|
Name |
Accession |
Description |
Interval |
E-value |
| Uso1_p115_head |
pfam04869 |
Uso1 / p115 like vesicle tethering protein, head region; Also known as General vesicular ... |
347-635 |
1.19e-66 |
|
Uso1 / p115 like vesicle tethering protein, head region; Also known as General vesicular transport factor, Transcytosis associated 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 part of the head region. The head region is highly conserved, but its function is unknown. It does not seem to be essential for vesicle tethering. The N-terminal part of the head region, not within this family, contains context-detected Armadillo/beta-catenin-like repeats (pfam00514).
Pssm-ID: 461460 Cd Length: 310 Bit Score: 225.54 E-value: 1.19e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 347 NQDYFASV--------------NAPSNPPRPAIVVLL--MSMVNERQPFVLRCAVLYCFQCFLYKNEKGQGEIVATLLPS 410
Cdd:pfam04869 2 LQEEFAKIdvpypdpslpsaanAADQPVKVPVIDLLLnwALSANSVHAFDLRVAACYCLKAYFYNNEEIRLHFLQRAIEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 411 TIDATGNSVSAGQLLCGGL-----FSTDSLSNWCAAVALAHALQGNATQKEQLLRVQLAT-SIGNPPVSLLQQCTNILSQ 484
Cdd:pfam04869 82 YKSGNDSSSTTANLLEVLLdydpdLKLDPYKLWFASVILMHLLEDNPEAKELARSVTEGDaESGEEVVTLIQTISELLIT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 485 GdkidRRGSKIQTRVGLLMLLCTWLSNCPIAVTHFLHNSANVPFLTGQIAENlGEEEQLVQGLCALLLGISIYFNDNSlE 564
Cdd:pfam04869 162 S----LQREDPRIPIGYLMLLIVWLFEDPDAVNDFLSEGSNLQSLLQFLSQS-SDEDVLVQGLCAMLLGIAYEFSTKD-S 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568936049 565 NYTKEKLKQLIEKRIGKENFIEKLGFISKHELYSRASQKPQPNFPSPEYMI----FDHEFTKLVKELEGVITKAI 635
Cdd:pfam04869 236 PIPRADLHSLLTKRLGRDNYIDKIKQLREHPLFRDFEVLPQLNPSLDDTGLpevyFDSYFVELFKDNFSRIRRAL 310
|
|
| Arm_vescicular |
pfam18770 |
Armadillo tether-repeat of vescicular transport factor; Armadillo-like tether-repeat of ... |
270-329 |
5.82e-33 |
|
Armadillo tether-repeat of vescicular transport factor; Armadillo-like tether-repeat of general vescicular transport factor. This entry contains a single copy of the repeat unit.
Pssm-ID: 465861 Cd Length: 60 Bit Score: 121.26 E-value: 5.82e-33
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 270 SGWSAQKVTNLHLMLQLVRVLVSPTNPPGATSSCQKAMFQCGLLQQLCTILMATGIPADI 329
Cdd:pfam18770 1 SGWSAQKVSNVHCMLQVVRTLVSPNNPSQVTSSCQKAMRACGLLEALCNILMASGVPADI 60
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
669-894 |
1.20e-11 |
|
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: 67.48 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 669 QDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNhhqgshgdgAQVNGIQpEEISRLREEIEE 748
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA---------RRIRALE-QELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 749 LKSQQALLQGQLAE-KDSLIENLKSSQASGMSEQASATCPPRDPEQVAELKQAKSVPVEGESEHVSA--AKTTDVEGRLS 825
Cdd:COG4942 88 LEKEIAELRAELEAqKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEElrADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568936049 826 ALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKI 894
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
666-905 |
3.04e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 666 IREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKdnhhqgshgdgaQVNGIQP--EEISRLR 743
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR------------LEQDIARleERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 744 EEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATcpprdpEQVAELKQAKSVPVEGESEHVSAAKttDVEGR 823
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE------AELAEAEEALLEAEAELAEAEEELE--ELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 824 LSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKD 903
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
..
gi 568936049 904 LG 905
Cdd:COG1196 468 LL 469
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
815-908 |
2.61e-09 |
|
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: 55.87 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 815 AKTTDVEGRLSALLQETKELKNEIKALS------EERTAIQKQLDSSNST----IAILQTEKDKLDLEVTDSKKEQDDLL 884
Cdd:pfam04871 1 AKKSELESEASSLKNENTELKAELQELSkqynslEQKESQAKELEAEVKKleeaLKKLKAELSEEKQKEKEKQSELDDLL 80
|
90 100
....*....|....*....|....
