE 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 251 NQRAEVAQREAETLREQLSSANHSLQLASQiqkapdvAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQAsltklrensa 330
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLEELRK-------ELEELEKKYSEEEYEELREEYLELSRELAGLRA---------- 680
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 601983272 331 sQISQLEQQLNAKNSTLKQLEEKLKgqaDYEEVKKELNTLKSM 373
Cdd:PRK03918 681 -ELEELEKRREEIKKTLEKLKEELE---EREKAKKELEKLEKA 719
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
58-372 |
5.69e-11 |
|
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: 67.79 E-value: 5.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 58 EDLRKQVAPLLK---SFQGEIDALSKRSKEAEAAFLTVYKRLidvpdpvpaLDVGQQLEIKVQRLHDIETENQKLRETLE 134
Cdd:TIGR02169 684 EGLKRELSSLQSelrRIENRLDELSQELSDASRKIGEIEKEI---------EQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 135 EYNKEFAEVknqEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQN--DFAEKERKLQETQmstTSKLEEAEHKLQTLQ 212
Cdd:TIGR02169 755 NVKSELKEL---EARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAelSKLEEEVSRIEAR---LREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 213 TALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS-----ANHSLQLASQIQKAPDV 287
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDlkkerDELEAQLRELERKIEEL 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 288 AIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASqISQLEQQLNAKNSTLKQLEE-KLKGQADYEEVKKE 366
Cdd:TIGR02169 909 EAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIRALEPvNMLAIQEYEEVLKR 987
|
....*.
gi 601983272 367 LNTLKS 372
Cdd:TIGR02169 988 LDELKE 993
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
82-370 |
8.57e-11 |
|
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: 66.52 E-value: 8.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 82 SKEAEAAFLTVYKRLIDVPDPVPALdvgQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT-----IKALKEK 156
Cdd:COG5185 221 LLEKAKEIINIEEALKGFQDPESEL---EDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANnlikqFENTKEK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 157 IREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYD-EETTA 235
Cdd:COG5185 298 IAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVElSKSSE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 236 KAD-----------EIEMIMTDLERANQRAE--------VAQREAETLREQLSSANHSLQLASQIQKA-------PDVAI 289
Cdd:COG5185 378 ELDsfkdtiestkeSLDEIPQNQRGYAQEILatledtlkAADRQIEELQRQIEQATSSNEEVSKLLNEliselnkVMREA 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 290 EVLTRSSLEVELAAKEREIAQ----LVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLK--GQADYEEV 363
Cdd:COG5185 458 DEESQSRLEEAYDEINRSVRSkkedLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKdfMRARGYAH 537
|
....*..
gi 601983272 364 KKELNTL 370
Cdd:COG5185 538 ILALENL 544
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
110-372 |
2.62e-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: 65.04 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 110 QQLEIKVQRLHDIETENQKLRETLEEYNKEfaeVKNQEVTIKALKEKIreyeQTLKSQAETIALEKEQKLQNDFAE---- 185
Cdd:TIGR04523 246 TEISNTQTQLNQLKDEQNKIKKQLSEKQKE---LEQNNKKIKELEKQL----NQLKSEISDLNNQKEQDWNKELKSelkn 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 186 KERKLQETQmSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEmimtDLERANQRaevAQREAETLR 265
Cdd:TIGR04523 319 QEKKLEEIQ-NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIE----KLKKENQS---YKQEIKNLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 266 EQLSSANHSLQLASQIQKAPDVAIEVltrssLEVELAAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLNAKNS 345
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKK-----LQQEKELLEKEIERLKETIIKNNSEIKDLTN----QDSVKELIIKNLDN 461
|
250 260
....*....|....*....|....*..
gi 601983272 346 TLKQLEEKLKgqadyeEVKKELNTLKS 372
Cdd:TIGR04523 462 TRESLETQLK------VLSRSINKIKQ 482
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
105-332 |
4.18e-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: 63.63 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 105 ALDVGQQLEIKVQRLH-DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIAL--EKEQKLQN 181
Cdd:COG4942 18 QADAAAEAEAELEQLQqEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEleKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 182 DFAEKERKLQET-----QMSTTSKLEEAEHKLQTLQTAlekTRTELFDLKTKYDEEttaKADEIEMIMTDLERANQRAEV 256
Cdd:COG4942 98 ELEAQKEELAELlralyRLGRQPPLALLLSPEDFLDAV---RRLQYLKYLAPARRE---QAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 601983272 257 AQREAETLREQLSSANHSLQLASQIQKApdvaievlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQ 332
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQK--------LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
112-371 |
6.44e-10 |
|
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: 64.32 E-value: 6.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 112 LEIKVQRLHDIETEnqklRETLEEYnkefaevknqevtiKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQ 191
Cdd:TIGR02169 193 IDEKRQQLERLRRE----REKAERY--------------QALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 192 ETQMSTTSKLEEAEHKLQTLQTALEKtrtelfdLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSsa 271
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKK-------IKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA-- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 272 nhslQLASQIQKApdvaieVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRensaSQISQLEQQLNAKNSTLKQLE 351
Cdd:TIGR02169 326 ----KLEAEIDKL------LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR----AELEEVDKEFAETRDELKDYR 391
|
250 260
....*....|....*....|
gi 601983272 352 EKLkgqadyEEVKKELNTLK 371
Cdd:TIGR02169 392 EKL------EKLKREINELK 405
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
127-351 |
6.84e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.17 E-value: 6.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 127 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALekEQKLQNDFAEKERKLQETQM-STTSKLEEAE 205
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYL--RAALRLWFAQRRLELLEAELeELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 206 HKLQTLQTALEKTRTELFDLKTKYDEettAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQiqkap 285
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRG---NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE----- 380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 601983272 286 dvaievltrsslevELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLE 351
Cdd:COG4913 381 --------------EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
15-316 |
1.44e-09 |
|
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: 63.15 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 15 FDLQQLQRELDATATVLANRQDESEQSRKRLIEQSREF--KKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfltv 92
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELesKLDELAEELAELEEKLEELKEELESLEAELEELEAE---- 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 93 ykrlidvpdpvpaldvgqqleikvqrLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIA 172
Cdd:TIGR02168 367 --------------------------LEELESRLEELEEQLETLRSKVAQLELQ---IASLNNEIERLEARLERLEDRRE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 173 LEKEQKLQNDFAEKERKLQETQMSTTSK---LEEAEHKLQTLQTALEKTRTELFDLKTKYDeETTAKADEIEMIMTDLER 249
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAELKELQAELEELeeeLEELQEELERLEEALEELREELEEAEQALD-AAERELAQLQARLDSLER 496
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 601983272 250 ANQRAEVAQREAETLREQLSSANHSLQLASQIqkapdvaIEVLTRSSLEVELAAKEREIAQLVEDVQ 316
Cdd:TIGR02168 497 LQENLEGFSEGVKALLKNQSGLSGILGVLSEL-------ISVDEGYEAAIEAALGGRLQAVVVENLN 556
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
110-283 |
1.62e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 110 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERK 189
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAE---LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 190 LQETQMSttskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAK----ADEIEMIMTDLERANQRAEVAQREAETLR 265
Cdd:COG4717 151 LEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATEEElqdlAEELEELQQRLAELEEELEEAQEELEELE 226
|
170
....*....|....*...
gi 601983272 266 EQLSSANHSLQLASQIQK 283
Cdd:COG4717 227 EELEQLENELEAAALEER 244
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
110-372 |
1.72e-09 |
|
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: 62.35 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 110 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKSQAETIALEKeQKLQNDFAE 185
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTRESLETQLKVLSRSINKIK-QNLEQKQKE 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 186 KERKLQETQMST--TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAET 263
Cdd:TIGR04523 491 LKSKEKELKKLNeeKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEI 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 264 lrEQLSSANHSLqLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLrensASQISQLEQQLNAK 343
Cdd:TIGR04523 571 --EELKQTQKSL-KKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKL----SSIIKNIKSKKNKL 643
|
250 260 270
....*....|....*....|....*....|
gi 601983272 344 NSTLKQLEEKLKG-QADYEEVKKELNTLKS 372
Cdd:TIGR04523 644 KQEVKQIKETIKEiRNKWPEIIKKIKESKT 673
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
16-370 |
2.54e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 16 DLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEidALSKRSKEAEaaflTVYKR 95
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE--ELEKKAEEYE----KLKEK 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 96 LIDVPDPVpaldvgQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEV-----TIKALKEKIREYEQtlksqaet 170
Cdd:PRK03918 534 LIKLKGEI------KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfeSVEELEERLKELEP-------- 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 171 iALEKEQKLQNDFAEKERKLQEtQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEiemIMTDLERA 250
Cdd:PRK03918 600 -FYNEYLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELRE---EYLELSRE 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 251 NQRAEVAQREAETLREQLSSanhslqlasqiqkapdvAIEVLTRSSLEVELAAKERE-IAQLVEDVQRLQASLTK----L 325
Cdd:PRK03918 675 LAGLRAELEELEKRREEIKK-----------------TLEKLKEELEEREKAKKELEkLEKALERVEELREKVKKykalL 737
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 601983272 326 RENSASQISQLEQQL-----NAKNS--TLKQLEEKLKGQADYEEVKKELNTL 370
Cdd:PRK03918 738 KERALSKVGEIASEIfeeltEGKYSgvRVKAEENKVKLFVVYQGKERPLTFL 789
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
36-355 |
4.02e-09 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 59.54 E-value: 4.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 36 DESEQSRKRLIEQSREFKKNtpedlRKQVAPLLKSFQGEIDALSKRSKE--AEAafltvyKRLIDVPDpvpalDVGQQL- 112
Cdd:COG1340 11 EELEEKIEELREEIEELKEK-----RDELNEELKELAEKRDELNAQVKElrEEA------QELREKRD-----ELNEKVk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 113 EIKVQRLhDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLksQAETIALEKEQKLQNDFAEKERKLQE 192
Cdd:COG1340 75 ELKEERD-ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ--QTEVLSPEEEKELVEKIKELEKELEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 193 TQmsttsKLEEAEHKLQTLQTALEKTRTELFDLKTKYdEETTAKADEIEMIMTDLeranqraevaQREAETLREQLSSAN 272
Cdd:COG1340 152 AK-----KALEKNEKLKELRAELKELRKEAEEIHKKI-KELAEEAQELHEEMIEL----------YKEADELRKEADELH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 273 HslqlasQIQKAPDVAIEVltrsslevelaakEREIAQLVEDVQRLQASLTKLRENSASqiSQLEQQLNAKNSTLKQLEE 352
Cdd:COG1340 216 K------EIVEAQEKADEL-------------HEEIIELQKELRELRKELKKLRKKQRA--LKREKEKEELEEKAEEIFE 274
|
...
gi 601983272 353 KLK 355
Cdd:COG1340 275 KLK 277
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
7-373 |
5.72e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 5.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 7 SMFQYWKRFDLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNtpedlrkqvapllksfQGEIDALSKRSKEAE 86
Cdd:COG4717 45 AMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL----------------QEELEELEEELEELE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 87 AAFLTVYKRLIDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYnkefaevKNQEVTIKALKEKIREYEQTLKS 166
Cdd:COG4717 109 AELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL-------RELEEELEELEAELAELQEELEE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 167 QAETIALEKEQKLQnDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKtkyDEETTAKADEIEMIMT- 245
Cdd:COG4717 182 LLEQLSLATEEELQ-DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA---LEERLKEARLLLLIAAa 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 246 ----------DLERANQRAEVAQ-------REAETLREQLSSANHSLQLASQIQKAPDVAIEVLTR--SSLEVELAAKER 306
Cdd:COG4717 258 llallglggsLLSLILTIAGVLFlvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEEllAALGLPPDLSPE 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 601983272 307 EIAQLVEDVQRLQASLTKLRE-NSASQISQLEQQLN-----AKNSTLKQLEEKLKGQADYEEVKKELNTLKSM 373
Cdd:COG4717 338 ELLELLDRIEELQELLREAEElEEELQLEELEQEIAallaeAGVEDEEELRAALEQAEEYQELKEELEELEEQ 410
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
172-368 |
9.47e-09 |
|
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: 57.63 E-value: 9.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 172 ALEKEQKLQNDFAEKERKLQETQMsttsKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERAN 251
Cdd:COG1579 8 ALLDLQELDSELDRLEHRLKELPA----ELAELEDELAALEARLEAAKTELEDLEKEIKR----LELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 252 QRAEVA--QREAETLREQLSSanhslqLASQIQKAPDVAIEVLTRssleveLAAKEREIAQLVEDVQRLQASLTKLRENS 329
Cdd:COG1579 80 EQLGNVrnNKEYEALQKEIES------LKRRISDLEDEILELMER------IEELEEELAELEAELAELEAELEEKKAEL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 601983272 330 ASQISQLEQQLNAKNSTLKQLEEKLKGQ--ADYEEVKKELN 368
Cdd:COG1579 148 DEELAELEAELEELEAEREELAAKIPPEllALYERIRKRKN 188
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
142-372 |
1.17e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 142 EVKNQEVTIKALKEKIREYEQ------TLKSQAETiaLEKEQKLQNDFAEKERKLQETQ-MSTTSKLEEAEHKLQTLQTA 214
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERahealeDAREQIEL--LEPIRELAERYAAARERLAELEyLRAALRLWFAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 215 LEKTRTELfdlktkydeettakadeiemimtdlERANQRAEVAQREAETLREQLssanhsLQLASQIQKAPDVAIEvltr 294
Cdd:COG4913 297 LEELRAEL-------------------------ARLEAELERLEARLDALREEL------DELEAQIRGNGGDRLE---- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 295 sSLEVELAAKEREIAQLVEDVQRLQASLTKL-------RENSASQISQLEQQLNAKNSTLKQLEEKL--------KGQAD 359
Cdd:COG4913 342 -QLEREIERLERELEERERRRARLEALLAALglplpasAEEFAALRAEAAALLEALEEELEALEEALaeaeaalrDLRRE 420
|
250
....*....|...
gi 601983272 360 YEEVKKELNTLKS 372
Cdd:COG4913 421 LRELEAEIASLER 433
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
141-380 |
1.19e-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: 59.01 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 141 AEVKNQEVTIKALKEKIREYEQTLKSQAETI--ALEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKT 218
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEkaLLKQLAALERRIAALARRIRALE----QELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 219 RTELFDLKTKYDE-----ETTAKADEIEMIM--TDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAiev 291
Cdd:COG4942 96 RAELEAQKEELAEllralYRLGRQPPLALLLspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE--- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 292 ltRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRensaSQISQLEQQLNAKNSTLKQLEEKLKGQAdyEEVKKELNTLK 371
Cdd:COG4942 173 --RAELEALLAELEEERAALEALKAERQKLLARLE----KELAELAAELAELQQEAEELEALIARLE--AEAAAAAERTP 244
|
....*....
gi 601983272 372 SMEFAPSEG 380
Cdd:COG4942 245 AAGFAALKG 253
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
106-425 |
5.69e-08 |
|
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: 57.67 E-value: 5.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 106 LDVGQQLEIKVQRLHDIETENQKLRETL--EEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQA----ETIA--LEKEQ 177
Cdd:TIGR00618 628 QDVRLHLQQCSQELALKLTALHALQLTLtqERVREHALSIRVLPKELLASRQLALQKMQSEKEQLtywkEMLAqcQTLLR 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 178 KLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRtELFDLKTKYDEETTAKADE----IEMIMTDLERANQR 253
Cdd:TIGR00618 708 ELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELM-HQARTVLKARTEAHFNNNEevtaALQTGAELSHLAAE 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 254 AEVAQREAETLREQLSsanhslQLASQI-QKAPDVAIEVLtrssLEVELAAKEREiaqlvedvqrlqASLTKLRENSASQ 332
Cdd:TIGR00618 787 IQFFNRLREEDTHLLK------TLEAEIgQEIPSDEDILN----LQCETLVQEEE------------QFLSRLEEKSATL 844
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 333 IsQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSMEFAPSEGAgtqdSTKPLEVLLLEKNRSLQSENATLRISN 412
Cdd:TIGR00618 845 G-EITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDA----LIKFLHEITLYANVRLANQSEGRFHGR 919
|
330
....*....|...
gi 601983272 413 SDLSGSARRKGRD 425
Cdd:TIGR00618 920 YADSHVNARKYQG 932
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
17-353 |
7.80e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 7.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 17 LQQLQRELDATATVLANRQDESEQSRkrlIEQSREFKKNTPEDLRKQVAPLlKSFQGEIDALSKRSKEAEAAfLTVYKRL 96
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEA---LEAELAELPERLEELEERLEEL-RELEEELEELEAELAELQEE-LEELLEQ 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 97 IDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNqEVTIKALKEKIREYEQTLKSQAETIALE-- 174
Cdd:COG4717 186 LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLLLIAAALLALLgl 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 175 -------------------------------KEQKLQNDFAE-----KERKLQETQMS------------TTSKLEEAEH 206
Cdd:COG4717 265 ggsllsliltiagvlflvlgllallflllarEKASLGKEAEElqalpALEELEEEELEellaalglppdlSPEELLELLD 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 207 KLQTLQTALEKTRTELFDLKTKYDEE------TTAKADEIEMIMTDLERANQRAEvAQREAETLREQLSSANHSLQLASQ 280
Cdd:COG4717 345 RIEELQELLREAEELEEELQLEELEQeiaallAEAGVEDEEELRAALEQAEEYQE-LKEELEELEEQLEELLGELEELLE 423
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 601983272 281 IQKAPDVAIEVltrSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAsqISQLEQQLNAKNSTLKQLEEK 353
Cdd:COG4717 424 ALDEEELEEEL---EELEEELEELEEELEELREELAELEAELEQLEEDGE--LAELLQELEELKAELRELAEE 491
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
13-358 |
7.94e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 7.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 13 KRFDLQQLQRELDATATVLAnrqdESEQSRKRLIEQSREfKKNTPEDLRKQVAPLLKSF---QGEIDALSKRSKEAEAAF 89
Cdd:PRK02224 249 RREELETLEAEIEDLRETIA----ETEREREELAEEVRD-LRERLEELEEERDDLLAEAgldDADAEAVEARREELEDRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 90 LTVYKRLIDVPdpVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEF----AEVKNQEVTIKALKEKIREYEQT-- 163
Cdd:PRK02224 324 EELRDRLEECR--VAAQAHNEEAESLREDADDLEERAEELREEAAELESELeearEAVEDRREEIEELEEEIEELRERfg 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 164 --------LKSQAETIALEKE-------------QKLQNDFAEKERKLQETQMST----------TSKLEEAEHKLQTLQ 212
Cdd:PRK02224 402 dapvdlgnAEDFLEELREERDelrereaeleatlRTARERVEEAEALLEAGKCPEcgqpvegsphVETIEEDRERVEELE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 213 TALEKTRTELFDLKTKYDEETTAK--ADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQ-LASQIQKAPDVAI 289
Cdd:PRK02224 482 AELEDLEEEVEEVEERLERAEDLVeaEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAeLEAEAEEKREAAA 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 290 EVLTRS-SLEVELAAKEREIAQLVEDVQRLQ--ASLTKLRENSASQISQLEQQ--------------LNAKNSTLKQLEE 352
Cdd:PRK02224 562 EAEEEAeEAREEVAELNSKLAELKERIESLEriRTLLAAIADAEDEIERLREKrealaelnderrerLAEKRERKRELEA 641
|
....*.
