|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
71-419 |
4.12e-56 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 191.67 E-value: 4.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 71 EKKEIMELNDRLASYIEKVRFLDAQNRKLDADLKMLQGRFGKSTGSVKVMYEMEITTATNVVKQTGKDHGETEKEIRKLQ 150
Cdd:pfam00038 2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 151 DQLDELRKKFEEAQRGRAEdrlkiddllvtlsnLEAEINLLKRrialleeevarlkkenfrltselqrvriELDQETLLR 230
Cdd:pfam00038 82 LAAEDFRQKYEDELNLRTS--------------AENDLVGLRK----------------------------DLDEATLAR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 231 IDNQNKVKTILEEIDFMKRGFETELKELQAQAARDTTS-ENREYFKNELANAMRDIRAEYDQIMNGNRNDMESWYQLRVQ 309
Cdd:pfam00038 120 VDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNvEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 310 EINTQSNRQNAENNYQKEEVKRLRNQTSELRQKLSDLESRNLLLEKQIEDLNYQLEDDQRSYEAALNDKDAQIRKLREEC 389
Cdd:pfam00038 200 ELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEM 279
|
330 340 350
....*....|....*....|....*....|
gi 17568557 390 QALMVELQMLLDTKQTLDGELKVYRQMLEG 419
Cdd:pfam00038 280 ARQLREYQELLNVKLALDIEIATYRKLLEG 309
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
128-391 |
1.07e-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: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 128 ATNVVKQTGKDHGETEKEIRKLQDQLDELRKKFEEAQRGRAEDRLKIDDLLVTLSNLEAEINLLKRRIALLEEEVARLKK 207
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 208 ENFRLTSELQRVRIeldqeTLLRIDNQNKVKTILEEIDFmkrgfetelkelqAQAARDttSENREYFKNELANAMRDIRA 287
Cdd:COG4942 98 ELEAQKEELAELLR-----ALYRLGRQPPLALLLSPEDF-------------LDAVRR--LQYLKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 288 EYDQImngnrndmeswyQLRVQEINTQSNRQNAENNYQKEEVKRLRNQTSELRQKLSDLESRNLLLEKQIEdlnyQLEDD 367
Cdd:COG4942 158 DLAEL------------AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA----ELQQE 221
|
250 260
....*....|....*....|....
gi 17568557 368 QRSYEAALNDKDAQIRKLREECQA 391
Cdd:COG4942 222 AEELEALIARLEAEAAAAAERTPA 245
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
124-381 |
3.38e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 124 EITTATNVVKQTGKDHGETEKEIRKLQDQLDELRKKFEEAQRGRAEDRLKIDDLLVTLSNLEAEINLLKRRIALLEEEVA 203
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 204 RLKKENFRLTSELQRVRIELDQETLLRIDNQNKVKTILEEIDFMKRGFETELKELQAQAARDTTSENREyfkNELANAMR 283
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE---EALLERLE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 284 DIRAEYDQImngnrndmeswyQLRVQEINTQSNRQNAENNYQKEEVKRLRNQTSELRQKLSDLESRNLLLEKQIEDLNYQ 363
Cdd:COG1196 418 RLEEELEEL------------EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
250
....*....|....*...
gi 17568557 364 LEDDQRSYEAALNDKDAQ 381
Cdd:COG1196 486 LAEAAARLLLLLEAEADY 503
|
|
| LTD |
pfam00932 |
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ... |
464-570 |
1.41e-09 |
|
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.
Pssm-ID: 460003 [Multi-domain] Cd Length: 108 Bit Score: 55.51 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 464 SAKGNVAIKE-----TSPEGKFVILENThRAKEEPLGDWKLKRKIDGkreiVFTFPSDYILHPFQSVKIFArGQGIANPP 538
Cdd:pfam00932 2 SATGDVVISEvvydgSGGNDEFIELYNT-GSKAVDLSGWKLQDASGG----TYTFPNGTTLAPGQTVVVWT-GSGTNSAT 75
|
90 100 110
....*....|....*....|....*....|..
gi 17568557 539 EVLIFEGDETFGVGaNVQTILYNNKGEERATH 570
Cdd:pfam00932 76 AGYWGPSNAVWNNG-GDAVALYDANGELVDSV 106
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
133-396 |
2.52e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 133 KQTGKDHGETEKEIRKLQDQLDELRKKFEEAQRGRAEDRLKIDDLlvtlsnLEAEINLLKRRIALLEEEVARLKKENFRL 212
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL------GEEEQLRVKEKIGELEAEIASLERSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 213 TSELQrvrieldqetllriDNQNKVKTILEEIDFMKRGFETELKELQAQAARdttsenREYFKNELANA---MRDIRAEY 289
Cdd:TIGR02169 314 ERELE--------------DAEERLAKLEAEIDKLLAEIEELEREIEEERKR------RDKLTEEYAELkeeLEDLRAEL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 290 DQIMNGNRN--DMESWYQLRVQEINTQSNRQNAENNYQKEEVKRLRNQTSELRQKLSDLESRNLLLEKQIEDLNYQLEDD 367
Cdd:TIGR02169 374 EEVDKEFAEtrDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
250 260 270
....*....|....*....|....*....|..
gi 17568557 368 QRSYE---AALNDKDAQIRKLREECQALMVEL 396
Cdd:TIGR02169 454 EWKLEqlaADLSKYEQELYDLKEEYDRVEKEL 485
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
121-407 |
3.02e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.08 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 121 YEMEITTATNVVKQTGKDHGETEKEIRKLQDQLDELRKKFEEAQRGRAEDRLKID----DLLVTLSNLEAEINLLKRRIA 196
Cdd:TIGR02169 168 FDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREyegyELLKEKEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 197 LLEEEVARLKKENFRLTSELQRVRIELDQETL----LRIDNQNKVKTILEEIDFMKRGFETELKEL-----QAQAARDTT 267
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdLGEEEQLRVKEKIGELEAEIASLERSIAEKereleDAEERLAKL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 268 SENREYFKNELANAMRDI---RAEYDQIMN--GNRNDMESWYQLRVQEINTQSNRQNAENNYQKEEVKRLRNQTSELRQK 342
Cdd:TIGR02169 328 EAEIDKLLAEIEELEREIeeeRKRRDKLTEeyAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRE 407
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17568557 343 LSDLESRNLLLEKQIEDLNYQL---EDDQRSYEAALNDKDAQIRKLREECQALMVEL----QMLLDTKQTLD 407
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLNAAIagiEAKINELEEEKEDKALEIKKQEWKLEQLAADLskyeQELYDLKEEYD 479
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
141-399 |
8.04e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 8.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 141 ETEKEIRKLQDQLDELRKKfEEAQRGRAED-RLKIDDLLVTLSNLEAEINLLKRRIALLEEEVARLKKENFRLTSELQRV 219
Cdd:TIGR02169 713 DASRKIGEIEKEIEQLEQE-EEKLKERLEElEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 220 RIELDQETLlridnqNKVKTILEEIDFMKRGFETELKELQAQaardttsenREYFKNELANAMRDIRAEYDQImNGNRND 299
Cdd:TIGR02169 792 RIPEIQAEL------SKLEEEVSRIEARLREIEQKLNRLTLE---------KEYLEKEIQELQEQRIDLKEQI-KSIEKE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 300 MESwYQLRVQEINTQ-SNRQNAENNYQKE------EVKRLRNQTSELRQKLSDLESRNLLLEKQIEDLNYQLE---DDQR 369
Cdd:TIGR02169 856 IEN-LNGKKEELEEElEELEAALRDLESRlgdlkkERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEaleEELS 934
|
250 260 270
....*....|....*....|....*....|....*.