gi 568936049 885 VLLADQDQKILSLKSKLKDLGHPV 908
Cdd:pfam04871 81 LLLGDLEEKVEKYKARLKELGEEV 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
664-904 |
3.77e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 664 NMIREQDLqLEELKQQVSTLKCQNEQlqtavtqqASQIQQHKDQYNLLKVQLgkdnhhQGSHGDGAQvngiqpEEISRLR 743
Cdd:COG1196 187 NLERLEDI-LGELERQLEPLERQAEK--------AERYRELKEELKELEAEL------LLLKLRELE------AELEELE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 744 EEIEELKSQQALLQGQLAEKDSLIENLKSSQAsgmseqasatcpprdpEQVAELKQAksvpveGESEHVSAAKTTDVEGR 823
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELE----------------ELELELEEA------QAEEYELLAELARLEQD 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 824 LSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKD 903
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
.
gi 568936049 904 L 904
Cdd:COG1196 384 L 384
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
663-904 |
1.98e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.11 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 663 KNMIREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNhhqgshgdgaQVNGIQPEEISRL 742
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ----------QEKELLEKEIERL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 743 REEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATCPPRDPEQvaELKQAKSVPVEGESEHVS-AAKTTDVE 821
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQ--NLEQKQKELKSKEKELKKlNEEKKELE 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 822 GRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTI---------AILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQ 892
Cdd:TIGR04523 510 EKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkddfelkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQE 589
|
250
....*....|..
gi 568936049 893 KILSLKSKLKDL 904
Cdd:TIGR04523 590 LIDQKEKEKKDL 601
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
666-904 |
2.67e-08 |
|
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: 58.16 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 666 IREQDLQLEELKQQVSTLKCQNEQLQtavtqqaSQIQQHKDQYNLLKVQLGKDNHHQGSHGDGAQVNgIQPE------EI 739
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLT-------EEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR-VKEKigeleaEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 740 SRLREEIEELKSQQALLQGQLAEKDSLIENLKsSQASGMSEQASATCPPRDP--EQVAELKQAKSVPV-EGESEHVSAA- 815
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLL-AEIEELEREIEEERKRRDKltEEYAELKEELEDLRaELEEVDKEFAe 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 816 ---KTTDVEGRLSALLQETKELKNEI-------KALSEERTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLV 885
Cdd:TIGR02169 383 trdELKDYREKLEKLKREINELKRELdrlqeelQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA 462
|
250
....*....|....*....
gi 568936049 886 LLADQDQKILSLKSKLKDL 904
Cdd:TIGR02169 463 DLSKYEQELYDLKEEYDRV 481
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
652-905 |
5.44e-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: 53.91 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 652 LEQHDNIVTHYKNMIREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNHHQGSHGDGAQV 731
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 732 N----GIQPEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATcpprdpEQVAELKQAKSvpveg 807
Cdd:TIGR02168 829 LerriAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE------EALALLRSELE----- 897
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 808 esehVSAAKTTDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAilqtEKDKLDLEVTDSKKEQDDLlvLL 887
Cdd:TIGR02168 898 ----ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS----EEYSLTLEEAEALENKIED--DE 967
|
250
....*....|....*...
gi 568936049 888 ADQDQKILSLKSKLKDLG 905
Cdd:TIGR02168 968 EEARRRLKRLENKIKELG 985
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
670-880 |
5.67e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.58 E-value: 5.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 670 DLQLEELKQqvstLKCQNEQLQTAVTQ-QASQIQQ-HKDQY-NLLKVQLGKDNHHQGSHGDGA---QVNGIQPE-EISRL 742
Cdd:pfam15921 527 DLKLQELQH----LKNEGDHLRNVQTEcEALKLQMaEKDKViEILRQQIENMTQLVGQHGRTAgamQVEKAQLEkEINDR 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 743 REEIEELKsqqaLLQGQlaeKDSLIENLKSsqasgmseqasatcpprdpeQVAELKQAKSVPVEGESEHVSAAKttDVEG 822
Cdd:pfam15921 603 RLELQEFK----ILKDK---KDAKIRELEA--------------------RVSDLELEKVKLVNAGSERLRAVK--DIKQ 653
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568936049 823 RLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAiLQTEKDKLDLEVTDSKKEQ 880
Cdd:pfam15921 654 ERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEME-TTTNKLKMQLKSAQSELEQ 710
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
662-904 |
6.61e-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: 53.10 E-value: 6.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 662 YKNMIREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGK------------DNHHQGSHGDGA 729
Cdd:TIGR04523 209 KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKikkqlsekqkelEQNNKKIKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 730 QVNGIQPE----------------------------------------------EISRLREEIEELKSQQALLQGQLAEK 763
Cdd:TIGR04523 289 QLNQLKSEisdlnnqkeqdwnkelkselknqekkleeiqnqisqnnkiisqlneQISQLKKELTNSESENSEKQRELEEK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 764 DSLIENLKSSQASGMSEQASATCPPRDPEQvaELKQAKSVPVEGESEHVSAAKTTDV-EGRLSALLQETKELKNEIKALS 842
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLES--KIQNQEKLNQQKDEQIKKLQQEKELlEKEIERLKETIIKNNSEIKDLT 446
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568936049 843 EERTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 904
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEL 508