gi 601983272 353 KLKGQA 358
Cdd:PRK02224 642 EFDEAR 647
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
117-264 |
1.05e-07 |
|
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: 54.55 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 117 QRLHDIETENQKLRETLEEYNKEF----AEVKNQEVTIKALKEKIREYEQTL---KSQAETIALEKEQklqnDFAEKERK 189
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELedleKEIKRLELEIEEVEARIKKYEEQLgnvRNNKEYEALQKEI----ESLKRRIS 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 601983272 190 LQETqmsttsKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERAN-QRAEVAQREAETL 264
Cdd:COG1579 107 DLED------EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEaEREELAAKIPPEL 176
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
108-372 |
1.53e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 108 VGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTI--------------KALKEKIREYEQTLKSQAETIAL 173
Cdd:PRK03918 198 KEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIeelekeleslegskRKLEEKIRELEERIEELKKEIEE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 174 EKEQ------------------KLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTA---LEKTRTELFDLKTKYD-- 230
Cdd:PRK03918 278 LEEKvkelkelkekaeeyiklsEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKeerLEELKKKLKELEKRLEel 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 231 -------EETTAKADEIEMIMTDL-----ERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLE 298
Cdd:PRK03918 358 eerhelyEEAKAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGK 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 299 VELAAKE--------------REIAQLVEDVQRLQASLTKLREN-------------------SASQISQLEQQLNAKNs 345
Cdd:PRK03918 438 CPVCGRElteehrkelleeytAELKRIEKELKEIEEKERKLRKElrelekvlkkeseliklkeLAEQLKELEEKLKKYN- 516
|
330 340
....*....|....*....|....*..
gi 601983272 346 tLKQLEEKLKgqaDYEEVKKELNTLKS 372
Cdd:PRK03918 517 -LEELEKKAE---EYEKLKEKLIKLKG 539
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
151-353 |
1.61e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 55.79 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 151 KALKEKIREYEQTLKSQAETIALEKEQ-KLQNDFAEKERKL-----QETQMSTTSKLEEAE-HKLQTLQT---------- 213
Cdd:PHA02562 170 KLNKDKIRELNQQIQTLDMKIDHIQQQiKTYNKNIEEQRKKngeniARKQNKYDELVEEAKtIKAEIEELtdellnlvmd 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 214 ------ALEKTRTELFDLKTKYdeETTAKadEIEMI---------MTDLERANQRaevaqreAETLREQLSSANHSL-QL 277
Cdd:PHA02562 250 iedpsaALNKLNTAAAKIKSKI--EQFQK--VIKMYekggvcptcTQQISEGPDR-------ITKIKDKLKELQHSLeKL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 278 ASQIQKAPDVAIEVLTRSS----LEVELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLNAKNSTLKQL 350
Cdd:PHA02562 319 DTAIDELEEIMDEFNEQSKklleLKNKISTNKQSLITLVDKAKKVKAAIEELqaeFVDNAEELAKLQDELDKIVKTKSEL 398
|
...
gi 601983272 351 EEK 353
Cdd:PHA02562 399 VKE 401
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
58-250 |
1.63e-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: 54.68 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 58 EDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfLTVYKRLIDvpdpvpalDVGQQLEIKVQRLHDI-ETENQKL-RETLEE 135
Cdd:cd22656 113 EEAKKTIKALLDDLLKEAKKYQDKAAKVVDK-LTDFENQTE--------KDQTALETLEKALKDLlTDEGGAIaRKEIKD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 136 YNKEFAevKNQEVTIKALKEKIREYEQTLKSQAETIAleKEQKLQNDFaekerKLQETQM-STTSKLEEAEHKLQTLQTA 214
Cdd:cd22656 184 LQKELE--KLNEEYAAKLKAKIDELKALIADDEAKLA--AALRLIADL-----TAADTDLdNLLALIGPAIPALEKLQGA 254
|
170 180 190
....*....|....*....|....*....|....*.
gi 601983272 215 LEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERA 250
Cdd:cd22656 255 WQAIATDLDSLKDLLEDDIS-KIPAAILAKLELEKA 289
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
31-374 |
2.03e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 31 LANRQDESEQSRKRLIEQSREF-----KKNTPEDLRKQVAPLlksfqgEIDALSKRSKEAEAAFLTVYKRLIDVPDPVPA 105
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYeeakaKKEELERLKKRLTGL------TPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 106 LD-VGQQLEIKVQRLHDIE----------TENQKLrETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKSQAET 170
Cdd:PRK03918 417 LKkEIKELKKAIEELKKAKgkcpvcgrelTEEHRK-ELLEEYTAELKRIEKELKEIEEkerkLRKELRELEKVLKKESEL 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 171 IALEK--------EQKLQNDFAEK-ERKLQE----------------TQMSTTSKLEEAEHKLQTLQTALEKTRTELFDL 225
Cdd:PRK03918 496 IKLKElaeqlkelEEKLKKYNLEElEKKAEEyeklkekliklkgeikSLKKELEKLEELKKKLAELEKKLDELEEELAEL 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 226 KTKYDEETTAKADEIEMIMTDLER----------ANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRS 295
Cdd:PRK03918 576 LKELEELGFESVEELEERLKELEPfyneylelkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 296 SLEVELAAKEREIAQLVEDVQRLQA---SLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKS 372
Cdd:PRK03918 656 YSEEEYEELREEYLELSRELAGLRAeleELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKA 735
|
..
gi 601983272 373 ME 374
Cdd:PRK03918 736 LL 737
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
117-357 |
2.17e-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: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 117 QRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALekeQKLQNDFAEKERKLQETQmS 196
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAE---LDALQERREALQRLAEYSWDEIDV---ASAEREIAELEAELERLD-A 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 197 TTSKLEEAEHKLQTLQTALEKTRTELFDLKTKY---DEETTAKADEIEMIMTDLERANQRAEVAQRE-AETLREQLSSAN 272
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIgrlEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 273 HSLQLASQIQKApdvaievltRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNA-KNSTLKQLE 351
Cdd:COG4913 763 VERELRENLEER---------IDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRlEEDGLPEYE 833
|
....*.
gi 601983272 352 EKLKGQ 357
Cdd:COG4913 834 ERFKEL 839
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
119-414 |
2.32e-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: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 119 LHDIETENQKLRETLEEYNKEFAevKNQEVTI--------KALKEKIREYEQTLKSqAETIALEKEQKLQNDFAEKERKL 190
Cdd:TIGR01612 988 LNDYEAKNNELIKYFNDLKANLG--KNKENMLyhqfdekeKATNDIEQKIEDANKN-IPNIEIAIHTSIYNIIDEIEKEI 1064
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 191 -QETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKydEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQls 269
Cdd:TIGR01612 1065 gKNIELLNKEILEEAEINITNFNEIKEKLKHYNFDDFGK--EENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKK-- 1140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 270 SANHSLQLASQIQKAPDVAIEVLTRSSLEvELAAKEREIA-------QLVEDVQRLQASLTKLRENSASqisqLEQQLNA 342
Cdd:TIGR01612 1141 SENYIDEIKAQINDLEDVADKAISNDDPE-EIEKKIENIVtkidkkkNIYDEIKKLLNEIAEIEKDKTS----LEEVKGI 1215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 601983272 343 KNSTLKQLEEKLKGQADyEEVKKELNTLKSMEfAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSD 414
Cdd:TIGR01612 1216 NLSYGKNLGKLFLEKID-EEKKKSEHMIKAME-AYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDD 1285
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
16-359 |
2.71e-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: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 16 DLQQLQRELDATATVLANRQDESEQSRKRLiEQSREFKKNTPEDLRkqvaplLKSFQGEIDALSKRSKEAEAAFLTVykr 95
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERR-EALQRLAEYSWDEID------VASAEREIAELEAELERLDASSDDL--- 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 96 lidvpdpvpaldvgQQLEikvQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEK 175
Cdd:COG4913 688 --------------AALE---EQLEELEAELEELEEELDELKGEIGRLEKE---LEQAEEELDELQDRLEAAEDLARLEL 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 176 EQKLQNDFAEKERKLQETQMSttsklEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEiemIMTDLERANQ-RA 254
Cdd:COG4913 748 RALLEERFAAALGDAVERELR-----ENLEERIDALRARLNRAEEELERAMRAFNREWPAETAD---LDADLESLPEyLA 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 255 EVAQREAETL-------REQLSSANHS--LQLASQIQKAPDVAIEVLTR--SSLE---------VELAAKEREiaqlVED 314
Cdd:COG4913 820 LLDRLEEDGLpeyeerfKELLNENSIEfvADLLSKLRRAIREIKERIDPlnDSLKripfgpgryLRLEARPRP----DPE 895
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 601983272 315 VQRLQASLTKLRENSASQIsqlEQQLNAKNSTLKQLEEKLKGQAD 359
Cdd:COG4913 896 VREFRQELRAVTSGASLFD---EELSEARFAALKRLIERLRSEEE 937
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
131-350 |
2.71e-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: 52.60 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 131 ETLEEYNKEFAEVKN--QEVT------IKALKEKIREyeqtLKSQAEtialEKEQKLQNDFAEKERkLQEtqmsttsKLE 202
Cdd:pfam13851 1 ELMKNHEKAFNEIKNyyNDITrnnlelIKSLKEEIAE----LKKKEE----RNEKLMSEIQQENKR-LTE-------PLQ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 203 EAEHKLQTLQTAL---EKTRTELfdlktkydEETTAKADEIEMIMTDLERAN----QRAEVAQREAETLREQLSSANHSL 275
Cdd:pfam13851 65 KAQEEVEELRKQLenyEKDKQSL--------KNLKARLKVLEKELKDLKWEHevleQRFEKVERERDELYDKFEAAIQDV 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 601983272 276 QlasqiQKApDVAIEVLTR--SSLEVELAAKEREIAQLvedvqrLQASltKLRENSASQISQ-LEQQLNAKNSTLKQL 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 |
3.18e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 110 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERK 189
Cdd:COG4913 274 LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 190 LQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLS 269
Cdd:COG4913 354 LEERE----RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
.
gi 601983272 270 S 270
Cdd:COG4913 430 S 430
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
19-426 |
3.94e-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: 55.23 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 19 QLQRELDATATVLANRQDESEqsrkRLIEQSREFKKNTPEDlRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTV---YKR 95
Cdd:pfam12128 305 ELNGELSAADAAVAKDRSELE----ALEDQHGAFLDADIET-AAADQEQLPSWQSELENLEERLKALTGKHQDVtakYNR 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 96 LIdvpdpvpaLDVGQQLEIKVQRLHDiETENQKlretlEEYNKEFAEVKNQ-EVTIKALKEKIREYEQTLKSQAETIALE 174
Cdd:pfam12128 380 RR--------SKIKEQNNRDIAGIKD-KLAKIR-----EARDRQLAVAEDDlQALESELREQLEAGKLEFNEEEYRLKSR 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 175 -KEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAkadeiemimtdLERANQR 253
Cdd:pfam12128 446 lGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEA-----------LRQASRR 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 254 AEVAQREAETLREQLSSANHSLqLASQIQKAPD--------VAIEVLTRSSLEVEL----AAKEREIAQLVEDVQRLQA- 320
Cdd:pfam12128 515 LEERQSALDELELQLFPQAGTL-LHFLRKEAPDweqsigkvISPELLHRTDLDPEVwdgsVGGELNLYGVKLDLKRIDVp 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 321 SLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLkGQAdyeevKKELNTLK-SMEFAPSEGAGTQDSTKPL----EVLLL 395
Cdd:pfam12128 594 EWAASEEELRERLDKAEEALQSAREKQAAAEEQL-VQA-----NGELEKASrEETFARTALKNARLDLRRLfdekQSEKD 667
|
410 420 430
....*....|....*....|....*....|.
gi 601983272 396 EKNRSLQSENATLRISNSDLSGSARRKGRDQ 426
Cdd:pfam12128 668 KKNKALAERKDSANERLNSLEAQLKQLDKKH 698
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
14-268 |
4.76e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 14 RFDLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTP-----EDLRKQVAPLLKSFQGEIDALSKRSKEAEAA 88
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaeaEAEIEELEAQIEQLKEELKALREALDELRAE 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 89 FLTVYKRlidvpdpvpALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFA----EVKNQEVTIKALKEKIREYEQTL 164
Cdd:TIGR02168 812 LTLLNEE---------AANLRERLESLERRIAATERRLEDLEEQIEELSEDIEslaaEIEELEELIEELESELEALLNER 882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 165 KSQAETIALEKE--QKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETtakADEIEM 242
Cdd:TIGR02168 883 ASLEEALALLRSelEELSEELRELESKRSELR----RELEELREKLAQLELRLEGLEVRIDNLQERLSEEY---SLTLEE 955
|
250 260
....*....|....*....|....*.
gi 601983272 243 IMTDLERANQRAEVAQREAETLREQL 268
Cdd:TIGR02168 956 AEALENKIEDDEEEARRRLKRLENKI 981
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
16-288 |
6.74e-07 |
|
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: 53.23 E-value: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 16 DLQQLQRELDAtatvLANRQDESEQSRKRLIEQsrefkkntpedlrkqvaplLKSFQGEIDALSKRSKEAEaafltvykr 95
Cdd:COG4942 28 ELEQLQQEIAE----LEKELAALKKEEKALLKQ-------------------LAALERRIAALARRIRALE--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 96 lidvpdpvpaldvgQQLEIKVQRLHDIETENQKLRETLEEYNKEFAevknqEVTIKALKEKIREYEQTLKSQAETIALEK 175
Cdd:COG4942 76 --------------QELAALEAELAELEKEIAELRAELEAQKEELA-----ELLRALYRLGRQPPLALLLSPEDFLDAVR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 176 EQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAE 255
Cdd:COG4942 137 RLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
|
250 260 270
....*....|....*....|....*....|...
gi 601983272 256 VAQREAETLREQLSSANHSLQLASQIQKAPDVA 288
Cdd:COG4942 217 ELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
150-375 |
6.81e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 6.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 150 IKALKEKIREYEqTLKSQAETIALEKEQKLQNDFAEKERKLQETQmSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKY 229
Cdd:COG4717 48 LERLEKEADELF-KPQGRKPELNLKELKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 230 D-EETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSsanhslQLASQIQKAPDVAIEVLTRSSLevelaAKEREI 308
Cdd:COG4717 126 QlLPLYQELEALEAELAELPERLEELEERLEELRELEEELE------ELEAELAELQEELEELLEQLSL-----ATEEEL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 601983272 309 AQLVEDVQRLQAsltklrensasQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSMEF 375
Cdd:COG4717 195 QDLAEELEELQQ-----------RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
17-408 |
7.19e-07 |
|
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: 54.35 E-value: 7.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 17 LQQLQRELDATATVLANRQDESEQSRKRL------IEQSREFKKNTPEDLRKQVAPLLK---SFQG---EIDALSKRSKE 84
Cdd:pfam15921 119 LQEMQMERDAMADIRRRESQSQEDLRNQLqntvheLEAAKCLKEDMLEDSNTQIEQLRKmmlSHEGvlqEIRSILVDFEE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 85 AEAAflTVYKRliDVPDPVPALDVG-------QQLEIKVQ-----------RLHDIETENQKLRETLEEYNKEFAE--VK 144
Cdd:pfam15921 199 ASGK--KIYEH--DSMSTMHFRSLGsaiskilRELDTEISylkgrifpvedQLEALKSESQNKIELLLQQHQDRIEqlIS 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 145 NQEVTIKALKEKI---REYEQTLKSQAETIALEKEQK----------LQNDFAEKERKLQETQMSTTSKLEEAEHKLQTL 211
Cdd:pfam15921 275 EHEVEITGLTEKAssaRSQANSIQSQLEIIQEQARNQnsmymrqlsdLESTVSQLRSELREAKRMYEDKIEELEKQLVLA 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 212 QTALEKTRTElfdlKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQlssanhslqlasqiQKAPDVAIEV 291
Cdd:pfam15921 355 NSELTEARTE----RDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDR--------------DTGNSITIDH 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 292 LTRsslevELAAKEREiaqlvedVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQ---LEEKLKGQADY-EEVKKEL 367
Cdd:pfam15921 417 LRR-----ELDDRNME-------VQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKvssLTAQLESTKEMlRKVVEEL 484
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 601983272 368 nTLKSMEFAPSEgagtqDSTKPLEVLLLEKNRSLQSENATL 408
Cdd:pfam15921 485 -TAKKMTLESSE-----RTVSDLTASLQEKERAIEATNAEI 519
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
18-419 |
7.61e-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: 54.07 E-value: 7.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 18 QQLQRELDATATVLANRQDESEQSRKRLIEQSrefkkntpedlrkqvapllksfqGEIDALSKRSKEAEAAFltvykrli 97
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVQAN-----------------------GELEKASREETFARTAL-------- 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 98 dvpdpvpaldvgQQLEIKVQRLHDietENQKLRETLEEYNKEFAEVKNQEVT-----IKALKEKIREYEQTLKSQAETIA 172
Cdd:pfam12128 649 ------------KNARLDLRRLFD---EKQSEKDKKNKALAERKDSANERLNsleaqLKQLDKKHQAWLEEQKEQKREAR 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 173 LEKEQKLQNdfAEKERKLQETQMSTTSKLEEAEHKLQtlQTALEKTRTElfDLKTK-YDEETTAK-ADEIEMIMTDLERA 250
Cdd:pfam12128 714 TEKQAYWQV--VEGALDAQLALLKAAIAARRSGAKAE--LKALETWYKR--DLASLgVDPDVIAKlKREIRTLERKIERI 787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 251 NQRAEVAQREAETLREQLSSANHSLQlasqiqkapdvaievltrssleVELAAKEREIAQLVEDVQRLQASlTKLRensa 330
Cdd:pfam12128 788 AVRRQEVLRYFDWYQETWLQRRPRLA----------------------TQLSNIERAISELQQQLARLIAD-TKLR---- 840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 331 sqISQLEQQLNAKNSTLKQLEEKLKGQADYEEvkkELNTLKsmEFAPSEGAGTQDSTKP--LEVLLLEKNR---SLQSEN 405
Cdd:pfam12128 841 --RAKLEMERKASEKQQVRLSENLRGLRCEMS---KLATLK--EDANSEQAQGSIGERLaqLEDLKLKRDYlseSVKKYV 913
|
410
....*....|....
