|
Name |
Accession |
Description |
Interval |
E-value |
| Uso1_p115_head |
pfam04869 |
Uso1 / p115 like vesicle tethering protein, head region; Also known as General vesicular ... |
347-628 |
1.62e-67 |
|
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: 228.23 E-value: 1.62e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 347 NQDYFASV--------------NAPSNPPRPAIVVLL--MSMVNERQPFVLRCAVLYCFQCFLYKNEKGQGEIVATLLPS 410
Cdd:pfam04869 2 LQEEFAKIdvpypdpslpsaanAADQPVKVPVIDLLLnwALSANSVHAFDLRVAACYCLKAYFYNNEEIRLHFLQRAIEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 411 TIDATGNSVSAGQLLCGGL-----FSTDSLSNWCAAVALAHALQGNATQKEQLLRVQLAT-SIGNPPVSLLQQCTNIL-- 482
Cdd:pfam04869 82 YKSGNDSSSTTANLLEVLLdydpdLKLDPYKLWFASVILMHLLEDNPEAKELARSVTEGDaESGEEVVTLIQTISELLit 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 483 -SQGSKIQTRVGLLMLLCTWLSNCPIAVTHFLHNSANVPFLTGQIAENlGEEEQLVQGLCALLLGISIYFNDNSlENYTK 561
Cdd:pfam04869 162 sLQREDPRIPIGYLMLLIVWLFEDPDAVNDFLSEGSNLQSLLQFLSQS-SDEDVLVQGLCAMLLGIAYEFSTKD-SPIPR 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23956096 562 EKLKQLIEKRIGKENFIEKLGFISKHELYSRASQKPQPNFPSPEYMI----FDHEFTKLVKELEGVITKAI 628
Cdd:pfam04869 240 ADLHSLLTKRLGRDNYIDKIKQLREHPLFRDFEVLPQLNPSLDDTGLpevyFDSYFVELFKDNFSRIRRAL 310
|
|
| Arm_vescicular |
pfam18770 |
Armadillo tether-repeat of vescicular transport factor; Armadillo-like tether-repeat of ... |
270-329 |
1.00e-32 |
|
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: 120.49 E-value: 1.00e-32
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 270 SGWSAQKVTNLHLMLQLVRVLVSPTNPPGATSSCQKAMFQCGLLQQLCTILMATGIPADI 329
Cdd:pfam18770 1 SGWSAQKVSNVHCMLQVVRTLVSPNNPSQVTSSCQKAMRACGLLEALCNILMASGVPADI 60
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
659-930 |
6.77e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.60 E-value: 6.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 659 IREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLgkDNHHQGSHGDGAQVNGIQpEEISRLREE 738
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL--EEAQAEEYELLAELARLE-QDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 739 IEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATcpprdpEQVAELKQELTALKSQLCSQSLEITRLQTENCEL 818
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAE------EELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 819 LQRAETLAKSVPVEGESEHVSAAKTTDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLE 898
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250 260 270
....*....|....*....|....*....|..
gi 23956096 899 VTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 930
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
644-930 |
4.37e-11 |
|
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: 66.97 E-value: 4.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 644 TLEQHDNIVTHYKNMIREQDLQLEELKQQVSTLKCQNEQLQTAVTQqaSQIQQHKDQYNLLKVQLGKDNHhqgshgdgaQ 723
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELK--SELKNQEKKLEEIQNQISQNNK---------I 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 724 VNGIQpEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATCPPRDPEQVAELKQELTALKSQlcs 803
Cdd:TIGR04523 337 ISQLN-EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE--- 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 804 qslEITRLQTENCELLQRAETLAKSVPVEG-------ESEHVSAAKTTDVEGRLSALLQETKELKNEIKALSEERTAIQK 876
Cdd:TIGR04523 413 ---QIKKLQQEKELLEKEIERLKETIIKNNseikdltNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK 489
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 23956096 877 QLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 930
Cdd:TIGR04523 490 ELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
659-916 |
6.19e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 6.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 659 IREQDLQLEELKQQVSTLKCQNEQLQTA----------VTQQASQIQQHKDQYNLLKVQLGKDNHHQGSHGDGAQvngiq 728
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKElyalaneisrLEQQKQILRERLANLERQLEELEAQLEELESKLDELA----- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 729 pEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQAS---GMSEQASAtcpprdpeqVAELKQELTALKSQLCSQS 805
Cdd:TIGR02168 337 -EELAELEEKLEELKEELESLEAELEELEAELEELESRLEEleeQLETLRSK---------VAQLELQIASLNNEIERLE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 806 LEITRLQTENCELLQRAETLAKSvPVEGESEHVSAAKTT------DVEGRLSALLQETKELKNEIKALSEERTAIQKQLD 879
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKK-LEEAELKELQAELEEleeeleELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 23956096 880 SSNSTIAILQTEKDKLD------LEVTDSKKEQDDLLVLLADQ 916
Cdd:TIGR02168 486 QLQARLDSLERLQENLEgfsegvKALLKNQSGLSGILGVLSEL 528
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
728-930 |
2.38e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.70 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 728 QPEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKS--SQASGMSEQASatcppRDPEQVAE----LKQELTALKSQL 801
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQelSDASRKIGEIE-----KEIEQLEQeeekLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 802 CSQSLEITRLQTE----NCELLQRAETLAK---------------SVP-VEGESEHVSA------AKTTDVEGRLSALLQ 855
Cdd:TIGR02169 747 SSLEQEIENVKSElkelEARIEELEEDLHKleealndlearlshsRIPeIQAELSKLEEevsrieARLREIEQKLNRLTL 826
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23956096 856 ETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 930
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
657-930 |
2.73e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 657 NMIREQDLqLEELKQQVSTLKCQNEQLQTAVTQQAS----QIQQHKDQYNLLKVQLGKDNHHQGSHGDG-----AQVNGI 727
Cdd:COG1196 187 NLERLEDI-LGELERQLEPLERQAEKAERYRELKEElkelEAELLLLKLRELEAELEELEAELEELEAEleeleAELAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 728 QpEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATcpprdpEQVAELKQELTALKSQLCSQSLE 807
Cdd:COG1196 266 E-AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE------ERLEELEEELAELEEELEELEEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 808 ITRLQTENCELLQRAETLAKSVPVEGESEHVSAAKTTDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAI 887
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 23956096 888 LQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 930