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
662-904 |
7.83e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.20 E-value: 7.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 662 YKNMIREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQ-----HKDQYNLlkvQLGKDNHHQ---GSHGDGAQVNG 733
Cdd:pfam15921 340 YEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKlladlHKREKEL---SLEKEQNKRlwdRDTGNSITIDH 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 734 IQPE------EISRLREEIEELKSQqalLQGQLAEKDSLIENLKSS--QASGMSEQASATcpPRDPEQVAELKQAKSVPV 805
Cdd:pfam15921 417 LRRElddrnmEVQRLEALLKAMKSE---CQGQMERQMAAIQGKNESleKVSSLTAQLEST--KEMLRKVVEELTAKKMTL 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 806 EGESEHVS----------------AAKTTDVEGRLSALLQETKELKNE---IKALSEERTAIQKQLDSSNSTIAIL---- 862
Cdd:pfam15921 492 ESSERTVSdltaslqekeraieatNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILrqqi 571
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 568936049 863 -----------------QTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 904
Cdd:pfam15921 572 enmtqlvgqhgrtagamQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL 630
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
651-904 |
9.38e-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: 9.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 651 TLEQHDNIVTHYKNMIREQDLQLEELKQQVSTLKCQNEQLQTAVTQqaSQIQQHKDQYNLLKVQLGKDNHhqgshgdgaQ 730
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELK--SELKNQEKKLEEIQNQISQNNK---------I 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 731 VNGIQpEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATCPPRD-------PEQVAELKQAKSV 803
Cdd:TIGR04523 337 ISQLN-EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDleskiqnQEKLNQQKDEQIK 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 804 PVEGESE---------------------------HVSAAKTTDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSN 856
Cdd:TIGR04523 416 KLQQEKEllekeierlketiiknnseikdltnqdSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE 495
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 568936049 857 STIAILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 904
Cdd:TIGR04523 496 KELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
651-848 |
1.72e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 651 TLEQhdnIVTHYKNmIREQDLQLEELKQQVSTLKCQNEQ-----LQTAVTQQASQIQQHKDQYNLLKVQLGK-DNHHQGS 724
Cdd:COG4913 253 LLEP---IRELAER-YAAARERLAELEYLRAALRLWFAQrrlelLEAELEELRAELARLEAELERLEARLDAlREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 725 HgdgAQVNGIQPEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSqasgmseqasatcPPRDPEQVAEL-KQAKSV 803
Cdd:COG4913 329 E---AQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLP-------------LPASAEEFAALrAEAAAL 392
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568936049 804 PVEGESEHVSAAKT-TDVEGRLSALLQETKELKNEIKALSEERTAI 848
Cdd:COG4913 393 LEALEEELEALEEAlAEAEAALRDLRRELRELEAEIASLERRKSNI 438
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
665-904 |
4.27e-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: 50.84 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 665 MIREQDLQLEELKQQVSTLKCQNEQLQtavtqqasqiqqhkdqynllkvqlgkdnhhqgshgdgaqvngiqpEEISRLRE 744
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELE---------------------------------------------EDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 745 EIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQAsatcpprdPEQVAELKQAKSvpvEGESEHVS-AAKTTDVEGR 823
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS--------HSRIPEIQAELS---KLEEEVSRiEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 824 LSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKD 903
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
.
gi 568936049 904 L 904
Cdd:TIGR02169 901 L 901
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
738-904 |
5.75e-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: 50.44 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 738 EISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATCPPRDPEQVAELKQAKSVPVEGESEHVS---- 813
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSkelt 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 814 --AAKTTDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLADQD 891
Cdd:TIGR02168 758 elEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
|
170
....*....|...
gi 568936049 892 QKILSLKSKLKDL 904
Cdd:TIGR02168 838 RRLEDLEEQIEEL 850
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
666-900 |
6.18e-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: 50.21 E-value: 6.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 666 IREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNHHQGshgdgaqvngiqpEEISRLREE 745
Cdd:pfam10174 410 LRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERL-------------EELESLKKE 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 746 IEELKSQQALLQGQLAEKDSLIENLK---SSQASGMSEQASatcppRDPEQVAELKQAKSVPVEGESEHVSAAKTTDVEG 822
Cdd:pfam10174 477 NKDLKEKVSALQPELTEKESSLIDLKehaSSLASSGLKKDS-----KLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVR 551
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568936049 823 RLSALLQETKELKNEIKALSEERTAIQKQLDssnSTIAIL-QTEKDKLDLEVTDSKKEQDDLLvLLADQDQKILSLKSK 900
Cdd:pfam10174 552 TNPEINDRIRLLEQEVARYKEESGKAQAEVE---RLLGILrEVENEKNDKDKKIAELESLTLR-QMKEQNKKVANIKHG 626
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
737-844 |
1.11e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.09 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 737 EEISRLREEIEELKSQQALLQGQLAEKDSLIENLKssqasgmseqasatcpprdpeqvAELKQAKSvpvEGESEHVSAAK 816
Cdd:COG2433 413 EEIRRLEEQVERLEAEVEELEAELEEKDERIERLE-----------------------RELSEARS---EERREIRKDRE 466
|
90 100
....*....|....*....|....*...