gi 601983272 406 ATLRISNSDLSGSA 419
Cdd:pfam12128 914 EHFKNVIADHSGSG 927
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
187-373 |
8.26e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 8.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 187 ERKLQETQMSTT---SKLEEAEHKLQTLQTALE--KTRTELFDLktkyDEETTAKADEIEMIMTDLERANQRAEVAQREA 261
Cdd:COG3206 167 ELRREEARKALEfleEQLPELRKELEEAEAALEefRQKNGLVDL----SEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 262 ETLREQLSSanhSLQLASQIQKAPDVAIEVLTRSSLEVELA--------------AKEREIA----QLVEDVQRLQASLT 323
Cdd:COG3206 243 AALRAQLGS---GPDALPELLQSPVIQQLRAQLAELEAELAelsarytpnhpdviALRAQIAalraQLQQEAQRILASLE 319
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 601983272 324 KLRENSASQISQLEQQLNAKNSTLKQLEEKlkgQADYEEVKKELNTLKSM 373
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPEL---EAELRRLEREVEVAREL 366
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
125-455 |
1.21e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 125 ENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIRE----YEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSK 200
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEvmklYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 201 LEEAEHKLQTLQTALEKTRTELFDLKTKyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQ 280
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAEEAKK-AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 281 IQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQ-----LEQQLNAKNSTLK-QLEEKL 354
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKekeavIEEELDEEDEKRRmEVDKKI 1800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 355 KGQADYEEVKKE--------LNTLKSMEF-APSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSgsarrKGRD 425
Cdd:PTZ00121 1801 KDIFDNFANIIEggkegnlvINDSKEMEDsAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFN-----KEKD 1875
|
330 340 350
....*....|....*....|....*....|.
gi 601983272 426 QPESRRPGPLPASPPPQLPRNTGE-QVSNTN 455
Cdd:PTZ00121 1876 LKEDDEEEIEEADEIEKIDKDDIErEIPNNN 1906
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
117-374 |
1.22e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.22 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 117 QRLHDIETENQKLRETLEEYNKEFAEVKNQEVT----IKALKEKIREYE----------QTLKSQAETIaLEKEQKLQND 182
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKELAEKRDElnaqVKELREEAQELRekrdelnekvKELKEERDEL-NEKLNELREE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 183 FAEKERKLQETQMSTTS------KLEEAEHKLQTLQTALEKTRtELFD----LKTKYDEetTAKADEIEmimTDLERANQ 252
Cdd:COG1340 94 LDELRKELAELNKAGGSidklrkEIERLEWRQQTEVLSPEEEK-ELVEkikeLEKELEK--AKKALEKN---EKLKELRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 253 RAEVAQREAETLREQLSsanhslQLASQIQKAPDvaievltrsslevELAAKEREIAQLVEDVQRLQASLTKLREnsasQ 332
Cdd:COG1340 168 ELKELRKEAEEIHKKIK------ELAEEAQELHE-------------EMIELYKEADELRKEADELHKEIVEAQE----K 224
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 601983272 333 ISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSME 374
Cdd:COG1340 225 ADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
734-917 |
1.26e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 53.40 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 734 SASPMSTVSTYPPLAISLKKTPAAPETST--AALPSAPALKKEAQDVPTLDPPGSADAAQGVLRPMksELVRGSTWKDPW 811
Cdd:PHA03247 269 PETARGATGPPPPPEAAAPNGAAAPPDGVwgAALAGAPLALPAPPDPPPPAPAGDAEEEDDEDGAM--EVVSPLPRPRQH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 812 WSPIQPERRNLTSSEETKADETTASGKERAGSSQPRAERsqlqgpsasaeywKEWPSAESPYSQSSELSLTGASRSETPQ 891
Cdd:PHA03247 347 YPLGFPKRRRPTWTPPSSLEDLSAGRHHPKRASLPTRKR-------------RSARHAATPFARGPGGDDQTRPAAPVPA 413
|
170 180
....*....|....*....|....*.
gi 601983272 892 NSPLPSSPIVPMAKPAKPSVPPLTPE 917
Cdd:PHA03247 414 SVPTPAPTPVPASAPPPPATPLPSAE 439
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
16-374 |
1.30e-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: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 16 DLQQLQRELDATATVLANRQDESEQSRKRLIEqsrefkKNTPEDLRKQVAPLLKSFQGeidalskrsKEAEAAFLtvykr 95
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVELEELKKILAE------DEKLLDEKKQFEKIAEELKG---------KEQELIFL----- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 96 lidvpdpvpaldvgqqLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtikALKEKIREYEqtLKSQAETIALEK 175
Cdd:pfam05483 445 ----------------LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTE-----LEKEKLKNIE--LTAHCDKLLLEN 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 176 eQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTaLEKTRTELFDLKTKYDEETTAKADEIE-----------MIM 244
Cdd:pfam05483 502 -KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEN-LEEKEMNLRDELESVREEFIQKGDEVKckldkseenarSIE 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 245 TDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKA---------PDVAIEVLTRSSLEVELAAKEREIAQLVEDV 315
Cdd:pfam05483 580 YEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAlkkkgsaenKQLNAYEIKVNKLELELASAKQKFEEIIDNY 659
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 601983272 316 QRlQASLTKLRENS-----------ASQISQLEQQLNA----KNSTLKQLEEKLKGQAD--YEEVKKELNTLKSME 374
Cdd:pfam05483 660 QK-EIEDKKISEEKlleevekakaiADEAVKLQKEIDKrcqhKIAEMVALMEKHKHQYDkiIEERDSELGLYKNKE 734
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
11-301 |
1.31e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 53.54 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 11 YWKRFDLQQLQRELDATaTVLANRQDESEQSRKRLIE---QSREFK--KNTPEDLRKQVAPLLKSFQGEIDALSKrSKEA 85
Cdd:COG5022 851 FGRSLKAKKRFSLLKKE-TIYLQSAQRVELAERQLQElkiDVKSISslKLVNLELESEIIELKKSLSSDLIENLE-FKTE 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 86 EAAFLTVYKRLIDVPDPvPALDVGQQLEikVQRLHdieTENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLK 165
Cdd:COG5022 929 LIARLKKLLNNIDLEEG-PSIEYVKLPE--LNKLH---EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELA 1002
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 166 S--------QAETIALEKEQK----LQND----FAEKERKLQETQMS---TTSKLEEAEHKLQTLQTALEKTRTELFDLK 226
Cdd:COG5022 1003 ElskqygalQESTKQLKELPVevaeLQSAskiiSSESTELSILKPLQklkGLLLLENNQLQARYKALKLRRENSLLDDKQ 1082
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 601983272 227 TKYDEETTAKADEIEmiMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQI-QKAPDVAIEVLTRSSLEVEL 301
Cdd:COG5022 1083 LYQLESTENLLKTIN--VKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLsQLVNTLEPVFQKLSVLQLEL 1156
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
101-355 |
1.58e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.99 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 101 DPVPALDVGQQLEiKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLK-SQAETIALEKeqkl 179
Cdd:PRK11281 34 DLPTEADVQAQLD-ALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRqAQAELEALKD---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 180 QNDFAEKER--KLQETQMSttSKLEEAEHKLQTLQTALEKTRTELFDLKTKydeettakadeiemimtdLERA-NQRAEV 256
Cdd:PRK11281 109 DNDEETRETlsTLSLRQLE--SRLAQTLDQLQNAQNDLAEYNSQLVSLQTQ------------------PERAqAALYAN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 257 AQREAEtLREQLSS--ANHSLQLASQIQKapdvaievltrssLEVELAAKEREIA---QLVEDVQRLQASLTKLRENSAS 331
Cdd:PRK11281 169 SQRLQQ-IRNLLKGgkVGGKALRPSQRVL-------------LQAEQALLNAQNDlqrKSLEGNTQLQDLLQKQRDYLTA 234
|
250 260 270
....*....|....*....|....*....|.
gi 601983272 332 QISQLEQQL-------NAKNstLKQLEEKLK 355
Cdd:PRK11281 235 RIQRLEHQLqllqeaiNSKR--LTLSEKTVQ 263
|
|
| ClyA_NheA-like |
cd22654 |
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This ... |
105-370 |
1.87e-06 |
|
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This model contains Bacillus cereus tripartite non-hemolytic enterotoxin (Nhe) component A (NheA), a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). Non-hemolytic enterotoxin (Nhe), despite its name, is hemolytic and able to lyse erythrocytes from various mammalian organisms. It consists of three proteins, NheA, NheB and NheC, encoded by one operon containing three genes nheA, nheB and nheC, respectively. Separately, these three proteins show no toxicity; maximal activity is seen only when all three components are presented. The NheB and NheC components are able to bind to cell membranes while NheA is not; NheC primes the host cell for the formation of ion permeable NheB/C pores. Binding of NheA to NheB/NheC is thought to be the final stage of pore formation. Structure of NheA shows an elongated, almost entirely alpha-helical protein with an enlarged "head" domain compared with other cytolysins, displaying on its surface an enlarged beta-tongue which is of amphipathic rather than hydrophobic nature. It has been proposed that NheA could even form beta-barrel pores.
Pssm-ID: 439152 [Multi-domain] Cd Length: 333 Bit Score: 51.88 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 105 ALDVGQQLEIKVQRLHDIeTENQKL-----RETLEEYNKEFAEVkNQEvtIKALKEKIREYEQTLKSQAETIALEKEQKl 179
Cdd:cd22654 18 ALVILKQPNVKIEAMPSL-TNHQQTakenvREWLDEYNPKLIDL-NQD--MINFSQRFNNYYDKLYDLAGKINEDEQAK- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 180 qNDFAEKERKLQEtqmsttskleeaehKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANqrAEVAQr 259
Cdd:cd22654 93 -EDFLNGINKLQS--------------QLQTIQNSMEQTSSNLNRFKTLLDADSKNFSTDAKKAIDSLSGSN--GEIAQ- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 260 eaetLREQLSSANHSLQ-------------------LASQI---------QKAPDVAI------EVLTRSSLEVELAAKe 305
Cdd:cd22654 155 ----LRTQIKTINDEIQeeltkilnrpievgdgsinIGKQVftitittatTKTVDVTSigglinGIGNASDDEVKEAAN- 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 601983272 306 rEIAQLVEDVQRLQASLTKLrENSASQISQLEQQLNAKNSTLKqleeklKGQADYEEVKKELNTL 370
Cdd:cd22654 230 -KIQQKQKELVDLIKKLSDA-EIQATQLTLVEDQVNGFTELIK------RQIATLENLVEDWEML 286
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
110-426 |
2.08e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.83 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 110 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIalekeQKLQNDFAEKERK 189
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEE---LEQARSELEQLEEELEELNEQL-----QAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 190 LQETQmSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLS 269
Cdd:COG4372 103 LESLQ-EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 270 SAnhslQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQ 349
Cdd:COG4372 182 EQ----ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVIL 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 601983272 350 LEEKLKGQADYEEVKKELNTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGSARRKGRDQ 426
Cdd:COG4372 258 KEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI 334
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
119-371 |
2.29e-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: 52.52 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 119 LHDIETENQKLRETLEEYNKEFAEVKN----------QEVTIKALKEKIREYEQTLKSQAETIALEKEQKlqndfaEKER 188
Cdd:pfam10174 201 LDQKEKENIHLREELHRRNQLQPDPAKtkalqtviemKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDR------EEEI 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 189 KLQETQMSTTSKLeeaEHKLQTLQTALEKTRTELFDLKTKYDEETTAKAD---EIEMIMTDLERANQRAEVAQREAETLR 265
Cdd:pfam10174 275 KQMEVYKSHSKFM---KNKIDQLKQELSKKESELLALQTKLETLTNQNSDckqHIEVLKESLTAKEQRAAILQTEVDALR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 266 EQLSSANHSLQ---------------LASQIQKAPDV------AIEVLTR--SSLEVELAAKEREIAQLVEDVQRLQASL 322
Cdd:pfam10174 352 LRLEEKESFLNkktkqlqdlteekstLAGEIRDLKDMldvkerKINVLQKkiENLQEQLRDKDKQLAGLKERVKSLQTDS 431
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 601983272 323 TklreNSASQISQLEQQLNAKNSTLKQLEEK--LKGQADYEEV---KKELNTLK 371
Cdd:pfam10174 432 S----NTDTALTTLEEALSEKERIIERLKEQreREDRERLEELeslKKENKDLK 481
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
16-336 |
3.05e-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: 51.99 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 16 DLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRkQVAPLLKSFQGEIDALSKRSKEAEAAfltvykr 95
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL-RVKEKIGELEAEIASLERSIAEKERE------- 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 96 lidvpdpvpALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIA--- 172
Cdd:TIGR02169 317 ---------LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE---YAELKEELEDLRAELEEVDKEFAetr 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 173 ---------LEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLqtlqTALEKTRTELfdlktkyDEETTAKADEIEMI 243
Cdd:TIGR02169 385 delkdyrekLEKLKREINELKRELDRLQEELQRLSEELADLNAAI----AGIEAKINEL-------EEEKEDKALEIKKQ 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 244 MTDLERANQRAEVAQREAETLREQLssanhslqlaSQIQKapdvaievlTRSSLEVELAAKEREiAQLVEDVQRLQASLT 323
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELYDLKEEY----------DRVEK---------ELSKLQRELAEAEAQ-ARASEERVRGGRAVE 513
|
330
....*....|....*..
gi 601983272 324 KLRENSAS----QISQL 336
Cdd:TIGR02169 514 EVLKASIQgvhgTVAQL 530
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
123-374 |
3.92e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 123 ETENQKLRETLEEYNKEFAEVKnqevtikalkEKIREYEqtlkSQAETiALEKEQKLQNDFAEKERKLQETQmsttsKLE 202
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELD----------EEIERYE----EQREQ-ARETRDEADEVLEEHEERREELE-----TLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 203 EAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQ 282
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 283 KAPDVAIEVLTRSSLEVELAAKE-REIAQLVEDvqRLQASLTKLREnSASQISQLEQQLNAKNSTLKQLEEKLKGQADY- 360
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEElREEAAELES--ELEEAREAVED-RREEIEELEEEIEELRERFGDAPVDLGNAEDFl 414
|
250
....*....|....
gi 601983272 361 EEVKKELNTLKSME 374
Cdd:PRK02224 415 EELREERDELRERE 428
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
26-362 |
4.27e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 26 ATATVLANRQDESEQSRKRLIEQSREFkkntpEDLRKQVAPLLKsfqgEIDALSKRSKEAEAAFLTVYKRLIDVPDPVpA 105
Cdd:PRK02224 234 ETRDEADEVLEEHEERREELETLEAEI-----EDLRETIAETER----EREELAEEVRDLRERLEELEEERDDLLAEA-G 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 106 LDVGQQlEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEqtlksqaetialEKEQKLQNDFAE 185
Cdd:PRK02224 304 LDDADA-EAVEARREELEDRDEELRDRLEECRVAAQAHNEE---AESLREDADDLE------------ERAEELREEAAE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 186 KERKLQETQMSTT---SKLEEAEHKLQTLQTALEKTRTELFDLKTkYDEETTAKADEIEMIMTDLERANQRAEVAQREAE 262
Cdd:PRK02224 368 LESELEEAREAVEdrrEEIEELEEEIEELRERFGDAPVDLGNAED-FLEELREERDELREREAELEATLRTARERVEEAE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 263 TLREQ---------LSSANHSLQLASQIQKAPDVAIEvltRSSLEVELAAKEREIAQLvEDVQRLQASLTKLRENSASQI 333
Cdd:PRK02224 447 ALLEAgkcpecgqpVEGSPHVETIEEDRERVEELEAE---LEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLE 522
|
330 340
....*....|....*....|....*....