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
662-920 |
3.62e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.86 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 662 QDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNhhqgshgdgAQVNGIQpEEISRLREEIEE 741
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA---------RRIRALE-QELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 742 LKSQQALLQGQLAE-KDSLIENLKSSQASGMSEQASATCPPRDPEQVAELKQELTALksqlcsqsleitrlqteNCELLQ 820
Cdd:COG4942 88 LEKEIAELRAELEAqKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL-----------------APARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 821 RAETLAksvpvegesehvsaAKTTDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLEVT 900
Cdd:COG4942 151 QAEELR--------------ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
|
250 260
....*....|....*....|
gi 23956096 901 DSKKEQDDLLVLLADQDQKI 920
Cdd:COG4942 217 ELQQEAEELEALIARLEAEA 236
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
659-930 |
5.81e-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: 63.55 E-value: 5.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 659 IREQDLQLEELKQQVSTLKCQNEQLQtavtqqaSQIQQHKDQYNLLKVQLGKDNHHQGSHGDGAQVNgIQPE------EI 732
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLT-------EEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR-VKEKigeleaEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 733 SRLREEIEELKSQQALLQGQLAEKDSLIENLKssqasgmseqasatcpprdpEQVAELKQELTALKSQLCSQSLEITRLQ 812
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLL--------------------AEIEELEREIEEERKRRDKLTEEYAELK 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 813 TENCELLQRAETLAKSVpvegeseHVSAAKTTDVEGRLSALLQETKELKNEI-------KALSEERTAIQKQLDSSNSTI 885
Cdd:TIGR02169 364 EELEDLRAELEEVDKEF-------AETRDELKDYREKLEKLKREINELKRELdrlqeelQRLSEELADLNAAIAGIEAKI 436
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 23956096 886 AILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 930
Cdd:TIGR02169 437 NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
841-934 |
4.32e-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: 55.48 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 841 AKTTDVEGRLSALLQETKELKNEIKALS------EERTAIQKQLDSSNST----IAILQTEKDKLDLEVTDSKKEQDDLL 910
Cdd:pfam04871 1 AKKSELESEASSLKNENTELKAELQELSkqynslEQKESQAKELEAEVKKleeaLKKLKAELSEEKQKEKEKQSELDDLL 80
|
90 100
....*....|....*....|....
gi 23956096 911 VLLADQDQKILSLKSKLKDLGHPV 934
Cdd:pfam04871 81 LLLGDLEEKVEKYKARLKELGEEV 104
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
655-930 |
8.50e-09 |
|
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: 59.75 E-value: 8.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 655 YKNMIREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQ-----HKDQYNLlkvQLGKDNHHQ---GSHGDGAQVNG 726
Cdd:pfam15921 340 YEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKlladlHKREKEL---SLEKEQNKRlwdRDTGNSITIDH 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 727 IQPE------EISRLREEIEELKSQqalLQGQLAEKDSLIENLKSS--QASGMSEQASATcpprdPEQVAELKQELTALK 798
Cdd:pfam15921 417 LRRElddrnmEVQRLEALLKAMKSE---CQGQMERQMAAIQGKNESleKVSSLTAQLEST-----KEMLRKVVEELTAKK 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 799 SQLCSQSLEITRLQTEncelLQRAETLAKSvpvegesehvSAAKTTDVEGRLSALLQETKELKNE---IKALSEERTAIQ 875
Cdd:pfam15921 489 MTLESSERTVSDLTAS----LQEKERAIEA----------TNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALK 554
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956096 876 KQLDSSNSTIAIL---------------------QTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 930
Cdd:pfam15921 555 LQMAEKDKVIEILrqqienmtqlvgqhgrtagamQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL 630
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
655-930 |
9.12e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 59.26 E-value: 9.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 655 YKNMIREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNHH-QGSHGDGAQVNGIQPE--- 730
Cdd:TIGR04523 209 KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQlSEKQKELEQNNKKIKElek 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 731 EISRLREEIEELKSQQA-----LLQGQLAEKDSLIENLKS------SQASGMSEQASATCPPRD---------PEQVAEL 790
Cdd:TIGR04523 289 QLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNqisqnnKIISQLNEQISQLKKELTnsesensekQRELEEK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 791 KQELTALKSQLCSQSLEITRLQTENCEL---LQRAETLAKSvpVEGESEHVSAAKTTdVEGRLSALLQETKELKNEIKAL 867
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLeskIQNQEKLNQQ--KDEQIKKLQQEKEL-LEKEIERLKETIIKNNSEIKDL 445
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23956096 868 SEERTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 930
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEL 508
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
722-879 |
1.10e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 56.86 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 722 AQVNGIQpEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEqasatcpprdpeqvaelkQELTALKSQL 801
Cdd:COG1579 38 DELAALE-ARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN------------------KEYEALQKEI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23956096 802 CSQSLEITRLQTENCELLQRAETLAKSVpveGESEHVSAAKTTDVEGRLSALLQETKELKNEIKALSEERTAIQKQLD 879
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEEL---AELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
644-880 |
4.54e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 644 TLEQHDNIVTHYKNmireqdlqLEELKQQVSTLKCQNEQLQtavtqqasQIQQHKDQYNLLKVQLGkdnhHQGSHGDGAQ 723
Cdd:COG4913 223 TFEAADALVEHFDD--------LERAHEALEDAREQIELLE--------PIRELAERYAAARERLA----ELEYLRAALR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 724 VNGIQpEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKsSQASGMSEQASAtcppRDPEQVAELKQELTALKSQLCS 803
Cdd:COG4913 283 LWFAQ-RRLELLEAELEELRAELARLEAELERLEARLDALR-EELDELEAQIRG----NGGDRLEQLEREIERLERELEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 804 QSLEITRLQtencellQRAETLAKSVPVEGES--EHVSAAKT--TDVEGRLSALLQETKELKNEIKALSEERTAIQKQLD 879
Cdd:COG4913 357 RERRRARLE-------ALLAALGLPLPASAEEfaALRAEAAAllEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
.
