|
Name |
Accession |
Description |
Interval |
E-value |
| Angiomotin_C |
pfam12240 |
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ... |
289-496 |
6.58e-105 |
|
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 and 211 amino acids in length. This family is the C terminal region of angiomotin. Angiomotin regulates the action of angiogenesis inhibitor angiostatin. The C terminal region of angiomotin appears to be involved in directing the protein chemotactically.
Pssm-ID: 463503 [Multi-domain] Cd Length: 200 Bit Score: 321.72 E-value: 6.58e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 289 YVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEYNAAALMELLREKEERILALEADM 368
Cdd:pfam12240 1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 369 TKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALeariqkeEEEILMANKRCLDMEGRIKTLHAQIIEK 448
Cdd:pfam12240 81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSYDSSF-------NEELLLANRRCQEMENRIKNLHAQILEK 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 569012030 449 DAMIKVLQQRSRKEPSKTEQlSSMRPAKSLMSISNAGSGLLAHSSTLT 496
Cdd:pfam12240 154 DAMIKVLQQRSRKDPGKTDQ-QSLRPARSVPSISAAATGLHSRQTSLS 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
123-367 |
9.51e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 9.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 123 RAQQMVEILSDENRNLRQELDgcyEKVARLQKVETEIQRVSEAYENL---VKSSSKREALEKAMRNKLEGEIRRMHDFNR 199
Cdd:COG1196 236 ELEAELEELEAELEELEAELE---ELEAELAELEAELEELRLELEELeleLEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 200 DLRDRLETANKQLAEKEYEGSEDTRKtISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKL 279
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEE-LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 280 EEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEYNAAALMELLREKEE 359
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
....*...
gi 569012030 360 RILALEAD 367
Cdd:COG1196 472 AALLEAAL 479
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
150-375 |
6.62e-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: 63.16 E-value: 6.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 150 ARLQKVETEIQRVSEAYENLvkssSKREALEKAMRNKLEGEIRRMHDFNRDLRDRLETANKQLAEKEYEgSEDTRKTISQ 229
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEEL----EREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE-LKDYREKLEK 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 230 LFAKHKENQREKEKLEAELatarstnedQRRHIEIRD--QALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAAC 307
Cdd:TIGR02169 397 LKREINELKRELDRLQEEL---------QRLSEELADlnAAIAGIEAKINELEEEKEDKA---LEIKKQEWKLEQLAADL 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569012030 308 EKREQLEHRLRT---RLERELESL-----RIQQRQGNSQPTnaSEYNAAAlMELLREKEERILALEADMTKWEQKY 375
Cdd:TIGR02169 465 SKYEQELYDLKEeydRVEKELSKLqrelaEAEAQARASEER--VRGGRAV-EEVLKASIQGVHGTVAQLGSVGERY 537
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
123-374 |
1.31e-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: 62.00 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 123 RAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQR--------VSEAYENLVKSSSKREALEKAMRNkLEGEIRRM 194
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKeleelsrqISALRKDLARLEAEVEQLEERIAQ-LSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 195 HDFNRDLRDRLETANKQLAEKEyEGSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQA 274
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAE-AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 275 KVVKLEEELKKKQvyvDKVEKMQQALVQLQAACEK-REQLEHRL--RTRLERELESLRIQQRQGNSQpTNASEYNAAALM 351
Cdd:TIGR02168 839 RLEDLEEQIEELS---EDIESLAAEIEELEELIEElESELEALLneRASLEEALALLRSELEELSEE-LRELESKRSELR 914
|
250 260
....*....|....*....|...
gi 569012030 352 ELLREKEERILALEADMTKWEQK 374
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVR 937
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
175-469 |
2.69e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 175 KREALEK--AMRNKLEgeirRMHDFNRDLRDRLETANKQlAEK-----EYEGSEDTRKtISQLFAKHKENQREKEKLEAE 247
Cdd:COG1196 174 KEEAERKleATEENLE----RLEDILGELERQLEPLERQ-AEKaeryrELKEELKELE-AELLLLKLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 248 LATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQvyvdkveKMQQALVQLQAACEKREQLEHRLRTRLERELES 327
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-------AEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 328 LRIQQRQGNSQptnaseynAAALMELLREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNT 407
Cdd:COG1196 321 LEEELAELEEE--------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569012030 408 SYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQL 469
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
123-375 |
4.12e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 123 RAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLR 202
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 203 DRLETANKQLAEKEYEGSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEE 282
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 283 LKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEynAAALMELLREKEERIL 362
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA--LAELLEELAEAAARLL 494
|
250
....*....|...
gi 569012030 363 ALEADMTKWEQKY 375
Cdd:COG1196 495 LLLEAEADYEGFL 507
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
151-471 |
6.38e-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: 59.69 E-value: 6.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 151 RLQKVETEiQRVSEAYENLVKSSSKREALEKAMrNKLEGEIRRMHDFnRDLRDRLETANKQLAEKEYEgseDTRKTISQL 230
Cdd:TIGR02168 171 KERRKETE-RKLERTRENLDRLEDILNELERQL-KSLERQAEKAERY-KELKAELRELELALLVLRLE---ELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 231 FAKHKENQREKEKLEAELATArstnedqrrhieirDQALSNAQAKVVKLEEELKKKQvyvdkveKMQQALVQLQAACEKR 310
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQEL--------------EEKLEELRLEVSELEEEIEELQ-------KELYALANEISRLEQQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 311 EQLEHRLRTRLERELESLRIQQRQGNSQPTNASEyNAAALMELLREKEERILALEADMTKWEQKYLEenvmrhfaldaaa 390
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAE-ELAELEEKLEELKEELESLEAELEELEAELEE------------- 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 391 tvaaqrdttvishspntsydtaLEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLS 470
Cdd:TIGR02168 370 ----------------------LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
.
