|
Name |
Accession |
Description |
Interval |
E-value |
| Uso1_p115_head |
pfam04869 |
Uso1 / p115 like vesicle tethering protein, head region; Also known as General vesicular ... |
346-627 |
1.64e-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: 1.64e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 346 NQDYFASV--------------NAPSNPPRPAIVVLL--MSMVNERQPFVLRCAVLYCFQCFLYKNEKGQGEIVATLLPS 409
Cdd:pfam04869 2 LQEEFAKIdvpypdpslpsaanAADQPVKVPVIDLLLnwALSANSVHAFDLRVAACYCLKAYFYNNEEIRLHFLQRAIEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 410 TIDATGNSVSAGQLLCGGL-----FSTDSLSNWCAAVALAHALQGNATQKEQLLRVQLAT-SIGNPPVSLLQQCTNIL-- 481
Cdd:pfam04869 82 YKSGNDSSSTTANLLEVLLdydpdLKLDPYKLWFASVILMHLLEDNPEAKELARSVTEGDaESGEEVVTLIQTISELLit 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 482 -SQGSKIQTRVGLLMLLCTWLSNCPIAVTHFLHNSANVPFLTGQIAENlGEEEQLVQGLCALLLGISIYFNDNSlENYTK 560
Cdd:pfam04869 162 sLQREDPRIPIGYLMLLIVWLFEDPDAVNDFLSEGSNLQSLLQFLSQS-SDEDVLVQGLCAMLLGIAYEFSTKD-SPIPR 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2451976109 561 EKLKQLIEKRIGKENFIEKLGFISKHELYSRASQKPQPNFPSPEYMI----FDHEFTKLVKELEGVITKAI 627
Cdd:pfam04869 240 ADLHSLLTKRLGRDNYIDKIKQLREHPLFRDFEVLPQLNPSLDDTGLpevyFDSYFVELFKDNFSRIRRAL 310
|
|
| Arm_vescicular |
pfam18770 |
Armadillo tether-repeat of vescicular transport factor; Armadillo-like tether-repeat of ... |
269-328 |
7.77e-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: 120.87 E-value: 7.77e-33
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 269 SGWSAQKVTNLHLMLQLVRVLVSPTNPPGATSSCQKAMFQCGLLQQLCTILMATGIPADI 328
Cdd:pfam18770 1 SGWSAQKVSNVHCMLQVVRTLVSPNNPSQVTSSCQKAMRACGLLEALCNILMASGVPADI 60
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
658-929 |
1.05e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.83 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 658 IREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLgkDNHHQGSHGDGAQVNGIQpEEISRLREE 737
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL--EEAQAEEYELLAELARLE-QDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 738 IEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATcpprdpEQVAELKQELTALKSQLCSQSLEITRLQTENCEL 817
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAE------EELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 818 LQRAETLAKSVPVEGESEHVSAAKTTDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLE 897
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250 260 270
....*....|....*....|....*....|..
gi 2451976109 898 VTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 929
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
643-929 |
7.35e-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: 66.20 E-value: 7.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 643 TLEQHDNIVTHYKNMIREQDLQLEELKQQVSTLKCQNEQLQTAVTQqaSQIQQHKDQYNLLKVQLGKDNHhqgshgdgaQ 722
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELK--SELKNQEKKLEEIQNQISQNNK---------I 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 723 VNGIQpEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATCPPRDPEQVAELKQELTALKSQlcs 802
Cdd:TIGR04523 337 ISQLN-EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE--- 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 803 qslEITRLQTENCELLQRAETLAKSVPVEG-------ESEHVSAAKTTDVEGRLSALLQETKELKNEIKALSEERTAIQK 875
Cdd:TIGR04523 413 ---QIKKLQQEKELLEKEIERLKETIIKNNseikdltNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK 489
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2451976109 876 QLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 929
Cdd:TIGR04523 490 ELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
658-915 |
1.03e-10 |
|
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: 65.85 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 658 IREQDLQLEELKQQVSTLKCQNEQLQTA----------VTQQASQIQQHKDQYNLLKVQLGKDNHHQGSHGDGAQvngiq 727
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKElyalaneisrLEQQKQILRERLANLERQLEELEAQLEELESKLDELA----- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 728 pEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQAS---GMSEQASAtcpprdpeqVAELKQELTALKSQLCSQS 804
Cdd:TIGR02168 337 -EELAELEEKLEELKEELESLEAELEELEAELEELESRLEEleeQLETLRSK---------VAQLELQIASLNNEIERLE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 805 LEITRLQTENCELLQRAETLAKSvPVEGESEHVSAAKTT------DVEGRLSALLQETKELKNEIKALSEERTAIQKQLD 878