gi 23956096 880 S 880
Cdd:COG4913 430 S 430
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
731-930 |
7.87e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 7.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 731 EISRLREEIEELKSQQALLQGQLAEKDslienlkssqasgmseqasatcpprdpEQVAELKQELTALKSQLCSQSLEITR 810
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELR---------------------------KELEELEEELEQLRKELEELSRQISA 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 811 LQTENCELLQRAETLAKSVPVEGESEHVSAAKTTDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQT 890
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 23956096 891 EKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 930
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
665-931 |
8.95e-08 |
|
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: 56.59 E-value: 8.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 665 QLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNllkVQLGKDNHHQGSHGDGA-QVNGIQPEE--ISRLREEIEE 741
Cdd:TIGR00606 574 QLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHIN---NELESKEEQLSSYEDKLfDVCGSQDEEsdLERLKEEIEK 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 742 LKSQQALLQGQLAEKDSLIENLkssqasgmSEQASATCP--PRDPEQVAELKQELTALKSQLCSQSLEITRLQTENCELL 819
Cdd:TIGR00606 651 SSKQRAMLAGATAVYSQFITQL--------TDENQSCCPvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKE 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 820 QRAETLAKSVPVEGESEHVSAAKTTDVEGRLSALLQETKELKNEIK--------ALSEERTA------------IQKQLD 879
Cdd:TIGR00606 723 KRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEeqetllgtIMPEEESAkvcltdvtimerFQMELK 802
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23956096 880 SSNSTIAILQTEKDKLDL-----EVTDSKKEQDDLL-----------VLLADQDQKILSLKSKLKDLG 931
Cdd:TIGR00606 803 DVERKIAQQAAKLQGSDLdrtvqQVNQEKQEKQHELdtvvskielnrKLIQDQQEQIQHLKSKTNELK 870
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
656-930 |
1.10e-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: 55.80 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 656 KNMIREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNhhqgshgdgaQVNGIQPEEISRL 735
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ----------QEKELLEKEIERL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 736 REEIEELKSQQALLQGQLAEKDSLIENLKSSQASgMSEQASATcpprdPEQVAELKQELTALKSQLCSQSLEITRLQTEN 815
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES-LETQLKVL-----SRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 816 CELlqraetlaksvpvegesehvsaakttdvEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTI---------A 886
Cdd:TIGR04523 506 KEL----------------------------EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkddfelkkE 557
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 23956096 887 ILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 930
Cdd:TIGR04523 558 NLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDL 601
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
662-898 |
4.95e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 662 QDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVqlgkdnhhqgshgdgaqvngiqPEEISRLREEIEE 741
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDL----------------------SEEAKLLLQQLSE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 742 LKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATcppRDP------EQVAELKQELTALKSQLCSQSLEITRLQTEN 815
Cdd:COG3206 224 LESQLAEARAELAEAEARLAALRAQLGSGPDALPELL---QSPviqqlrAQLAELEAELAELSARYTPNHPDVIALRAQI 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 816 CELLQRAETLAKSVPVEGESEHVSAakttdvEGRLSALLQETKELKNEIKALSE---ERTAIQKQLDSSNSTIAILQTEK 892
Cdd:COG3206 301 AALRAQLQQEAQRILASLEAELEAL------QAREASLQAQLAQLEARLAELPEleaELRRLEREVEVARELYESLLQRL 374
|
....*.
gi 23956096 893 DKLDLE 898
Cdd:COG3206 375 EEARLA 380
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
645-931 |
6.03e-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: 53.52 E-value: 6.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 645 LEQHDNIVTHYKNMIREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKvqlgkdnhhqgshgdgaqv 724
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR------------------- 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 725 ngiqpEEISRLREEIEELKSQQALLQGQLAEKDSLIENLkSSQASGMSEQ-ASATcpprdpEQVAELKQELTALKSQLCS 803
Cdd:TIGR02168 810 -----AELTLLNEEAANLRERLESLERRIAATERRLEDL-EEQIEELSEDiESLA------AEIEELEELIEELESELEA 877
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 804 QSLEITRLQTENCELLQRAETLAKSVpvegesehvsaaktTDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNS 883
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEEL--------------RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 23956096 884 TIAilqtEKDKLDLEVTDSKKEQDDLlvLLADQDQKILSLKSKLKDLG 931
Cdd:TIGR02168 944 RLS----EEYSLTLEEAEALENKIED--DEEEARRRLKRLENKIKELG 985
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
655-909 |
6.29e-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: 53.52 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 655 YKNMIREQDLQLeeLKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLgkDNHHQGSHGDGAQVNGIQPE---- 730
Cdd:TIGR02168 218 LKAELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKL--EELRLEVSELEEEIEELQKElyal 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 731 --EISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQAsgmseqasatcppRDPEQVAELKQELTALKSQLCSQSLEI 808
Cdd:TIGR02168 294 anEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD-------------ELAEELAELEEKLEELKEELESLEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 809 TRLQTENCELLQRAETLAKSVpvegesehvsaaktTDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAIL 888
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQL--------------ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL 426
|
250 260
....*....|....*....|....*.
gi 23956096 889 QT-----EKDKLDLEVTDSKKEQDDL 909
Cdd:TIGR02168 427 LKkleeaELKELQAELEELEEELEEL 452
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
658-923 |
1.38e-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: 52.38 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 658 MIREQDLQLEELKQQVSTLKCQNEQLQTavtqQASQIQQHKDQYNLLKVQLGKDnhhqgshgdgaqvngIQP--EEISRL 735
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEE----DLSSLEQEIENVKSELKELEAR---------------IEEleEDLHKL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 736 REEIEELKsqQALLQGQLAEKDSLIENLKssqasgmseqasatcpprdpEQVAELKQELTALKSQLCSQSLEITRLQTEN 815
Cdd:TIGR02169 778 EEALNDLE--ARLSHSRIPEIQAELSKLE--------------------EEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 816 CELL-QRAETLAKSVPVEGESEhvsaakttDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDK 894
Cdd:TIGR02169 836 QELQeQRIDLKEQIKSIEKEIE--------NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
250 260
....*....|....*....|....*....
gi 23956096 895 LDLEVTDSKKEQDDLLVLLADQDQKILSL 923
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
659-909 |
1.78e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 52.13 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 659 IREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNHHQGshgdgaqvngiqpEEISRLREE 738
Cdd:pfam10174 410 LRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERL-------------EELESLKKE 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 739 IEELKSQQALLQGQLAEKDSLIENLK---SSQASGMSEQASATcppRDPE-QVAELKQELTALKSQL-CSQSLEITrlQT 813
Cdd:pfam10174 477 NKDLKEKVSALQPELTEKESSLIDLKehaSSLASSGLKKDSKL---KSLEiAVEQKKEECSKLENQLkKAHNAEEA--VR 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 814 ENCELLQRAETLAKSVPVEGESehvSAAKTTDVEgRLSALLQETKELKNEI-KALSEERTAIQKQLDSSNSTIAILQT-- 890
Cdd:pfam10174 552 TNPEINDRIRLLEQEVARYKEE---SGKAQAEVE-RLLGILREVENEKNDKdKKIAELESLTLRQMKEQNKKVANIKHgq 627
|
250 260
....*....|....*....|.