gi 17568557 370 SYEAALND------KDAQIRKLREECQALMVELQML 399
Cdd:TIGR02169 935 EIEDPKGEdeeipeEELSLEDVQAELQRVEEEIRAL 970
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
69-414 |
1.47e-08 |
|
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: 57.82 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 69 EREKKEIMELNDRLasyiEKVRFLDAQnrkLDADLKMLQGRFGKSTGSVKVMYEMEITTA--TNVVKQTGKDHGETEKEI 146
Cdd:pfam15921 447 ERQMAAIQGKNESL----EKVSSLTAQ---LESTKEMLRKVVEELTAKKMTLESSERTVSdlTASLQEKERAIEATNAEI 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 147 RKLQDQLDelrKKFEEAQRGRAED------RLKIDDLLVTLSNLEAEINLLKRRIalleEEVARLKKENFRLTSELQRVR 220
Cdd:pfam15921 520 TKLRSRVD---LKLQELQHLKNEGdhlrnvQTECEALKLQMAEKDKVIEILRQQI----ENMTQLVGQHGRTAGAMQVEK 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 221 IELDQETllridnqNKVKTILEEIDFMKRGFETELKELQAQAArDTTSENREYFK--NELANAMRDIRAEYDQIMN---G 295
Cdd:pfam15921 593 AQLEKEI-------NDRRLELQEFKILKDKKDAKIRELEARVS-DLELEKVKLVNagSERLRAVKDIKQERDQLLNevkT 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 296 NRNDMESW---YQLRVQEINTQSNRQNAENNYQKEEVKRLRNQTSELRQKLSDLESRN-------LLLEKQIEDLNYQLE 365
Cdd:pfam15921 665 SRNELNSLsedYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDghamkvaMGMQKQITAKRGQID 744
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 17568557 366 DDQRS---YEAALNDKDAQIRKLREECQALMVELQMLLDTKQTLDGELKVYR 414
Cdd:pfam15921 745 ALQSKiqfLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLR 796
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
72-388 |
3.26e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 72 KKEIMELNdrlasyiEKVRFLDAQNRKLDADLKMLQGRFGKSTgSVKVMYEMEITTATNVVKQTGKDHGETEKEIRKLQD 151
Cdd:TIGR02168 676 RREIEELE-------EKIEELEEKIAELEKALAELRKELEELE-EELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 152 QLDELRKKFEEAQRGRAEDRLKIDDLLVTLSNLEAEINLLKRRIALLEEEVARLKKENFRLTSELQRVRIELDQETLLRI 231
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 232 DNQNKVKTILEEIDFMKRgfetELKELQAQAARdtTSENREYFKNELANAMRDIRAEYDQIMNGNRNDMEswyqLRVQEI 311
Cdd:TIGR02168 828 SLERRIAATERRLEDLEE----QIEELSEDIES--LAAEIEELEELIEELESELEALLNERASLEEALAL----LRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 312 NTQSNRQNAEnnyqkEEVKRLRNQTSELRQKLSDLESRNLLLEKQIEDLNYQL-EDDQRSYEAAL---NDKDAQIRKLRE 387
Cdd:TIGR02168 898 ELSEELRELE-----SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEaleNKIEDDEEEARR 972
|
.
gi 17568557 388 E 388
Cdd:TIGR02168 973 R 973
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
66-423 |
1.64e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 66 DNREREK---KEIMELNDRLASyiekvrfLDAQNRKLDADLKMLQGRFGKSTGsVKVMYEMEIttatnvvkqtgkDHGET 142
Cdd:COG4913 607 DNRAKLAaleAELAELEEELAE-------AEERLEALEAELDALQERREALQR-LAEYSWDEI------------DVASA 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 143 EKEIRKLQDQLDELRK---KFEEAQRgraedrlKIDDLLVTLSNLEAEINLLKRRIALLEEEVARLKKENFRLTSELQRV 219
Cdd:COG4913 667 EREIAELEAELERLDAssdDLAALEE-------QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 220 RIELDQETLLRIDNQNKVKTILEEIDFMKRGFETELKELQAQAARDTTsenreyfknELANAMRDIRAEYDQIMNGNRND 299
Cdd:COG4913 740 EDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE---------ELERAMRAFNREWPAETADLDAD 810
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 300 MESwyqlrVQEINTQSNRQNAENNYQKEE-VKRLRNQTSElrQKLSDLESRnllLEKQIEDLNYQLEDdqrsyeaaLNDK 378
Cdd:COG4913 811 LES-----LPEYLALLDRLEEDGLPEYEErFKELLNENSI--EFVADLLSK---LRRAIREIKERIDP--------LNDS 872
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 17568557 379 DAQI-----RKLReecqalmvelqmlLDTKQTLDGELKVYRQMLEGNSEG 423
Cdd:COG4913 873 LKRIpfgpgRYLR-------------LEARPRPDPEVREFRQELRAVTSG 909
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
67-436 |
1.67e-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: 54.29 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 67 NREREKKEimELND-RLASYIEKVRFLDAQNRKLDADLKMLQGRFGKSTGsvkvmyemEITTATNVVKQTGKDHGETEKE 145
Cdd:TIGR02168 213 ERYKELKA--ELRElELALLVLRLEELREELEELQEELKEAEEELEELTA--------ELQELEEKLEELRLEVSELEEE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 146 IRKLQDQLDELRKKFEEAQRGRAEDRLKIDDLLVTLSNLEAEINLLKRRIALLEEEVARLKKENFRLTSELQRVRIELDq 225
Cdd:TIGR02168 283 IEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE- 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 226 etllridnqnKVKTILEEidfmkrgFETELKELQAQaardttsenREYFKNELANAMRDIRAEYDQIMNgNRNDMESwyq 305
Cdd:TIGR02168 362 ----------ELEAELEE-------LESRLEELEEQ---------LETLRSKVAQLELQIASLNNEIER-LEARLER--- 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 306 lrvqeinTQSNRQNAENNYQKEEVKRLRNQTSELRQKLSDLESRNLLLEKQIEDLNYQLEDDQRSYEAALNdkdaQIRKL 385
Cdd:TIGR02168 412 -------LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ----ALDAA 480
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 17568557 386 REECQALMVELQMLLDTKQTLDGELKVYRQMLEGNSEGNGLRQLVEKVVRT 436
Cdd:TIGR02168 481 ERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISV 531
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
124-413 |
5.69e-07 |
|
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: 52.72 E-value: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 124 EITTATNVVKQTGKDHGETEKEIRKLQDQLDELRKKFEEAQRGRAEDRLKIDDLLVTLSNLEAEI---NLLKRRIALLEE 200
Cdd:TIGR04523 146 EIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIqknKSLESQISELKK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 201 EVARLKKENFRLTSELQRVRIEL---DQETLLRIDNQNKVKTILEE-----------IDFMKRGF---ETELKELQAQAA 263
Cdd:TIGR04523 226 QNNQLKDNIEKKQQEINEKTTEIsntQTQLNQLKDEQNKIKKQLSEkqkeleqnnkkIKELEKQLnqlKSEISDLNNQKE 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 264 RDTTSEnreyFKNELANAMRDIRAEYDQIMNGN----------------RNDMESWYQLRVQEINTQSNR---QNAENNY 324
Cdd:TIGR04523 306 QDWNKE----LKSELKNQEKKLEEIQNQISQNNkiisqlneqisqlkkeLTNSESENSEKQRELEEKQNEiekLKKENQS 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 325 QKEEVKRLRNQTSELRQKLSDLESRNLLLEKQIEDLNYQLEDDQRSYE---AALNDKDAQIRKLREECQALMVELQMLLD 401
Cdd:TIGR04523 382 YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIErlkETIIKNNSEIKDLTNQDSVKELIIKNLDN 461
|
330
....*....|..