gi 601983272 334 SQLEQQLNAKNSTLKQLEEKLKGQADYEE 362
Cdd:PRK02224 523 ELIAERRETIEEKRERAEELRERAAELEA 551
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
117-368 |
5.08e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 117 QRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQtlKSQAETIALEKEQKLQNDFAEKERKLQETQMS 196
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLN--LVQTALRQQEKIERYQADLEELEERLEEQNEV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 197 T---TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERANQ--------------RAEVAQR 259
Cdd:PRK04863 371 VeeaDEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQT-RAIQYQQAVQALERAKQlcglpdltadnaedWLEEFQA 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 260 EAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVElaakeREIAQlvedvQRLQASLTKLRE--NSASQISQLE 337
Cdd:PRK04863 450 KEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVS-----RSEAW-----DVARELLRRLREqrHLAEQLQQLR 519
|
250 260 270
....*....|....*....|....*....|.
gi 601983272 338 QQLNAknstlkqLEEKLKGQADYEEVKKELN 368
Cdd:PRK04863 520 MRLSE-------LEQRLRQQQRAERLLAEFC 543
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
196-541 |
5.51e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 5.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 196 STTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL 275
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 276 QLASQIQKAPDV---------------AIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQ 338
Cdd:COG3883 96 YRSGGSVSYLDVllgsesfsdfldrlsALSKIADADADLleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 339 QLNAKNSTLKQLEEKlkgQADYEEVKKEL-NTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSG 417
Cdd:COG3883 176 QQAEQEALLAQLSAE---EAAAEAQLAELeAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 418 SARRKGRDQPESRRPGPLPASPPPQLPRNTGEQVSNTNGTHHFSPAGLSQDFFSSNLASPSLPLASTGKFALNSLLQRQL 497
Cdd:COG3883 253 GAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGG 332
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 601983272 498 MQSFYSKAMQEAGSTSTIFSTGPYSTNSISSPSPLQQSPDVNGM 541
Cdd:COG3883 333 GSGGGGGSSGGGSGGGGGGGGGGGGSSSGGGGGGVGLSVGGGYV 376
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
17-372 |
6.07e-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: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 17 LQQLQRELDATATVLANRQDE---------SEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQ---------GEIDAL 78
Cdd:TIGR00618 402 LDILQREQATIDTRTSAFRDLqgqlahakkQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQslkereqqlQTKEQI 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 79 SKRSKEAEAAFLTVYKRLIDVPDPV--------PALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtI 150
Cdd:TIGR00618 482 HLQETRKKAVVLARLLELQEEPCPLcgscihpnPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQ---R 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 151 KALKEKIREYEQTLKSQAETIALEKE------------QKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKT 218
Cdd:TIGR00618 559 ASLKEQMQEIQQSFSILTQCDNRSKEdipnlqnitvrlQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCS 638
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 219 RTELFDLKTKYDEETTAKADEIE----MIMTDLERANQRAEVAQREAETLREQLSSA----NHSLQLASQIQKA-----P 285
Cdd:TIGR00618 639 QELALKLTALHALQLTLTQERVRehalSIRVLPKELLASRQLALQKMQSEKEQLTYWkemlAQCQTLLRELETHieeydR 718
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 286 DVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQ---LEQQLNAKNSTLKQLEEKLKGQAdyEE 362
Cdd:TIGR00618 719 EFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEevtAALQTGAELSHLAAEIQFFNRLR--EE 796
|
410
....*....|
gi 601983272 363 VKKELNTLKS 372
Cdd:TIGR00618 797 DTHLLKTLEA 806
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
125-369 |
7.05e-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: 51.13 E-value: 7.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 125 ENQKLRETLE---EYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKL 201
Cdd:pfam02463 174 ALKKLIEETEnlaELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 202 EEAEhKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEmimTDLERANQRAEVAQREAETLREQLSSANHSLQLASQI 281
Cdd:pfam02463 254 ESSK-QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLA---KEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 282 QKAPDVAIE---------VLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEE 352
Cdd:pfam02463 330 LKKEKEEIEelekelkelEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQL 409
|
250
....*....|....*..
gi 601983272 353 KLKGQADYEEVKKELNT 369
Cdd:pfam02463 410 LLELARQLEDLLKEEKK 426
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
130-469 |
7.98e-06 |
|
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: 50.82 E-value: 7.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 130 RETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETialekEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQ 209
Cdd:TIGR00606 237 REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR-----KKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQ 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 210 TlqtalektrtelfdlktkydeETTAKADEIEMIMTDLERANQ-RAEVAQREAETLREQLSSANHSLQLASQIQKAPDVA 288
Cdd:TIGR00606 312 R---------------------TVREKERELVDCQRELEKLNKeRRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLI 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 289 IEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKLrenSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKE 366
Cdd:TIGR00606 371 QSLATRLELDGfeRGPFSERQIKNFHTLVIERQEDEAKT---AAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 367 LNTLK--SMEFAPSEGAGTQDSTKPL------------EVLLLEKNRS---LQSENATLRISNSDLSGSARRKGRDQPES 429
Cdd:TIGR00606 448 ILEKKqeELKFVIKELQQLEGSSDRIleldqelrkaerELSKAEKNSLtetLKKEVKSLQNEKADLDRKLRKLDQEMEQL 527
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 601983272 430 RRPGPLPASPPPQLPRNTG--EQVSNTNGTHHFSPAGLSQDF 469
Cdd:TIGR00606 528 NHHTTTRTQMEMLTKDKMDkdEQIRKIKSRHSDELTSLLGYF 569
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
112-358 |
1.15e-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: 50.22 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 112 LEIKVQRLH--------DIETENQKLRETLEEYNKEFAEVKNQevtikaLKEKIREYEQTLKSQAETIALEKEQ------ 177
Cdd:pfam12128 256 AELRLSHLHfgyksdetLIASRQEERQETSAELNQLLRTLDDQ------WKEKRDELNGELSAADAAVAKDRSElealed 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 178 ---KLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETtakADEIEMIMTDLE-----R 249
Cdd:pfam12128 330 qhgAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQN---NRDIAGIKDKLAkireaR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 250 ANQRAE---VAQREAETLREQLSSANHSL-----QLASQI------QKAPDVAIEVLTRSSLEVELAAKEREIAQL---- 311
Cdd:pfam12128 407 DRQLAVaedDLQALESELREQLEAGKLEFneeeyRLKSRLgelklrLNQATATPELLLQLENFDERIERAREEQEAanae 486
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 601983272 312 VEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQA 358
Cdd:pfam12128 487 VERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQA 533
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
128-417 |
1.22e-05 |
|
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: 49.97 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 128 KLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTL--KSQAETIALEKEQKLQN---DFAEKERKLQETQMSTT---- 198
Cdd:pfam02463 230 DYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKlaQVLKENKEEEKEKKLQEeelKLLAKEEEELKSELLKLerrk 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 199 ----SKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMImTDLERANQRAEVAQREAETLREQLSSANHS 274
Cdd:pfam02463 310 vddeEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEE-EELEKLQEKLEQLEEELLAKKKLESERLSS 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 275 LQLASQIQKAPDVaiEVLTRSSLEVELAAKEREIAQLvedvqrlqASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKL 354
Cdd:pfam02463 389 AAKLKEEELELKS--EEEKEAQLLLELARQLEDLLKE--------EKKEELEILEEEEESIELKQGKLTEEKEELEKQEL 458
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 601983272 355 KGQADYEEVKKELNTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSG 417
Cdd:pfam02463 459 KLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVG 521
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
32-366 |
1.29e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 32 ANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSfqgeiDALSKRSKEAEaafltvyKRLIDVPDPVPALDVGQQ 111
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA-----DEAKKKAEEDK-------KKADELKKAAAAKKKADE 1422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 112 LEIKVQRLHDIETENQKLRET--LEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALE---KEQKLQNDFAEK 186
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKAEEAkkADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEakkKAEEAKKKADEA 1502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 187 ERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELF---DLKTKYDE----ETTAKADEIEMImTDLERANQRAEVAQR 259
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAkkaEEKKKADElkkaEELKKAEEKKKA-EEAKKAEEDKNMALR 1581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 260 EAETLR----------------------EQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQR 317
Cdd:PTZ00121 1582 KAEEAKkaeearieevmklyeeekkmkaEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 601983272 318 LQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKE 366
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
141-385 |
1.40e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 141 AEVKNQEVTIKALKEKIREYEQTLKSQAETiALEKEQKLQNDFAEKERKLQETQM---STTSKLEEAEHKLQTLQTALEK 217
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRK-ALFELDKLQEELEQLREELEQAREeleQLEEELEQARSELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 218 TRTELfdlkTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEvltrsSL 297
Cdd:COG4372 85 LNEQL----QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK-----EL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 298 EVELAAKEREIAQLVEDVQRLqaSLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSMEFAP 377
Cdd:COG4372 156 EEQLESLQEELAALEQELQAL--SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
....*...
gi 601983272 378 SEGAGTQD 385
Cdd:COG4372 234 ALSALLDA 241
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
18-237 |
1.52e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 18 QQLQRELDATATVLANRQDESEQSRKRLIEQS---REFKKNT----PEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFL 90
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEaalEEFRQKNglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 91 TVYKRLIDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAET 170
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAALRAQLQQEAQRILASLEA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 171 ---IALEKEQKLQNDFAEKERKLQEtqmsttskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKA 237
Cdd:COG3206 321 eleALQAREASLQAQLAQLEARLAE--------LPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
127-374 |
1.56e-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: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 127 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIAlekeqKLQNDFAEKERKLQETQMSTTS------- 199
Cdd:pfam15921 454 QGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVS-----DLTASLQEKERAIEATNAEITKlrsrvdl 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 200 KLEEAEHkLQTLQTALEKTRTELFDLK---TKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQ 276
Cdd:pfam15921 529 KLQELQH-LKNEGDHLRNVQTECEALKlqmAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQ 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 277 LASQIQKAPDVAIEVLTRSSLEVEL-------AAKER---------EIAQLVEDVQRLQASLTKLRENsasqISQLEQQL 340
Cdd:pfam15921 608 EFKILKDKKDAKIRELEARVSDLELekvklvnAGSERlravkdikqERDQLLNEVKTSRNELNSLSED----YEVLKRNF 683
|
250 260 270
....*....|....*....|....*....|....*.
gi 601983272 341 NAKNSTLKQLEEKLKGQ--ADYEEVKKELNTLKSME 374
Cdd:pfam15921 684 RNKSEEMETTTNKLKMQlkSAQSELEQTRNTLKSME 719
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
196-365 |
1.74e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 196 STTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEeTTAKADEIEMI----MTDLERANQRAEVAQREAEtlREQLSSA 271
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDA-LQERREALQRLaeysWDEIDVASAEREIAELEAE--LERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 272 NHSL-QLASQIQKapdvaievltrssLEVELAAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLNAKNSTLKQ- 349
Cdd:COG4913 684 SDDLaALEEQLEE-------------LEAELEELEEELDELKGEIGRLEKELEQAEE----ELDELQDRLEAAEDLARLe 746
|
170 180
....*....|....*....|
gi 601983272 350 ----LEEKLKGQADYEEVKK 365
Cdd:COG4913 747 lralLEERFAAALGDAVERE 766
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
17-371 |
2.59e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 17 LQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNtpEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfLTVYKRL 96
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE--EALLELLAELLEEAALLEAALAELLEELAEA-AARLLLL 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 97 IDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYnkefaEVKNQEVTIKALKEKIREYEQTLksqAETIALEKE 176
Cdd:COG1196 497 LEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY-----EAALEAALAAALQNIVVEDDEVA---AAAIEYLKA 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 177 QKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEV 256
Cdd:COG1196 569 AKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 257 AQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQI--- 333
Cdd:COG1196 649 VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAlee 728
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 601983272 334 -------SQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLK 371
Cdd:COG1196 729 qleaereELLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
50-388 |
2.71e-05 |
|
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: 48.95 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 50 REFKKNTpEDLRKQVAPLLksfqgeIDALSKRSKEAEAAFLTVYKRlidvpdpvpalDVGQQLEIKVQrlhdIETENqkL 129
Cdd:pfam05483 229 EEYKKEI-NDKEKQVSLLL------IQITEKENKMKDLTFLLEESR-----------DKANQLEEKTK----LQDEN--L 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 130 RETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETI-ALEKEQKLQNDFAEKER---------------KLQET 193
Cdd:pfam05483 285 KELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTIcQLTEEKEAQMEELNKAKaahsfvvtefeattcSLEEL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 194 QMSTTSKLEEAEHKLQTLQTALEKTRTELFDLkTKYDEETTAKADEIEMIMTDleraNQRAEVAQREAETLREQLSSANH 273
Cdd:pfam05483 365 LRTEQQRLEKNEDQLKIITMELQKKSSELEEM-TKFKNNKEVELEELKKILAE----DEKLLDEKKQFEKIAEELKGKEQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 274 SLQ--LASQIQKAPDVAIEV-LTRSS----------LEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQL 340
Cdd:pfam05483 440 ELIflLQAREKEIHDLEIQLtAIKTSeehylkevedLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQ 519
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 601983272 341 NAKNSTLKQLEEKLKGQADYEEvkKELNTLKSMEFAPSEGAGTQDSTK 388
Cdd:pfam05483 520 EDIINCKKQEERMLKQIENLEE--KEMNLRDELESVREEFIQKGDEVK 565
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
115-353 |
2.89e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.80 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 115 KVQRLH-DIETENQKLRE---TLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKSQaETIALEKEQKLQNdFAEK 186
Cdd:COG3096 348 KIERYQeDLEELTERLEEqeeVVEEAAEQLAEAEARleaaEEEVDSLKSQLADYQQALDVQ-QTRAIQYQQAVQA-LEKA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 187 ERKLQETQMSttskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKA--DE----IEMIMTDLER--ANQRAE--- 255
Cdd:COG3096 426 RALCGLPDLT----PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRqfEKayelVCKIAGEVERsqAWQTARell 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 256 --------VAQReAETLREQLSSANhslQLASQIQKAPDVAIEVLTRSSLEVELAAK-EREIAQLVEDVQRLQASLTKLR 326
Cdd:COG3096 502 rryrsqqaLAQR-LQQLRAQLAELE---QRLRQQQNAERLLEEFCQRIGQQLDAAEElEELLAELEAQLEELEEQAAEAV 577
|
250 260
....*....|....*....|....*..
gi 601983272 327 EnsasQISQLEQQLNAKNSTLKQLEEK 353
Cdd:COG3096 578 E----QRSELRQQLEQLRARIKELAAR 600
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
221-371 |
2.96e-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: 48.70 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 221 ELFD-LKTKYDEETTAKADEIEMIMTDLERANQRAEV--AQREAETLREQLSSANHSLQlasQIQKAPDVAIEVLTRSSL 297
Cdd:pfam06160 45 EKFEeWRKKWDDIVTKSLPDIEELLFEAEELNDKYRFkkAKKALDEIEELLDDIEEDIK---QILEELDELLESEEKNRE 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 601983272 298 EVElaakereiaQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEkLKGQADYEEVKKELNTLK 371
Cdd:pfam06160 122 EVE---------ELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSQFEE-LTESGDYLEAREVLEKLE 185
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
118-227 |
3.08e-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: 47.70 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 118 RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAET---IALEKEQKLQNDFA---EKERKLQ 191
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQlkqLEDELEDCDPTELDrakEKLKKLL 217
|
90 100 110
....*....|....*....|....*....|....*.
gi 601983272 192 ETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKT 227
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNT 253
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
126-351 |
3.34e-05 |
|
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: 48.59 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 126 NQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQA-ETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEA 204
Cdd:pfam07111 58 SQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAmELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 205 EHK-LQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLE--RANQRAE--VAQREAETLREQLSSANHSLQlaS 279
Cdd:pfam07111 138 SQReLEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkRAGEAKQlaEAQKEAELLRKQLSKTQEELE--A 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 280 QIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQ---------ASLTKLRENSASQISQL-EQQLNAKNSTLKQ 349
Cdd:pfam07111 216 QVTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQedradlqatVELLQVRVQSLTHMLALqEEELTRKIQPSDS 295
|
..
gi 601983272 350 LE 351
Cdd:pfam07111 296 LE 297
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
72-372 |
3.59e-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: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 72 QGEIDALSKRSKEAEAAFLTVYKRLIDVPDPVPAL-----DVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ 146
Cdd:pfam10174 344 QTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLageirDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKER 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 147 evtIKALKEKIREYEQTLKSQAETIAlEKE---QKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELF 223
Cdd:pfam10174 424 ---VKSLQTDSSNTDTALTTLEEALS-EKEriiERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLI 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 224 DLKtkydEETTAKADEieMIMTDLERANQRAEVAQREAETLReqlssanhslqLASQIQKAPDVAIEVLTRSSLEVELAA 303
Cdd:pfam10174 500 DLK----EHASSLASS--GLKKDSKLKSLEIAVEQKKEECSK-----------LENQLKKAHNAEEAVRTNPEINDRIRL 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 304 KEREIAQLVEDVQRLQASLTKL------RENSAS----QISQLE---------QQLNAKNSTLKQLEEKLKGQADYEEVK 364
Cdd:pfam10174 563 LEQEVARYKEESGKAQAEVERLlgilreVENEKNdkdkKIAELEsltlrqmkeQNKKVANIKHGQQEMKKKGAQLLEEAR 642
|
....*...