gi 23956096 891 --EKDKLDLEVTDSKKEQDDL 909
Cdd:pfam10174 628 qeMKKKGAQLLEEARRREDNL 648
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
665-911 |
3.64e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 665 QLEELKQQVStlkcqneQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNHHQGshgdgaQVNGIQPE----EISRLREEIE 740
Cdd:PRK04863 838 ELRQLNRRRV-------ELERALADHESQEQQQRSQLEQAKEGLSALNRLLP------RLNLLADEtladRVEEIREQLD 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 741 ELKSQQALLQ---GQLAEKDSLIENLKSsqasgmseqasatcpprDPEQVAELKQELTALKSQLCSQSLEITRLQtencE 817
Cdd:PRK04863 905 EAEEAKRFVQqhgNALAQLEPIVSVLQS-----------------DPEQFEQLKQDYQQAQQTQRDAKQQAFALT----E 963
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 818 LLQRAETLAKSVPVEgesehvSAAKTTDVEGRLSALLQETKELKNEIKalsEERTAIQKQLDSSNSTIAILQTEKDKLDL 897
Cdd:PRK04863 964 VVQRRAHFSYEDAAE------MLAKNSDLNEKLRQRLEQAEQERTRAR---EQLRQAQAQLAQYNQVLASLKSSYDAKRQ 1034
|
250
....*....|....
gi 23956096 898 EVTDSKKEQDDLLV 911
Cdd:PRK04863 1035 MLQELKQELQDLGV 1048
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
645-931 |
8.09e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 8.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 645 LEQHDNIVTHYKNMIREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKvqlgkdnhhqgshgdgAQV 724
Cdd:PRK02224 337 AQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELR----------------ERF 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 725 NGIqPEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATCP---------PR------DPEQVAE 789
Cdd:PRK02224 401 GDA-PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPecgqpvegsPHvetieeDRERVEE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 790 LKQELTALKSQLCSQSLEITRLqTENCELLQRAETLAKSvpVEGESEHVSAAKTTDVEGRLSA--LLQETKELKNEIKAL 867
Cdd:PRK02224 480 LEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEER--REDLEELIAERRETIEEKRERAeeLRERAAELEAEAEEK 556
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23956096 868 SEERTAIQKQLDSSNSTIAILQTEKDKLDLEVtDSKKEQDDLLVLLADQDQKILSLKSKLKDLG 931
Cdd:PRK02224 557 REAAAEAEEEAEEAREEVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKREALA 619
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
728-892 |
9.18e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 9.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 728 QPEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATCPPR---DPEQVAELKQELTALKSQLcsq 804
Cdd:COG4717 86 KEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElaeLPERLEELEERLEELRELE--- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 805 sLEITRLQTENCELLQRAETLAKSVPVEGESEHVSAAKttdvegRLSALLQETKELKNEIKALSEERTAIQKQLDSSNST 884
Cdd:COG4717 163 -EELEELEAELAELQEELEELLEQLSLATEEELQDLAE------ELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
....*...
gi 23956096 885 IAILQTEK 892
Cdd:COG4717 236 LEAAALEE 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
645-842 |
9.36e-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: 9.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 645 LEQHDNIVTHYKNMIREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQH------KDQYNLLKVQLGKDNHHQGSH 718
Cdd:COG4942 57 LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlralyrLGRQPPLALLLSPEDFLDAVR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 719 GDG--AQVNGIQPEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATcpprdpEQVAELKQELTA 796
Cdd:COG4942 137 RLQylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQ------KLLARLEKELAE 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 23956096 797 LKSQLCSQSLEITRLQtencELLQRAETLAKSVPVEGESEHVSAAK 842
Cdd:COG4942 211 LAAELAELQQEAEELE----ALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
663-906 |
1.02e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.73 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 663 DLQLEELKQqvstLKCQNEQLQTAVTQ-QASQIQQ-HKDQY-NLLKVQLGKDNHHQGSHGDGA---QVNGIQPE-EISRL 735
Cdd:pfam15921 527 DLKLQELQH----LKNEGDHLRNVQTEcEALKLQMaEKDKViEILRQQIENMTQLVGQHGRTAgamQVEKAQLEkEINDR 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 736 REEIEELKSQQALLQGQLAEKDSLIENL---KSSQASGMSEQASAtcpprdpeqVAELKQELTALKSQLCSQSLEITRLq 812
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRELEARVSDLeleKVKLVNAGSERLRA---------VKDIKQERDQLLNEVKTSRNELNSL- 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 813 TENCELLQRAetlaksvpVEGESEHVSAAkTTDVEGRLSALLQETKELKNEIKALS-------EERTAIQKQLDSSNSTI 885
Cdd:pfam15921 673 SEDYEVLKRN--------FRNKSEEMETT-TNKLKMQLKSAQSELEQTRNTLKSMEgsdghamKVAMGMQKQITAKRGQI 743
|
250 260
....*....|....*....|.
gi 23956096 886 AILQTEKDKLDLEVTDSKKEQ 906
Cdd:pfam15921 744 DALQSKIQFLEEAMTNANKEK 764
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
656-906 |
1.03e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.73 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 656 KNMIRE-------QDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLlKVQlgkdnhhqgshgdgaqvngiq 728
Cdd:pfam15921 474 KEMLRKvveeltaKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDL-KLQ--------------------- 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 729 peEISRLREEIEELKSQQA---LLQGQLAEKDSLIENLKSsQASGMSE---QASATCPPRDPEQvAELKQELTALKSQLc 802
Cdd:pfam15921 532 --ELQHLKNEGDHLRNVQTeceALKLQMAEKDKVIEILRQ-QIENMTQlvgQHGRTAGAMQVEK-AQLEKEINDRRLEL- 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 803 sQSLEITRLQTENC--ELLQRAE--TLAKSVPVEGESEHVSAAKttDVEGRLSALLQETKELKNEIKALSEERTAIQKQL 878
Cdd:pfam15921 607 -QEFKILKDKKDAKirELEARVSdlELEKVKLVNAGSERLRAVK--DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNF 683
|
250 260
....*....|....*....|....*...