gi 17568557 402 TKQTLDGELKVY 413
Cdd:TIGR04523 462 TRESLETQLKVL 473
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
137-383 |
1.51e-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: 51.22 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 137 KDHGETEKEIRKLQDQLDELRKKFEEAQRGRAEDRLKIDDLLVTLSNLEAEINLLKRRIALLEEEVARLKKENFRLTSEL 216
Cdd:TIGR02169 294 EKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 217 QrvriELDQETLLRIDNQNKVKTILEEIDFMKRGFETELKELQAQAARdtTSENREYFKNELANAMRDIrAEYDQIMNGN 296
Cdd:TIGR02169 374 E----EVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR--LSEELADLNAAIAGIEAKI-NELEEEKEDK 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 297 RndmeswYQLRVQEINTQSNRQNAENnyQKEEVKRLRNQTSELRQKLSDLESRNLLLEKQIEdlnyQLEDDQRSYEAALN 376
Cdd:TIGR02169 447 A------LEIKKQEWKLEQLAADLSK--YEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR----ASEERVRGGRAVEE 514
|
....*..
gi 17568557 377 DKDAQIR 383
Cdd:TIGR02169 515 VLKASIQ 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
64-361 |
3.43e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 64 IRDNREREKK---EIMELNDRLASYIEKVRFLDAQNRKLDADLKMLQGRFGKSTGSVKVMyEMEITTATNVVKQTGKDHG 140
Cdd:TIGR02168 679 IEELEEKIEEleeKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL-EAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 141 ETEKEIRKLQDQLDELRKKFEEAQRGRAEDRLKIDDLLVTLSNLEAEINLLKRRIALLEEEVARLKKENFRLTSELQRVR 220
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 221 IELDQETLLRIDNQNKVKTILEEIDFMKRGFETELKELQ-AQAARDTTSENREYFKNELANAMRDIRAEYDQIMNGNR-- 297
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEaLLNERASLEEALALLRSELEELSEELRELESKRSELRRel 917
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 298 ---NDMESWYQLRVQEI--NTQSNRQNAENNYQ--------------------KEEVKRLRNQTSE-------------- 338
Cdd:TIGR02168 918 eelREKLAQLELRLEGLevRIDNLQERLSEEYSltleeaealenkieddeeeaRRRLKRLENKIKElgpvnlaaieeyee 997
|
330 340 350
....*....|....*....|....*....|
gi 17568557 339 -------LRQKLSDLESRNLLLEKQIEDLN 361
Cdd:TIGR02168 998 lkerydfLTAQKEDLTEAKETLEEAIEEID 1027
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
137-367 |
1.21e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 137 KDHGETEKEIRKLQDQ---LDELRKKFEEAQRGRAE-DRLKIDDLLVTLSNLEAEINLLKRRIALLEEEVARLKKENFRL 212
Cdd:COG4913 235 DDLERAHEALEDAREQielLEPIRELAERYAAARERlAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 213 TSELQRVRIELD--QETLLRIDNQNkvktiLEEIdfmkrgfETELKelQAQAARDTTSENREyfknELANAMRDIRAEYD 290
Cdd:COG4913 315 EARLDALREELDelEAQIRGNGGDR-----LEQL-------EREIE--RLERELEERERRRA----RLEALLAALGLPLP 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 291 QimngnrnDMESWYQLR------VQEINTQSNRQNAENNYQKEEVKRLRNQTSELRQKLSDLESRNLLLEKQIEDLNYQL 364
Cdd:COG4913 377 A-------SAEEFAALRaeaaalLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
...
gi 17568557 365 EDD 367
Cdd:COG4913 450 AEA 452
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
68-417 |
1.38e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.25 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 68 REREKKEIMELNDRLASYIEKVRFLDAQNRKLDADLKMLQGRFG-------------KSTGSVKVMYEMEITTATNVVKQ 134
Cdd:pfam01576 119 RQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISeftsnlaeeeekaKSLSKLKNKHEAMISDLEERLKK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 135 TGKDHGETEKEIRK-------LQDQLDELRKKFEE--AQRGRAEDRL-----KIDDLLVTLSNLEAEINLLKRRIALLEE 200
Cdd:pfam01576 199 EEKGRQELEKAKRKlegestdLQEQIAELQAQIAElrAQLAKKEEELqaalaRLEEETAQKNNALKKIRELEAQISELQE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 201 EV-----ARLKKENFR--LTSELQRVRIELdQETLLRIDNQNKVKTILE-EIDFMKRGFETELK--ELQAQAARDTTSEN 270
Cdd:pfam01576 279 DLeseraARNKAEKQRrdLGEELEALKTEL-EDTLDTTAAQQELRSKREqEVTELKKALEEETRshEAQLQEMRQKHTQA 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 271 REYFKNELANAMRDIRA--EYDQIMNGNRNDMESWYQL-----------------RVQEINTQSNRQNAENNYQKEEVKR 331
Cdd:pfam01576 358 LEELTEQLEQAKRNKANleKAKQALESENAELQAELRTlqqakqdsehkrkklegQLQELQARLSESERQRAELAEKLSK 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 332 LRNQTSELRQKLSDLESRNLLLEKQIEDLNYQLEDDQRSYEAALNDK---DAQIRKLREECQALMVELQMLLDTKQTLDG 408
Cdd:pfam01576 438 LQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKlnlSTRLRQLEDERNSLQEQLEEEEEAKRNVER 517
|
....*....
gi 17568557 409 ELKVYRQML 417
Cdd:pfam01576 518 QLSTLQAQL 526
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
141-411 |
1.77e-05 |
|
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: 47.07 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 141 ETEKEIRKLQDQLDELRKKFEEAQRGRAEDRLKIDDLLVTLSNLEAEINLLKRRIALLEEEVARLKKENFRLTSELQRVR 220
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 221 IELDQE--TLLRIDNQNKVKTILEEIDFmkrgfetelkelqAQAARdttsenreyfknelanamrdiRAEYDQIMNGNRN 298
Cdd:COG4942 104 EELAELlrALYRLGRQPPLALLLSPEDF-------------LDAVR---------------------RLQYLKYLAPARR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 299 DmeswyqlrvqeintqsnrqnaennyQKEEVKRLRNQTSELRQKLSDlesrnllLEKQIEDLNYQLEDDQRSYEAALNDK 378
Cdd:COG4942 150 E-------------------------QAEELRADLAELAALRAELEA-------ERAELEALLAELEEERAALEALKAER 197
|
250 260 270
....*....|....*....|....*....|...