gi 569012030 471 S 471
Cdd:TIGR02168 428 K 428
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
118-378 |
8.57e-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: 59.31 E-value: 8.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 118 FAMVSRAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDf 197
Cdd:TIGR02169 708 SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA- 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 198 nRDLRDRLETANKQLAEKEYEGSEdTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVV 277
Cdd:TIGR02169 787 -RLSHSRIPEIQAELSKLEEEVSR-IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 278 KLEEELKKKQVYVDKVEK------------------MQQALVQLQAACEKREQLEHRLRTRLERELESLR-IQQRQGNSQ 338
Cdd:TIGR02169 865 ELEEELEELEAALRDLESrlgdlkkerdeleaqlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSeIEDPKGEDE 944
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 569012030 339 PTNASEYNAAALMELLREKEERILALEADMTKWEQKYLEE 378
Cdd:TIGR02169 945 EIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEV 984
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
116-336 |
1.15e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 116 DPFAMVSRAQQMVEILSDENRnLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALE----KAMRNKLEGEI 191
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLER-AHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRlwfaQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 192 RRmhdfnrdLRDRLETANKQLAEKEyEGSEDTRKTISQLFAKHKENQ-REKEKLEAELATARSTNEDQRRHIEIRDQALS 270
Cdd:COG4913 298 EE-------LRAELARLEAELERLE-ARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569012030 271 NAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAACE--------KREQLEHRLRtRLERELESLRiqQRQGN 336
Cdd:COG4913 370 ALGLPLPASAEEFAALR---AEAAALLEALEEELEALEealaeaeaALRDLRRELR-ELEAEIASLE--RRKSN 437
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
114-447 |
1.51e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 114 PADPF--AMVSRAQQMVEIL-SDENRN--LRQELD-GCYEKVAR-LQKVETEIQRVSEAYENLVKSSSKREALEKAMRNK 186
Cdd:PRK03918 122 PYHVFlnAIYIRQGEIDAILeSDESREkvVRQILGlDDYENAYKnLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKE 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 187 LEGEIRRMHDFNRDLRDRLETANKqlAEKEYEGSEDTRKTISQLfakhkenQREKEKLEAELatarstnedqrRHIEIRD 266
Cdd:PRK03918 202 LEEVLREINEISSELPELREELEK--LEKEVKELEELKEEIEEL-------EKELESLEGSK-----------RKLEEKI 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 267 QALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQaacEKREQLEHRLRtRLERELESLRiQQRQGnsqptnaseyn 346
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLS---EFYEEYLDELR-EIEKRLSRLE-EEING----------- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 347 AAALMELLREKEERILALEADMTKWEQKY--LEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEE--E 422
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEKRLeeLEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEieE 405
|
330 340
....*....|....*....|....*
gi 569012030 423 EILMANKRCLDMEGRIKTLHAQIIE 447
Cdd:PRK03918 406 EISKITARIGELKKEIKELKKAIEE 430
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
209-379 |
3.10e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 209 NKQLAEKEYEGSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQ--AKVVKLEEELKKK 286
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 287 QVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPT---NASEYNAAALMELLREKEERILA 363
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAeelEELQQRLAELEEELEEAQEELEE 224
|
170
....*....|....*.
gi 569012030 364 LEADMTKWEQKYLEEN 379
Cdd:COG4717 225 LEEELEQLENELEAAA 240
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
150-374 |
1.69e-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: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 150 ARLQKVETEIQRVSEAYENLVKSSSKREALEKAmrnklegeirrmhdfnRDLRDRLETANKQLAEKEYEGSEdtrktisq 229
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELLEPI----------------RELAERYAAARERLAELEYLRAA-------- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 230 lfAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELkkKQVYVDKVEKMQQALVQLQAACEK 309
Cdd:COG4913 281 --LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI--RGNGGDRLEQLEREIERLERELEE 356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569012030 310 REqlehRLRTRLERELESLriqqrqGNSQPTNASEY--NAAALMELLREKEERILALEADMTKWEQK 374
Cdd:COG4913 357 RE----RRRARLEALLAAL------GLPLPASAEEFaaLRAEAAALLEALEEELEALEEALAEAEAA 413
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
140-319 |
1.78e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 140 QELDGCYEKVARLQKVETEIQrvsEAYENLVKSSSKREALEKAmRNKLEGEIRRMHDF--NRDLRDRLETANKQLAE--K 215
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYA---ELQEELEELEEELEELEAE-LEELREELEKLEKLlqLLPLYQELEALEAELAElpE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 216 EYEGSEDTRKTISQLFAKHKENQREKEKLEAELATA-RSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVE 294
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180
....*....|....*....|....*
gi 569012030 295 KMQQALVQLQAACEKREQLEHRLRT 319
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLL 251
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
137-377 |
3.41e-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: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 137 NLRQELDGCYEKVARLQKVETEIQRVSEAYEnlvkssSKREALEKAMR--NKLEGEIRRMHDFNRDLRDRLETANKQLAE 214
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELR------KELEELEEELEqlRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 215 KeyegSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVE 294
Cdd:TIGR02168 748 R----IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 295 KMQQALVQLQAACEKR-EQLEHRLR------TRLERELESLRIQ------QRQGNSQPTNASEYNAAALMELLREKEERI 361
Cdd:TIGR02168 824 ERLESLERRIAATERRlEDLEEQIEelsediESLAAEIEELEELieelesELEALLNERASLEEALALLRSELEELSEEL 903
|
250
....*....|....*.
gi 569012030 362 LALEADMTKWEQKYLE 377
Cdd:TIGR02168 904 RELESKRSELRRELEE 919
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
62-340 |
9.24e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.04 E-value: 9.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 62 LSRHQQHLLSSQSHQGdHYRHAQASLTSAQQQPGeaysAMPRAQQSASyqpmpadpfAMVSRAQQMVEILSDENRNLRQE 141
Cdd:PRK04863 399 LADYQQALDVQQTRAI-QYQQAVQALERAKQLCG----LPDLTADNAE---------DWLEEFQAKEQEATEELLSLEQK 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 142 LD------GCYEKVARL-QKVETEIQRvSEAY----ENLVKSSSKREALEK--AMRNKLeGEIRRMHDFNRDLRDRLETA 208
Cdd:PRK04863 465 LSvaqaahSQFEQAYQLvRKIAGEVSR-SEAWdvarELLRRLREQRHLAEQlqQLRMRL-SELEQRLRQQQRAERLLAEF 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 209 NKQLaEKEYEGSEDtrktisqLFAKHKENQREKEKLEAELATARSTNEDQRRHIE----------IRDQALSNAQAKVVK 278
Cdd:PRK04863 543 CKRL-GKNLDDEDE-------LEQLQEELEARLESLSESVSEARERRMALRQQLEqlqariqrlaARAPAWLAAQDALAR 614
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569012030 279 LEE----ELKKKQvyvDKVEKMQQALVQLQAACEKREQLEHRlRTRLERELESLriQQRQGNSQPT 340
Cdd:PRK04863 615 LREqsgeEFEDSQ---DVTEYMQQLLERERELTVERDELAAR-KQALDEEIERL--SQPGGSEDPR 674
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
131-328 |
2.05e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 131 LSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKS------------SSKREALEKAMRNKLE-----GEIRR 193