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKK-LEEAELKELQAELEEleeeleELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2451976109 879 SSNSTIAILQTEKDKLD------LEVTDSKKEQDDLLVLLADQ 915
Cdd:TIGR02168 486 QLQARLDSLERLQENLEgfsegvKALLKNQSGLSGILGVLSEL 528
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
656-929 |
4.14e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 4.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 656 NMIREQDLqLEELKQQVSTLKCQNEQLQTAVTQQAS----QIQQHKDQYNLLKVQLGKDNHHQGSHGDG-----AQVNGI 726
Cdd:COG1196 187 NLERLEDI-LGELERQLEPLERQAEKAERYRELKEElkelEAELLLLKLRELEAELEELEAELEELEAEleeleAELAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 727 QpEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATcpprdpEQVAELKQELTALKSQLCSQSLE 806
Cdd:COG1196 266 E-AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE------ERLEELEEELAELEEELEELEEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 807 ITRLQTENCELLQRAETLAKSVPVEGESEHVSAAKTTDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAI 886
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2451976109 887 LQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 929
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
661-919 |
4.39e-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: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 661 QDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNhhqgshgdgAQVNGIQpEEISRLREEIEE 740
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA---------RRIRALE-QELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 741 LKSQQALLQGQLAE-KDSLIENLKSSQASGMSEQASATCPPRDPEQVAELKQELTALksqlcsqsleitrlqteNCELLQ 819
Cdd:COG4942 88 LEKEIAELRAELEAqKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL-----------------APARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 820 RAETLAksvpvegesehvsaAKTTDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLEVT 899
Cdd:COG4942 151 QAEELR--------------ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
|
250 260
....*....|....*....|
gi 2451976109 900 DSKKEQDDLLVLLADQDQKI 919
Cdd:COG4942 217 ELQQEAEELEALIARLEAEA 236
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
727-929 |
4.73e-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: 63.93 E-value: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 727 QPEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKS--SQASGMSEQASatcppRDPEQVAE----LKQELTALKSQL 800
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQelSDASRKIGEIE-----KEIEQLEQeeekLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 801 CSQSLEITRLQTE----NCELLQRAETLAK---------------SVP-VEGESEHVSA------AKTTDVEGRLSALLQ 854
Cdd:TIGR02169 747 SSLEQEIENVKSElkelEARIEELEEDLHKleealndlearlshsRIPeIQAELSKLEEevsrieARLREIEQKLNRLTL 826
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2451976109 855 ETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 929
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
658-929 |
1.02e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 658 IREQDLQLEELKQQVSTLKCQNEQLQtavtqqaSQIQQHKDQYNLLKVQLGKDNHHQGSHGDGAQVNgIQPE------EI 731
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLT-------EEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR-VKEKigeleaEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 732 SRLREEIEELKSQQALLQGQLAEKDSLIENLKssqasgmseqasatcpprdpEQVAELKQELTALKSQLCSQSLEITRLQ 811
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLL--------------------AEIEELEREIEEERKRRDKLTEEYAELK 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 812 TENCELLQRAETLAKSVpvegeseHVSAAKTTDVEGRLSALLQETKELKNEI-------KALSEERTAIQKQLDSSNSTI 884
Cdd:TIGR02169 364 EELEDLRAELEEVDKEF-------AETRDELKDYREKLEKLKREINELKRELdrlqeelQRLSEELADLNAAIAGIEAKI 436
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2451976109 885 AILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 929
Cdd:TIGR02169 437 NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
840-933 |
1.01e-08 |
|
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: 54.33 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 840 AKTTDVEGRLSALLQETKELKNEIKALS------EERTAIQKQLDSSNST----IAILQTEKDKLDLEVTDSKKEQDDLL 909
Cdd:pfam04871 1 AKKSELESEASSLKNENTELKAELQELSkqynslEQKESQAKELEAEVKKleeaLKKLKAELSEEKQKEKEKQSELDDLL 80
|
90 100
....*....|....*....|....