gi 601983272 365 KELNTLKS 372
Cdd:pfam10174 643 RREDNLAD 650
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
110-372 |
4.76e-05 |
|
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: 48.09 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 110 QQLEIKVQRL-HDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIReyeqTLKSQaETIALEKEQKLQND--FAEK 186
Cdd:TIGR04523 36 KQLEKKLKTIkNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIK----DLNDK-LKKNKDKINKLNSDlsKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 187 ERKLQETQMSTT----SKLE----EAEHKLQTLQTALEKTRTELFDLKTKYDEETTakadEIEMIMTDLERANQRAEVAQ 258
Cdd:TIGR04523 111 EIKNDKEQKNKLevelNKLEkqkkENKKNIDKFLTEIKKKEKELEKLNNKYNDLKK----QKEELENELNLLEKEKLNIQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 259 REAETLREQLSSANHSL-QLASQIQKAPDVAIEVL----TRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQI 333
Cdd:TIGR04523 187 KNIDKIKNKLLKLELLLsNLKKKIQKNKSLESQISelkkQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIK 266
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 601983272 334 SQLE---QQLNAKNSTLKQLEEKLKgqadyeEVKKELNTLKS 372
Cdd:TIGR04523 267 KQLSekqKELEQNNKKIKELEKQLN------QLKSEISDLNN 302
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
119-376 |
5.05e-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: 47.89 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 119 LHDIETENQKLRET----LEEYNKEFAEVKNQEVTIKALKEKIREYEQTL-KSQAETIALE-KEQKLQNDFAEKERKLQE 192
Cdd:pfam10174 249 IRDLEDEVQMLKTNgllhTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELsKKESELLALQtKLETLTNQNSDCKQHIEV 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 193 TQMSTTSKleeaEHKLQTLQTALEKTRTEL------FDLKTKY----DEETTAKADEIEMIMTDLERANQRAEVAQREAE 262
Cdd:pfam10174 329 LKESLTAK----EQRAAILQTEVDALRLRLeekesfLNKKTKQlqdlTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 263 TLREQLSSANhslqlaSQIQKAPDVAIEVLTRSS--------LEVELAAKEREIAQLVEDVQRLQ-------ASLTKLRE 327
Cdd:pfam10174 405 NLQEQLRDKD------KQLAGLKERVKSLQTDSSntdtalttLEEALSEKERIIERLKEQREREDrerleelESLKKENK 478
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 601983272 328 NSASQISQLEQQLNAKNSTLKQLEEKLKGQADyEEVKKElNTLKSMEFA 376
Cdd:pfam10174 479 DLKEKVSALQPELTEKESSLIDLKEHASSLAS-SGLKKD-SKLKSLEIA 525
|
|
| COG5576 |
COG5576 |
Homeodomain-containing transcription factor [Transcription]; |
1229-1286 |
5.86e-05 |
|
Homeodomain-containing transcription factor [Transcription];
Pssm-ID: 227863 [Multi-domain] Cd Length: 156 Bit Score: 45.12 E-value: 5.86e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 601983272 1229 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRRE 1286
Cdd:COG5576 52 KSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKKK 109
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
119-374 |
6.82e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 119 LHDIETENQKLRETLEEYNKEFAEVKNQEVtIKALKEKIREYEQTLKSQAETIALEKEQKlqndfAEKERKLQEtqmstt 198
Cdd:PRK03918 141 LESDESREKVVRQILGLDDYENAYKNLGEV-IKEIKRRIERLEKFIKRTENIEELIKEKE-----KELEEVLRE------ 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 199 skLEEAEHKLQTLQTALEKTRTELFDLKtKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLA 278
Cdd:PRK03918 209 --INEISSELPELREELEKLEKEVKELE-ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 279 SQIQKapdVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKlrensasQISQLEQqlnaKNSTLKQLEEKLKG-Q 357
Cdd:PRK03918 286 KELKE---KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE-------RIKELEE----KEERLEELKKKLKElE 351
|
250 260
....*....|....*....|
gi 601983272 358 ADYEEVK---KELNTLKSME 374
Cdd:PRK03918 352 KRLEELEerhELYEEAKAKK 371
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
21-246 |
9.48e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 9.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 21 QRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEaafltvykrlidvP 100
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE-------------E 1658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 101 DPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKsqAETIALEKEQKLQ 180
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK--AEEENKIKAEEAK 1736
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 601983272 181 NDFAEKERKLQETQmsttsKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTD 246
Cdd:PTZ00121 1737 KEAEEDKKKAEEAK-----KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
114-325 |
9.49e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 9.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 114 IKVQRLHdIETENQKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKSQAETIalekeQKLQNDFAEKERK 189
Cdd:PHA02562 197 IKTYNKN-IEEQRKKNGENIARKQNKYDELVEEAKTIKAeieeLTDELLNLVMDIEDPSAAL-----NKLNTAAAKIKSK 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 190 LQ----ETQMST--------TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETtakadeiemimtdlERANQRAEvA 257
Cdd:PHA02562 271 IEqfqkVIKMYEkggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELE--------------EIMDEFNE-Q 335
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 601983272 258 QREAETLREQLSSANHSLQLASQIQKAPDVAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKL 325
Cdd:PHA02562 336 SKKLLELKNKISTNKQSLITLVDKAKKVKAAIE-----ELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
696-941 |
1.05e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 47.00 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 696 ILQQARREMEAQQAALDPALKPAPLSQPdltiltpkhLSASPMSTVSTYPPLAISLKKTPAAPETSTAALPSAPALKKEA 775
Cdd:PRK10263 292 VLFSGNRATQPEYDEYDPLLNGAPITEP---------VAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVAWQP 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 776 QDVPTLDPPGSADAAQGvLRPMKSELVRGSTWKDPWWSPIQPERRNLTSSEETKADETTASGKERAGSSQPRAERSQLQG 855
Cdd:PRK10263 363 VPGPQTGEPVIAPAPEG-YPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQP 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 856 PSASA-------EYWKEWPSAEsPYSQSSELSLTGASRSETPQNSPLPSSPIVPMAKPAKPSVPPLtpeqyevYMYQEVD 928
Cdd:PRK10263 442 VAGNAwqaeeqqSTFAPQSTYQ-TEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPPL-------YYFEEVE 513
|
250
....*....|...
gi 601983272 929 tiELTRQVKEKLA 941
Cdd:PRK10263 514 --EKRAREREQLA 524
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
49-367 |
1.14e-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: 46.89 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 49 SREFKKNtpEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDpvpALDVGQQLEIKVQRLHDIETENQK 128
Cdd:TIGR00618 183 LMEFAKK--KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLRE---ALQQTQQSHAYLTQKREAQEEQLK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 129 LRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEK--------EQKLQNDFAEKERKLQETQ--MSTT 198
Cdd:TIGR00618 258 KQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQieqqaqriHTELQSKMRSRAKLLMKRAahVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 199 SKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADE--IEMIMTDLERANQRAEVAQREAETLREQLSSAN--HS 274
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTqhIHTLQQQKTTLTQKLQSLCKELDILQREQATIDtrTS 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 275 LQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLREnsasqisqLEQQLNAKNSTLKQLEEKL 354
Cdd:TIGR00618 418 AFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKE--------REQQLQTKEQIHLQETRKK 489
|
330
....*....|...
gi 601983272 355 KGQADYEEVKKEL 367
Cdd:TIGR00618 490 AVVLARLLELQEE 502
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
13-374 |
1.15e-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: 46.96 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 13 KRFD-LQQLQRELDATATVLANRQDESE-----QSRKRLIEQSREFKKNTPEDLRKQVAPL------LKSFQGEIDALSK 80
Cdd:TIGR00606 173 QKFDeIFSATRYIKALETLRQVRQTQGQkvqehQMELKYLKQYKEKACEIRDQITSKEAQLessreiVKSYENELDPLKN 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 81 RSKEAEAAFLTVYKrlidvpdpvpaldvgqqLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtIKALKE----K 156
Cdd:TIGR00606 253 RLKEIEHNLSKIMK-----------------LDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQ--LNDLYHnhqrT 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 157 IREYEQTL-KSQAETIALEKEQKLQNdfaeKERKLQETQMSTTSkLEEAEHKLQTLQTALEK----TRTELFDLKTKYDE 231
Cdd:TIGR00606 314 VREKERELvDCQRELEKLNKERRLLN----QEKTELLVEQGRLQ-LQADRHQEHIRARDSLIqslaTRLELDGFERGPFS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 232 ETTAK----------ADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEvLTRSSLEvEL 301
Cdd:TIGR00606 389 ERQIKnfhtlvierqEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELK-FVIKELQ-QL 466
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 601983272 302 AAKEREIAQLVEDVQRLQASLTKLRENSASQiSQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSME 374
Cdd:TIGR00606 467 EGSSDRILELDQELRKAERELSKAEKNSLTE-TLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQME 538
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
16-356 |
1.15e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 16 DLQQLQRELDATATVLANRQDESEQSRKRL------------IEQSREFKKNTPEDLRKQVApLLKSFQGEIDALSKRSK 83
Cdd:PRK04863 308 RLVEMARELAELNEAESDLEQDYQAASDHLnlvqtalrqqekIERYQADLEELEERLEEQNE-VVEEADEQQEENEARAE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 84 EAEAAFLTVYKRLIDVpdpVPALDVGQ----QLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtiKALKEKIRE 159
Cdd:PRK04863 387 AAEEEVDELKSQLADY---QQALDVQQtraiQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKE---QEATEELLS 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 160 YEQTLkSQAETIALEKEQKLQ---------------NDFAEKERKLQETQMSTTSkLEEAEHKLQTLQTALEKTRTeLFD 224
Cdd:PRK04863 461 LEQKL-SVAQAAHSQFEQAYQlvrkiagevsrseawDVARELLRRLREQRHLAEQ-LQQLRMRLSELEQRLRQQQR-AER 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 225 LKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL-QLASQIQK----APD--VAIEVLTRSSL 297
Cdd:PRK04863 538 LLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLeQLQARIQRlaarAPAwlAAQDALARLRE 617
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 601983272 298 EVELAAKERE-IAQLVEDVQRLQASLTKLRENSASQISQLEQQLN-------AKNSTLKQLEEKLKG 356
Cdd:PRK04863 618 QSGEEFEDSQdVTEYMQQLLERERELTVERDELAARKQALDEEIErlsqpggSEDPRLNALAERFGG 684
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
122-352 |
1.21e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 122 IETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYeqtlKSQAETIALEKEQKLqndFAEKERKLQETQMSTTSKL 201
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKE---LEEAEAALEEF----RQKNGLVDLSEEAKL---LLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 202 EEAEHKLQTLQTALEKT----------------RTELFDLKTKYDEE-TTAKADEIEMIMTDLERANQRAEVAQREAETL 264
Cdd:COG3206 236 AEAEARLAALRAQLGSGpdalpellqspviqqlRAQLAELEAELAELsARYTPNHPDVIALRAQIAALRAQLQQEAQRIL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 265 REQLSSANHSLQLASQIQKApdvaIEVLTRSSLEveLAAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLNAKN 344
Cdd:COG3206 316 ASLEAELEALQAREASLQAQ----LAQLEARLAE--LPELEAELRRLEREVEVARELYESLLQ----RLEEARLAEALTV 385
|
....*...
gi 601983272 345 STLKQLEE 352
Cdd:COG3206 386 GNVRVIDP 393
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
164-366 |
1.40e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 164 LKSQAETIALEKEQKlqndfAEKerklqetqmsttsKLEEAEHKLQTL-QTALEKTRTELFDLKTKYDEETTAKADEIEm 242
Cdd:PRK12704 25 RKKIAEAKIKEAEEE-----AKR-------------ILEEAKKEAEAIkKEALLEAKEEIHKLRNEFEKELRERRNELQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 243 imtDLERANQraevaQREaETLREQLSSANHSlqlasqiqkapdvaievltrsslEVELAAKEREIAQLVEDVQRLQASL 322
Cdd:PRK12704 86 ---KLEKRLL-----QKE-ENLDRKLELLEKR-----------------------EEELEKKEKELEQKQQELEKKEEEL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 601983272 323 TKLREnsaSQISQLEQ--QLN---AKNSTLKQLEEKLKGQA-----DYEEVKKE 366
Cdd:PRK12704 134 EELIE---EQLQELERisGLTaeeAKEILLEKVEEEARHEAavlikEIEEEAKE 184
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
123-362 |
2.20e-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: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 123 ETENQKLRETLEEYNKEFAEV--KNQEVTikalKEKIREYEQTlksQAETIALEKEQKLQNDFAEKERKLQETQMSTTSK 200
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELekKHQQLC----EEKNALQEQL---QAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 201 LEEAEHKLQTLQTALEKTRTELFDLKTKYDEE-------------TTAKADEIEMIMTDLERANQRaevAQREAETLREQ 267
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEeaarqklqlekvtTEAKIKKLEEDILLLEDQNSK---LSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 268 LSsaNHSLQLASQIQKAPDVAI------------------EVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLR--- 326
Cdd:pfam01576 161 IS--EFTSNLAEEEEKAKSLSKlknkheamisdleerlkkEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRaql 238
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 601983272 327 ----ENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEE 362
Cdd:pfam01576 239 akkeEELQAALARLEEETAQKNNALKKIRELEAQISELQE 278
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
17-232 |
2.73e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 17 LQQLQRELDATATVLA---------NRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPL---LKSFQGEIDALSKRSKE 84
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSriearlreiEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIekeIENLNGKKEELEEELEE 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 85 AEAAFLTVYKRLIDVPDPVPALDvgQQLEIKVQRLHDIETENQKLRETLEEynkefaevknQEVTIKALKEKIREYEQTL 164
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELE--AQLRELERKIEELEAQIEKKRKRLSE----------LKAKLEALEEELSEIEDPK 940
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 601983272 165 KS----QAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQ---TALEKTRTELFDLKTKYDEE 232
Cdd:TIGR02169 941 GEdeeiPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKekrAKLEEERKAILERIEEYEKK 1015
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
141-357 |
2.82e-04 |
|
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: 44.21 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 141 AEVKNQEVTIKALKEKIREYEQTL----KSQAETIALEKEQKLQNDFAEKERKLQE------TQMSTTSKLEEAEHKLQT 210
Cdd:pfam12795 3 DELEKAKLDEAAKKKLLQDLQQALslldKIDASKQRAAAYQKALDDAPAELRELRQelaalqAKAEAAPKEILASLSLEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 211 LQTALEKTRTELFDLKTKYDEETtakaDEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQkapdvaie 290
Cdd:pfam12795 83 LEQRLLQTSAQLQELQNQLAQLN----SQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQ-------- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 601983272 291 vltRSSLEVELAAKEREIAQLvedvQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQ 357
Cdd:pfam12795 151 ---RWALQAELAALKAQIDML----EQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQALQELLNEK 210
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
60-266 |
2.91e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 60 LRKQVAPLLKSFQgEIDALSKRSKEAEAAFLTVYKR--LIDVPDPVPALDVGQQLEIKVQRLHDIETENQKLR------- 130
Cdd:COG4717 293 LAREKASLGKEAE-ELQALPALEELEEEELEELLAAlgLPPDLSPEELLELLDRIEELQELLREAEELEEELQleeleqe 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 131 --ETLEEYN----KEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIaleKEQKLQNDFAEKERKLQETQMsttsKLEEA 204
Cdd:COG4717 372 iaALLAEAGvedeEELRAALEQAEEYQELKEELEELEEQLEELLGEL---EELLEALDEEELEEELEELEE----ELEEL 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 601983272 205 EHKLQTLQTALEKTRTELFDLKTkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLRE 266
Cdd:COG4717 445 EEELEELREELAELEAELEQLEE--DGELAELLQELEELKAELRELAEEWAALKLALELLEE 504
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
28-410 |
3.14e-04 |
|
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: 45.27 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 28 ATVLANRQDESEQSRKRLIeQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTvykrlidvpdpvpALD 107
Cdd:pfam07888 29 AELLQNRLEECLQERAELL-QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQ-------------SRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 108 VGQQLEIKVQRLHDIETENQKLRETLEEYNKE-FAEVKNQEVTIKALKEKIREYEQTLKSQAETIalEKEQKLQNDFAEK 186
Cdd:pfam07888 95 KHEELEEKYKELSASSEELSEEKDALLAQRAAhEARIRELEEDIKTLTQRVLERETELERMKERA--KKAGAQRKEEEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 187 ERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLK----TKYDEETTA--KADEIEMIMTDLERANQRAEVAQRE 260
Cdd:pfam07888 173 RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQdtitTLTQKLTTAhrKEAENEALLEELRSLQERLNASERK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 261 AETLREQLSSanhslqLASQiqkapdvaievltRSSLEVELAAKEREIAQLveDVQRLQASLtKLRENSASQISQLEQQL 340
Cdd:pfam07888 253 VEGLGEELSS------MAAQ-------------RDRTQAELHQARLQAAQL--TLQLADASL-ALREGRARWAQERETLQ 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 601983272 341 NA----KNSTLKQLEEKLKGQADYEEVKKELNTLKsmefapSEGAGTQDSTKpleVLLLEKNRSLQSENATLRI 410
Cdd:pfam07888 311 QSaeadKDRIEKLSAELQRLEERLQEERMEREKLE------VELGREKDCNR---VQLSESRRELQELKASLRV 375
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
174-428 |
3.18e-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: 45.12 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 174 EKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRtELFDLKTKYDEETTAKADEIEMIMTDLERANQR 253
Cdd:pfam05557 48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLN-EKESQLADAREVISCLKNELSELRRQIQRAELE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 254 AEVAQREAETLREQL----SSANHSLQLASQIQKAPDVAIEVLTR-SSLEVELAAKERE-------------IAQLVEDV 315
Cdd:pfam05557 127 LQSTNSELEELQERLdllkAKASEAEQLRQNLEKQQSSLAEAEQRiKELEFEIQSQEQDseivknskselarIPELEKEL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 316 QRLQASLTKLRENSASqISQLEQQLNAKNSTLKQLE----EKLKGQADYEEVKKELNTLKSMefapsegAGTQDSTKPLE 391
Cdd:pfam05557 207 ERLREHNKHLNENIEN-KLLLKEEVEDLKRKLEREEkyreEAATLELEKEKLEQELQSWVKL-------AQDTGLNLRSP 278
|
250 260 270
....*....|....*....|....*....|....*..