gi 568936049 817 TTDVEGRLSALLQETKELKNEIKALSEE 844
Cdd:COG2433 467 ISRLDREIERLERELEEERERIEELKRK 494
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
652-856 |
1.23e-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: 48.61 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 652 LEQHDNIVTHYKNMIREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQH------KDQYNLLKVQLGKDNHHQGSH 725
Cdd:COG4942 57 LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlralyrLGRQPPLALLLSPEDFLDAVR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 726 GDG--AQVNGIQPEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATcpprdpEQVAELKQAKSv 803
Cdd:COG4942 137 RLQylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQ------KLLARLEKELA- 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568936049 804 pvegesehvsaakttDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSN 856
Cdd:COG4942 210 ---------------ELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
662-882 |
1.34e-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: 49.28 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 662 YKNMIREQDLQLeeLKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLgkDNHHQGSHGDGAQVNGIQPE---- 737
Cdd:TIGR02168 218 LKAELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKL--EELRLEVSELEEEIEELQKElyal 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 738 --EISRLREEIEELKSQQALLQGQLAEKDSLIENLKSsqasgMSEQASAtcpprDPEQVAELKQAKSVPVEGESEHVSAA 815
Cdd:TIGR02168 294 anEISRLEQQKQILRERLANLERQLEELEAQLEELES-----KLDELAE-----ELAELEEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568936049 816 KTT--DVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDD 882
Cdd:TIGR02168 364 EAEleELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
651-883 |
1.39e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 651 TLEQHDNIVTHYKNmireqdlqLEELKQQVSTLKCQNEQLQtavtqqasQIQQHKDQYNLLKVQLGkdnhHQGSHGDGAQ 730
Cdd:COG4913 223 TFEAADALVEHFDD--------LERAHEALEDAREQIELLE--------PIRELAERYAAARERLA----ELEYLRAALR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 731 VNGIQpEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKsSQASGMSEQASAtcppRDPEQVAELKQaksvpvEGESE 810
Cdd:COG4913 283 LWFAQ-RRLELLEAELEELRAELARLEAELERLEARLDALR-EELDELEAQIRG----NGGDRLEQLER------EIERL 350
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568936049 811 HVSAAKTTDVEGRLSALLQETK-ELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDL 883
Cdd:COG4913 351 ERELEERERRRARLEALLAALGlPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL 424
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
663-853 |
1.52e-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: 47.23 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 663 KNMIREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNHHQGSHGDgaqvngiqPEEISRL 742
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN--------NKEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 743 REEIEELKSQQALLQGQLAEKDSLIENLKssqasgmseqasatcpprdpEQVAELKQAKsvpvegesehvsAAKTTDVEG 822
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELE--------------------EELAELEAEL------------AELEAELEE 142
|
170 180 190
....*....|....*....|....*....|.
gi 568936049 823 RLSALLQETKELKNEIKALSEERTAIQKQLD 853
Cdd:COG1579 143 KKAELDEELAELEAELEELEAEREELAAKIP 173
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
663-891 |
1.55e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 663 KNMIREQDLQLEELKQQVSTLK---CQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNH--HQGSHGDGAQVNGIQP- 736
Cdd:PRK04863 910 KRFVQQHGNALAQLEPIVSVLQsdpEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHfsYEDAAEMLAKNSDLNEk 989
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 737 --EEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQasgmseQASAtcpprdpEQVAELKQ---AKSVPVEGESEH 811
Cdd:PRK04863 990 lrQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSY------DAKR-------QMLQELKQelqDLGVPADSGAEE 1056
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 812 VSAAKTTDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTekdkldlEVTDSKKEQDDLLVLLADQD 891
Cdd:PRK04863 1057 RARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMRE-------QVVNAKAGWCAVLRLVKDNG 1129
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
735-904 |
1.70e-05 |
|
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: 48.91 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 735 QPEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKS--SQASGMSEQASATCPP--RDPEQVAELKQAKSVPVEGESE 810
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQelSDASRKIGEIEKEIEQleQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 811 HVSAAKT--TDVEGRLSAL------LQET-------------KELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKL 869
Cdd:TIGR02169 752 EIENVKSelKELEARIEELeedlhkLEEAlndlearlshsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190
....*....|....*....|....*....|....*
gi 568936049 870 DLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 904
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL 866
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
669-904 |
3.14e-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: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 669 QDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVqlgkdnhhqgshgdgaqvngiqPEEISRLREEIEE 748
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDL----------------------SEEAKLLLQQLSE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 749 LKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATCPPRDPEQVAELKQAksvpvegESEHVSAAKT-TDVEGRLSAL 827
Cdd:COG3206 224 LESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAEL-------EAELAELSARyTPNHPDVIAL 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 828 LQETKELKNEIKALSEE-RTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLADQD--QKIL-SLKSKLKD 903
Cdd:COG3206 297 RAQIAALRAQLQQEAQRiLASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEvaRELYeSLLQRLEE 376
|
.