Cdd:PRK03918 537 LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEleelgfesveelEERLKELEPFYNEYLElkdaeKELER 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 194 MHDFNRDLRDRLETANKQLAEKEYEgSEDTRKTISQLFAK-----HKENQREKEKLEAELATARSTNEDQRRHieiRDQA 268
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELAETEKR-LEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKR---REEI 692
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 269 LSNAQakvvKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESL 328
Cdd:PRK03918 693 KKTLE----KLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGEI 748
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
152-370 |
2.25e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 152 LQKVETEIQRVSEAYENlVKS--SSKREALEKamrnkLEGEIRRMHDfnRDLRDRLETANKQLAE-----KEYEGSED-- 222
Cdd:PRK02224 161 LGKLEEYRERASDARLG-VERvlSDQRGSLDQ-----LKAQIEEKEE--KDLHERLNGLESELAEldeeiERYEEQREqa 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 223 --TRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKkkqvyvDKVEKMQQAL 300
Cdd:PRK02224 233 reTRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERD------DLLAEAGLDD 306
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 301 VQLQAACEKREQLEHRlRTRLERELESLRIQQRQGNSQPTNASEyNAAALMELLREKEERILALEADMTK 370
Cdd:PRK02224 307 ADAEAVEARREELEDR-DEELRDRLEECRVAAQAHNEEAESLRE-DADDLEERAEELREEAAELESELEE 374
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
131-367 |
3.94e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 131 LSDENRNLRQELDGCYEKVARLQ-KVETEIQRVSEAYENL-----------VKSSSKREALE--KAMRNKLEGEIRRMHD 196
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEaTLRTARERVEEAEALLeagkcpecgqpVEGSPHVETIEedRERVEELEAELEDLEE 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 197 FNRDLRDRLETANK-QLAEKEYEGSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRhiEIRDQAlsnaqak 275
Cdd:PRK02224 490 EVEEVEERLERAEDlVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAE--EKREAA------- 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 276 vVKLEEELKKKQVYVDKVEKmqqalvQLQAACEKREQLEhRLRTRL------ERELESLRIQQRQGNSQPTNASEYnaaa 349
Cdd:PRK02224 561 -AEAEEEAEEAREEVAELNS------KLAELKERIESLE-RIRTLLaaiadaEDEIERLREKREALAELNDERRER---- 628
|
250
....*....|....*...
gi 569012030 350 lmelLREKEERILALEAD 367
Cdd:PRK02224 629 ----LAEKRERKRELEAE 642
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
125-476 |
3.99e-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: 50.59 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 125 QQMVEILSDENRNLRQELDGCYEKVARLQK----VETEIQRVSEAY-------ENLvkssskREALEKAMRNKLEgEIRR 193
Cdd:pfam10174 400 QKKIENLQEQLRDKDKQLAGLKERVKSLQTdssnTDTALTTLEEALsekeriiERL------KEQREREDRERLE-ELES 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 194 MHDFNRDLRDRLETANKQLAEKEYEGSEDTRKTISQLFAKHKENQREKE-------------KLEAELATARSTNEDQRR 260
Cdd:pfam10174 473 LKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSleiaveqkkeecsKLENQLKKAHNAEEAVRT 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 261 HIEIRDQaLSNAQAKVVKLEEELKKKQVyvdKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPT 340
Cdd:pfam10174 553 NPEINDR-IRLLEQEVARYKEESGKAQA---EVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQ 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 341 NASEYNAAALMELLREKEERilaleadMTKWEQKYLEENVMRHFALDAAATVAAQR-DTTVISHSPNTSYDTALEARIQK 419
Cdd:pfam10174 629 EMKKKGAQLLEEARRREDNL-------ADNSQQLQLEELMGALEKTRQELDATKARlSSTQQSLAEKDGHLTNLRAERRK 701
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 569012030 420 EEEEILmankrcldmEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSSMRPAK 476
Cdd:pfam10174 702 QLEEIL---------EMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALKREK 749
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
132-334 |
7.38e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 132 SDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRDRLETANKQ 211
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 212 LAEKEYEGSEDTR---KTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQV 288
Cdd:COG4942 99 LEAQKEELAELLRalyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 569012030 289 YVDKVEKMQQALVQLQAaceKREQLEHRLRTRLERELESLRIQQRQ 334
Cdd:COG4942 179 LLAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQE 221
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
151-334 |
1.20e-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: 47.61 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 151 RLQKVETEIQRVseayenlvkssskrealeKAMRNKLEGEIrrmhdfnRDLRDRLETANKQLAEKEyEGSEDTRKTISQL 230
Cdd:COG1579 11 DLQELDSELDRL------------------EHRLKELPAEL-------AELEDELAALEARLEAAK-TELEDLEKEIKRL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 231 FAKHKENQREKEKLEAELATARSTNEdqrrhIEIRDQALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAACEKR 310
Cdd:COG1579 65 ELEIEEVEARIKKYEEQLGNVRNNKE-----YEALQKEIESLKRRISDLEDEILELM---ERIEELEEELAELEAELAEL 136
|
170 180
....*....|....*....|....
gi 569012030 311 EQLEHRLRTRLERELESLRIQQRQ 334
Cdd:COG1579 137 EAELEEKKAELDEELAELEAELEE 160
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
131-378 |
1.41e-05 |
|
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: 48.53 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 131 LSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENL------VKSSSKREALEKAMRNKLEGEIRRMHDfnrdLRDR 204
Cdd:pfam05622 109 LAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLgdlrrqVKLLEERNAEYMQRTLQLEEELKKANA----LRGQ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 205 LETANKQLAEKEYEGSEDTRKTISQLF------AKHKENQREKEKLEAELATARSTNED------QRRHIEIRDQALS-- 270
Cdd:pfam05622 185 LETYKRQVQELHGKLSEESKKADKLEFeykkleEKLEALQKEKERLIIERDTLRETNEElrcaqlQQAELSQADALLSps 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 271 -----NAQA---------KVVKLEEE-----LKKKQVYVDKVEKMQQalvQLQAACEKREQLEHRLRTRLERELE-SLRI 330
Cdd:pfam05622 265 sdpgdNLAAeimpaeireKLIRLQHEnkmlrLGQEGSYRERLTELQQ---LLEDANRRKNELETQNRLANQRILElQQQV 341
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 569012030 331 QQRQGNSQPTNASEYNAAALMELLREKEERILALEADMTKwEQKYLEE 378
Cdd:pfam05622 342 EELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQK-KKEQIEE 388
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
133-275 |
1.49e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 133 DENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAmRNKLEGEIRRMHDFN-------------R 199
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL-EAELAELPERLEELEerleelreleeelE 166
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569012030 200 DLRDRLETANKQLAEKEYEGSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAK 275
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
129-369 |
2.02e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 129 EILSDENRNLRQELDGCYEkvaRLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNK---LEGEIRRMHDFNRDLRDRL 205
Cdd:PRK02224 310 EAVEARREELEDRDEELRD---RLEECRVAAQAHNEEAESLREDADDLEERAEELREEaaeLESELEEAREAVEDRREEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 206 ETANKQL--AEKEYEGSEDTR---KTISQLFAKHKENQREKEK-LEAELATARSTNEDQRRHIE----------IRD--- 266
Cdd:PRK02224 387 EELEEEIeeLRERFGDAPVDLgnaEDFLEELREERDELREREAeLEATLRTARERVEEAEALLEagkcpecgqpVEGsph 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 267 -QALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAAC-------EKREQLEHRLRTRLER-ELESLRIQQRQGNS 337
Cdd:PRK02224 467 vETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEdrierleERREDLEELIAERRETiEEKRERAEELRERA 546
|
250 260 270
....*....|....*....|....*....|....*.