gi 2451976109 910 VLLADQDQKILSLKSKLKDLGHPV 933
Cdd:pfam04871 81 LLLGDLEEKVEKYKARLKELGEEV 104
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
654-929 |
1.25e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 58.98 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 654 YKNMIREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQ-----HKDQYNLlkvQLGKDNHHQ---GSHGDGAQVNG 725
Cdd:pfam15921 340 YEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKlladlHKREKEL---SLEKEQNKRlwdRDTGNSITIDH 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 726 IQPE------EISRLREEIEELKSQqalLQGQLAEKDSLIENLKSS--QASGMSEQASATcpprdPEQVAELKQELTALK 797
Cdd:pfam15921 417 LRRElddrnmEVQRLEALLKAMKSE---CQGQMERQMAAIQGKNESleKVSSLTAQLEST-----KEMLRKVVEELTAKK 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 798 SQLCSQSLEITRLQTEncelLQRAETLAKSvpvegesehvSAAKTTDVEGRLSALLQETKELKNE---IKALSEERTAIQ 874
Cdd:pfam15921 489 MTLESSERTVSDLTAS----LQEKERAIEA----------TNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALK 554
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2451976109 875 KQLDSSNSTIAIL---------------------QTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 929
Cdd:pfam15921 555 LQMAEKDKVIEILrqqienmtqlvgqhgrtagamQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL 630
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
654-929 |
1.35e-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: 58.88 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 654 YKNMIREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNHH-QGSHGDGAQVNGIQPE--- 729
Cdd:TIGR04523 209 KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQlSEKQKELEQNNKKIKElek 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 730 EISRLREEIEELKSQQA-----LLQGQLAEKDSLIENLKS------SQASGMSEQASATCPPRD---------PEQVAEL 789
Cdd:TIGR04523 289 QLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNqisqnnKIISQLNEQISQLKKELTnsesensekQRELEEK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 790 KQELTALKSQLCSQSLEITRLQTENCEL---LQRAETLAKSvpVEGESEHVSAAKTTdVEGRLSALLQETKELKNEIKAL 866
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLeskIQNQEKLNQQ--KDEQIKKLQQEKEL-LEKEIERLKETIIKNNSEIKDL 445
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2451976109 867 SEERTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 929
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEL 508
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
721-878 |
1.74e-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: 56.09 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 721 AQVNGIQpEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEqasatcpprdpeqvaelkQELTALKSQL 800
Cdd:COG1579 38 DELAALE-ARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN------------------KEYEALQKEI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2451976109 801 CSQSLEITRLQTENCELLQRAETLAKSVpveGESEHVSAAKTTDVEGRLSALLQETKELKNEIKALSEERTAIQKQLD 878
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEEL---AELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
643-879 |
6.70e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 643 TLEQHDNIVTHYKNmireqdlqLEELKQQVSTLKCQNEQLQtavtqqasQIQQHKDQYNLLKVQLGkdnhHQGSHGDGAQ 722
Cdd:COG4913 223 TFEAADALVEHFDD--------LERAHEALEDAREQIELLE--------PIRELAERYAAARERLA----ELEYLRAALR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 723 VNGIQpEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKsSQASGMSEQASAtcppRDPEQVAELKQELTALKSQLCS 802
Cdd:COG4913 283 LWFAQ-RRLELLEAELEELRAELARLEAELERLEARLDALR-EELDELEAQIRG----NGGDRLEQLEREIERLERELEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 803 QSLEITRLQtencellQRAETLAKSVPVEGES--EHVSAAKT--TDVEGRLSALLQETKELKNEIKALSEERTAIQKQLD 878
Cdd:COG4913 357 RERRRARLE-------ALLAALGLPLPASAEEfaALRAEAAAllEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
.