gi 23956096 879 DSSNSTIAiLQTEKDKLDLEVTDSKKEQ 906
Cdd:pfam15921 684 RNKSEEME-TTTNKLKMQLKSAQSELEQ 710
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
730-829 |
1.21e-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: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 730 EEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATcpPRDPEqVAELKQELTALKSQLCSQSLEIT 809
Cdd:COG2433 413 EEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREI--RKDRE-ISRLDREIERLERELEEERERIE 489
|
90 100
....*....|....*....|
gi 23956096 810 RLQTEncelLQRAETLAKSV 829
Cdd:COG2433 490 ELKRK----LERLKELWKLE 505
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
666-909 |
9.83e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.48 E-value: 9.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 666 LEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLK-----VQLGKDNHHQgshgdgaqvngiqpEEISRLREEIE 740
Cdd:COG3096 838 LAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNkllpqANLLADETLA--------------DRLEELREELD 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 741 ELKSQQALLQGQ---LAEKDSLIENLKSsqasgmseqasatcpprDPEQVAELKQELTALKSQLcsqsleiTRLQtence 817
Cdd:COG3096 904 AAQEAQAFIQQHgkaLAQLEPLVAVLQS-----------------DPEQFEQLQADYLQAKEQQ-------RRLK----- 954
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 818 llQRAETLAKsvpVEGESEHVSAAKTTDVEGRLSALLQETKE-LKNEIKALSEERTA---IQKQLDSSNSTIAILQTEKD 893
Cdd:COG3096 955 --QQIFALSE---VVQRRPHFSYEDAVGLLGENSDLNEKLRArLEQAEEARREAREQlrqAQAQYSQYNQVLASLKSSRD 1029
|
250
....*....|....*.
gi 23956096 894 KLDLEVTDSKKEQDDL 909
Cdd:COG3096 1030 AKQQTLQELEQELEEL 1045
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
665-878 |
1.05e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 665 QLEELKQQVSTLKCQNEQLQtavtQQASQIQQHKDQYNLLKVQLGKDNHHQGSHgdgaqvngiqpEEISRLREEIEEL-K 743
Cdd:COG4913 618 ELAELEEELAEAEERLEALE----AELDALQERREALQRLAEYSWDEIDVASAE-----------REIAELEAELERLdA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 744 SQQAL--LQGQLAEKDSLIENLKssqasgmseqasatcpprdpEQVAELKQELTALKSQLCSQSLEITRLQtencELLQR 821
Cdd:COG4913 683 SSDDLaaLEEQLEELEAELEELE--------------------EELDELKGEIGRLEKELEQAEEELDELQ----DRLEA 738
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 23956096 822 AETLAKSVPVEGESEHVSAAKTTDVEGRLSALLQEtkelknEIKALSEERTAIQKQL 878
Cdd:COG4913 739 AEDLARLELRALLEERFAAALGDAVERELRENLEE------RIDALRARLNRAEEEL 789
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
665-859 |
1.43e-04 |
|
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: 45.82 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 665 QLEELKQQV-------STLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNHHQGSHgdGAQVNGIQpEEISRLRE 737
Cdd:TIGR02168 345 KLEELKEELesleaelEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL--EARLERLE-DRRERLQQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 738 EIEEL-----KSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATcpprdpEQVAELKQELTALKSQLCSQSLEITRLQ 812
Cdd:TIGR02168 422 EIEELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELR------EELEEAEQALDAAERELAQLQARLDSLE 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23956096 813 T--ENCE--------LLQRAETLAKSVPVEGESEHV----SAAKTTDVEGRLSALLQETKE 859
Cdd:TIGR02168 496 RlqENLEgfsegvkaLLKNQSGLSGILGVLSELISVdegyEAAIEAALGGRLQAVVVENLN 556
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
656-882 |
1.47e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 656 KNMIREQDLQLEELKQQVSTLK---CQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNH--HQGSHGDGAQVNGIQP- 729
Cdd:PRK04863 910 KRFVQQHGNALAQLEPIVSVLQsdpEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHfsYEDAAEMLAKNSDLNEk 989
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 730 --EEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQasgmseQASAtcpprdpEQVAELKQELTALKSQLCSQSLE 807
Cdd:PRK04863 990 lrQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSY------DAKR-------QMLQELKQELQDLGVPADSGAEE 1056
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23956096 808 ITRLQTEncELLQRAetlaksvpvegeseHVSAAKTTDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSN 882
Cdd:PRK04863 1057 RARARRD--ELHARL--------------SANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAK 1115
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
659-913 |
1.61e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 659 IREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKvqlgkdnhhqgshgdgaqvngiqpEEISRLREE 738
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE------------------------EELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 739 IEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATcpprdpEQVAELKQELTALKSQLCSQSLEITRLQTENCEL 818
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLE------QQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 819 LQRAETLAKSVPVEGESEHVSAAKTTDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLE 898
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250
....*....|....*
gi 23956096 899 VTDSKKEQDDLLVLL 913
Cdd:COG4372 243 ELEEDKEELLEEVIL 257
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
659-914 |
1.64e-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: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 659 IREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQ-----------HKDQYNLLKVQLGKDNHHQGSHGDGAQVNGI 727
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAfrdlqgqlahaKKQQELQQRYAELCAAAITCTAQCEKLEKIH 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 728 QPEEISRLREEIEELKSQQALLQgQLAEKDSLIENLKssqasgmSEQASATCP----PRDPEQVAELKQELTALKSQLCS 803
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHL-QETRKKAVVLARL-------LELQEEPCPlcgsCIHPNPARQDIDNPGPLTRRMQR 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 804 QSLEITRLQTEN-------CELLQRAETLAKSVPVEGESEHVSAAKTTDVEGRLSALLQETKELKNEIKALSEERtaiQK 876
Cdd:TIGR00618 533 GEQTYAQLETSEedvyhqlTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE---DM 609
|
250 260 270
....*....|....*....|....*....|....*...