gi 568936049 904 L 904
Cdd:COG3206 377 A 377
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
666-899 |
3.59e-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: 47.74 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 666 IREQDLQLEELKQQVSTLKCQNEQLQTA----------VTQQASQIQQHKDQYNLLKVQLGKDNHHQGSHGDGAQvngiq 735
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKElyalaneisrLEQQKQILRERLANLERQLEELEAQLEELESKLDELA----- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 736 pEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQAS---GMSEQASAtcpprdpeqVAELKQAKSVpvegESEHV 812
Cdd:TIGR02168 337 -EELAELEEKLEELKEELESLEAELEELEAELEELESRLEEleeQLETLRSK---------VAQLELQIAS----LNNEI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 813 SAAKT--TDVEGRLSALLQETKEL-----KNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLV 885
Cdd:TIGR02168 403 ERLEArlERLEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
250
....*....|....
gi 568936049 886 LLADQDQKILSLKS 899
Cdd:TIGR02168 483 ELAQLQARLDSLER 496
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
652-873 |
4.64e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.42 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 652 LEQHDNIVT-HYKNMIREQDLQLEELKQQVSTLKCQ----NEQLQTAVTQQASQI----QQHKDQYNLL----KVQLGKD 718
Cdd:pfam15921 204 IYEHDSMSTmHFRSLGSAISKILRELDTEISYLKGRifpvEDQLEALKSESQNKIelllQQHQDRIEQLisehEVEITGL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 719 NHHQGSHGdgAQVNGIQpeeiSRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQasgmsEQASATCPPRDPEQVAELK 798
Cdd:pfam15921 284 TEKASSAR--SQANSIQ----SQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSEL-----REAKRMYEDKIEELEKQLV 352
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568936049 799 QAKSVPVEGESEHVS-AAKTTDVEGRLSALLQETKELKNEIkALSEERTAIQKQLDSSNS-TIAILQTEKDKLDLEV 873
Cdd:pfam15921 353 LANSELTEARTERDQfSQESGNLDDQLQKLLADLHKREKEL-SLEKEQNKRLWDRDTGNSiTIDHLRRELDDRNMEV 428
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
670-881 |
1.12e-04 |
|
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: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 670 DLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLgkdnhhqgshgDGAQvngiqpEEISRLREEIEEL 749
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL-----------EALQ------AEIDKLQAEIAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 750 KSQQALLQGQLAE----------KDSLIENLKSSQ-ASGMSEQASA--TCPPRDPEQVAELKQAKsvpvegesehvsaak 816
Cdd:COG3883 78 EAEIEERREELGEraralyrsggSVSYLDVLLGSEsFSDFLDRLSAlsKIADADADLLEELKADK--------------- 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568936049 817 tTDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQD 881
Cdd:COG3883 143 -AELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
666-893 |
1.55e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 666 IREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQ-----------HKDQYNLLKVQLGKDNHHQGSHGDGAQVNGI 734
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAfrdlqgqlahaKKQQELQQRYAELCAAAITCTAQCEKLEKIH 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 735 QPEEISRLREEIEELKSQQALLQgQLAEKDSLIENLKSSQASGMSEQASATCPPRDPEQVAELKQAKSVPVE-GESEHVS 813
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHL-QETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQrGEQTYAQ 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 814 AAKT-TDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQ 892
Cdd:TIGR00618 540 LETSeEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLR 619
|
.
gi 568936049 893 K 893
Cdd:TIGR00618 620 K 620
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
672-888 |
1.59e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 672 QLEELKQQVSTLKCQNEQLQTAVTQQAS---QIQQHKDQYNLLKVQLGKDNHHQGSHGDGAQVNGIQpEEISRLREEIEE 748
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEEleeELEELEAELEELREELEKLEKLLQLLPLYQELEALE-AELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 749 LKSQQALLQGQLAEKDSLIENLKSSQasgmseqasatcpprdpEQVAELKQAKSVPVEGESEhvsaakttDVEGRLSALL 828
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQ-----------------EELEELLEQLSLATEEELQ--------DLAEELEELQ 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 829 QETKELKNEIKALSEERTAIQKQLDssnstiailQTEKDKLDLEVTDSKKEQDDLLVLLA 888
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELE---------QLENELEAAALEERLKEARLLLLIAA 256
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
672-878 |
2.00e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 672 QLEELKQQVStlkcqneQLQTAVTQQASQIQQHKDQYNLLKVQLG------------KDNHHQ----------------- 722
Cdd:PRK04863 838 ELRQLNRRRV-------ELERALADHESQEQQQRSQLEQAKEGLSalnrllprlnllADETLAdrveeireqldeaeeak 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 723 ---GSHGDGA-----QVNGIQ--PEEISRLREEIEELKSQQALLQGQ---LAEKDSLIENLKSSQASGMSEQASATCPP- 788
Cdd:PRK04863 911 rfvQQHGNALaqlepIVSVLQsdPEQFEQLKQDYQQAQQTQRDAKQQafaLTEVVQRRAHFSYEDAAEMLAKNSDLNEKl 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 789 -RDPEQV-AELKQAKSVPVEGESEHVSAAKT-TDVEGRLSALLQETKELKNEIKAL-------SEERTAIQK-----QLD 853
Cdd:PRK04863 991 rQRLEQAeQERTRAREQLRQAQAQLAQYNQVlASLKSSYDAKRQMLQELKQELQDLgvpadsgAEERARARRdelhaRLS 1070
|
250 260
....*....|....*....|....*
gi 568936049 854 SSNSTIAILQTEKDKLDLEVTDSKK 878