gi 2451976109 879 S 879
Cdd:COG4913 430 S 430
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
730-929 |
1.04e-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: 56.22 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 730 EISRLREEIEELKSQQALLQGQLAEKDslienlkssqasgmseqasatcpprdpEQVAELKQELTALKSQLCSQSLEITR 809
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELR---------------------------KELEELEEELEQLRKELEELSRQISA 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 810 LQTENCELLQRAETLAKSVPVEGESEHVSAAKTTDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQT 889
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2451976109 890 EKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 929
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
664-930 |
1.42e-07 |
|
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: 55.82 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 664 QLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNllkVQLGKDNHHQGSHGDGA-QVNGIQPEE--ISRLREEIEE 740
Cdd:TIGR00606 574 QLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHIN---NELESKEEQLSSYEDKLfDVCGSQDEEsdLERLKEEIEK 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 741 LKSQQALLQGQLAEKDSLIENLkssqasgmSEQASATCP--PRDPEQVAELKQELTALKSQLCSQSLEITRLQTENCELL 818
Cdd:TIGR00606 651 SSKQRAMLAGATAVYSQFITQL--------TDENQSCCPvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKE 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 819 QRAETLAKSVPVEGESEHVSAAKTTDVEGRLSALLQETKELKNEIK--------ALSEERTA------------IQKQLD 878
Cdd:TIGR00606 723 KRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEeqetllgtIMPEEESAkvcltdvtimerFQMELK 802
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2451976109 879 SSNSTIAILQTEKDKLDL-----EVTDSKKEQDDLL-----------VLLADQDQKILSLKSKLKDLG 930
Cdd:TIGR00606 803 DVERKIAQQAAKLQGSDLdrtvqQVNQEKQEKQHELdtvvskielnrKLIQDQQEQIQHLKSKTNELK 870
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
655-929 |
1.73e-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: 55.41 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 655 KNMIREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNhhqgshgdgaQVNGIQPEEISRL 734
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ----------QEKELLEKEIERL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 735 REEIEELKSQQALLQGQLAEKDSLIENLKSSQASgMSEQASATcpprdPEQVAELKQELTALKSQLCSQSLEITRLQTEN 814
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES-LETQLKVL-----SRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 815 CELlqraetlaksvpvegesehvsaakttdvEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTI---------A 885
Cdd:TIGR04523 506 KEL----------------------------EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkddfelkkE 557
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2451976109 886 ILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 929
Cdd:TIGR04523 558 NLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDL 601
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
661-897 |
5.77e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.48 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 661 QDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVqlgkdnhhqgshgdgaqvngiqPEEISRLREEIEE 740
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDL----------------------SEEAKLLLQQLSE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 741 LKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATcppRDP------EQVAELKQELTALKSQLCSQSLEITRLQTEN 814
Cdd:COG3206 224 LESQLAEARAELAEAEARLAALRAQLGSGPDALPELL---QSPviqqlrAQLAELEAELAELSARYTPNHPDVIALRAQI 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 815 CELLQRAETLAKSVPVEGESEHVSAakttdvEGRLSALLQETKELKNEIKALSE---ERTAIQKQLDSSNSTIAILQTEK 891
Cdd:COG3206 301 AALRAQLQQEAQRILASLEAELEAL------QAREASLQAQLAQLEARLAELPEleaELRRLEREVEVARELYESLLQRL 374
|
....*.
gi 2451976109 892 DKLDLE 897
Cdd:COG3206 375 EEARLA 380
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
644-930 |
8.97e-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: 53.14 E-value: 8.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 644 LEQHDNIVTHYKNMIREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKvqlgkdnhhqgshgdgaqv 723
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR------------------- 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 724 ngiqpEEISRLREEIEELKSQQALLQGQLAEKDSLIENLkSSQASGMSEQ-ASATcpprdpEQVAELKQELTALKSQLCS 802
Cdd:TIGR02168 810 -----AELTLLNEEAANLRERLESLERRIAATERRLEDL-EEQIEELSEDiESLA------AEIEELEELIEELESELEA 877
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 803 QSLEITRLQTENCELLQRAETLAKSVpvegesehvsaaktTDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNS 882
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEEL--------------RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2451976109 883 TIAilqtEKDKLDLEVTDSKKEQDDLlvLLADQDQKILSLKSKLKDLG 930
Cdd:TIGR02168 944 RLS----EEYSLTLEEAEALENKIED--DEEEARRRLKRLENKIKELG 985
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
654-908 |
9.05e-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: 53.14 E-value: 9.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 654 YKNMIREQDLQLeeLKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNHHQGShgDGAQVNGIQPE---- 729
Cdd:TIGR02168 218 LKAELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE--LEEEIEELQKElyal 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 730 --EISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQAsgmseqasatcppRDPEQVAELKQELTALKSQLCSQSLEI 807
Cdd:TIGR02168 294 anEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD-------------ELAEELAELEEKLEELKEELESLEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 808 TRLQTENCELLQRAETLAKSVpvegesehvsaaktTDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAIL 887
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQL--------------ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL 426
|
250 260
....*....|....*....|....*.