gi 17568557 379 DAQIRKLREECQALMVELQMLLDTKQTLDGELK 411
Cdd:COG4942 198 QKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
141-358 |
2.00e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 141 ETEKEIRKLQDQLDELRKKFEEAQRGRAEDRLKIDdllvtLSNLEAEINLLKRRIALLEEEVARLKKENFRLTSELQRVR 220
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEFRQKNG-----LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 221 --IELDQETLLRIDNQNKVKTILEEIDFMkrgfETELKELQAQAardtTSENREY--FKNELANAMRDIRAEYDQIMNGN 296
Cdd:COG3206 247 aqLGSGPDALPELLQSPVIQQLRAQLAEL----EAELAELSARY----TPNHPDViaLRAQIAALRAQLQQEAQRILASL 318
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17568557 297 RNDMESwYQLRVQEINTQSNRqnaennyQKEEVKRLRNQTSELRQKLSDLESR----NLLLEKQIE 358
Cdd:COG3206 319 EAELEA-LQAREASLQAQLAQ-------LEARLAELPELEAELRRLEREVEVArelyESLLQRLEE 376
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
141-220 |
2.22e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.55 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 141 ETEKEIRKLQDQLDELRKKFEEAQRGRAEDRLKIDDLLVTLSNL----------EAEINLLKRRIALLEEEVARLKKENF 210
Cdd:COG2433 410 EEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEArseerreirkDREISRLDREIERLERELEEERERIE 489
|
90
....*....|
gi 17568557 211 RLTSELQRVR 220
Cdd:COG2433 490 ELKRKLERLK 499
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
149-408 |
2.70e-05 |
|
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: 47.04 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 149 LQDQLDELRKKFEEAQRGRAEdrlkIDDLLVTLSNLEAEIN-----------------LLKRRIALLEEEVARLKKENFR 211
Cdd:pfam05557 226 LKEEVEDLKRKLEREEKYREE----AATLELEKEKLEQELQswvklaqdtglnlrspeDLSRRIEQLQQREIVLKEENSS 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 212 LTSE---LQRVRIELDQETLLRIDN------------------QNKVKTILEEIDFMKRGFETELKELQAQAARDTTSEN 270
Cdd:pfam05557 302 LTSSarqLEKARRELEQELAQYLKKiedlnkklkrhkalvrrlQRRVLLLTKERDGYRAILESYDKELTMSNYSPQLLER 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 271 REYF-----KNELANAMRDIRAEYDQIMNGNRNDMESWYQLRVQEINTQSnrQNAENNYQKEEVKRLRNQTSELRQKLSD 345
Cdd:pfam05557 382 IEEAedmtqKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQE--SLADPSYSKEEVDSLRRKLETLELERQR 459
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17568557 346 LESRNLLLEKQIEDLNYQLEDDQRSYE----------AALNDKDAQIRKLREECQALMVELQMLLDTKQTLDG 408
Cdd:pfam05557 460 LREQKNELEMELERRCLQGDYDPKKTKvlhlsmnpaaEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLR 532
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
143-292 |
2.99e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 143 EKEIRKLQDQLDELRKKFEEAQRGRAEDRLKIDDLLVTLSNLEAEINLLKRRIALLEEEVARLKKENfrltsELQRVRIE 222
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-----EYEALQKE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 223 LDQETLLRIDNQNKVKTILEEIDfmkrGFETELKELQAQaaRDTTSENREYFKNELANAMRDIRAEYDQI 292
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIE----ELEEELAELEAE--LAELEAELEEKKAELDEELAELEAELEEL 161
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
185-397 |
6.61e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 6.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 185 EAEINLLKRRIALLEEEVARLKKENFRLTSELQRVRIELDQetllridNQNKVKTILEEIDfmkrGFETELKELQAQAAR 264
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE-------LQAELEALQAEID----KLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 265 DttsenreyfKNELANAMRDIRaeydqiMNGNRNDM-------ESWYQL--RVQEINTQSNRQNAENNYQKEEVKRLRNQ 335
Cdd:COG3883 84 R---------REELGERARALY------RSGGSVSYldvllgsESFSDFldRLSALSKIADADADLLEELKADKAELEAK 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17568557 336 TSELRQKLSDLESRNLLLEKQIEDLNYQLEDdqrsYEAALNDKDAQIRKLREECQALMVELQ 397
Cdd:COG3883 149 KAELEAKLAELEALKAELEAAKAELEAQQAE----QEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
139-388 |
9.53e-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: 45.60 E-value: 9.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 139 HGETEKEIRKLQDQLDELRKKFEEAQRGRAEDRLKIDDLLVTLSNLEAEIN-LLKRRIALLEEEVARLKKENFRLTSELQ 217
Cdd:pfam12128 620 QAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNkALAERKDSANERLNSLEAQLKQLDKKHQ 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 218 RVRIELDQETL-LRIDNQNKVKTILEEIDFMKRGFETELKELQAQAARDTTSENREYfKNELANamRDIRAEYDQIMNGN 296
Cdd:pfam12128 700 AWLEEQKEQKReARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWY-KRDLAS--LGVDPDVIAKLKRE 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 297 RNDME-SWYQLRVQEINTQSNRQNAENNYQKEEvKRLRNQTSELRQKLSDLESRNLLLEKQIEDLNYQLEDDQRSYEAAL 375
Cdd:pfam12128 777 IRTLErKIERIAVRRQEVLRYFDWYQETWLQRR-PRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQ 855
|
250
....*....|...
gi 17568557 376 NDKDAQIRKLREE 388
Cdd:pfam12128 856 VRLSENLRGLRCE 868
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
58-388 |
1.12e-04 |
|
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: 45.10 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 58 QNAASTIRDNREREKKEIMELNDRLASYIEKVRFLDAQNRKLDADLKMLQGRFGKSTGSVKVMyEMEITTATNVVKQTGK 137
Cdd:pfam05483 320 QIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKII-TMELQKKSSELEEMTK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 138 DHGETEKEIRKLQDQLDELRK---------KFEEAQRGRAEDRL--------KIDDLLVTLSNLEAEINLLKRRIALLEE 200
Cdd:pfam05483 399 FKNNKEVELEELKKILAEDEKlldekkqfeKIAEELKGKEQELIfllqarekEIHDLEIQLTAIKTSEEHYLKEVEDLKT 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 201 EVARLKKENFRLTSELQRVRIELDQETLLRIDNQNKVKTILEEIDFMKRGFETELKELQAQAARDTTSENR-EYFKNELA 279
Cdd:pfam05483 479 ELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDElESVREEFI 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 280 NAMRDIRAEYDQIMNGNRN----DMESWYQLRVQEINTQSNRQNAENnyQKEEVKRLRNQTSELRQKlSDLESRNL-LLE 354
Cdd:pfam05483 559 QKGDEVKCKLDKSEENARSieyeVLKKEKQMKILENKCNNLKKQIEN--KNKNIEELHQENKALKKK-GSAENKQLnAYE 635
|
330 340 350
....*....|....*....|....*....|....*.