gi 23956096 877 QLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLA 914
Cdd:TIGR00618 610 LACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTA 647
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
659-852 |
2.71e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 659 IREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNHHQgshgdgaQVNGIQPEEISRL--- 735
Cdd:COG3883 39 LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL-------YRSGGSVSYLDVLlgs 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 736 --------------------REEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATcpprdpEQVAELKQELT 795
Cdd:COG3883 112 esfsdfldrlsalskiadadADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE------AQQAEQEALLA 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 23956096 796 ALKSQLCSQSLEITRLQTENCELLQRAETLAKSVPVEGESEHVSAAKTTDVEGRLSA 852
Cdd:COG3883 186 QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
656-930 |
3.23e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 656 KNMIREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLG-----KDNHHqgshgdgaqvngiqpE 730
Cdd:COG1340 21 REEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKelkeeRDELN---------------E 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 731 EISRLREEIEELKSQQALLQGQLAEKDSL---IENLKSsqasgmsEQASATCPPRD----PEQVAELKQELTALKSQLcS 803
Cdd:COG1340 86 KLNELREELDELRKELAELNKAGGSIDKLrkeIERLEW-------RQQTEVLSPEEekelVEKIKELEKELEKAKKAL-E 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 804 QSLEITRLQTENCELLQRAETLAKsvpvegesehvsaakttdvegRLSALLQETKELKNEIKALSEERTAIQKQLDSSNS 883
Cdd:COG1340 158 KNEKLKELRAELKELRKEAEEIHK---------------------KIKELAEEAQELHEEMIELYKEADELRKEADELHK 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 23956096 884 TIAILQTEKDKLdlevtdsKKEQDDLLVLLADQDQKILSLKSKLKDL 930
Cdd:COG1340 217 EIVEAQEKADEL-------HEEIIELQKELRELRKELKKLRKKQRAL 256
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
660-930 |
3.59e-04 |
|
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: 44.43 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 660 REQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDnhhQGSHGDGAQVNGIQPEEISRLREEI 739
Cdd:pfam10174 49 KEEAARISVLKEQYRVTQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTS---PVDGEDKFSTPELTEENFRRLQSEH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 740 EELKSQQALLQGQLAEKDSLIENLKssQASGMSEQA---------SATCPPRDPEQVAELKQELTALKSQLcsQSLEITr 810
Cdd:pfam10174 126 ERQAKELFLLRKTLEEMELRIETQK--QTLGARDESikkllemlqSKGLPKKSGEEDWERTRRIAEAEMQL--GHLEVL- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 811 LQTENCELLQRAETLAKSVPVEGESEHVSAAKTT--DVEGRLSALLQETKELKNEIKAL-------SEERTAIQKQLDSS 881
Cdd:pfam10174 201 LDQKEKENIHLREELHRRNQLQPDPAKTKALQTVieMKDTKISSLERNIRDLEDEVQMLktngllhTEDREEEIKQMEVY 280
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 23956096 882 NSTIAILQTEKDKLDLEVtdSKKEQDdllvlladqdqkILSLKSKLKDL 930
Cdd:pfam10174 281 KSHSKFMKNKIDQLKQEL--SKKESE------------LLALQTKLETL 315
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
652-928 |
3.62e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 652 VTHYKNMIREQ----DLQLEELKQ-QVSTLKCQNEQLQTA--------VTQQASQIQQHKDQYNLLKVQLGKDNHHQGSH 718
Cdd:pfam01576 329 VTELKKALEEEtrshEAQLQEMRQkHTQALEELTEQLEQAkrnkanleKAKQALESENAELQAELRTLQQAKQDSEHKRK 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 719 GDGAQVNGIQPE--EISRLREEIEELKSQqalLQGQLAEKDSLIENLKSSQASGMSEQASATCPPRDpeqVAELKQELTA 796
Cdd:pfam01576 409 KLEGQLQELQARlsESERQRAELAEKLSK---LQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQD---TQELLQEETR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 797 LKSQLCSQsleITRLQTENCELLQRAEtlaksvpvegesEHVSAAKTtdVEGRLSALLQETKELKNE-------IKALSE 869
Cdd:pfam01576 483 QKLNLSTR---LRQLEDERNSLQEQLE------------EEEEAKRN--VERQLSTLQAQLSDMKKKleedagtLEALEE 545
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 23956096 870 ERTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLK 928
Cdd:pfam01576 546 GKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQK 604
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
856-930 |
3.81e-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: 3.81e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23956096 856 ETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 930
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
653-882 |
5.01e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 653 THYKNMIREQDLQLEELKQQVSTLKCQNEQLQTAVTQqaSQIQQHKDQYNLLKVQLgKDNHHQGSHGDGAqVNGIQPEEI 732
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEV-SRIEARLREIEQK-LNRLTLEKE 829
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 733 SrLREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATCPPRDPE--------QVAELKQELTALKSQLCSQ 804
Cdd:TIGR02169 830 Y-LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLEsrlgdlkkERDELEAQLRELERKIEEL 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 805 SLEITRLQTENCELLQRAETLA-------------KSVPVEGESEHVSAAKTTDVEGRLSAL----------LQETKELK 861
Cdd:TIGR02169 909 EAQIEKKRKRLSELKAKLEALEeelseiedpkgedEEIPEEELSLEDVQAELQRVEEEIRALepvnmlaiqeYEEVLKRL 988
|
250 260
....*....|....*....|....*
gi 23956096 862 NEIKA----LSEERTAIQKQLDSSN 882
Cdd:TIGR02169 989 DELKEkrakLEEERKAILERIEEYE 1013
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
731-914 |
5.25e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 731 EISRLREEIEELKSQQALLQGQLAEKDSLIENLKssqasgmseqasatcpprdpEQVAELKQELTALKSQLCSQSLEITR 810
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELN--------------------EEYNELQAELEALQAEIDKLQAEIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 811 LQTENCELLQRAETLAKSVPVEGESEH-----VSAAKTTDVEGRLSAL----------LQETKELKNEI----KALSEER 871
Cdd:COG3883 77 AEAEIEERREELGERARALYRSGGSVSyldvlLGSESFSDFLDRLSALskiadadadlLEELKADKAELeakkAELEAKL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 23956096 872 TAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLA 914
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
657-909 |
5.49e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 657 NMIREQDLQLEELKQQVSTLKcqneqlqtavtqqaSQIQQHKDQYNLLKVQLGKdnhhqgshgdgaqvngiQPEEISRLR 736
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELR--------------EEIEELKEKRDELNEELKE-----------------LAEKRDELN 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 737 EEIEELKSQqalLQGQLAEKDSLIENLKSSQASgmseqasatcppRDP--EQVAELKQELTALKSQ---LCSQSLEITRL 811
Cdd:COG1340 50 AQVKELREE---AQELREKRDELNEKVKELKEE------------RDElnEKLNELREELDELRKElaeLNKAGGSIDKL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 812 QTENCELLQRAETlaKSVPVEGESEHVSAAKttdvegRLSALLQETK---ELKNEIKALSEERTAIQKQLDSSNSTIAIL 888
Cdd:COG1340 115 RKEIERLEWRQQT--EVLSPEEEKELVEKIK------ELEKELEKAKkalEKNEKLKELRAELKELRKEAEEIHKKIKEL 186
|
250 260
....*....|....*....|.