gi 2451976109 888 QT-----EKDKLDLEVTDSKKEQDDL 908
Cdd:TIGR02168 427 LKkleeaELKELQAELEELEEELEEL 452
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
657-922 |
2.30e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 657 MIREQDLQLEELKQQVSTLKCQNEQLQTavtqQASQIQQHKDQYNLLKVQLGKDnhhqgshgdgaqvngIQP--EEISRL 734
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEE----DLSSLEQEIENVKSELKELEAR---------------IEEleEDLHKL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 735 REEIEELKsqQALLQGQLAEKDSLIENLKssqasgmseqasatcpprdpEQVAELKQELTALKSQLCSQSLEITRLQTEN 814
Cdd:TIGR02169 778 EEALNDLE--ARLSHSRIPEIQAELSKLE--------------------EEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 815 CELL-QRAETLAKSVPVEGESEhvsaakttDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDK 893
Cdd:TIGR02169 836 QELQeQRIDLKEQIKSIEKEIE--------NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
250 260
....*....|....*....|....*....
gi 2451976109 894 LDLEVTDSKKEQDDLLVLLADQDQKILSL 922
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
658-908 |
2.56e-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: 51.36 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 658 IREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNHHQGshgdgaqvngiqpEEISRLREE 737
Cdd:pfam10174 410 LRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERL-------------EELESLKKE 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 738 IEELKSQQALLQGQLAEKDSLIENLK---SSQASGMSEQASATcppRDPE-QVAELKQELTALKSQL-CSQSLEITrlQT 812
Cdd:pfam10174 477 NKDLKEKVSALQPELTEKESSLIDLKehaSSLASSGLKKDSKL---KSLEiAVEQKKEECSKLENQLkKAHNAEEA--VR 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 813 ENCELLQRAETLAKSVPVEGESehvSAAKTTDVEgRLSALLQETKELKNEI-KALSEERTAIQKQLDSSNSTIAILQT-- 889
Cdd:pfam10174 552 TNPEINDRIRLLEQEVARYKEE---SGKAQAEVE-RLLGILREVENEKNDKdKKIAELESLTLRQMKEQNKKVANIKHgq 627
|
250 260
....*....|....*....|.
gi 2451976109 890 --EKDKLDLEVTDSKKEQDDL 908
Cdd:pfam10174 628 qeMKKKGAQLLEEARRREDNL 648
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
664-910 |
4.77e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 664 QLEELKQQVStlkcqneQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNHHQGshgdgaQVNGIQPE----EISRLREEIE 739
Cdd:PRK04863 838 ELRQLNRRRV-------ELERALADHESQEQQQRSQLEQAKEGLSALNRLLP------RLNLLADEtladRVEEIREQLD 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 740 ELKSQQALLQ---GQLAEKDSLIENLKSsqasgmseqasatcpprDPEQVAELKQELTALKSQLCSQSLEITRLQtencE 816
Cdd:PRK04863 905 EAEEAKRFVQqhgNALAQLEPIVSVLQS-----------------DPEQFEQLKQDYQQAQQTQRDAKQQAFALT----E 963
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 817 LLQRAETLAKSVPVEgesehvSAAKTTDVEGRLSALLQETKELKNEIKalsEERTAIQKQLDSSNSTIAILQTEKDKLDL 896
Cdd:PRK04863 964 VVQRRAHFSYEDAAE------MLAKNSDLNEKLRQRLEQAEQERTRAR---EQLRQAQAQLAQYNQVLASLKSSYDAKRQ 1034
|
250
....*....|....