gi 601983272 392 VLLLEKNRSLQSENATLRISNSDLSGSARRKGRDQPE 428
Cdd:pfam05557 279 EDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRE 315
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
717-917 |
3.36e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.70 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 717 PAPLSQPDLTILTPKhlSASPMSTVSTYPPLAISLKKTPAAPETSTAALPSAPALKKEAQDVPTLDPPGSADAAQGVLRP 796
Cdd:PHA03247 2754 PARPARPPTTAGPPA--PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP 2831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 797 MKSELVRGSTWKDPWWSPIQPERRNLTSSEETKADETTASGKERAGSSQPRAERSQLQGPSASAEywkewPSAESPYSQS 876
Cdd:PHA03247 2832 TSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTE-----SFALPPDQPE 2906
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 601983272 877 SELSLTGASRSETPQNSPLPSSPIVPMAKPAKPSvPPLTPE 917
Cdd:PHA03247 2907 RPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQ-PPLAPT 2946
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
23-371 |
3.84e-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: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 23 ELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLR----------KQVAPLLKSFQGEIDALSKRSKE---AEAAF 89
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNdlyhnhqrtvREKERELVDCQRELEKLNKERRLlnqEKTEL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 90 LTVYKRLIDVPDPVPALDVGQQLEIKVQRLH------------DIETEN--QKLRETLEEYNKEFAEVKNQEVTIKALKE 155
Cdd:TIGR00606 346 LVEQGRLQLQADRHQEHIRARDSLIQSLATRleldgfergpfsERQIKNfhTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 156 K-IREYEQTLKSQAETIALEKE--QKLQNDFAEKERKLQ--ETQMSTTSKLEEAEHK-LQTLQTALEKTRTElfdlkTKY 229
Cdd:TIGR00606 426 EqADEIRDEKKGLGRTIELKKEilEKKQEELKFVIKELQqlEGSSDRILELDQELRKaERELSKAEKNSLTE-----TLK 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 230 DEETTAKADEIEMIMTdLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLT--------RSSLEVEL 301
Cdd:TIGR00606 501 KEVKSLQNEKADLDRK-LRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTsllgyfpnKKQLEDWL 579
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 302 AAKEREIAQLVEDVQRLQASLTKLRENSasqiSQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLK 371
Cdd:TIGR00606 580 HSKSKEINQTRDRLAKLNKELASLEQNK----NHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLK 645
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
33-374 |
4.35e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 33 NRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEA----------EAAFLTVYKRLIDVPDP 102
Cdd:PTZ00121 1087 NRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDArkaeearkaeDAKRVEIARKAEDARKA 1166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 103 VPALDVGQQLEIKVQRLHDIETENQKLRETLE----EYNKEFAEVKNQEVTIKALKEK----IREYEQTLKSQAETIALE 174
Cdd:PTZ00121 1167 EEARKAEDAKKAEAARKAEEVRKAEELRKAEDarkaEAARKAEEERKAEEARKAEDAKkaeaVKKAEEAKKDAEEAKKAE 1246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 175 KEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTElfDLK----TKYDEETTAKADEIEmimtDLERA 250
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD--EAKkaeeKKKADEAKKKAEEAK----KADEA 1320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 251 NQRAEVAQREAETLREQlssanhslqlASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSA 330
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKK----------AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK 1390
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 601983272 331 SQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSME 374
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAD 1434
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
117-341 |
5.21e-04 |
|
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: 43.48 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 117 QRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKsQAETIALEKEQKL-----QNDFAEKERK-L 190
Cdd:pfam00261 8 EELDEAEERLKEAMKKLEEAEKRAEKAEAE---VAALNRRIQLLEEELE-RTEERLAEALEKLeeaekAADESERGRKvL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 191 QETQMSTTSKLEEAEHKL-QTLQTALEKTRtelfdlktKYDEettaKADEIEMIMTDLERANQRAEVAQREAETLREQLS 269
Cdd:pfam00261 84 ENRALKDEEKMEILEAQLkEAKEIAEEADR--------KYEE----VARKLVVVEGDLERAEERAELAESKIVELEEELK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 270 SANHSLQ-LASQIQKAPD------VAIEVLTRSSLEVELAAK--EREIAQLVEDVQRLQASLTKLRENSASQISQLEQQL 340
Cdd:pfam00261 152 VVGNNLKsLEASEEKASEredkyeEQIRFLTEKLKEAETRAEfaERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTL 231
|
.
gi 601983272 341 N 341
Cdd:pfam00261 232 A 232
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
22-359 |
5.25e-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: 44.73 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 22 RELDATATVLANRQDESEQSRKRLIEQSREFKK---------NTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAF--- 89
Cdd:pfam05557 51 QELQKRIRLLEKREAEAEEALREQAELNRLKKKylealnkklNEKESQLADAREVISCLKNELSELRRQIQRAELELqst 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 90 ---LTVYKRLIDVPDP--VPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKN--QEV----TIKALKEKIR 158
Cdd:pfam05557 131 nseLEELQERLDLLKAkaSEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNskSELaripELEKELERLR 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 159 EYEQTLKSQAETIALEKEQKlqndfAEKERKLqetqmsttSKLEEAEHKLQTLQTALEKTRTELfdlktkYDEETTAKAD 238
Cdd:pfam05557 211 EHNKHLNENIENKLLLKEEV-----EDLKRKL--------EREEKYREEAATLELEKEKLEQEL------QSWVKLAQDT 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 239 EIEMIMTDLERAnqRAEVAQREAETLREQLSSANHSlqlASQIQKA-PDVAIEVLTRSSLEVELAAKEREIAQLVEDVQR 317
Cdd:pfam05557 272 GLNLRSPEDLSR--RIEQLQQREIVLKEENSSLTSS---ARQLEKArRELEQELAQYLKKIEDLNKKLKRHKALVRRLQR 346
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 601983272 318 LQASLTKLRENSASQISQLEQQLNAKNSTlKQLEEKLKGQAD 359
Cdd:pfam05557 347 RVLLLTKERDGYRAILESYDKELTMSNYS-PQLLERIEEAED 387
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
117-222 |
5.33e-04 |
|
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: 42.97 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 117 QRLHDIETENQKLRETLEE--------------YNKEFAEVKNQEVTIKALKEKIR--EYEQTLKSQaetiALEKEQKLQ 180
Cdd:pfam13851 47 KLMSEIQQENKRLTEPLQKaqeeveelrkqlenYEKDKQSLKNLKARLKVLEKELKdlKWEHEVLEQ----RFEKVERER 122
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 601983272 181 NDFAEK-ERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTEL 222
Cdd:pfam13851 123 DELYDKfEAAIQDVQQKTGLKNLLLEKKLQALGETLEKKEAQL 165
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
23-359 |
5.67e-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: 44.78 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 23 ELDATATVLANRQDESEQSRKRLIEQSREF--KKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVP 100
Cdd:pfam01576 388 ELQAELRTLQQAKQDSEHKRKKLEGQLQELqaRLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLE 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 101 DPVPalDVGQQLEIKVQ-------RLHDIETENQKLRETLEEynkEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIAL 173
Cdd:pfam01576 468 SQLQ--DTQELLQEETRqklnlstRLRQLEDERNSLQEQLEE---EEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 174 EKEQKlqndfaekeRKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYD---------EETTAKAD----EI 240
Cdd:pfam01576 543 LEEGK---------KRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDhqrqlvsnlEKKQKKFDqmlaEE 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 241 EMIMTDLERANQRAEVAQREAETlreqlssanHSLQLASQIQKAPDvaievlTRSSLEVELAAKEREIAQLV---EDVQR 317
Cdd:pfam01576 614 KAISARYAEERDRAEAEAREKET---------RALSLARALEEALE------AKEELERTNKQLRAEMEDLVsskDDVGK 678
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 601983272 318 LQASLTKLREnsasqisQLEQQLNAKNSTLKQLEEKLKGQAD 359
Cdd:pfam01576 679 NVHELERSKR-------ALEQQVEEMKTQLEELEDELQATED 713
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
29-417 |
7.53e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 44.27 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 29 TVLANRQDESEQSRKRLiEQSREFKknTPEDlrkqvAPLLKSFQGEIDALSKRSKEAEAAflTVYKRLIDvpdpvpaldv 108
Cdd:PRK10929 16 GAYAATAPDEKQITQEL-EQAKAAK--TPAQ-----AEIVEALQSALNWLEERKGSLERA--KQYQQVID---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 109 gqqleikvqrlhDIETENQKLRETLEEYNKEFAEVkNQEVTIKALKEKIREYEQTLKSQAETiaLEKEQKLQNDFAEKER 188
Cdd:PRK10929 76 ------------NFPKLSAELRQQLNNERDEPRSV-PPNMSTDALEQEILQVSSQLLEKSRQ--AQQEQDRAREISDSLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 189 KLQETQMSTTSKLEEAEHKLQTL--------QTALEKTRTELFDLKtkydeettAKADEIEMIMTDL----ERANQRAEV 256
Cdd:PRK10929 141 QLPQQQTEARRQLNEIERRLQTLgtpntplaQAQLTALQAESAALK--------ALVDELELAQLSAnnrqELARLRSEL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 257 AQREAETLREQLSSANHslQLASQIQKAPDVAIEvltrsslEVELAAKE---------------REIAQ-LVEDVQRLQA 320
Cdd:PRK10929 213 AKKRSQQLDAYLQALRN--QLNSQRQREAERALE-------STELLAEQsgdlpksivaqfkinRELSQaLNQQAQRMDL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 321 SLTKLREnSASQISQLEQQLN-----------------AKNSTLKQLEEKLKGQA-DYEEVKKELNTLK---SMEFAPSE 379
Cdd:PRK10929 284 IASQQRQ-AASQTLQVRQALNtlreqsqwlgvsnalgeALRAQVARLPEMPKPQQlDTEMAQLRVQRLRyedLLNKQPQL 362
|
410 420 430
....*....|....*....|....*....|....*....
gi 601983272 380 GAGTQDSTKPLEVlllEKNRSLQSENATLR-ISNSDLSG 417
Cdd:PRK10929 363 RQIRQADGQPLTA---EQNRILDAQLRTQReLLNSLLSG 398
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
111-408 |
7.80e-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: 44.27 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 111 QLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKireyeqtlKSQAETIALEKEQKLQNDFAEKERKL 190
Cdd:TIGR00606 232 QLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR--------KKQMEKDNSELELKMEKVFQGTDEQL 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 191 QETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADeiEMIMTDLERANQRAEVAQREAETLREQLSS 270
Cdd:TIGR00606 304 NDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGR--LQLQADRHQEHIRARDSLIQSLATRLELDG 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 271 ANHSLQLASQIQKAPDVAIEVLTR-----SSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNS 345
Cdd:TIGR00606 382 FERGPFSERQIKNFHTLVIERQEDeaktaAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIK 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 601983272 346 TLKQLEEKLKG--QADYEEVKKELNTLKSMEFAPSEGAGTQD-STKPLEVLLLEKNRSLQSENATL 408
Cdd:TIGR00606 462 ELQQLEGSSDRilELDQELRKAERELSKAEKNSLTETLKKEVkSLQNEKADLDRKLRKLDQEMEQL 527
|
|
| iSH2_PIK3R2 |
cd12926 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
108-248 |
8.62e-04 |
|
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: 41.61 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 108 VGQQLEIKVQRLHDIETENQKLretLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQaetialekeQKLQNDFAEKE 187
Cdd:cd12926 6 VGAQLKVYHQQYQDKSREYDQL---YEEYTRTSQELQMKRTAIEAFNETIKIFEEQGQTQ---------EKCSKEYLERF 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 601983272 188 RKlqetqmsttsklEEAEHKLQTLQTALEKTR---TELFDLKTKYDEETTAKAD---EIEMIMTDLE 248
Cdd:cd12926 74 RR------------EGNEKEMQRILLNSERLKsriAEIHESRTKLEQDLRAQASdnrEIDKRMNSLK 128
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
131-388 |
9.12e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 9.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 131 ETLEEYNKEFAEVKNQEVtIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKER------------KLQETQMSTT 198
Cdd:PTZ00121 1030 EELTEYGNNDDVLKEKDI-IDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDnradeateeafgKAEEAKKTET 1108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 199 SKLEEAEHKLQTLQTALEKTRTELF---DLKTKYDEETTAKADEIEMIMTDLERAnQRAEVAQREAETLREQLSSANHSL 275
Cdd:PTZ00121 1109 GKAEEARKAEEAKKKAEDARKAEEArkaEDARKAEEARKAEDAKRVEIARKAEDA-RKAEEARKAEDAKKAEAARKAEEV 1187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 276 QLASQIQKAPDV-AIEVL-----TRSSLEVELAAKEREIAQL--VEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTL 347
Cdd:PTZ00121 1188 RKAEELRKAEDArKAEAArkaeeERKAEEARKAEDAKKAEAVkkAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFAR 1267
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 601983272 348 KQLEEKLKGQADYEEVKKELNTLKSMEFAPSEGAGTQDSTK 388
Cdd:PTZ00121 1268 RQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAK 1308
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
118-431 |
9.29e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 43.88 E-value: 9.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 118 RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALkEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQmST 197
Cdd:PTZ00108 1047 RFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEEL-GAAVSYDYLLSMPIWSLTKEKVEKLNAELEKKEKELEKLK-NT 1124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 198 TSK---LEEaehkLQTLQTALEKTRtelfdlktKYDEETTAKADEIEMIMTDLERANQRAEvAQREAETLREqlSSANHS 274
Cdd:PTZ00108 1125 TPKdmwLED----LDKFEEALEEQE--------EVEEKEIAKEQRLKSKTKGKASKLRKPK-LKKKEKKKKK--SSADKS 1189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 275 LQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKL 354
Cdd:PTZ00108 1190 KKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEG 1269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 355 KGQADYEE---VKKELNTLKSMEFAPSEGAGTQDST------KPLEVLLLEKNRSLQSENATLRISNSD---LSGSARRK 422
Cdd:PTZ00108 1270 KPKNAPKRvsaVQYSPPPPSKRPDGESNGGSKPSSPtkkkvkKRLEGSLAALKKKKKSEKKTARKKKSKtrvKQASASQS 1349
|
....*....
gi 601983272 423 GRDQPESRR 431
Cdd:PTZ00108 1350 SRLLRRPRK 1358
|
|
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
111-409 |
9.75e-04 |
|
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: 43.05 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 111 QLEIKVQRLhDIET-ENQKLRETlEEYNKEfaevknqevtIKALKEKIREYEQTLKSQAETIA---LEKEQKLQNDFAEK 186
Cdd:pfam14915 5 QDEIAMLRL-EIDTiKNQNQEKE-KKYLED----------IEILKEKNDDLQKTLKLNEETLTktvFQYNGQLNVLKAEN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 187 ERklqetqmsTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKadeiemimTDLERANQRaevAQREAETLRE 266
Cdd:pfam14915 73 TM--------LNSKLENEKQNKERLETEVESYRSRLAAAIQDHEQSQTSK--------RDLELAFQR---ERDEWLRLQD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 267 QLSSanhslqlasqiqkapDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASltkLRENSaSQISQLEQQLNAKNST 346
Cdd:pfam14915 134 KMNF---------------DVSNLRDENEILSQQLSKAESKANSLENELHRTRDA---LREKT-LLLESVQRDLSQAQCQ 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 601983272 347 LKQLEEKLkgQADYEEVKKELNTLKSMEfapsegagtqdstkplevlllEKNRSLQSENATLR 409
Cdd:pfam14915 195 KKELEHMY--QNEQDKVNKYIGKQESLE---------------------ERLAQLQSENMLLR 234
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
129-355 |
1.05e-03 |
|
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: 43.15 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 129 LRETLEEYNKEFAEVknqevtIKALKEKIREYEQTLKSQAETIAL------EKEQKLQNDFAEkERKLQETQMSTTSKLE 202
Cdd:pfam04108 54 LEKVLNELKKDFKQL------LKDLDAALERLEETLDKLRNTPVEpalppgEEKQKTLLDFID-EDSVEILRDALKELID 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 203 EAEHKLQTLQTALEKTRTELFDLKtKYDEETTAKADEIEMIMTDLERANQRAEvaqrEAETLREQLssANH---SLQLAS 279
Cdd:pfam04108 127 ELQAAQESLDSDLKRFDDDLRDLQ-KELESLSSPSESISLIPTLLKELESLEE----EMASLLESL--TNHydqCVTAVK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 280 QIQKAPDVAIEVLTRSSLEV-----ELAAKEREIAQLVEDVQRLQASLTKLRENSAS---QISQLEQQLNAKNSTLKQLE 351
Cdd:pfam04108 200 LTEGGRAEMLEVLENDARELddvvpELQDRLDEMENNYERLQKLLEQKNSLIDELLSalqLIAEIQSRLPEYLAALKEFE 279
|
....
gi 601983272 352 EKLK 355
Cdd:pfam04108 280 ERWE 283
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
133-351 |
1.12e-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: 42.82 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 133 LEEYNKEFAEVKNQEVTIKALKEKIReyeQTLK--SQAETIALEKEQKLQNDFAEKERKLQETQmsttskleeaehkLQT 210
Cdd:pfam09787 2 LESAKQELADYKQKAARILQSKEKLI---ASLKegSGVEGLDSSTALTLELEELRQERDLLREE-------------IQK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 211 LQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLasqiqkapdvaie 290
Cdd:pfam09787 66 LRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRR------------- 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 601983272 291 vlTRSSLEVELAAKEREIaqlvedvQRLQASLTkLRENSASQISQLEQQLNA------------------KNSTLKQLE 351
Cdd:pfam09787 133 --SKATLQSRIKDREAEI-------EKLRNQLT-SKSQSSSSQSELENRLHQltetliqkqtmlealsteKNSLVLQLE 201
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
297-371 |
1.14e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 297 LEVELAAKEREIAQLVEDVQRLQASLTKLRENS-------------------ASQISQLEQQ---LNAKNSTLKQLEEKL 354
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidvasaEREIAELEAElerLDASSDDLAALEEQL 694
|
90
....*....|....*...