gi 17568557 355 KQIEDLNYQLEDDQRSYEAALND--KDAQIRKLREE 388
Cdd:pfam05483 636 IKVNKLELELASAKQKFEEIIDNyqKEIEDKKISEE 671
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
133-357 |
1.19e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 133 KQTGKDHGETEKEIRKLQDQLDELRKKFEEAQRGRAEdrlkiddllvtLSNLEAEINLLKRRIALLEEEVARLKK--ENF 210
Cdd:COG4717 60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEE-----------LEELEEELEELEAELEELREELEKLEKllQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 211 RLTSELQRVRIELDQEtllridnQNKVKTILEEIDfmkrgfetELKELQAQAARdttsenreyFKNELANAMRDIRAEYD 290
Cdd:COG4717 129 PLYQELEALEAELAEL-------PERLEELEERLE--------ELRELEEELEE---------LEAELAELQEELEELLE 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17568557 291 QIMNGNRNDMESWyQLRVQEINTQSNRQNAENNYQKEEVKRLRNQTSELRQKLSDLESRNLLLEKQI 357
Cdd:COG4717 185 QLSLATEEELQDL-AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
176-392 |
1.50e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 176 DLLVTLSNLEAEINLLKRRIALLEEEVARLKKENFRLTSELQRVRIEldqetllridnqnkvktiLEEIDFMKRGFETEL 255
Cdd:COG1579 7 RALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE------------------LEDLEKEIKRLELEI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 256 KELQAQAARDTtsenreyfknELANAMRDIRaEYDQIMngnrndmeswyqlrvQEINTqsnrqnaennyQKEEVKRLRNQ 335
Cdd:COG1579 69 EEVEARIKKYE----------EQLGNVRNNK-EYEALQ---------------KEIES-----------LKRRISDLEDE 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17568557 336 TSELRQKLSDLESRNLLLEKQIEDLNYQLEDDQRSYEAALNDKDAQIRKLREECQAL 392
Cdd:COG1579 112 ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
326-418 |
1.53e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 326 KEEVKRLRNQTSELRQKLSDLESRNLLLEKQIEDLNYQLEDDQRSYEAALnDKDAQIRKLREECQALMVELQMLLDTKQT 405
Cdd:COG2433 412 EEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREI-RKDREISRLDREIERLERELEEERERIEE 490
|
90
....*....|...
gi 17568557 406 LDGELKVYRQMLE 418
Cdd:COG2433 491 LKRKLERLKELWK 503
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
84-388 |
1.89e-04 |
|
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: 44.44 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 84 SYIEKVRFLDAQNRKldaDLKMLQGRFGKSTGS---------VKVMYEMEIT--TATNVVKQTGKDHGETEKEIRKLQDQ 152
Cdd:pfam12128 146 SIIQNDRTLLGRERV---ELRSLARQFALCDSEsplrhidkiAKAMHSKEGKfrDVKSMIVAILEDDGVVPPKSRLNRQQ 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 153 L-------DELRKKFEEAQR--GRAEDRLKIDDLLVTLSNLEAEINLLKRRIALLEEEVARLKKE-NFRL---TSELQRV 219
Cdd:pfam12128 223 VehwirdiQAIAGIMKIRPEftKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAElNQLLrtlDDQWKEK 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 220 RIELDQETLLRIDNQNKVKTILEEIDFMKRGFETELKELQAQAArdttsENREYFKNELANAMRDIRAeydqiMNGNRND 299
Cdd:pfam12128 303 RDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQ-----EQLPSWQSELENLEERLKA-----LTGKHQD 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 300 MESWYQLRVQEINTQSNRQNAENNY----QKEEVKRLR--------NQTSELR----QKLSDLESRNLLLEKQIEDLNYQ 363
Cdd:pfam12128 373 VTAKYNRRRSKIKEQNNRDIAGIKDklakIREARDRQLavaeddlqALESELReqleAGKLEFNEEEYRLKSRLGELKLR 452
|
330 340
....*....|....*....|....*..
gi 17568557 364 LEDDQRSYEAALN--DKDAQIRKLREE 388
Cdd:pfam12128 453 LNQATATPELLLQleNFDERIERAREE 479
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
70-226 |
2.08e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 70 REKKEIMELNDRLASYIEKVRFLDAQNRKLDADLKMLQGRFGKSTGSVKVMYEMEITTATNVVKQtgkdhgETEKEIRKL 149
Cdd:COG3206 202 RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQ------QLRAQLAEL 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 150 QDQLDELRKKFEE---------AQRGRAEDRLKiDDLLVTLSNLEAEINLLKRRIALLEEEVARLKKENFRLtSELQRVR 220
Cdd:COG3206 276 EAELAELSARYTPnhpdvialrAQIAALRAQLQ-QEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL-PELEAEL 353
|
....*.
gi 17568557 221 IELDQE 226
Cdd:COG3206 354 RRLERE 359
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
145-496 |
2.78e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 145 EIRKLQDQLDELRKKFEEAQRGRAEDRLKIDDLLVTLSNLEAEINLLKRRIALLEEEVARLKKenFRLTSELQRVRIELD 224
Cdd:PRK03918 225 KLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE--LKEKAEEYIKLSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 225 QETLLRIDNQNKVKTILEEidfMKRGFETELKELQAQAAR-DTTSENREYFKNELANAMRDIRaEYDQImngnRNDMESW 303
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEE---EINGIEERIKELEEKEERlEELKKKLKELEKRLEELEERHE-LYEEA----KAKKEEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 304 YQLRVQEINTQSNRQNAENNYQKEEVKRLRNQTSELRQKLSDLESRNLLLEKQIEDL----------NYQLEDDQRsyEA 373
Cdd:PRK03918 375 ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELkkakgkcpvcGRELTEEHR--KE 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 374 ALNDKDAQIRKLREECQALMVELQMLLDTKQTLDGELKVYRQMLEGNSEGNGLRQLVEKVVRTSAINEEADTETMRVVKG 453
Cdd:PRK03918 453 LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKE 532
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 17568557 454 EHSSRTSYQRSAKGNVAiKETSPEGKFVILENTHRAKEEPLGD 496
Cdd:PRK03918 533 KLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAE 574
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
58-255 |
3.22e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 58 QNAASTIRDNREREKKEIMELNDRLASYIEKVRFLDAQNRKLD---ADLKMLQGRFGKstgsVKVMYEMEITTATnvVKQ 134
Cdd:PHA02562 219 QNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNtaaAKIKSKIEQFQK----VIKMYEKGGVCPT--CTQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 135 TGKDHGEtekEIRKLQDQLDELRKKFEEAQRGRAEDRLKIDDLL---VTLSNLEAEINLLKRRIALLEEEVARLKKENFR 211
Cdd:PHA02562 293 QISEGPD---RITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNeqsKKLLELKNKISTNKQSLITLVDKAKKVKAAIEE 369
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17568557 212 LTSElqRVRIELDQETLlridNQNKVKTILEEIDFMK----RGFETEL 255
Cdd:PHA02562 370 LQAE--FVDNAEELAKL----QDELDKIVKTKSELVKekyhRGIVTDL 411
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
124-202 |
3.80e-04 |
|
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.
Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 40.46 E-value: 3.80e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17568557 124 EITTATNVVKQTGKDHGETEKEIRKLQDQLDELRKKFEEAQRGRAEDRLKIDDLLVTLSNLEAEINLLKRRIALLEEEV 202
Cdd:pfam04871 26 ELSKQYNSLEQKESQAKELEAEVKKLEEALKKLKAELSEEKQKEKEKQSELDDLLLLLGDLEEKVEKYKARLKELGEEV 104
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
69-404 |
3.90e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 69 EREKKEIMELNDRLASYIEKVRFLDAQN---RKLDADLKMLQGRFGKSTGSVKVMYEmEITTATNVVKQTGKDHGETEKE 145
Cdd:pfam15921 513 EATNAEITKLRSRVDLKLQELQHLKNEGdhlRNVQTECEALKLQMAEKDKVIEILRQ-QIENMTQLVGQHGRTAGAMQVE 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 146 IRKLQDQLDELRKKFEEAQRGRAEDRLKIDDLLVTLSNLEAE----INLLKRRIalleEEVARLKKENFRLTSELQRVRI 221
Cdd:pfam15921 592 KAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEkvklVNAGSERL----RAVKDIKQERDQLLNEVKTSRN 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 222 ELDQET----LLRIDNQNKVktilEEIDFMKRGFETELKelQAQAARDTTSENREYFKNELANAMRDIRAEYDQIM--NG 295
Cdd:pfam15921 668 ELNSLSedyeVLKRNFRNKS----EEMETTTNKLKMQLK--SAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITakRG 741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 296 NRNDMESWYQLrVQEINTQSNRQN------------------AENNYQKEEVKRLRNQTSELRQKLSDLEsrnLLLEKqi 357
Cdd:pfam15921 742 QIDALQSKIQF-LEEAMTNANKEKhflkeeknklsqelstvaTEKNKMAGELEVLRSQERRLKEKVANME---VALDK-- 815
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 17568557 358 edlnyqleddqrsyeAALNDKDAQIRKLREECQALMVELQMLLDTKQ 404
Cdd:pfam15921 816 ---------------ASLQFAECQDIIQRQEQESVRLKLQHTLDVKE 847
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
68-227 |
4.64e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 68 REREKKEIMELNDRLASYIEKVRFLDAQNRKLDADLKMLQGRFGKSTGSVKVMYEMEITTATNVVKQTGKDHGETEKEIR 147
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLA 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 148 KLQDQLDELRKKFEEAQRGRAEDRLKIDDLLVTLSN----LEAEINLLKRRIALLEEEVARLKKENFRLTSELQRVRIEL 223
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEalaeAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
....
gi 17568557 224 DQET 227
Cdd:COG4913 450 AEAL 453
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
141-418 |
8.59e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 8.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 141 ETEKEIRKLQDQLDELRKKFEEAQRgrAEDRLkidDLLVTLSNLEAEINLLKRRIALLEEEVARLKKENFRLTSELQRVR 220
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALED--AREQI---ELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 221 IELDQETLLRIdnqnkvktileeidfmkrgfETELKELQAQAArdttsenreyfknELANAMRDIRAEYDQimNGNRndm 300
Cdd:COG4913 297 LEELRAELARL--------------------EAELERLEARLD-------------ALREELDELEAQIRG--NGGD--- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 301 eswyqlRVQEINTQSNRQNAENNYQKEEVKRLRNQTSELRQKLSDLESRNLLLEKQIEDLNYQLEDDQRSYEAALNDKDA 380
Cdd:COG4913 339 ------RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA 412
|
250 260 270
....*....|....*....|....*....|....*...
gi 17568557 381 QIRKLREECQALMVELQMLLDTKQTLDGELKVYRQMLE 418
Cdd:COG4913 413 ALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
143-366 |
9.29e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 9.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 143 EKEIRKLQDQLDELRKKFEEAQRGRAEDR--LKIDDLLVTLSNLEAEINLL-KRRIALLEEEVARLKKENFRLTSELQRV 219
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESelIKLKELAEQLKELEEKLKKYnLEELEKKAEEYEKLKEKLIKLKGEIKSL 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 220 RIELDQETLLridnQNKVKTILEEIDFMKR---GFETELKELQAQAARDTTSENREYFK-----NELANAMRDIRAEYDQ 291
Cdd:PRK03918 545 KKELEKLEEL----KKKLAELEKKLDELEEelaELLKELEELGFESVEELEERLKELEPfyneyLELKDAEKELEREEKE 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17568557 292 IMNGNRNDMESWYQLRVQEINTQSNR---QNAENNYQKEEVKRLRNQTSELRQKLSDLESRNLLLEKQIEDLNYQLED 366
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEELRkelEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
141-292 |
1.00e-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: 41.06 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 141 ETEKEIRKLQDQLDELRKKFEEAQRgraedrlKIDDLLVTLSNLEAEINLLKRRIALLEEEVARLKKenfrltselqrvR 220
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELED-------ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA------------R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 221 IELDQETLLRIDNQNKVKTILEEIDFMKR---GFETELKEL-----QAQAARDTTSENREYFKNELANAMRDIRAEYDQI 292
Cdd:COG1579 75 IKKYEEQLGNVRNNKEYEALQKEIESLKRrisDLEDEILELmerieELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
64-422 |
1.03e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 64 IRDNREREKKEIMELNDRLASYIEKVRFLDAQNRKLDADLKMLQgrfgKSTGSVKVMYEMEITTATNVVKQTgkdHGETE 143
Cdd:pfam15921 262 LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQ----EQARNQNSMYMRQLSDLESTVSQL---RSELR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 144 KEIRKLQDQLDELRKKFEEAQRGRAEDRLKIDDLLVTLSNLEAEINLLKRRIALLEEEVARLKKENFRL-------TSEL 216
Cdd:pfam15921 335 EAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwdrdtgnSITI 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 217 QRVRIELDQ--------ETLLR----------------IDNQN----KVKTILEEIDFMKRGFETELKELqaqAARDTTS 268
Cdd:pfam15921 415 DHLRRELDDrnmevqrlEALLKamksecqgqmerqmaaIQGKNesleKVSSLTAQLESTKEMLRKVVEEL---TAKKMTL 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 269 ENREYFKNELANAMRDiRAEYDQIMNGNRNDMESWYQLRVQEINTQSNRQNAENNYQKeEVKRLRNQTSE-------LRQ 341
Cdd:pfam15921 492 ESSERTVSDLTASLQE-KERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQT-ECEALKLQMAEkdkvieiLRQ 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 342 KLSDL--------------ESRNLLLEKQIEDLNYQLEDdqrsYEAALNDKDAQIRKLREECQALMVE-----------L 396
Cdd:pfam15921 570 QIENMtqlvgqhgrtagamQVEKAQLEKEINDRRLELQE----FKILKDKKDAKIRELEARVSDLELEkvklvnagserL 645
|
410 420
....*....|....*....|....*....