gi 2451976109 897 EVTDSKKEQDDLLV 910
Cdd:PRK04863 1035 MLQELKQELQDLGV 1048
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
644-841 |
1.02e-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: 48.99 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 644 LEQHDNIVTHYKNMIREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQH------KDQYNLLKVQLGKDNHHQGSH 717
Cdd:COG4942 57 LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlralyrLGRQPPLALLLSPEDFLDAVR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 718 GDG--AQVNGIQPEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATcpprdpEQVAELKQELTA 795
Cdd:COG4942 137 RLQylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQ------KLLARLEKELAE 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2451976109 796 LKSQLCSQSLEITRLQtencELLQRAETLAKSVPVEGESEHVSAAK 841
Cdd:COG4942 211 LAAELAELQQEAEELE----ALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
655-905 |
1.30e-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: 49.35 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 655 KNMIRE-------QDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLlKVQlgkdnhhqgshgdgaqvngiq 727
Cdd:pfam15921 474 KEMLRKvveeltaKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDL-KLQ--------------------- 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 728 peEISRLREEIEELKSQQA---LLQGQLAEKDSLIENLKSsQASGMSE---QASATCPPRDPEQvAELKQELTALKSQLc 801
Cdd:pfam15921 532 --ELQHLKNEGDHLRNVQTeceALKLQMAEKDKVIEILRQ-QIENMTQlvgQHGRTAGAMQVEK-AQLEKEINDRRLEL- 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 802 sQSLEITRLQTENC--ELLQRAE--TLAKSVPVEGESEHVSAAKttDVEGRLSALLQETKELKNEIKALSEERTAIQKQL 877
Cdd:pfam15921 607 -QEFKILKDKKDAKirELEARVSdlELEKVKLVNAGSERLRAVK--DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNF 683
|
250 260
....*....|....*....|....*...
gi 2451976109 878 DSSNSTIAiLQTEKDKLDLEVTDSKKEQ 905
Cdd:pfam15921 684 RNKSEEME-TTTNKLKMQLKSAQSELEQ 710
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
727-891 |
1.42e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 727 QPEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATCPPR---DPEQVAELKQELTALKSQLcsq 803
Cdd:COG4717 86 KEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElaeLPERLEELEERLEELRELE--- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 804 sLEITRLQTENCELLQRAETLAKSVPVEGESEHVSAAKttdvegRLSALLQETKELKNEIKALSEERTAIQKQLDSSNST 883
Cdd:COG4717 163 -EELEELEAELAELQEELEELLEQLSLATEEELQDLAE------ELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
....*...
gi 2451976109 884 IAILQTEK 891
Cdd:COG4717 236 LEAAALEE 243
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
644-930 |
1.45e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 644 LEQHDNIVTHYKNMIREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKvqlgkdnhhqgshgdgAQV 723
Cdd:PRK02224 337 AQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELR----------------ERF 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 724 NGIqPEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATCP---------PR------DPEQVAE 788
Cdd:PRK02224 401 GDA-PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPecgqpvegsPHvetieeDRERVEE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 789 LKQELTALKSQLCSQSLEITRLqTENCELLQRAETLAKSvpVEGESEHVSAAKTTDVEGRLSA--LLQETKELKNEIKAL 866
Cdd:PRK02224 480 LEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEER--REDLEELIAERRETIEEKRERAeeLRERAAELEAEAEEK 556
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2451976109 867 SEERTAIQKQLDSSNSTIAILQTEKDKLDLEVtDSKKEQDDLLVLLADQDQKILSLKSKLKDLG 930
Cdd:PRK02224 557 REAAAEAEEEAEEAREEVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKREALA 619
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
729-828 |
1.47e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.70 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 729 EEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATcpPRDPEqVAELKQELTALKSQLCSQSLEIT 808
Cdd:COG2433 413 EEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREI--RKDRE-ISRLDREIERLERELEEERERIE 489
|
90 100
....*....|....*....|
gi 2451976109 809 RLQTEncelLQRAETLAKSV 828
Cdd:COG2433 490 ELKRK----LERLKELWKLE 505
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
662-905 |
1.53e-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: 48.96 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 662 DLQLEELKQqvstLKCQNEQLQTAVTQ-QASQIQQ-HKDQY-NLLKVQLGKDNHHQGSHGDGA---QVNGIQPE-EISRL 734
Cdd:pfam15921 527 DLKLQELQH----LKNEGDHLRNVQTEcEALKLQMaEKDKViEILRQQIENMTQLVGQHGRTAgamQVEKAQLEkEINDR 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 735 REEIEELKSQQALLQGQLAEKDSLIENL---KSSQASGMSEQASAtcpprdpeqVAELKQELTALKSQLCSQSLEITRLq 811
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRELEARVSDLeleKVKLVNAGSERLRA---------VKDIKQERDQLLNEVKTSRNELNSL- 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 812 TENCELLQRAetlaksvpVEGESEHVSAAkTTDVEGRLSALLQETKELKNEIKALS-------EERTAIQKQLDSSNSTI 884
Cdd:pfam15921 673 SEDYEVLKRN--------FRNKSEEMETT-TNKLKMQLKSAQSELEQTRNTLKSMEgsdghamKVAMGMQKQITAKRGQI 743
|
250 260
....*....|....*....|.