gi 569012030 338 QPTNAS----EYNAAALMELLREKEERILALEADMT 369
Cdd:PRK02224 547 AELEAEaeekREAAAEAEEEAEEAREEVAELNSKLA 582
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
138-463 |
4.11e-05 |
|
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: 47.36 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 138 LRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALE-KAMRNKLEGEIRRMHDFNRDLRDRLETANKQLAEKE 216
Cdd:TIGR02168 194 ILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEElREELEELQEELKEAEEELEELTAELQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 217 YEGSEDtRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKM 296
Cdd:TIGR02168 274 LEVSEL-EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 297 QQALV-QLQAACEKREQLEHRLRTrLERELESLRIQQRQGNSQptnaseynAAALMELLREKEERILALEADMTKWEQKY 375
Cdd:TIGR02168 353 LESLEaELEELEAELEELESRLEE-LEEQLETLRSKVAQLELQ--------IASLNNEIERLEARLERLEDRRERLQQEI 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 376 LEENvmRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIiekdAMIKVL 455
Cdd:TIGR02168 424 EELL--KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL----DSLERL 497
|
....*...
gi 569012030 456 QQRSRKEP 463
Cdd:TIGR02168 498 QENLEGFS 505
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
123-323 |
4.43e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 123 RAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAmrnklEGEIRRmhdfNRDLR 202
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASA-----EREIAE----LEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 203 DRLETANKQLAEKEyEGSEDTRKTISQLFAKHKENQREKEKLEAELATArstnEDQRRHIEIRDQALSNAQAKVVKLEEE 282
Cdd:COG4913 678 ERLDASSDDLAALE-EQLEELEAELEELEEELDELKGEIGRLEKELEQA----EEELDELQDRLEAAEDLARLELRALLE 752
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 569012030 283 LKKKQVYVDKVEK-MQQALV-QLQAACEKREQLEHRLRTRLER 323
Cdd:COG4913 753 ERFAAALGDAVEReLRENLEeRIDALRARLNRAEEELERAMRA 795
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
175-473 |
4.44e-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: 47.27 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 175 KREALEKAMRNKLEGEIRRMHDFNRDLRDRLETANKQLAEKEYEGSEDTRKT------ISQLFAKHKENQREKEKLEAEL 248
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEeeyllyLDYLKLNEERIDLLQELLRDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 249 ATARSTNEDQRRHIEIRDQALSNA--QAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRL----- 321
Cdd:pfam02463 251 EEIESSKQEIEKEEEKLAQVLKENkeEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKaekel 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 322 -ERELESLRIQQRQGNSQPTNASEYNAAALMELLREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTV 400
Cdd:pfam02463 331 kKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLL 410
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569012030 401 ISHSPNTSYDTALEariQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSSMR 473
Cdd:pfam02463 411 LELARQLEDLLKEE---KKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
124-365 |
9.10e-05 |
|
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: 46.10 E-value: 9.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 124 AQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIR------RMHDF 197
Cdd:COG5185 303 KSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVElsksseELDSF 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 198 N---RDLRDRLETANKQLAEKEYEGSEDTRKTIsqlfakhKENQREKEKLEAELATARSTNEDQRRHIeirdQALSNAQA 274
Cdd:COG5185 383 KdtiESTKESLDEIPQNQRGYAQEILATLEDTL-------KAADRQIEELQRQIEQATSSNEEVSKLL----NELISELN 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 275 KVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTrLERELESLRIQ-QRQGNSQPTNASEYNAAALMEL 353
Cdd:COG5185 452 KVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVST-LKATLEKLRAKlERQLEGVRSKLDQVAESLKDFM 530
|
250
....*....|..
gi 569012030 354 LREKEERILALE 365
Cdd:COG5185 531 RARGYAHILALE 542
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
156-263 |
1.15e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.62 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 156 ETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRDRLETANKQLAEKEYEGSEDTRKTISQLFAKHK 235
Cdd:COG2433 387 EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDRE 466
|
90 100 110
....*....|....*....|....*....|
gi 569012030 236 ENQREKE--KLEAELATARSTNEDQRRHIE 263
Cdd:COG2433 467 ISRLDREieRLERELEEERERIEELKRKLE 496
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
124-328 |
2.16e-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: 45.17 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 124 AQQMVEILSDENRNLRQEldgcYEKVARLQKVETEIQRV-SEAYENLVKSSSKREALEKAMRnKLEGEIRRMHDFNRDLR 202
Cdd:pfam01576 154 RKLLEERISEFTSNLAEE----EEKAKSLSKLKNKHEAMiSDLEERLKKEEKGRQELEKAKR-KLEGESTDLQEQIAELQ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 203 DRLETANKQLAEKEYE------GSEDTRKTISQLFAKHKENQRE----KEKLEAELAtARSTNEDQRRHIEIRDQAL--- 269
Cdd:pfam01576 229 AQIAELRAQLAKKEEElqaalaRLEEETAQKNNALKKIRELEAQiselQEDLESERA-ARNKAEKQRRDLGEELEALkte 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569012030 270 -------SNAQAKV-VKLEEELKKKQVYVDKVEKMQQALVQ------LQAACEKREQLEH--RLRTRLERELESL 328
Cdd:pfam01576 308 ledtldtTAAQQELrSKREQEVTELKKALEEETRSHEAQLQemrqkhTQALEELTEQLEQakRNKANLEKAKQAL 382
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
221-519 |
2.58e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 221 EDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQ----VYVDKVEKM 296
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQeeaeELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 297 QQALVQLQAACEKREQLEHRLRTRL---ERELESLRIQQRQGNSQPTNASEYNAAALMELLREKEERILALEADMTKWEQ 373
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIaerEEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 374 KYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIK 453
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569012030 454 VLQQRSRKEPSKTEQLSSMRPAKSLMSISNAGSGLLAHSSTLTGAPIMEEKRDDKSWKGSLGVLLG 519
Cdd:COG4372 281 AALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
123-325 |
4.25e-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: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 123 RAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREAL---------EKAMRNKLEGEIRR 193
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELdgfergpfsERQIKNFHTLVIER 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 194 MHDFNR-------DLRDRLETANKQLAEKEYEGSEDTRkTISQLFAKHKENQREKEKLEAELATARSTNEDqrrhIEIRD 266
Cdd:TIGR00606 403 QEDEAKtaaqlcaDLQSKERLKQEQADEIRDEKKGLGR-TIELKKEILEKKQEELKFVIKELQQLEGSSDR----ILELD 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569012030 267 QALSNAQAKVVKLEE----ELKKKQVYVDKVEKMqQALVQLQAACEKREQLEHRLRTRLEREL 325
Cdd:TIGR00606 478 QELRKAERELSKAEKnsltETLKKEVKSLQNEKA-DLDRKLRKLDQEMEQLNHHTTTRTQMEM 539
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
728-760 |
7.78e-04 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 41.00 E-value: 7.78e-04
10 20 30
....*....|....*....|....*....|...