gi 23956096 889 QTEKDKLDLEVTDSKKEQDDL 909
Cdd:COG1340 187 AEEAQELHEEMIELYKEADEL 207
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
730-930 |
7.21e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 730 EEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQA--SAtcpprDPEQVAELKQELTALKSQlCSQSLE 807
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGldDA-----DAEAVEARREELEDRDEE-LRDRLE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 808 ITRLQTEncELLQRAETLAKSVpvegesehvsaaktTDVEGRlsallqeTKELKNEIKALSEERTAIQKQLDSSNSTIAI 887
Cdd:PRK02224 332 ECRVAAQ--AHNEEAESLREDA--------------DDLEER-------AEELREEAAELESELEEAREAVEDRREEIEE 388
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 23956096 888 LQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 930
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEL 431
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
660-813 |
8.50e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 8.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 660 REQDLQLEELKQQVSTL----KCQNEQLQTAVTQQASQIQQHKDQYNLLKVQL---GKDNHHQGSHGDGAQVNgiqpEEI 732
Cdd:COG4717 359 LEEELQLEELEQEIAALlaeaGVEDEEELRAALEQAEEYQELKEELEELEEQLeelLGELEELLEALDEEELE----EEL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 733 SRLREEIEELKSQQALLQGQLAEKDSLIENLKSSqasgmseqasatcpprdpEQVAELKQELTALKSQLCSQSLEITRLQ 812
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELEQLEED------------------GELAELLQELEELKAELRELAEEWAALK 496
|
.
gi 23956096 813 T 813
Cdd:COG4717 497 L 497
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
645-904 |
8.55e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 8.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 645 LEQHDNIvthyKNMIREQDLQLEELKQQVSTLKCQNEQLQ---TAVTQQASQIQQHKDQYNLLKVQLGKDNHHQGshGDG 721
Cdd:PRK03918 185 IKRTENI----EELIKEKEKELEEVLREINEISSELPELReelEKLEKEVKELEELKEEIEELEKELESLEGSKR--KLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 722 AQVNGIQpEEISRLREEIEELKSQQALLQG--QLAEKDSLIENLKSSQASGMSE-QASATCPPRDPEQVAELKQELTALK 798
Cdd:PRK03918 259 EKIRELE-ERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREiEKRLSRLEEEINGIEERIKELEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 799 SQLCSQSLEITRLQTENCELLQRAETLAKSVPVEGESEHVSAAKTTdvegrlsallQETKELKNEIKALSEERTAIQKQL 878
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTG----------LTPEKLEKELEELEKAKEEIEEEI 407
|
250 260
....*....|....*....|....*.
gi 23956096 879 DSSNSTIAILQTEKDKLDLEVTDSKK 904
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKK 433
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
679-915 |
9.06e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 9.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 679 QNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNHHQGSHGDgaqvngiqpeEISRLREEIEELKSQQALLQGQLAEKDS 758
Cdd:PHA02562 179 LNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQN----------KYDELVEEAKTIKAEIEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 759 LIENLKSSqasgmseqasatcpprdpeqVAELKQELTALKSQL------------------CSQSLE-----ITRLQTEN 815
Cdd:PHA02562 249 DIEDPSAA--------------------LNKLNTAAAKIKSKIeqfqkvikmyekggvcptCTQQISegpdrITKIKDKL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 816 CELLQRAETLAKSVPVEGESEHVSAAKTTDV----------EGRLSALLQETKELKNEIKALSEERTaiqkqldSSNSTI 885
Cdd:PHA02562 309 KELQHSLEKLDTAIDELEEIMDEFNEQSKKLlelknkistnKQSLITLVDKAKKVKAAIEELQAEFV-------DNAEEL 381
|
250 260 270
....*....|....*....|....*....|...
gi 23956096 886 AILQTEKDKLDLEVTDSKKEQDDLLV---LLAD 915
Cdd:PHA02562 382 AKLQDELDKIVKTKSELVKEKYHRGIvtdLLKD 414
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
785-930 |
1.05e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 785 EQVAELKQELTALKSQLCSQSLEITRLQTENCELLQRAETLAKSVpvegesehvsaakttdvegRLSALLQETKELKNEI 864
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLA-------------------EYSWDEIDVASAEREI 670
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956096 865 KALSEERtaiqKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 930
Cdd:COG4913 671 AELEAEL----ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL 732
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
722-928 |
1.08e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 722 AQVNGIQPEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSE-QA---SATCPPRDPE-QVAELKQELTA 796
Cdd:PHA02562 166 SEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARkQNkydELVEEAKTIKaEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 797 LKSQLCSQSLEITRLQTENCELLQRAETLAKSV--------------PVEGESEHVSAAKT--TDVEGRLSALL---QET 857
Cdd:PHA02562 246 LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIkmyekggvcptctqQISEGPDRITKIKDklKELQHSLEKLDtaiDEL 325
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23956096 858 KELKNEIKALSEERTAIQKQLDSSNSTIAIL-------QTEKDKLDLEVTDSKKEqddlLVLLADQDQKILSLKSKLK 928
Cdd:PHA02562 326 EEIMDEFNEQSKKLLELKNKISTNKQSLITLvdkakkvKAAIEELQAEFVDNAEE----LAKLQDELDKIVKTKSELV 399
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
663-907 |
1.40e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 663 DLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKvqlgkdnhhqgshgdgaqvngiqpEEISRLREEIEEL 742
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQ------------------------AELEALQAEIDKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 743 KSQQALLQGQLAEK-DSLIENLKSSQASGMSEQAsatcpprdpeqvaelkqeLTALksqLCSQSLEitrlqtencELLQR 821
Cdd:COG3883 71 QAEIAEAEAEIEERrEELGERARALYRSGGSVSY------------------LDVL---LGSESFS---------DFLDR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 822 AETLAKSVPVEGES-EHVSAAKTtDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLEVT 900
Cdd:COG3883 121 LSALSKIADADADLlEELKADKA-ELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
....*..