Cdd:PRK04863 1071 ANRSRRNQLEKQLTFCEAEMDNLTK 1095
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
830-904 |
3.04e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 3.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568936049 830 ETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 904
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
674-890 |
3.04e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 674 EELKQQVSTLKCQN-EQLQ---TAVTQQAsQI------QQHKDQYNLLKV-QLGKDNhhqgshgdGAQVNGIQpEEISRL 742
Cdd:COG4913 553 AELGRRFDYVCVDSpEELRrhpRAITRAG-QVkgngtrHEKDDRRRIRSRyVLGFDN--------RAKLAALE-AELAEL 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 743 REEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQ--ASATcpprdpEQVAELKQAKsvpvegesEHVSAAKttdv 820
Cdd:COG4913 623 EEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAE------REIAELEAEL--------ERLDASS---- 684
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 821 eGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLADQ 890
Cdd:COG4913 685 -DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
672-852 |
3.79e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 672 QLEELKQQVSTLKCQNEQLQtavtQQASQIQQHKDQYNLLKVQLGKDNHHQGSHGDGAQVNgiqpEEISRLRE---EIEE 748
Cdd:COG4913 618 ELAELEEELAEAEERLEALE----AELDALQERREALQRLAEYSWDEIDVASAEREIAELE----AELERLDAssdDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 749 LKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATcpprdpEQVAELKQAksvpVEGESEHVSAAKTTDVEGRLSALL 828
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE------EELDELQDR----LEAAEDLARLELRALLEERFAAAL 759
|
170 180 190
....*....|....*....|....*....|
gi 568936049 829 QETKE------LKNEIKALSEERTAIQKQL 852
Cdd:COG4913 760 GDAVErelrenLEERIDALRARLNRAEEEL 789
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
664-900 |
1.21e-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: 42.70 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 664 NMIREQDLQLEE----LKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNHHQgshgdgaQVNGIQpEEI 739
Cdd:TIGR04523 499 KKLNEEKKELEEkvkdLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEK-------EIDEKN-KEI 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 740 SRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQasgmseqasatcpprdpeqvaELKQAKSVPVEGESEHVSAakttd 819
Cdd:TIGR04523 571 EELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI---------------------EEKEKKISSLEKELEKAKK----- 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 820 vegrlsallqETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKS 899
Cdd:TIGR04523 625 ----------ENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYK 694
|
.
gi 568936049 900 K 900
Cdd:TIGR04523 695 K 695
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
672-890 |
2.14e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 672 QLEELKQQVstlkcqnEQLQTAVTQQASQIQQHKDQYNLLKvqlgkdnhhqgshgdgaqvngiqpEEISRLREEIEELKS 751
Cdd:TIGR02168 345 KLEELKEEL-------ESLEAELEELEAELEELESRLEELE------------------------EQLETLRSKVAQLEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 752 QQALLQGQLAEKDSLIENLKSSQASGMSEQasatcpprdPEQVAELKQAKSVPVEGESEHVSAAKtTDVEGRLSALLQET 831
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEI---------EELLKKLEEAELKELQAELEELEEEL-EELQEELERLEEAL 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568936049 832 KELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLD------LEVTDSKKEQDDLLVLLADQ 890
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgfsegvKALLKNQSGLSGILGVLSEL 528
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
673-905 |
2.43e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.86 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 673 LEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLK-----VQLGKDNHHQ--------------------GSHGD 727
Cdd:COG3096 838 LAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNkllpqANLLADETLAdrleelreeldaaqeaqafiQQHGK 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 728 GA-----QVNGIQ--PEEISRLREEIEELKSQQALLQGQLAEKDSLIEN---LKSSQASGMSEQASATCPP-----RDPE 792
Cdd:COG3096 918 ALaqlepLVAVLQsdPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRrphFSYEDAVGLLGENSDLNEKlrarlEQAE 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 793 QvaELKQAKSVPVEGESEHVSAAKT-TDVEGRLSALLQETKELKNEIKAL-------SEERTAIqkqldssnstiailqt 864
Cdd:COG3096 998 E--ARREAREQLRQAQAQYSQYNQVlASLKSSRDAKQQTLQELEQELEELgvqadaeAEERARI---------------- 1059
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568936049 865 EKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDLG 905
Cdd:COG3096 1060 RRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAE 1100
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
738-904 |
2.44e-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: 40.68 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 738 EISRLREEIEELKSQQALLQGQLAEKDSLIENLKssqasgmseqasatcpprdpEQVAELKQAKSVpVEGESEHVSAAKT 817
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAK--------------------TELEDLEKEIKR-LELEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 818 TDvEGRLS---------ALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDllvLLA 888
Cdd:COG1579 77 KY-EEQLGnvrnnkeyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE---ELA 152
|
170
....*....|....*.