gi 569012030 728 PATSAPVPSPASIPAPATAQASAPTPTQASTPA 760
Cdd:PRK05641 46 SAVQEQVPTPAPAPAPAVPSAPTPVAPAAPAPA 78
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
150-360 |
7.81e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 7.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 150 ARLQKVETEIQRVSEAYENLVKSSSKreaLEKAMRNklEGEIRRMH---DFNRDLRDRLETANKQLAEKEYEGSEDTR-- 224
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRE---LEKVLKK--ESELIKLKelaEQLKELEEKLKKYNLEELEKKAEEYEKLKek 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 225 ---------------KTISQLFAKHKENQREKEKLEAELA-------------------TARSTNEDQRRHIEIRD--QA 268
Cdd:PRK03918 534 liklkgeikslkkelEKLEELKKKLAELEKKLDELEEELAellkeleelgfesveeleeRLKELEPFYNEYLELKDaeKE 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 269 LSNAQAKVVKLEEELKKKQVYVDKVEK-MQQALVQLQAACEKREQLEHR----LRTRLERELESLRIQQRQGNSQptnaS 343
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKrLEELRKELEELEKKYSEEEYEelreEYLELSRELAGLRAELEELEKR----R 689
|
250
....*....|....*..
gi 569012030 344 EYNAAALMELLREKEER 360
Cdd:PRK03918 690 EEIKKTLEKLKEELEER 706
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
125-303 |
7.85e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.09 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 125 QQMVEILSDENRNLRQELDgcyEKVARLQKVETEIQRVSEAYENL---VKSSSKREALEKAMRNKLEGEIRRMHDFNRDL 201
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLE---QKQKELKSKEKELKKLNEEKKELeekVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 202 RDRLETANKQLAEKEYEGSEDTR-KTISQLfaKH-----KENQREKEKLEAELATARStneDQRRHIEIRDQALSNAQAK 275
Cdd:TIGR04523 544 EDELNKDDFELKKENLEKEIDEKnKEIEEL--KQtqkslKKKQEEKQELIDQKEKEKK---DLIKEIEEKEKKISSLEKE 618
|
170 180
....*....|....*....|....*...
gi 569012030 276 VVKLEEELKKKQVYVDKVEKMQQALVQL 303
Cdd:TIGR04523 619 LEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
121-405 |
9.50e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 9.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 121 VSRAQQMVEILSDENRNLRQELDGCYEKVARLQKVE-------TEIQRVSEAY--------------ENLVKSSSKREaL 179
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEeaekarqAEMDRQAAIYaeqermamererelERIRQEERKRE-L 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 180 EKAMRNKLEGEIRRMHDF----------NRDLRDRLETANKQ-LAEKEYEGSEDTRKTISQLFAKHKENQREKEkleael 248
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELerlqmerqqkNERVRQELEAARKVkILEEERQRKIQQQKVEMEQIRAEQEEARQRE------ 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 249 atARSTNEDQRRHIEIRDQALSNAQAKVVKL---EEELKKKQVYVDKVEKMQQALVQ-----LQAACEKREQL---EHRL 317
Cdd:pfam17380 437 --VRRLEEERAREMERVRLEEQERQQQVERLrqqEEERKRKKLELEKEKRDRKRAEEqrrkiLEKELEERKQAmieEERK 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 318 RTRLERELESLRIQQRQGNSQPTNASEYNAAALMELLREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRD 397
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
....*...
gi 569012030 398 TTVISHSP 405
Cdd:pfam17380 595 TPITTIKP 602
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
126-473 |
1.21e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 126 QMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENL-VKSSSKREALEKAMRNKLEGEIRRmhdfnrDLRDR 204
Cdd:TIGR02169 146 DFISMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLdLIIDEKRQQLERLRREREKAERYQ------ALLKE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 205 LEtankqlaekEYEGSEDTRktisqlfakhkenqrEKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELK 284
Cdd:TIGR02169 220 KR---------EYEGYELLK---------------EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 285 KKQVYVDKVEKMQQALVQlqaacEKREQLEHRLRtRLERELESLRIQQRQGNSQPTNA-SEYNaaALMELLREKEERILA 363
Cdd:TIGR02169 276 ELNKKIKDLGEEEQLRVK-----EKIGELEAEIA-SLERSIAEKERELEDAEERLAKLeAEID--KLLAEIEELEREIEE 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 364 LEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSpntSYDTALEARIQKEEE-----EILMANKRCLDMEGR- 437
Cdd:TIGR02169 348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK---DYREKLEKLKREINElkrelDRLQEELQRLSEELAd 424
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 569012030 438 ----IKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSSMR 473
Cdd:TIGR02169 425 lnaaIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
131-471 |
1.23e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 131 LSDENRNLRQELDgcyEKVARLQKVETEIQRVSEAYENLvksSSKREALEKAMRNKlEGEIRRMHDFNRDLRDRLETANK 210
Cdd:TIGR04523 223 LKKQNNQLKDNIE---KKQQEINEKTTEISNTQTQLNQL---KDEQNKIKKQLSEK-QKELEQNNKKIKELEKQLNQLKS 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 211 QLAEKEYEGSEDTRKTI-SQLfakhKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVY 289
Cdd:TIGR04523 296 EISDLNNQKEQDWNKELkSEL----KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 290 VDKVEKMQQALVQ-----------LQAACEKREQLEHRLRTRLER-ELESLRIQQRQGNSQPTNASeyNAAALMELlrEK 357
Cdd:TIGR04523 372 IEKLKKENQSYKQeiknlesqindLESKIQNQEKLNQQKDEQIKKlQQEKELLEKEIERLKETIIK--NNSEIKDL--TN 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 358 EERILALEADMTKWEQKYLEENVmrhfaldaaatvaaqrDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGR 437
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQL----------------KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK 511
|
330 340 350
....*....|....*....|....*....|....