gi 601983272 355 KG-QADYEEVKKELNTLK 371
Cdd:COG4913 695 EElEAELEELEEELDELK 712
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
16-192 |
1.30e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 16 DLQQLQRELDATATVLAN-------RQDESEQSRKRLIEQSREFkkntpEDLRKQvaplLKSFQGEIDALSKRSKEAEaa 88
Cdd:COG1579 11 DLQELDSELDRLEHRLKElpaelaeLEDELAALEARLEAAKTEL-----EDLEKE----IKRLELEIEEVEARIKKYE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 89 fltvyKRLIDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQA 168
Cdd:COG1579 80 -----EQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE---LAELEAELEEKKAELDEEL 151
|
170 180
....*....|....*....|....
gi 601983272 169 ETIAlEKEQKLQNDFAEKERKLQE 192
Cdd:COG1579 152 AELE-AELEELEAEREELAAKIPP 174
|
|
| Homeobox_KN |
pfam05920 |
Homeobox KN domain; This is a homeobox transcription factor KN domain conserved from fungi to ... |
1248-1282 |
1.31e-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: 37.88 E-value: 1.31e-03
10 20 30
....*....|....*....|....*....|....*
gi 601983272 1248 QQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSR 1282
Cdd:pfam05920 5 LHNPYPSEEEKAELAKETGLSRKQISNWFINARRR 39
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
17-354 |
1.39e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.29 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 17 LQQLQRELDATATVLANRQDESEQSRKRlIEQSREfkknTPEDLRKQVapLLKSFQ-GE-IDALSKRSKEAEAAFlTVYK 94
Cdd:PRK04778 114 LDLIEEDIEQILEELQELLESEEKNREE-VEQLKD----LYRELRKSL--LANRFSfGPaLDELEKQLENLEEEF-SQFV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 95 RLIDVPDPVPALDVGQQLEIKV------------------------------------------------QRLHDIETEN 126
Cdd:PRK04778 186 ELTESGDYVEAREILDQLEEELaaleqimeeipellkelqtelpdqlqelkagyrelveegyhldhldieKEIQDLKEQI 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 127 QKLRETLEEYNKEFAEVKNQEvtikaLKEKIRE-YEQtlksqaetiaLEKEQKLQNdfaekerklqetqmsttskleEAE 205
Cdd:PRK04778 266 DENLALLEELDLDEAEEKNEE-----IQERIDQlYDI----------LEREVKARK---------------------YVE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 206 HKLQTLQTALEKTRTELFDLKTKydeettakadeiemimtdLERANQRAEVAQREAETLR---EQLSSANHSLQLASQIQ 282
Cdd:PRK04778 310 KNSDTLPDFLEHAKEQNKELKEE------------------IDRVKQSYTLNESELESVRqleKQLESLEKQYDEITERI 371
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 601983272 283 KAPDVAIevltrSSLEVELAAKEREIAQLVEDVQRLQASLTKLR--ENSASQ-ISQLEQQLnaknSTLKQLEEKL 354
Cdd:PRK04778 372 AEQEIAY-----SELQEELEEILKQLEEIEKEQEKLSEMLQGLRkdELEAREkLERYRNKL----HEIKRYLEKS 437
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
127-270 |
1.46e-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: 42.56 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 127 QKLRETLEEYNKE-FAEVKNQEVTIKALKEKIREYE---QTLKSQAETIALEKEQKLQNDFAEKERK-LQETQMSTTSKL 201
Cdd:cd16269 149 EDREKLVEKYRQVpRKGVKAEEVLQEFLQSKEAEAEailQADQALTEKEKEIEAERAKAEAAEQERKlLEEQQRELEQKL 228
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 601983272 202 EEAEHKLQTLQTALEKtrtelfdlktKYDEETTAKADEIEMIMTDLERANQR--AEVAQREAETLREQLSS 270
Cdd:cd16269 229 EDQERSYEEHLRQLKE----------KMEEERENLLKEQERALESKLKEQEAllEEGFKEQAELLQEEIRS 289
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
34-372 |
1.63e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 43.09 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 34 RQDESEQSRKRLIEQSREFKKNTPE---DLRKQVAPLLKSFQ------GEIDALSKRSKEAEAAFLTVYKRLIDVPdPVP 104
Cdd:pfam05667 241 RKRKRTKLLKRIAEQLRSAALAGTEatsGASRSAQDLAELLSsfsgssTTDTGLTKGSRFTHTEKLQFTNEAPAAT-SSP 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 105 ALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQ-KLQNDF 183
Cdd:pfam05667 320 PTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTlDLLPDA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 184 AEKERKLQetqmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERanqraevaqreaet 263
Cdd:pfam05667 400 EENIAKLQ-------ALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKE-------------- 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 264 LREQlssanhslqlasqIQKAPDvaievltrsslevELAAKEREIAQLVEDVQRLQasltklRENSASQISQ--LEQQLN 341
Cdd:pfam05667 459 LREK-------------IKEVAE-------------EAKQKEELYKQLVAEYERLP------KDVSRSAYTRriLEIVKN 506
|
330 340 350
....*....|....*....|....*....|.
gi 601983272 342 AKnstlKQLEEKLKGQADYEEVKKELNTLKS 372
Cdd:pfam05667 507 IK----KQKEEITKILSDTKSLQKEINSLTG 533
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
111-359 |
1.64e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 42.97 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 111 QLEIKVQRLH-DIETENQKLRETLEEYNKEFA-EVKNQEVTIKALKEKIREyeqtLKSQAETIALEKeQKLQNDFAEKER 188
Cdd:pfam15964 364 ELERQKERLEkELASQQEKRAQEKEALRKEMKkEREELGATMLALSQNVAQ----LEAQVEKVTREK-NSLVSQLEEAQK 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 189 KLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQR-------EA 261
Cdd:pfam15964 439 QLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQdaarareEC 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 262 ETLREQLSSANHSLQLASQ----IQK--APDVAIEVLTRSSLEVELAAK-----------ERE-----------IAQLVE 313
Cdd:pfam15964 519 LKLTELLGESEHQLHLTRLekesIQQsfSNEAKAQALQAQQREQELTQKmqqmeaqhdktVNEqyslltsqntfIAKLKE 598
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 601983272 314 DVQRLQASLTKLRENSASQISQLEQQlnakNSTLKQLEEKLKGQAD 359
Cdd:pfam15964 599 ECCTLAKKLEEITQKSRSEVEQLSQE----KEYLQDRLEKLQKRNE 640
|
|
| BBC |
smart00502 |
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
127-217 |
1.80e-03 |
|
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
Pssm-ID: 128778 Cd Length: 127 Bit Score: 39.94 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 127 QKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKSQAETI--ALEK-EQKLQND----FAEKERKLQETQM 195
Cdd:smart00502 3 EALEELLTKLRKKAAELEDALKQLISiiqeVEENAADVEAQIKAAFDELrnALNKrKKQLLEDleeqKENKLKVLEQQLE 82
|
90 100
....*....|....*....|..
gi 601983272 196 STTSKLEEAEHKLQTLQTALEK 217
Cdd:smart00502 83 SLTQKQEKLSHAINFTEEALNS 104
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
12-206 |
1.99e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 12 WKRFDLQQLQRELDATATVLAN-------------RQDESEQSRKRLIEQSREFKKN--TPEDLRKQVAPLLKSFQGEID 76
Cdd:COG4913 658 WDEIDVASAEREIAELEAELERldassddlaaleeQLEELEAELEELEEELDELKGEigRLEKELEQAEEELDELQDRLE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 77 ALSKRSKEAEAAFLTvyKRLIDVPDPVPALDVGQQLEIKVQRLH-DIETENQKLRETLEEYNKEF-AEVKNQEVTIKALk 154
Cdd:COG4913 738 AAEDLARLELRALLE--ERFAAALGDAVERELRENLEERIDALRaRLNRAEEELERAMRAFNREWpAETADLDADLESL- 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 601983272 155 ekiREYEQTLKSQAETIALEKEQKLqndfaeKERKLQETQMSTT---SKLEEAEH 206
Cdd:COG4913 815 ---PEYLALLDRLEEDGLPEYEERF------KELLNENSIEFVAdllSKLRRAIR 860
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
17-416 |
2.01e-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: 42.73 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 17 LQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDlrkQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRL 96
Cdd:TIGR00606 739 IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEE---ESAKVCLTDVTIMERFQMELKDVERKIAQQAAKL 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 97 IDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEfaevknqevtIKALKEKIREyeqtLKSQAETIALEKE 176
Cdd:TIGR00606 816 QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQ----------IQHLKSKTNE----LKSEKLQIGTNLQ 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 177 QKLQndFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMI----------MTD 246
Cdd:TIGR00606 882 RRQQ--FEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIkekvknihgyMKD 959
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 247 LERANQraEVAQREAETLREQLSSANHSLQLASQIQK---------APDVAIEVLTRSSLEVELAAKEREiAQLVEDVQR 317
Cdd:TIGR00606 960 IENKIQ--DGKDDYLKQKETELNTVNAQLEECEKHQEkinedmrlmRQDIDTQKIQERWLQDNLTLRKRE-NELKEVEEE 1036
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 318 LQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKG-QADYEEVKKELNT-LKSMEFAPSEgagtqdstkplevlll 395
Cdd:TIGR00606 1037 LKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGrQKGYEKEIKHFKKeLREPQFRDAE---------------- 1100
|
410 420
....*....|....*....|.
gi 601983272 396 EKNRSLQSENATLRISNSDLS 416
Cdd:TIGR00606 1101 EKYREMMIVMRTTELVNKDLD 1121
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
204-372 |
2.28e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 204 AEHKLQTLQTALEKTRTELFDLKTKYDeettAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQL------ 277
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELD----ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreelg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 278 ----ASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEK 353
Cdd:COG3883 90 erarALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180
....*....|....*....|
gi 601983272 354 LKG-QADYEEVKKELNTLKS 372
Cdd:COG3883 170 KAElEAQQAEQEALLAQLSA 189
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
142-310 |
2.31e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 142 EVKNQEVTIKALKEKIREYEQTLksqaetiALEKEQKLQndfaekerkLQETQMSTTSKLEEAEH---KLQTLQTALEKT 218
Cdd:PRK09039 47 EISGKDSALDRLNSQIAELADLL-------SLERQGNQD---------LQDSVANLRASLSAAEAersRLQALLAELAGA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 219 RTELfdlkTKYDEETTAKADEIEMIMtdlERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRsSLE 298
Cdd:PRK09039 111 GAAA----EGRAGELAQELDSEKQVS---ARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGR-RLN 182
|
170
....*....|..
gi 601983272 299 VELAAKEREIAQ 310
Cdd:PRK09039 183 VALAQRVQELNR 194
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
115-371 |
2.32e-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: 42.63 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 115 KVQRLH-----------------DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQ 177
Cdd:COG3096 810 KLQRLHqafsqfvgghlavafapDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADE 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 178 KLQNDFAEKERKLQETQMSTTS------KLEEAEHKLQTLQT------ALEKTRTELFDLKTKYDEETTA---------- 235
Cdd:COG3096 890 TLADRLEELREELDAAQEAQAFiqqhgkALAQLEPLVAVLQSdpeqfeQLQADYLQAKEQQRRLKQQIFAlsevvqrrph 969
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 236 --KADEIEMIM--TDL-ERANQRAEVAQREAETLREQLSSANHSLQLASQIQKApdvaievlTRSSLEV---ELAAKERE 307
Cdd:COG3096 970 fsYEDAVGLLGenSDLnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLAS--------LKSSRDAkqqTLQELEQE 1041
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 601983272 308 IAQL------------VEDVQRLQASLTKLRensaSQISQLEQQLNAKNSTLKQLEEKL-KGQADYEEVKKELNTLK 371
Cdd:COG3096 1042 LEELgvqadaeaeeraRIRRDELHEELSQNR----SRRSQLEKQLTRCEAEMDSLQKRLrKAERDYKQEREQVVQAK 1114
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
288-428 |
2.41e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 288 AIEVLTRSSLEVEL-AAKEREIAQlVED---VQRLQASLTKLrensaSQISQLEQQLNAKNSTLKQLEEKLKgqadyeEV 363
Cdd:PRK11281 32 NGDLPTEADVQAQLdALNKQKLLE-AEDklvQQDLEQTLALL-----DKIDRQKEETEQLKQQLAQAPAKLR------QA 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 601983272 364 KKELNTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGSarrkgRDQPE 428
Cdd:PRK11281 100 QAELEALKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSL-----QTQPE 159
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
16-356 |
2.59e-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: 42.63 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 16 DLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKkntpeDLRKQVApllkSFQGEIDALSKRSKEAEAAF--LTVY 93
Cdd:COG3096 355 DLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVD-----SLKSQLA----DYQQALDVQQTRAIQYQQAVqaLEKA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 94 KRLIDVPDPVPALDVGQQLEIKV-------------QRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKAlKEKIREY 160
Cdd:COG3096 426 RALCGLPDLTPENAEDYLAAFRAkeqqateevleleQKLSVADAARRQFEKAYELVCKIAGEVERSQAWQTA-RELLRRY 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 161 --EQTLKSQAETIAL---EKEQKLQNDfAEKERKLQETQMSTTSKLEEAEhKLQTLQTALEKTRTELFDLKTKYDEETTA 235
Cdd:COG3096 505 rsQQALAQRLQQLRAqlaELEQRLRQQ-QNAERLLEEFCQRIGQQLDAAE-ELEELLAELEAQLEELEEQAAEAVEQRSE 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 236 KADEIEMIMTDLERANQRAEV---AQREAETLREQLSSA-NHSLQLASQIQkapdvaievltrsslevELAAKEREIAQL 311
Cdd:COG3096 583 LRQQLEQLRARIKELAARAPAwlaAQDALERLREQSGEAlADSQEVTAAMQ-----------------QLLEREREATVE 645
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 601983272 312 VEDVQRLQASLtklrensASQISQLEQQLNAKNSTLKQLEEKLKG 356
Cdd:COG3096 646 RDELAARKQAL-------ESQIERLSQPGGAEDPRLLALAERLGG 683
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
32-277 |
2.62e-03 |
|
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: 42.44 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 32 ANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVpdpvpaldVGQQ 111
Cdd:pfam09731 231 VEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREIDQ--------LSKK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 112 L-EIKVQRLHDIETENQKLRETL----EEYNKEFAEVKNQE-----VTIKALKEKIRE-YEQTLKSQAETIALEKEQKLQ 180
Cdd:pfam09731 303 LaELKKREEKHIERALEKQKEELdklaEELSARLEEVRAADeaqlrLEFEREREEIREsYEEKLRTELERQAEAHEEHLK 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 181 NDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTAlektrtelfdlktkydeETTAKADEIEMIMT---DLERANQRAEVA 257
Cdd:pfam09731 383 DVLVEQEIELQREFLQDIKEKVEEERAGRLLKLN-----------------ELLANLKGLEKATSshsEVEDENRKAQQL 445
|
250 260
....*....|....*....|
gi 601983272 258 QREAETLREQLSSANHSLQL 277
Cdd:pfam09731 446 WLAVEALRSTLEDGSADSRP 465
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
119-405 |
2.65e-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: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 119 LHDIETENQK-LRETLEEYNKEFAEVKNQEVTIKAlkeKIREYEQTLKSQAETIALEKE--QKLQNDFAEKERKLQETQM 195
Cdd:pfam05483 65 LKDSDFENSEgLSRLYSKLYKEAEKIKKWKVSIEA---ELKQKENKLQENRKIIEAQRKaiQELQFENEKVSLKLEEEIQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 196 STTSKLEE--AEHKL-----QTLQTALEKTRtelfdlKTKYDEETTAKA-----DEIEMIMTDLERANQRAEVAQREAE- 262
Cdd:pfam05483 142 ENKDLIKEnnATRHLcnllkETCARSAEKTK------KYEYEREETRQVymdlnNNIEKMILAFEELRVQAENARLEMHf 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 263 TLREQLSSANHslqLASQIQKapdvaievltrsslevELAAKEREIA----QLVEDVQRLQaSLTKLRENSASQISQLEQ 338
Cdd:pfam05483 216 KLKEDHEKIQH---LEEEYKK----------------EINDKEKQVSllliQITEKENKMK-DLTFLLEESRDKANQLEE 275
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 601983272 339 QLNAKNSTLKQLEEKLKG-QADYEEVKKELNtlKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSEN 405
Cdd:pfam05483 276 KTKLQDENLKELIEKKDHlTKELEDIKMSLQ--RSMSTQKALEEDLQIATKTICQLTEEKEAQMEELN 341
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
235-359 |
2.90e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 41.76 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 235 AKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQkapdvaievlTRSSLEVELAAKEREIAQLved 314
Cdd:COG3524 174 AREDAVRFAEEEVERAEERLRDAREALLAFRNRNGILDPEATAEALLQ----------LIATLEGQLAELEAELAAL--- 240
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 601983272 315 vqrlqasLTKLRENSAsQISQLEQQLNAKNSTLKQLEEKLKGQAD 359
Cdd:COG3524 241 -------RSYLSPNSP-QVRQLRRRIAALEKQIAAERARLTGASG 277
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
18-404 |
2.99e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 18 QQLQRELDATATVLANRQDESEQSRKRLIEQSREFK-KNTPEDLRKQVApllksfQGEIDALSKRSKEAEAAfLTVYKRL 96
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEeKKKADEAKKAEE------KKKADEAKKKAEEAKKA-DEAKKKA 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 97 IDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKE 176
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK 1404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 177 QKlqndfAEKERKLQETQmsttSKLEEAEHKLQTLQTALE-KTRTElfdlKTKYDEETTAKADEIEmimtDLERANQRAE 255
Cdd:PTZ00121 1405 KK-----ADELKKAAAAK----KKADEAKKKAEEKKKADEaKKKAE----EAKKADEAKKKAEEAK----KAEEAKKKAE 1467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 256 VAqREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRsslevELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQ 335
Cdd:PTZ00121 1468 EA-KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA-----AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK 1541
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 601983272 336 LEQQLNA----KNSTLKQLEEKLKG-QADYEEVKKELNTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSE 404
Cdd:PTZ00121 1542 AEEKKKAdelkKAEELKKAEEKKKAeEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
15-364 |
3.09e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 15 FDLQQLQRELDATATVLANRQDESEQSRKRLIEQSREfkkntpedlrkqvaplLKSFQGEIDALSKRSKEAEAafltvyk 94
Cdd:COG4372 38 FELDKLQEELEQLREELEQAREELEQLEEELEQARSE----------------LEQLEEELEELNEQLQAAQA------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 95 rlidvpdpvpaldvgqQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtiKALKEKIREYEQTLKSQAETIale 174
Cdd:COG4372 95 ----------------ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR---KQLEAQIAELQSEIAEREEEL--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 175 keQKLQNDFAEKERKLQETQMST-TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQR 253
Cdd:COG4372 153 --KELEEQLESLQEELAALEQELqALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 254 AEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQI 333
Cdd:COG4372 231 LGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLI 310
|
330 340 350
....*....|....*....|....*....|.