gi 17568557 397 QMLLDTKQTLD---GELKVYRQMLEGNSE 422
Cdd:pfam15921 646 RAVKDIKQERDqllNEVKTSRNELNSLSE 674
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
141-356 |
1.25e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 141 ETEKEIRKLQDQLDELRKKFEEAQRgraedrlKIDDLLVTLSNLEAEINLLKRRIALLEEEVARLKKENFRLTSELQRVR 220
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNE-------EYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 221 IELDqeTLLRIDNQNKVKTILEEIDFMKRGFETELKELQAQAARdttsenreyfKNELANAMRDIRAEYDQIMNgNRNDM 300
Cdd:COG3883 100 GSVS--YLDVLLGSESFSDFLDRLSALSKIADADADLLEELKAD----------KAELEAKKAELEAKLAELEA-LKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17568557 301 ESwyqlRVQEINTQSNRQNAENNYQKEEVKRLRNQTSELRQKLSDLESRNLLLEKQ 356
Cdd:COG3883 167 EA----AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
121-387 |
1.48e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 121 YEMEITTATNVVKQTGKDHGETEKEIRKLQDQLDELRKKF----EEAQRGRAEDRLKIDDLLVTLSNLEAEINLLKRRIA 196
Cdd:PRK01156 361 YEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQeidpDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLD 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 197 LLEEEVARLKKENfrlTSELQRVRIELDQETLLRIDNQNKVKTILEEIDFMKR---GFETELKELQAQAARDTTSENREY 273
Cdd:PRK01156 441 ELSRNMEMLNGQS---VCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIevkDIDEKIVDLKKRKEYLESEEINKS 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 274 FKNElaNAMRDIRAEYDQIMNGNRNDMESwyQLRVQEINTQSNRQNAENNYQKEE-------------VKRLRNQTSELR 340
Cdd:PRK01156 518 INEY--NKIESARADLEDIKIKINELKDK--HDKYEEIKNRYKSLKLEDLDSKRTswlnalavislidIETNRSRSNEIK 593
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 17568557 341 QKLSDLESRNLLLEKQIEDLNY-------QLEDDQRSYEAALN---DKDAQIRKLRE 387
Cdd:PRK01156 594 KQLNDLESRLQEIEIGFPDDKSyidksirEIENEANNLNNKYNeiqENKILIEKLRG 650
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
69-366 |
2.20e-03 |
|
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: 41.11 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 69 EREKKEIMELNDRLASYIEKVRFLDAQNRKLDADLKMLQGRFGKSTGSVKVMYEMEITTATNVVKQTGKDHGETEKEIRK 148
Cdd:pfam02463 204 EQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 149 LQDQLDELRKKFEEAQRGRAEDRLKIDDLLVTLSNLEAEINLLKRRIALLEEEVARLKKENFRLTSELQRVRIELDQETL 228
Cdd:pfam02463 284 QEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEK 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 229 LRIDNQNKVKTILEEIDFMKRGFETELKELQAQAARDTTSENREYFKNELANAMRDIRAEYDQimngnrndmeswyQLRV 308
Cdd:pfam02463 364 LQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKK-------------EELE 430
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 17568557 309 QEINTQSNRQNAENNYQKEEVKRLRNQTSELRQKLSDLESRNLLLEKQIEDLNYQLED 366
Cdd:pfam02463 431 ILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLEL 488
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
69-374 |
2.50e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 69 EREKKEIMELNDRLASYIEKVRFLDAQNRKLDADLKMLQGRFGKSTGSVKVMYEMEITTATNVVKQTGKDHGETEKEIRK 148
Cdd:COG4717 138 EAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 149 LQDQLDELRKKFE--EAQRGRAEDRLKIDDLLVTL-----------------SNLEAEINLLKRRIALLEEEVARLKKEN 209
Cdd:COG4717 218 AQEELEELEEELEqlENELEAAALEERLKEARLLLliaaallallglggsllSLILTIAGVLFLVLGLLALLFLLLAREK 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 210 FRLTSELQRV-----RIELDQETLLRI-------------------DNQNKVKTILEEIDFMKR-----GFETELKELQA 260
Cdd:COG4717 298 ASLGKEAEELqalpaLEELEEEELEELlaalglppdlspeellellDRIEELQELLREAEELEEelqleELEQEIAALLA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 261 QAarDTTSENREYFKNELANAMRDIRAEY----DQIMNGNRNDMESWYQLRVQEINTQSNRQNAENNYQKEEVKRLRNQT 336
Cdd:COG4717 378 EA--GVEDEEELRAALEQAEEYQELKEELeeleEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREEL 455
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 17568557 337 SELRQKLSDLESRNLL--LEKQIEDLNYQLEDDQRSYEAA 374
Cdd:COG4717 456 AELEAELEQLEEDGELaeLLQELEELKAELRELAEEWAAL 495
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
87-367 |
2.56e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 87 EKVRFLDAQNRKLDADLKMLQGRFGKSTGSVKVMYEMEITTATNVVK--QTGKDHGETEKEIRKLQDQLDELRKKfEEAQ 164
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKaaEEAKKAEEDKKKAEEAKKAEEDEKKA-AEAL 1694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 165 RGRAEDRLKIDDLLVTLSNLEAEINLLKRriallEEEVARLKKENFRLTSELQRVRIELdqetlLRIDNQNKVKtiLEEI 244
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKK-----AEEENKIKAEEAKKEAEEDKKKAEE-----AKKDEEEKKK--IAHL 1762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 245 DFMKRGFETELKELQAQAARDTTSENREYFKNELANAMRDIRAEYDQIMNGNR------NDMESWYQLRVQEINTQSNRQ 318
Cdd:PTZ00121 1763 KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKegnlviNDSKEMEDSAIKEVADSKNMQ 1842
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17568557 319 NAENNYQKEEVKRLRNQTSELRQKLSDLESRNLLLEKQIE-----DLNYQLEDD 367
Cdd:PTZ00121 1843 LEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEeieeaDEIEKIDKD 1896
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
74-225 |
2.94e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 38.76 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 74 EIMELNDRLAsyiEKVRFLDAQNRKLDADLKMLQGRFGKSTGSVKVMYEMEITTATNVVKQTG-------KDHGETEKEI 146
Cdd:pfam08614 4 ELIDAYNRLL---DRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLReelaelyRSRGELAQRL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17568557 147 RKLQDQLDELRKKFEEAQRgraedrlkiddllvTLSNLEAEINLLKRRIALLEEEVARLKKENFRLTSELQRVRIELDQ 225
Cdd:pfam08614 81 VDLNEELQELEKKLREDER--------------RLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNM 145
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
138-465 |
2.95e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 138 DHGETEKEIRKLQDQLDELRKKFEEAQRGRAEDRLKIDDLLVTLSNLEAEINLLKRRIALLEEEVARLKKENFRLTSELQ 217
Cdd:PRK02224 245 EHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 218 RVRIELDQETLLRIDNQNKVKTILEEIDfmkrGFETELKELQAQAAR-DTTSENREYFKNELANAMRDIRAEYDQIMNgn 296