gi 569012030 438 IKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSS 471
Cdd:TIGR04523 512 VKDLTKKISSLKEKIEKLESEKKEKESKISDLED 545
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
147-367 |
1.60e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 147 EKVARLQKVEtEIQRVSEAY---ENLVKSSSKREALEKAMRNKLEgeiRRMHDFNRDLRDRLETANKQLAEK----EYEG 219
Cdd:PTZ00121 1552 KKAEELKKAE-EKKKAEEAKkaeEDKNMALRKAEEAKKAEEARIE---EVMKLYEEEKKMKAEEAKKAEEAKikaeELKK 1627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 220 SEDTRKTISQLFAKHKENQREKEKLEAELAT--------ARSTNEDQRRHIEIRdqalsNAQAKVVKLEEELKKKQVYVD 291
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkikaaeeAKKAEEDKKKAEEAK-----KAEEDEKKAAEALKKEAEEAK 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 292 KVEKMQQALV-------QLQAACEKREQLEHRLRTRLE---RELESLRIQQRQGNSQPTNASEYNAAAlmELLREKEERI 361
Cdd:PTZ00121 1703 KAEELKKKEAeekkkaeELKKAEEENKIKAEEAKKEAEedkKKAEEAKKDEEEKKKIAHLKKEEEKKA--EEIRKEKEAV 1780
|
....*.
gi 569012030 362 LALEAD 367
Cdd:PTZ00121 1781 IEEELD 1786
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
137-370 |
1.69e-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: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 137 NLRQELDGCYEKVARLQKV----ETEIQRVSEayENLVKSSSKREALEKAmrNKLEGEIRRMHDFNRDLRDRLETANKQL 212
Cdd:pfam15921 416 HLRRELDDRNMEVQRLEALlkamKSECQGQME--RQMAAIQGKNESLEKV--SSLTAQLESTKEMLRKVVEELTAKKMTL 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 213 aekeyegsEDTRKTISQLFAKHKENQREKEKLEAELATARSTNE---DQRRHIEIRDQALSNAQAKVVKLEEELKKK--- 286
Cdd:pfam15921 492 --------ESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDlklQELQHLKNEGDHLRNVQTECEALKLQMAEKdkv 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 287 -QVYVDKVEKMQQALVQ----LQAACEKREQLEHRLRTRlERELESLRIQQRQGNSQptnaseynaaalmelLREKEERI 361
Cdd:pfam15921 564 iEILRQQIENMTQLVGQhgrtAGAMQVEKAQLEKEINDR-RLELQEFKILKDKKDAK---------------IRELEARV 627
|
....*....
gi 569012030 362 LALEADMTK 370
Cdd:pfam15921 628 SDLELEKVK 636
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
199-370 |
1.81e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 199 RDLRDRLETANKQLAEKEyegsedtrKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVK 278
Cdd:COG4942 23 AEAEAELEQLQQEIAELE--------KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 279 LEEELKK-KQVYVDKVEKMQ----QALVQLQAACEKREQLEHRLR------TRLERELESLRIQQRQGNSQpTNASEYNA 347
Cdd:COG4942 95 LRAELEAqKEELAELLRALYrlgrQPPLALLLSPEDFLDAVRRLQylkylaPARREQAEELRADLAELAAL-RAELEAER 173
|
170 180
....*....|....*....|...
gi 569012030 348 AALMELLREKEERILALEADMTK 370
Cdd:COG4942 174 AELEALLAELEEERAALEALKAE 196
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
123-311 |
1.97e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 123 RAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQ-RVSEAYENLVKSSSKR-EALEKAMRNkLEGEIRRMhdfnRD 200
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALReELDELEAQIRGNGGDRlEQLEREIER-LERELEER----ER 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 201 LRDRLETANKQLAEKEYEGSEDtrktisqlFAkhkENQREKEKLEAELATARSTNEDQRRHIEirdQALSNAQAKVVKLE 280
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEE--------FA---ALRAEAAALLEALEEELEALEEALAEAE---AALRDLRRELRELE 425
|
170 180 190
....*....|....*....|....*....|....
gi 569012030 281 EE---LKKKQVYVDkvEKMQQALVQLQAACEKRE 311
Cdd:COG4913 426 AEiasLERRKSNIP--ARLLALRDALAEALGLDE 457
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
175-361 |
3.19e-03 |
|
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: 41.31 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 175 KREALEKAMRNKLEGEIRrmhdfnrDLRDRLETANK------------QLAEKEYEGS-EDTRKTISQLFAKHKENQREK 241
Cdd:pfam01576 763 KQRAQAVAAKKKLELDLK-------ELEAQIDAANKgreeavkqlkklQAQMKDLQRElEEARASRDEILAQSKESEKKL 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 242 EKLEAELATAR---STNEDQRRHI---------EIRDQALSNA---------QAKVVKLEEELKKKQVYV----DKVEKM 296
Cdd:pfam01576 836 KNLEAELLQLQedlAASERARRQAqqerdeladEIASGASGKSalqdekrrlEARIAQLEEELEEEQSNTellnDRLRKS 915
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569012030 297 QQALVQLQA-------ACEKREQlehrLRTRLERELESLRIQQRQGNSQPTNASEYNAAALMELLREKEERI 361
Cdd:pfam01576 916 TLQVEQLTTelaaersTSQKSES----ARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQL 983
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
136-460 |
3.53e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 136 RNLRQELDGCYEKVARLqkvETEIQRVSEAYENLvkssskREALekAMRNKLEGEIRRMHDfnRDLRDRLETANKQLAEk 215
Cdd:PRK04863 840 RQLNRRRVELERALADH---ESQEQQQRSQLEQA------KEGL--SALNRLLPRLNLLAD--ETLADRVEEIREQLDE- 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 216 eyegSEDTRKTISQlfakhkeNQREKEKLEAELATARSTNED----QRRHIEIrDQALSNAQAKVVKLEEELKKKQVYvd 291
Cdd:PRK04863 906 ----AEEAKRFVQQ-------HGNALAQLEPIVSVLQSDPEQfeqlKQDYQQA-QQTQRDAKQQAFALTEVVQRRAHF-- 971
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 292 kveKMQQALVQLQAACEKREQLEHRLRtRLERELESLRIQQRQGNSQptnASEYNA--AALMELLREKEERILALEADMT 369
Cdd:PRK04863 972 ---SYEDAAEMLAKNSDLNEKLRQRLE-QAEQERTRAREQLRQAQAQ---LAQYNQvlASLKSSYDAKRQMLQELKQELQ 1044
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 370 KWEQKYLEENVMRhfaldaaatVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKD 449
Cdd:PRK04863 1045 DLGVPADSGAEER---------ARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAK 1115
|
330
....*....|.