gi 23956096 901 DSKKEQD 907
Cdd:COG3883 200 ELEAELA 206
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
731-925 |
2.08e-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: 42.12 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 731 EISRLREEIEELK-----SQQAL--LQGQLAEKDSLIENLKssqasgmsEQASATCPPRdPEQVAELKQELTALKSQLCS 803
Cdd:pfam10174 416 QLAGLKERVKSLQtdssnTDTALttLEEALSEKERIIERLK--------EQREREDRER-LEELESLKKENKDLKEKVSA 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 804 QSLEITRLQTENCELLQRAETLAKSvPVEGESehvsaaKTTDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNS 883
Cdd:pfam10174 487 LQPELTEKESSLIDLKEHASSLASS-GLKKDS------KLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDR 559
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 23956096 884 tIAILQTEKDKLDLEVTDSKKEQDDLLVLL-------ADQDQKILSLKS 925
Cdd:pfam10174 560 -IRLLEQEVARYKEESGKAQAEVERLLGILrevenekNDKDKKIAELES 607
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
745-910 |
2.18e-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: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 745 QQALLQgqLAEKDSLIENLKSSQASGMSEQASATcpprdpEQVAELKQELTALKSQLCSQSLEITRLQTENCELLQRAET 824
Cdd:COG1579 6 LRALLD--LQELDSELDRLEHRLKELPAELAELE------DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 825 LaksvpvEGESEHVSAAKT-TDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTE----KDKLDLEV 899
Cdd:COG1579 78 Y------EEQLGNVRNNKEyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEleekKAELDEEL 151
|
170
....*....|.
gi 23956096 900 TDSKKEQDDLL 910
Cdd:COG1579 152 AELEAELEELE 162
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
665-832 |
4.40e-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: 39.91 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 665 QLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQynllkvqlgkdnhhQGSHGDgaqvngiqPEEISRLREEIEELKS 744
Cdd:COG1579 46 RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ--------------LGNVRN--------NKEYEALQKEIESLKR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 745 QQALLQGQLAEKDSLIENLKssqasgmSEQASATcpprdpEQVAELKQELTALKSQLCSqslEITRLQTENCELLQRAET 824
Cdd:COG1579 104 RISDLEDEILELMERIEELE-------EELAELE------AELAELEAELEEKKAELDE---ELAELEAELEELEAEREE 167
|
....*...
gi 23956096 825 LAKSVPVE 832
Cdd:COG1579 168 LAAKIPPE 175
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
663-860 |
6.32e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 40.05 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 663 DLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNHHQGSHGD-GAQVNGIQpEEISRLREEIEE 741
Cdd:pfam15742 185 DQNVNELQQQVRSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKSNQElSEKLSSLQ-QEKEALQEELQQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 742 LKSQQALLQGQLAEKDSLIENlKSSQASGMSEQASATcppRDpEQVAELKQELTALKSQLCSQSLEITRLQTENCELLQR 821
Cdd:pfam15742 264 VLKQLDVHVRKYNEKHHHHKA-KLRRAKDRLVHEVEQ---RD-ERIKQLENEIGILQQQSEKEKAFQKQVTAQNEILLLE 338
|
170 180 190
....*....|....*....|....*....|....*....
gi 23956096 822 AETLAKSVPVEGESEHVSAAKTTDVEGRLSALLQETKEL 860
Cdd:pfam15742 339 KRKLLEQLTEQEELIKNNKRTISSVQNRVNFLDEENKQL 377
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
785-930 |
6.92e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 785 EQVAELKQELTALKSQLCSQSLEITRLQTEncelLQRAETLAKSVpvegesehvsAAKTTDVEGRLSALLQETKELKNEI 864
Cdd:COG4372 38 FELDKLQEELEQLREELEQAREELEQLEEE----LEQARSELEQL----------EEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956096 865 KALSEERTAIQKQLDSsnstiaiLQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 930
Cdd:COG4372 104 ESLQEEAEELQEELEE-------LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
669-821 |
7.35e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 38.37 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 669 LKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQynllkvqlgkdnhhqGSHGDGAQVNGIQPEeISRLREEIEELKSQQAL 748
Cdd:pfam08614 12 LLDRTALLEAENAKLQSEPESVLPSTSSSKLS---------------KASPQSASIQSLEQL-LAQLREELAELYRSRGE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 749 LQGQLAEKDSLIENLKSS---------QASGMSEQASATCPPRDPE------QVAELKQELTALKSQLCSQSLEITRLQT 813
Cdd:pfam08614 76 LAQRLVDLNEELQELEKKlrederrlaALEAERAQLEEKLKDREEElrekrkLNQDLQDELVALQLQLNMAEEKLRKLEK 155
|
....*...
gi 23956096 814 ENCELLQR 821
Cdd:pfam08614 156 ENRELVER 163
|
|
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
738-894 |
7.51e-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: 38.83 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 738 EIEELKSQQALLQGQLAEKDSLIENLKSSQASgmseqasatcppRDPEqVAELKQELTALKSQLCSQSLEITRLQTENCE 817
Cdd:pfam06818 32 EIVALRAQLRELRAKLEEKEEQIQELEDSLRS------------KTLE-LEVCENELQRKKNEAELLREKVGKLEEEVSG 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23956096 818 LlQRAETLAKSVPVEGESEHVSAAKTTDVEGRLSALLQETKELKNEikaLSEERTAIQKQLDSSNSTIAILQTEKDK 894
Cdd:pfam06818 99 L-REALSDVSPSGYESVYESDEAKEQRQEEADLGSLRREVERLRAE---LREERQRRERQASSFEQERRTWQEEKEK 171
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
669-861 |
9.42e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.18 E-value: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 669 LKQQVSTlkcQNEQLQtavtQQASQIQQHKDQYNLLKvqlgkdnhhQGSHGDGAQVNGIQPE------EISRLREEIEEL 742
Cdd:PRK09039 44 LSREISG---KDSALD----RLNSQIAELADLLSLER---------QGNQDLQDSVANLRASlsaaeaERSRLQALLAEL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956096 743 KSQQALLQGQLAEKDSLIENLKssqasGMSEQASAtcpprdpeQVAELKQELTALKSQLcsQSLEitrlqtencELLQRA 822
Cdd:PRK09039 108 AGAGAAAEGRAGELAQELDSEK-----QVSARALA--------QVELLNQQIAALRRQL--AALE---------AALDAS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 23956096 823 ETLAKSvpvegesehvSAAKTTDVEGRL-SALLQETKELK 861
Cdd:PRK09039 164 EKRDRE----------SQAKIADLGRRLnVALAQRVQELN 193
|
|
| |