Cdd:PRK02224 325 ELRDRLEECRVAAQAHNEEAESLREDAD----DLEERAEELREEAAElESELEEAREAVEDRREEIEELEEEIEELRE-- 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 297 rndmeswyqlRVQEINTQSNRQNAENNYQKEEVKRLRNQTSELRQKLSDL-----ESRNLLLEKQIEDLNYQLEDDQRSy 371
Cdd:PRK02224 399 ----------RFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTArerveEAEALLEAGKCPECGQPVEGSPHV- 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 372 eAALNDKDAQIRKLREecqalmvELQMLLDTKQTLDGELKVYRQMLEGNSEGNGLRQLVEKVV-----RTSAINEEADT- 445
Cdd:PRK02224 468 -ETIEEDRERVEELEA-------ELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEeliaeRRETIEEKRERa 539
|
330 340
....*....|....*....|
gi 17568557 446 ETMRVVKGEHSSRTSYQRSA 465
Cdd:PRK02224 540 EELRERAAELEAEAEEKREA 559
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
154-418 |
3.29e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 154 DELRKKFEEA--------QRGRAEDRLK--------IDDLLvtlsnleAEinlLKRRIALLEEEVARLKKenFR-LTSEL 216
Cdd:COG1196 155 EERRAIIEEAagiskykeRKEEAERKLEateenlerLEDIL-------GE---LERQLEPLERQAEKAER--YReLKEEL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 217 QRVRIELdqeTLLRIDN-QNKVKTILEEIDfmkrGFETELKELQAQAArdttsenreyfknELANAMRDIRAEYDQImng 295
Cdd:COG1196 223 KELEAEL---LLLKLRElEAELEELEAELE----ELEAELEELEAELA-------------ELEAELEELRLELEEL--- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 296 nrndmeswyQLRVQEINTQSNRQNAENNYQKEEVKRLRNQTSELRQKLSDLESRNLLLEKQIEDLNYQLEDDQRSYEAAL 375
Cdd:COG1196 280 ---------ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 17568557 376 NDKDAQIRKLREECQALMVELQMLLDTKQTLDGELKVYRQMLE 418
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
132-361 |
3.38e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 132 VKQTGKDHGETEKEIRKLQDQLDELRKKFEEAQRGRAEDRLKIDDLLVTLSNLEAEINLLKRRIALLEEEVARLKKENFR 211
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 212 LTSELQRVRIELDQETLLRIDNQNKVKTILEEIDFMKRGFETELKELQAQAARDTTSENREYFKNELANAMRDIRAEYDQ 291
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAE 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 292 IMNGNRNDMESWYQLRVQEINTQSNRQNAENNYQKEEVKRLRNQTSELRQKLSDLESRNLLLEKQIEDLN 361
Cdd:COG4372 207 KLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEE 276
|
|
| COG4192 |
COG4192 |
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
141-407 |
3.70e-03 |
|
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];
Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 40.05 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 141 ETEKEIRKLQDQLDELRKKFEEAQRGRAEDRlkIDDLLVTLSNLEAEINLLKRRIALLEEEVARLKKENFRLTSELQRvr 220
Cdd:COG4192 59 KLEENSNELVAALPEFAAATNTTERSQLRNQ--LNTQLADIEELLAELEQLTQDAGDLRAAVADLRNLLQQLDSLLTQ-- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 221 ieldqetllRIDNQNKVKTILEEIDFMKRGFETELKEL------QAQAARD--TTSENREYFKNELaNAMRDIRAEYDQI 292
Cdd:COG4192 135 ---------RIALRRRLQELLEQINWLHQDFNSELTPLlqeaswQQTRLLDsvETTESLRNLQNEL-QLLLRLLAIENQI 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 293 MngnrndmeswYQLR-VQEINTQSNRQNAEN--NYQKEEVKR----LRNQTSE--LRQKLSDL----ESRNLLLEKQIED 359
Cdd:COG4192 205 V----------SLLReVAAARDQADVDNLFDrlQYLKDELDRnlqaLKNYPSTitLRQLIDELlaigSGEGGLPSLRRDE 274
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 17568557 360 LNYqleddQRSYEAALNDKDAQIRKLREECQalmvelQMLLDTKQTLD 407
Cdd:COG4192 275 LAA-----QATLEALAEENNSILEQLRTQIS------GLVGNSREQLV 311
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
161-375 |
5.13e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 38.49 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 161 EEAQRGRAEDRLKIddllVTLSNLEAEINLLKRRIALLEEEVARLKKENFRLTSELQ--RVRIElDQETLLRIDNQNKVK 238
Cdd:pfam15665 25 EEIQQILAETREKI----LQYKSKIGEELDLKRRIQTLEESLEQHERMKRQALTEFEqyKRRVE-ERELKAEAEHRQRVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 239 TILEEIDFMKRGFETELKELQAQAardttsenreyfknelanamrdirAEYDQIMNGNRNDMESWYQLRVQEINTQSNRQ 318
Cdd:pfam15665 100 ELSREVEEAKRAFEEKLESFEQLQ------------------------AQFEQEKRKALEELRAKHRQEIQELLTTQRAQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17568557 319 NAENNYQKEEVKRL-RNQTSELRQKLSDLESRNLlleKQIEDLNYQLEDDQRSYEAAL 375
Cdd:pfam15665 156 SASSLAEQEKLEELhKAELESLRKEVEDLRKEKK---KLAEEYEQKLSKAQAFYEREL 210
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
72-228 |
5.88e-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: 38.75 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 72 KKEIMELNDRLASYIEKVRFLDAQNRKLDADLKMLQGRFGKSTGSVK-VMYEMEITTATNVVKQTGKDHGETEKEIRKLQ 150
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnVRNNKEYEALQKEIESLKRRISDLEDEILELM 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17568557 151 DQLDELRKKFEEAQrgraedrlkiddllvtlSNLEAEINLLKRRIALLEEEVARLKKENFRLTSELQRVRIELDQETL 228
Cdd:COG1579 117 ERIEELEEELAELE-----------------AELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPELL 177
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
138-351 |
8.33e-03 |
|
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: 39.07 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 138 DHGETEKEIRKLQDQLDELRKKFEEAQRGRAEDRL-----KIDDLLVTlsnLEAEI---NLLKRRIALLEEEVARLKKEN 209
Cdd:pfam06160 231 EHLNVDKEIQQLEEQLEENLALLENLELDEAEEALeeieeRIDQLYDL---LEKEVdakKYVEKNLPEIEDYLEHAEEQN 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568557 210 FRLTSELQRV--RIELDQETLLRIdnqnkvktileeidfmkRGFETELKELQAQAARDTtsenreyfknelaNAMRDIRA 287
Cdd:pfam06160 308 KELKEELERVqqSYTLNENELERV-----------------RGLEKQLEELEKRYDEIV-------------ERLEEKEV 357
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17568557 288 EYDQImngnRNDMESWYQlRVQEINT-QSNRQNAENNYQKEEvKRLRNQTSELRQKLSD----LESRNL 351
Cdd:pfam06160 358 AYSEL----QEELEEILE-QLEEIEEeQEEFKESLQSLRKDE-LEAREKLDEFKLELREikrlVEKSNL 420
|
|
| ZapB |
pfam06005 |
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ... |
181-245 |
9.85e-03 |
|
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.
Pssm-ID: 428718 [Multi-domain] Cd Length: 71 Bit Score: 34.93 E-value: 9.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17568557 181 LSNLEAEINLLKRRIALLEEEVARLKKENFRLTSELQRVRIELDQETLLRIDNQNKVKTILEEID 245
Cdd:pfam06005 6 LEQLETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQERIRGLLGKLD 70
|
|
| |