gi 569012030 450 AMIKVLQQRSR 460
Cdd:PRK04863 1116 AGWCAVLRLVK 1126
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
121-382 |
3.70e-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: 41.19 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 121 VSRAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRD 200
Cdd:TIGR00606 880 LQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKD 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 201 LRDRL-ETANKQLAEKEYEgsedtrktISQLFAKHKENQREKEKLEAELATARSTNEDQR-RHIEIRDQ-ALSNAQAKVV 277
Cdd:TIGR00606 960 IENKIqDGKDDYLKQKETE--------LNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKiQERWLQDNlTLRKRENELK 1031
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 278 KLEEELKK--KQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEYNAAALMELLR 355
Cdd:TIGR00606 1032 EVEEELKQhlKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMR 1111
|
250 260
....*....|....*....|....*..
gi 569012030 356 EKEERIlaleADMTKWeQKYLEENVMR 382
Cdd:TIGR00606 1112 TTELVN----KDLDIY-YKTLDQAIMK 1133
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
203-374 |
4.13e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 203 DRLETANKQLAEKEYEGSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEE 282
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 283 LKKKQvyvDKVEKMQQALVQLQAACEKREQLEHRLRTRLER---ELESLRIQQRQGNSQptnaseynAAALMELLREKEE 359
Cdd:COG4372 82 LEELN---EQLQAAQAELAQAQEELESLQEEAEELQEELEElqkERQDLEQQRKQLEAQ--------IAELQSEIAEREE 150
|
170
....*....|....*
gi 569012030 360 RILALEADMTKWEQK 374
Cdd:COG4372 151 ELKELEEQLESLQEE 165
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
121-282 |
4.24e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 121 VSRAQQMVEILSDENRNLRQELDGCYEKVA-----RLQKVETEIQRVSEAYENLvksSSKREALEKAMRN---KLEGEIR 192
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRgnggdRLEQLEREIERLERELEER---ERRRARLEALLAAlglPLPASAE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 193 RMHDFNRDLRDRLETANKQLAEkeyegsedTRKTISQLFAKHKENQREKEKLEAELA--TARSTNEDQRRHiEIRD---Q 267
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEA--------LEEALAEAEAALRDLRRELRELEAEIAslERRKSNIPARLL-ALRDalaE 451
|
170 180
....*....|....*....|...
gi 569012030 268 ALSNAQAKV--------VKLEEE 282
Cdd:COG4913 452 ALGLDEAELpfvgelieVRPEEE 474
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
725-809 |
4.27e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 40.74 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 725 QVAPATSAPVPSPASIPAPATAQASAPTPTQASTPAPTEPPSPVP-----TPTPALVQTEGPANPGASSGPRRLSTPNLM 799
Cdd:PRK07764 409 APAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGApspppAAAPSAQPAPAPAAAPEPTAAPAPAPPAAP 488
|
90
....*....|
gi 569012030 800 CNPDKPDAPA 809
Cdd:PRK07764 489 APAAAPAAPA 498
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
122-378 |
4.69e-03 |
|
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: 40.58 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 122 SRAQQMVEILSDENrNLRQELDgcyEKVARLQKVETEIQRVSEayenLVKSSSKREALEKAMRNKlEGEIRRMHDFNRDL 201
Cdd:pfam10174 182 ERTRRIAEAEMQLG-HLEVLLD---QKEKENIHLREELHRRNQ----LQPDPAKTKALQTVIEMK-DTKISSLERNIRDL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 202 RDRLETANKQLAEkeyeGSEDTRKTISQL--------FAKHKENQREKE---------KLEAELATARSTNEDQRRHIEI 264
Cdd:pfam10174 253 EDEVQMLKTNGLL----HTEDREEEIKQMevykshskFMKNKIDQLKQElskkesellALQTKLETLTNQNSDCKQHIEV 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 265 -------RDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQ----LQAACE------------------KREQLEH 315
Cdd:pfam10174 329 lkesltaKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEekstLAGEIRdlkdmldvkerkinvlqkKIENLQE 408
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569012030 316 RLRTRlERELESLRiQQRQGNSQPTNASEYNAAALMELLREKEERILALEADMTKWEQKYLEE 378
Cdd:pfam10174 409 QLRDK-DKQLAGLK-ERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEE 469
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
119-373 |
4.71e-03 |
|
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: 40.59 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 119 AMVSRAQQMVEILSDEnrnLRQELDGCYEKVA----RLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGE-IRR 193
Cdd:pfam12128 315 AAVAKDRSELEALEDQ---HGAFLDADIETAAadqeQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnNRD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 194 MHDFNRDLRDRLETANKQLAEKE--YEGSEdtrktiSQLfakhkenqreKEKLEAELATARstneDQRRHIEIRDQALSN 271
Cdd:pfam12128 392 IAGIKDKLAKIREARDRQLAVAEddLQALE------SEL----------REQLEAGKLEFN----EEEYRLKSRLGELKL 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 272 AQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEynaaaLM 351
Cdd:pfam12128 452 RLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDE-----LE 526
|
250 260
....*....|....*....|...
gi 569012030 352 ELLREKEERILA-LEADMTKWEQ 373
Cdd:pfam12128 527 LQLFPQAGTLLHfLRKEAPDWEQ 549
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
69-310 |
5.71e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 69 LLSSQSHQGDHYRHAQASLTSAQQQPGEAYSAMPRAQQSAsyqpmpADPFAMVSRAQQMVEILSDENRNLRQELDGCYEK 148
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEE------KALLKQLAALERRIAALARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 149 VARLQKVETEIQRVSEAYENLVKSSSKreALEKAMRNKLEGEIRRMHDFNRDLRDRleTANKQLAEKEYEGSEDTRKTIS 228
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLR--ALYRLGRQPPLALLLSPEDFLDAVRRL--QYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 229 QLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACE 308
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
..
gi 569012030 309 KR 310
Cdd:COG4942 241 ER 242
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
724-757 |
6.01e-03 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 38.30 E-value: 6.01e-03
10 20 30
....*....|....*....|....*....|....