gi 601983272 334 SQLEQQLNAKNSTLKQLEEKLKGQADYEEVK 364
Cdd:COG4372 311 GALEDALLAALLELAKKLELALAILLAELAD 341
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
177-364 |
4.16e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.22 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 177 QKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTA---LEKTRTELFDLKTKYDEETTAKAdeiemimtdleranqR 253
Cdd:PRK11637 50 KSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQAsrkLRETQNTLNQLNKQIDELNASIA---------------K 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 254 AEVAQREAET-LREQLSSA----NHS-LQL-----ASQ-----------IQKAPDVAIEVLTRSSleVELAAKEREIaql 311
Cdd:PRK11637 115 LEQQQAAQERlLAAQLDAAfrqgEHTgLQLilsgeESQrgerilayfgyLNQARQETIAELKQTR--EELAAQKAEL--- 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 601983272 312 vEDVQRLQASLtkLRENSASQiSQLEQQLNAKNSTLKQLEEKL-KGQADYEEVK 364
Cdd:PRK11637 190 -EEKQSQQKTL--LYEQQAQQ-QKLEQARNERKKTLTGLESSLqKDQQQLSELR 239
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
234-369 |
4.29e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 234 TAKADEIEmimtdlERANQRAEVAQREAETLREQLSsanhsLQLASQIQKApdvaievltRSSLEVELAAKEREIAQLVE 313
Cdd:PRK12704 30 EAKIKEAE------EEAKRILEEAKKEAEAIKKEAL-----LEAKEEIHKL---------RNEFEKELRERRNELQKLEK 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 601983272 314 DVQRLQASLtklrENSASQISQLEQQLNAKNSTLKQLEEKLKG-QADYEEVKKELNT 369
Cdd:PRK12704 90 RLLQKEENL----DRKLELLEKREEELEKKEKELEQKQQELEKkEEELEELIEEQLQ 142
|
|
| iSH2_PIK3R1 |
cd12924 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
238-371 |
4.33e-03 |
|
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 1, PIK3R1, also called p85alpha; 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. In addition, p85alpha, also called PIK3R1, contains N-terminal SH3 and GAP domains. p85alpha carry functions independent of its PI3K regulatory role. It can independently stimulate signaling pathways involved in cytoskeletal rearrangements. Insulin-sensitive tissues express splice variants of the PIK3R1 gene, p50alpha and p55alpha, which may play important roles in insulin signaling during lipid and glucose metabolism. Mice deficient with PIK3R1 die perinatally, indicating its importance in development.
Pssm-ID: 214017 [Multi-domain] Cd Length: 161 Bit Score: 39.68 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 238 DEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVltrssLEVELAAKEREIAQLVEDVQR 317
Cdd:cd12924 1 DNIEAVGKKLHEYNTQFQEKSREYDRLYEEYTRTSQEIQMKRTAIEAFNETIKI-----FEEQCQTQERYSKEYIEKFKR 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 601983272 318 L--QASLTKLRENSASQISQLEQQLNAKnstlKQLEEKLKGQ-ADYEEVKKELNTLK 371
Cdd:cd12924 76 EgnEKEIQRIMHNYEKLKSRISEIVDSR----RRLEEDLKKQaAEYREIDKRMNSIK 128
|
|
| Wtap |
pfam17098 |
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ... |
295-413 |
5.07e-03 |
|
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and pre-mRNA-splicing regulator WTAP from mammals. The former is required for female-specific splicing of Sex-lethal RNA, and the latter is a regulatory subunit of the RNA N6-methyladenosine methyltransferase. The family also includes the yeast Mum2p protein which is part of the Mis complex.
Pssm-ID: 465345 [Multi-domain] Cd Length: 155 Bit Score: 39.20 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 295 SSLEVELAAKEREIAQLVEDVQRLQASLTKlrENSASQISQLEQQLNAKNSTLKQLEEKLKgqADYEEVKKELNTLKsme 374
Cdd:pfam17098 7 NLLLARLAEKEQEIQELKAQLQDLKQSLQP--PSSQLRSLLLDPAVNLEFLRLKKELEEKK--KKLKEAQLELAAWK--- 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 601983272 375 FAPSEGAGTQdstkplevlLLEKNRSLQSENATLRISNS 413
Cdd:pfam17098 80 FTPDSTTGKR---------LMAKCRLLQQENEELGRQLS 109
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
701-912 |
6.37e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.46 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 701 RREMEAQQAALDPALKPAP----LSQPDLTILTPKHLSASPMSTVSTYPPLAISLKKTPAAPETSTAALPSAPALKKEAQ 776
Cdd:PHA03247 2863 RRRPPSRSPAAKPAAPARPpvrrLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPP 2942
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 777 DVPTLDPPGSADAAQGVLRPMKSELVRGSTwkdpwwspiqPERRNLTSSEETKADETTASGKERAGSSQPRAER--SQL- 853
Cdd:PHA03247 2943 LAPTTDPAGAGEPSGAVPQPWLGALVPGRV----------AVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSwaSSLa 3012
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 601983272 854 ----QGPSASAEYWKEWPSAESPYSQSSELSLTGASRSETPQNSPLPSSPIVPMAKPAKPSVP 912
Cdd:PHA03247 3013 lheeTDPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLEALDPLPPEPHDPFAHEPDPATP 3075
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
119-372 |
6.81e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 41.36 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 119 LHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEkirEYEQTLKSQAETIA----------------LEKEQKLQND 182
Cdd:PTZ00440 723 LNQYTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKN---EFILHLYENDKDLPdgkntyeeflqykdtiLNKENKISND 799
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 183 FAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEET-TAKADEIEM-----------IMTDLERA 250
Cdd:PTZ00440 800 INILKENKKNNQ----DLLNSYNILIQKLEAHTEKNDEELKQLLQKFPTEDeNLNLKELEKefnennqivdnIIKDIENM 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 251 NQRAEVAQreaeTLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLE------VELAAKEREIAQLVEDVQRLQASLtk 324
Cdd:PTZ00440 876 NKNINIIK----TLNIAINRSNSNKQLVEHLLNNKIDLKNKLEQHMKIintdniIQKNEKLNLLNNLNKEKEKIEKQL-- 949
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 325 lrenSASQISQLEQQLNAKNSTLKQLEEKLKG------------QADYEEVKKELNTLKS 372
Cdd:PTZ00440 950 ----SDTKINNLKMQIEKTLEYYDKSKENINGndgthlekldkeKDEWEHFKSEIDKLNV 1005
|
|
| COG0610 |
COG0610 |
Type I site-specific restriction-modification system, R (restriction) subunit and related ... |
5-216 |
7.11e-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: 41.01 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 5 VGSMFQYWKRFDLQQLQRELDATATVlANRQDESEQSRKRLIEQSREFKKntpedLRKQVAPLLKSFQGEIDALSKRSke 84
Cdd:COG0610 690 LRALFPEGVDFSAFDPTEKLEALDEA-VERFLGDEEARKEFKKLFKELSR-----LYNLLSPDDEFGDLELEKYRDDV-- 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 85 aeAAFLTVYKRLIDVPDPVPAldvgQQLEIKVQRLHD--IETENQKLRETLEE---YNKEFAE-VKNqevTIKALKEKIR 158
Cdd:COG0610 762 --SFYLALRAKLRKLGEKLDL----KEYEEKIRQLLDeaIDLERKEIKPRIKQnpvQYRKFSElLEE---IIEEYNNGAL 832
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 601983272 159 EYEQTLKsqaETIALEKEQKLQNDFAEKErKLQETQMSTTSKLEEAEHKLQTLQTALE 216
Cdd:COG0610 833 DADEVLE---ELEELAKEVKEEEERAEEE-GLNEEELAFYDALAENLGDEKLKELAKE 886
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
154-352 |
7.17e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 154 KEKIREYEQTLKSQAETIA----LEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTAL------EKTRTELF 223
Cdd:PRK04863 279 NERRVHLEEALELRRELYTsrrqLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALrqqekiERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 224 DLKTKYDE--ETTAKADEIemimtdLERANQRAEVAQREAETLREQLSSANHSLQL----ASQIQKApdvaievltrssl 297
Cdd:PRK04863 359 ELEERLEEqnEVVEEADEQ------QEENEARAEAAEEEVDELKSQLADYQQALDVqqtrAIQYQQA------------- 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 601983272 298 eVELAAKEREIAQL----VEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEE 352
Cdd:PRK04863 420 -VQALERAKQLCGLpdltADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQ 477
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
114-368 |
7.37e-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: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 114 IKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIAL--------EKEQKLQNDFAE 185
Cdd:COG3096 282 ELSERALELRRELFGARRQLAEEQYRLVEMARE---LEELSARESDLEQDYQAASDHLNLvqtalrqqEKIERYQEDLEE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 186 KERKLQETQMSttskLEEAEHKLQTLQTALEKTRTELFDLKTKY-------DEETT------------AKADEI-EMIMT 245
Cdd:COG3096 359 LTERLEEQEEV----VEEAAEQLAEAEARLEAAEEEVDSLKSQLadyqqalDVQQTraiqyqqavqalEKARALcGLPDL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 246 DLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASltkl 325
Cdd:COG3096 435 TPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERSQAWQTARELLRRYRSQQAL---- 510
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 601983272 326 rensASQISQLEQQLnaknstlKQLEEKLKGQADYEEVKKELN 368
Cdd:COG3096 511 ----AQRLQQLRAQL-------AELEQRLRQQQNAERLLEEFC 542
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
117-278 |
7.50e-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: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 117 QRLHDIETENQKLRETLE-------EYNKEFA------EVKNQevTIKALKEKIREYEQTLKSQAETIALEKEQKLQN-- 181
Cdd:COG3096 991 ARLEQAEEARREAREQLRqaqaqysQYNQVLAslkssrDAKQQ--TLQELEQELEELGVQADAEAEERARIRRDELHEel 1068
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 182 -------DFAEKERKLQETQM-STTSKLEEAEHKLQTLQTALEktrtelfdlktkydeetTAKA---DEIEMIM-TDLER 249
Cdd:COG3096 1069 sqnrsrrSQLEKQLTRCEAEMdSLQKRLRKAERDYKQEREQVV-----------------QAKAgwcAVLRLARdNDVER 1131
|
170 180
....*....|....*....|....*....
gi 601983272 250 ANQRAEVAQREAETLREQLSSANHSLQLA 278
Cdd:COG3096 1132 RLHRRELAYLSADELRSMSDKALGALRLA 1160
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
134-221 |
7.88e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.33 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 134 EEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHK-----L 208
Cdd:smart00935 21 KQLEKEFKKRQAE---LEKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEelqkiL 97
|
90
....*....|...
gi 601983272 209 QTLQTALEKTRTE 221
Cdd:smart00935 98 DKINKAIKEVAKK 110
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
54-371 |
8.46e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 54 KNTPEDLRKQVAPL------LKSFQGEIDALSK--------------RSKEAEAAFLTVYKRLIDVPDPVPAL----DVG 109
Cdd:PRK01156 172 KDVIDMLRAEISNIdyleekLKSSNLELENIKKqiaddekshsitlkEIERLSIEYNNAMDDYNNLKSALNELssleDMK 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 110 QQLEIKVQ----RLHDIETENQKLRETLEEYNK--------------EFAEVKNQEVT----IKALKEKIREYEQTLKSq 167
Cdd:PRK01156 252 NRYESEIKtaesDLSMELEKNNYYKELEERHMKiindpvyknrnyinDYFKYKNDIENkkqiLSNIDAEINKYHAIIKK- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 168 aetiaLEKEQKLQNDFAEKERKLQETQmSTTSKLEEAEHKLQTLQTALE----------KTRTELFDLKTKYDEETTAKA 237
Cdd:PRK01156 331 -----LSVLQKDYNDYIKKKSRYDDLN-NQILELEGYEMDYNSYLKSIEslkkkieeysKNIERMSAFISEILKIQEIDP 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 238 DEI----EMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAP----DVAIEVLTR---------SSLEVE 300
Cdd:PRK01156 405 DAIkkelNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPvcgtTLGEEKSNHiinhynekkSRLEEK 484
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 601983272 301 LAAKEREIAQLVEDVQRLQASLTKLR-------ENSASQISQLEQQLNAKNSTLKQLEEKlkgQADYEEVKKELNTLK 371
Cdd:PRK01156 485 IREIEIEVKDIDEKIVDLKKRKEYLEseeinksINEYNKIESARADLEDIKIKINELKDK---HDKYEEIKNRYKSLK 559
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
106-293 |
8.82e-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: 39.34 E-value: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 106 LDVGQQLEIK-VQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAEtialekeqKLQNDFA 184
Cdd:pfam17078 33 LEIAQQKESKfLENLASLKHENDNLSSMLNRKERRLKDLEDQLSELKNSYEELTESNKQLKKRLE--------NSSASET 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 185 EKERKLQETQMS----TTSKLEEAEH---KLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVA 257
Cdd:pfam17078 105 TLEAELERLQIQydalVDSQNEYKDHyqqEINTLQESLEDLKLENEKQLENYQQRISSNDKDIDTKLDSYNNKFKNLDNI 184
|
170 180 190
....*....|....*....|....*....|....*..
gi 601983272 258 QREAET-LREQLSSANHSLQLASQIQKAPDVAIEVLT 293
Cdd:pfam17078 185 YVNKNNkLLTKLDSLAQLLDLPSWLNLYPESRNKILE 221
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
221-371 |
8.91e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.59 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 221 ELFD-LKTKYDEETTAKADEIEMIMTDLERANqraevaqreaETLReqLSSANHSL-QLASQIQkapdvAIEVLTRSSLE 298
Cdd:PRK04778 64 EKFEeWRQKWDEIVTNSLPDIEEQLFEAEELN----------DKFR--FRKAKHEInEIESLLD-----LIEEDIEQILE 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 601983272 299 -----VELAAKER-EIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEkLKGQADYEEVKKELNTLK 371
Cdd:PRK04778 127 elqelLESEEKNReEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEFSQFVE-LTESGDYVEAREILDQLE 204
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
122-293 |
9.42e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 122 IETENQKLRETLEEYNKEfAEVKNQEVTIKAlKEKIREyeqtLKSQAEtialekeqklqNDFAEKERKLQETQMSTTSK- 200
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKE-AEAIKKEALLEA-KEEIHK----LRNEFE-----------KELRERRNELQKLEKRLLQKe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 201 ---------LEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIE------------MIMTDLErANQRAEVAQ- 258
Cdd:PRK12704 96 enldrklelLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELErisgltaeeakeILLEKVE-EEARHEAAVl 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 601983272 259 -REAETLREQLSS--ANHSLQLAsqIQK-APDVAIEVLT 293
Cdd:PRK12704 175 iKEIEEEAKEEADkkAKEILAQA--IQRcAADHVAETTV 211
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
115-367 |
9.69e-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: 40.49 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 115 KVQRLHDIETENQKLRETLEEYNKEFaevKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQ 194
Cdd:pfam17380 235 KMERRKESFNLAEDVTTMTPEYTVRY---NGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKARE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 195 MSTTSKLEEAEHKLQTL------------QTALEKTRT-ELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA 261
Cdd:pfam17380 312 VERRRKLEEAEKARQAEmdrqaaiyaeqeRMAMERERElERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKN 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 262 ETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVElAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLN 341
Cdd:pfam17380 392 ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQE-EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEE 470
|
250 260
....*....|....*....|....*.
gi 601983272 342 AKNSTLKQLEEKLKGQADYEEVKKEL 367
Cdd:pfam17380 471 ERKRKKLELEKEKRDRKRAEEQRRKI 496
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
122-253 |
9.91e-03 |
|
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. The function is not known.
Pssm-ID: 464008 [Multi-domain] Cd Length: 177 Bit Score: 38.74 E-value: 9.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 601983272 122 IETENQKLRETLEEYNKEFAEVKNQEV----TIKALKEKIREYEQTLKSQAETIAlekeqKLQNDFAEKERKLQETQMsT 197
Cdd:pfam13870 47 LQIENQALNEKIEERNKELKRLKLKVTntvhALTHLKEKLHFLSAELSRLKKELR-----ERQELLAKLRKELYRVKL-E 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 601983272 198 TSKLEEAEHKLqtlqtaleKTRTELF---DLKTKYD---EETTAKADEIEMIMTDLERANQR 253
Cdd:pfam13870 121 RDKLRKQNKKL--------RQQGGLLhvpALLHDYDktkAEVEEKRKSVKKLRRKVKILEMR 174
|
|
| |