gi 568936049 889 DQDQKILSLKSKLKDL 904
Cdd:COG1579 153 ELEAELEELEAEREEL 168
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
667-775 |
2.93e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 667 REQDLQLEELKQQVSTL----KCQNEQLQTAVTQQASQIQQHKDQYNLLKVQL---GKDNHHQGSHGDGAQVNgiqpEEI 739
Cdd:COG4717 359 LEEELQLEELEQEIAALlaeaGVEDEEELRAALEQAEEYQELKEELEELEEQLeelLGELEELLEALDEEELE----EEL 434
|
90 100 110
....*....|....*....|....*....|....*.
gi 568936049 740 SRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQA 775
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELEQLEEDGE 470
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
667-873 |
3.32e-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: 41.35 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 667 REQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDnhhQGSHGDGAQVNGIQPEEISRLREEI 746
Cdd:pfam10174 49 KEEAARISVLKEQYRVTQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTS---PVDGEDKFSTPELTEENFRRLQSEH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 747 EELKSQQALLQGQLAEKDSLIENLKSsqasgmseqasaTCPPRDP--EQVAELKQAKSVP-VEGESEHVSAAKTTDVEGR 823
Cdd:pfam10174 126 ERQAKELFLLRKTLEEMELRIETQKQ------------TLGARDEsiKKLLEMLQSKGLPkKSGEEDWERTRRIAEAEMQ 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568936049 824 L----SALLQETKEL---------KNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLEV 873
Cdd:pfam10174 194 LghleVLLDQKEKENihlreelhrRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEV 256
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
666-844 |
3.69e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 666 IREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNH--HQGSHGDGAQVNGIQP--EEISR 741
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEqlQAAQAELAQAQEELESlqEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 742 LREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATcpprdpEQVAELKQAksvpVEGESEHVSAAKTTDVE 821
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE------EQLESLQEE----LAALEQELQALSEAEAE 182
|
170 180
....*....|....*....|...
gi 568936049 822 GRLSALLQETKELKNEIKALSEE 844
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAEA 205
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
672-905 |
4.02e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.65 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 672 QLEELKQQvstlkcQNEQLQTavtQQASQIQQHKDQYNLLKVQLGKDNHHQGSHGDGAQVNgiqpEEISRLREEIEELKS 751
Cdd:pfam07888 35 RLEECLQE------RAELLQA---QEAANRQREKEKERYKRDREQWERQRRELESRVAELK----EELRQSREKHEELEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 752 QQALLQ---GQLA-EKDSLIENLKSSQASGMS-EQASATCPPRDPEQVAEL-------KQAKSVPVEGESEH-VSAAKTT 818
Cdd:pfam07888 102 KYKELSassEELSeEKDALLAQRAAHEARIRElEEDIKTLTQRVLERETELermkeraKKAGAQRKEEEAERkQLQAKLQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 819 DVEGRLSALLQETKELKNEIkalsEERTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLK 898
Cdd:pfam07888 182 QTEEELRSLSKEFQELRNSL----AQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLG 257
|
....*..
gi 568936049 899 SKLKDLG 905
Cdd:pfam07888 258 EELSSMA 264
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
666-858 |
4.72e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 666 IREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNHHQgshgdgaQVNGIQPEEISRL--R 743
Cdd:COG3883 39 LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL-------YRSGGSVSYLDVLlgS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 744 EEIEELKSQQALLQgQLAEKD-SLIENLKSSQASGMSEQASATcpprdpEQVAELKQAKSvpvEGESEHVSA-AKTTDVE 821
Cdd:COG3883 112 ESFSDFLDRLSALS-KIADADaDLLEELKADKAELEAKKAELE------AKLAELEALKA---ELEAAKAELeAQQAEQE 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 568936049 822 GRLSALLQETKELKNEIKALSEERTAIQKQLDSSNST 858
Cdd:COG3883 182 ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
676-868 |
5.84e-03 |
|
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.