gi 569012030 724 IQVAPATSAPVPSPASIPAPATAQASAPTPTQAS 757
Cdd:PRK05641 48 VQEQVPTPAPAPAPAVPSAPTPVAPAAPAPAPAS 81
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
293-468 |
6.13e-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: 39.14 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 293 VEKMQQALVQLQAACEKREQLEHRLRTrLERELESLRIQQRQGNSQPTNASEyNAAALMELLREKEERILALEADMTKWE 372
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKE-LPAELAELEDELAALEARLEAAKT-ELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 373 QKyleenvmrhfaldaAATVAAQRDTTVISHSpntsyDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMI 452
Cdd:COG1579 80 EQ--------------LGNVRNNKEYEALQKE-----IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL 140
|
170
....*....|....*.
gi 569012030 453 KVLQQRSRKEPSKTEQ 468
Cdd:COG1579 141 EEKKAELDEELAELEA 156
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
227-378 |
6.70e-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: 39.14 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 227 ISQLFAKHKENQREKEKLEAELATARSTnedqrrhIEIRDQALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAA 306
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEAR-------LEAAKTELEDLEKEIKRLELEIEEVE---ARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569012030 307 cekREQlehrlrTRLERELESLRIQQRQgnsqptnaSEYNAAALMELLREKEERILALEADMTKWEQKYLEE 378
Cdd:COG1579 89 ---KEY------EALQKEIESLKRRISD--------LEDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
131-335 |
6.78e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.51 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 131 LSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLV-----------KSSSKREALEKAMR-NKLEGEIRRMHDFN 198
Cdd:COG1340 90 LREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVlspeeekelveKIKELEKELEKAKKaLEKNEKLKELRAEL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 199 RDLRDRLETANKQLAEKeYEGSEDTRKTISQLFakhkenqREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVK 278
Cdd:COG1340 170 KELRKEAEEIHKKIKEL-AEEAQELHEEMIELY-------KEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 569012030 279 LEEELKKKQVYVDKVEKMQQAlvqlQAACEKREQLEHRLRTRLERELESLRIQQRQG 335
Cdd:COG1340 242 LRKELKKLRKKQRALKREKEK----EELEEKAEEIFEKLKKGEKLTTEELKLLQKSG 294
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
121-284 |
7.61e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.04 E-value: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 121 VSRAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRD 200
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 201 LRDRLETANKQLA--EKEYEGSEDTRKTIsqlfakhKENQREKEKLEAELATArstnedqrrHIEIRDQALSNAQAKVVK 278
Cdd:TIGR02168 913 LRRELEELREKLAqlELRLEGLEVRIDNL-------QERLSEEYSLTLEEAEA---------LENKIEDDEEEARRRLKR 976
|
....*.
gi 569012030 279 LEEELK 284
Cdd:TIGR02168 977 LENKIK 982
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
147-328 |
7.64e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 38.88 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 147 EKVARLQKVETEIQRVSEAYENLVKsssKREALEKAMrnklegeirrmHDFNRdlrdrletANKQLAEKEYEGSEDTRKT 226
Cdd:cd07596 8 EAKDYILKLEEQLKKLSKQAQRLVK---RRRELGSAL-----------GEFGK--------ALIKLAKCEEEVGGELGEA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 227 ISQLFAKHKE-NQREKEKLEAELATARSTNEDQ-----------------RRHIEIRDQALSNAQAKVVKLEEELKKKQv 288
Cdd:cd07596 66 LSKLGKAAEElSSLSEAQANQELVKLLEPLKEYlrycqavketlddradaLLTLQSLKKDLASKKAQLEKLKAAPGIKP- 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 569012030 289 yvDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESL 328
Cdd:cd07596 145 --AKVEELEEELEEAESALEEARKRYEEISERLKEELKRF 182
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
83-218 |
7.69e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 83 AQASLTSAQQQPGEAYSAMPRAQQSASYQPMPADPFAMVSRAQQMVEILSDEN---RNLRQELDgcyekvARLQKVETEI 159
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHpdvIALRAQIA------ALRAQLQQEA 311
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 569012030 160 QRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRdRLEtANKQLAEKEYE 218
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELR-RLE-REVEVARELYE 368
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
126-374 |
7.80e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 7.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 126 QMVEILSDENRnlrqeldGCYEKVARLQKVETEIQRVSEAYENLVKSS-SKREALEKAMRNK-------------LEGEI 191
Cdd:TIGR00606 667 QFITQLTDENQ-------SCCPVCQRVFQTEAELQEFISDLQSKLRLApDKLKSTESELKKKekrrdemlglapgRQSII 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 192 RRMHDFNRDLRDRLETANKQLAEKEYEGSEDTRK-------------------TISQLFAKHKENQREKEKLEAELATA- 251
Cdd:TIGR00606 740 DLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLlgtimpeeesakvcltdvtIMERFQMELKDVERKIAQQAAKLQGSd 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 252 -RSTNEDQRRHIEIRDQALSNAQAKVVKL----EEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTrLERELE 326
Cdd:TIGR00606 820 lDRTVQQVNQEKQEKQHELDTVVSKIELNrkliQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVE-LSTEVQ 898
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 569012030 327 SL--RIQQRQGNSQPtnaseyNAAALMELLREKEERILALEADMTKWEQK 374
Cdd:TIGR00606 899 SLirEIKDAKEQDSP------LETFLEKDQQEKEELISSKETSNKKAQDK 942
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
128-382 |
7.84e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.13 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 128 VEILSDENRNLRQELDgcyekvARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRDRLET 207
Cdd:pfam00038 20 VRFLEQQNKLLETKIS------ELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 208 --ANKQLAEKEYEGsedTRKTISQLFAKHKENQREKEKL-----------EAELATARSTNEDQRRHIEI---RDQALSN 271
Cdd:pfam00038 94 elNLRTSAENDLVG---LRKDLDEATLARVDLEAKIESLkeelaflkknhEEEVRELQAQVSDTQVNVEMdaaRKLDLTS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012030 272 AQAKVVKLEEELKKK------QVYVDKVEKMQQALVQ----LQAACEKREQLEHRLRtRLERELESLRIQqrqgnsqptn 341
Cdd:pfam00038 171 ALAEIRAQYEEIAAKnreeaeEWYQSKLEELQQAAARngdaLRSAKEEITELRRTIQ-SLEIELQSLKKQ---------- 239
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 569012030 342 aseynAAALMELLREKEERiLALEADMTKWEQKYLEENVMR 382
Cdd:pfam00038 240 -----KASLERQLAETEER-YELQLADYQELISELEAELQE 274
|
|
| |