Pssm-ID: 462015 [Multi-domain] Cd Length: 198 Bit Score: 39.21 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 676 LKQQvstLK-CQNEqlqtaVTQQASQIQQhkdqynlLKVQLgKDnhhqgshgdgaqvngiqpeeisrLREEIEELKSQQA 754
Cdd:pfam06818 15 LKQQ---LKdSQAE-----VTQKLNEIVA-------LRAQL-RE-----------------------LRAKLEEKEEQIQ 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 755 LLQGQLAEKDSLIENL------KSSQASGMSEQASatcppRDPEQVAELKQA----KSVPVEGESEHVSAAKTTDVEGRL 824
Cdd:pfam06818 56 ELEDSLRSKTLELEVCenelqrKKNEAELLREKVG-----KLEEEVSGLREAlsdvSPSGYESVYESDEAKEQRQEEADL 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568936049 825 SALLQETKELKNEikaLSEERTAIQKQLDSSNSTIAILQTEKDK 868
Cdd:pfam06818 131 GSLRREVERLRAE---LREERQRRERQASSFEQERRTWQEEKEK 171
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
564-879 |
5.85e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.48 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 564 ENYTKE---KLKQ---LIEKRIGKENFIEKLGFISKhELYSRASQKPqpnfpspEYMIFDHEFTKLVKELEGVITKAIYK 637
Cdd:pfam05483 229 EEYKKEindKEKQvslLLIQITEKENKMKDLTFLLE-ESRDKANQLE-------EKTKLQDENLKELIEKKDHLTKELED 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 638 SSEEDKKEEEVKKTLEQHDNIVTH-YKNMIREQDLQLEELKQQ-------VSTLKCQNEQLQTAVTQQASQIQQHKDQYN 709
Cdd:pfam05483 301 IKMSLQRSMSTQKALEEDLQIATKtICQLTEEKEAQMEELNKAkaahsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLK 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 710 LLKVQLGKDNHhqgshgdgaqvngiQPEEISRLRE----EIEELKSQQALLQGQLAEK---DSLIENLKssqasGMSEQA 782
Cdd:pfam05483 381 IITMELQKKSS--------------ELEEMTKFKNnkevELEELKKILAEDEKLLDEKkqfEKIAEELK-----GKEQEL 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 783 SATCPPRDPE------QVAE--------LKQAKSVPVEGESEHVSAAKTTDVEGRLS----ALLQETKELKNEIKALSEE 844
Cdd:pfam05483 442 IFLLQAREKEihdleiQLTAiktseehyLKEVEDLKTELEKEKLKNIELTAHCDKLLlenkELTQEASDMTLELKKHQED 521
|
330 340 350
....*....|....*....|....*....|....*
gi 568936049 845 RTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKE 879
Cdd:pfam05483 522 IINCKKQEERMLKQIENLEEKEMNLRDELESVREE 556
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
672-883 |
6.23e-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: 40.42 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 672 QLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNllkVQLGKDNHHQGSHGDGA-QVNGIQPEE--ISRLREEIEE 748
Cdd:TIGR00606 574 QLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHIN---NELESKEEQLSSYEDKLfDVCGSQDEEsdLERLKEEIEK 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 749 LKSQQALLQGQLAEKDSLIENLkssqasgmSEQASATCP--PRDPEQVAELKQAKSvpvegesehvsaakttDVEGRLSA 826
Cdd:TIGR00606 651 SSKQRAMLAGATAVYSQFITQL--------TDENQSCCPvcQRVFQTEAELQEFIS----------------DLQSKLRL 706
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568936049 827 LLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTE----KDKLDLEVTDSKKEQDDL 883
Cdd:TIGR00606 707 APDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEipelRNKLQKVNRDIQRLKNDI 767
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
737-904 |
7.57e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 737 EEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATcpprdpEQVAELKQaksvpvegesehvsaak 816
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE------EELEELNE----------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 817 ttdvegRLSALLQETKELKNEIKALSEERTAIQKQLDSsnstiaiLQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILS 896
Cdd:COG4372 88 ------QLQAAQAELAQAQEELESLQEEAEELQEELEE-------LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE 154
|
....*...
gi 568936049 897 LKSKLKDL 904
Cdd:COG4372 155 LEEQLESL 162
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
665-776 |
8.29e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 38.65 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 665 MIREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQH---------KDQYNLLKVQLGKDNHHQgshgdgAQVNGIQ 735
Cdd:COG1842 31 AIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWeekarlaleKGREDLAREALERKAELE------AQAEALE 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 568936049 736 pEEISRLREEIEELKSQQALLQGQL----AEKDSLIENLKSSQAS 776
Cdd:COG1842 105 -AQLAQLEEQVEKLKEALRQLESKLeelkAKKDTLKARAKAAKAQ 148
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
816-890 |
8.89e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 8.89e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568936049 816 KTTDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLADQ 890
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
652-905 |
9.00e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 9.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 652 LEQHDNIVTHYKNMIREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKvqlgkdnhhqgshgdgAQV 731
Cdd:PRK02224 337 AQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELR----------------ERF 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 732 NGIqPEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATCPprdpeqvaELKQaksvPVEGeSEH 811
Cdd:PRK02224 401 GDA-PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCP--------ECGQ----PVEG-SPH 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568936049 812 VSAA-------------------KTTDVEGRLSAlLQETKELKNEIKALSEERTAIQKQLDSSNSTI-------AILQTE 865
Cdd:PRK02224 467 VETIeedrerveeleaeledleeEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIeekreraEELRER 545
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 568936049 866 KDKLDLE-------VTDSKKEQDDLLVLLADQDQKILSLKSKLKDLG 905
Cdd:PRK02224 546 AAELEAEaeekreaAAEAEEEAEEAREEVAELNSKLAELKERIESLE 592
|
|
| |