gi 2451976109 885 AILQTEKDKLDLEVTDSKKEQ 905
Cdd:pfam15921 744 DALQSKIQFLEEAMTNANKEK 764
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
664-877 |
1.17e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 664 QLEELKQQVSTLKCQNEQLQtavtQQASQIQQHKDQYNLLKVQLGKDNHHQGSHgdgaqvngiqpEEISRLREEIEEL-K 742
Cdd:COG4913 618 ELAELEEELAEAEERLEALE----AELDALQERREALQRLAEYSWDEIDVASAE-----------REIAELEAELERLdA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 743 SQQAL--LQGQLAEKDSLIENLKssqasgmseqasatcpprdpEQVAELKQELTALKSQLCSQSLEITRLQtencELLQR 820
Cdd:COG4913 683 SSDDLaaLEEQLEELEAELEELE--------------------EELDELKGEIGRLEKELEQAEEELDELQ----DRLEA 738
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2451976109 821 AETLAKSVPVEGESEHVSAAKTTDVEGRLSALLQEtkelknEIKALSEERTAIQKQL 877
Cdd:COG4913 739 AEDLARLELRALLEERFAAALGDAVERELRENLEE------RIDALRARLNRAEEEL 789
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
665-908 |
1.30e-04 |
|
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: 46.10 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 665 LEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLK-----VQLGKDNHHQgshgdgaqvngiqpEEISRLREEIE 739
Cdd:COG3096 838 LAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNkllpqANLLADETLA--------------DRLEELREELD 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 740 ELKSQQALLQGQ---LAEKDSLIENLKSsqasgmseqasatcpprDPEQVAELKQELTALKSQLcsqsleiTRLQtence 816
Cdd:COG3096 904 AAQEAQAFIQQHgkaLAQLEPLVAVLQS-----------------DPEQFEQLQADYLQAKEQQ-------RRLK----- 954
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 817 llQRAETLAKsvpVEGESEHVSAAKTTDVEGRLSALLQETKE-LKNEIKALSEERTA---IQKQLDSSNSTIAILQTEKD 892
Cdd:COG3096 955 --QQIFALSE---VVQRRPHFSYEDAVGLLGENSDLNEKLRArLEQAEEARREAREQlrqAQAQYSQYNQVLASLKSSRD 1029
|
250
....*....|....*.
gi 2451976109 893 KLDLEVTDSKKEQDDL 908
Cdd:COG3096 1030 AKQQTLQELEQELEEL 1045
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
655-881 |
1.91e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 655 KNMIREQDLQLEELKQQVSTLK---CQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNH--HQGSHGDGAQVNGIQP- 728
Cdd:PRK04863 910 KRFVQQHGNALAQLEPIVSVLQsdpEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHfsYEDAAEMLAKNSDLNEk 989
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 729 --EEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQasgmseQASAtcpprdpEQVAELKQELTALKSQLCSQSLE 806
Cdd:PRK04863 990 lrQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSY------DAKR-------QMLQELKQELQDLGVPADSGAEE 1056
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2451976109 807 ITRLQTEncELLQRAetlaksvpvegeseHVSAAKTTDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSN 881
Cdd:PRK04863 1057 RARARRD--ELHARL--------------SANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAK 1115
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
664-858 |
2.09e-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: 45.43 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 664 QLEELKQQV-------STLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNHHQGSHgdGAQVNGIQpEEISRLRE 736
Cdd:TIGR02168 345 KLEELKEELesleaelEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL--EARLERLE-DRRERLQQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 737 EIEEL-----KSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATcpprdpEQVAELKQELTALKSQLCSQSLEITRLQ 811
Cdd:TIGR02168 422 EIEELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELR------EELEEAEQALDAAERELAQLQARLDSLE 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2451976109 812 T--ENCE--------LLQRAETLAKSVPVEGESEHV----SAAKTTDVEGRLSALLQETKE 858
Cdd:TIGR02168 496 RlqENLEgfsegvkaLLKNQSGLSGILGVLSELISVdegyEAAIEAALGGRLQAVVVENLN 556
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
658-913 |
2.50e-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: 44.96 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 658 IREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQ-----------HKDQYNLLKVQLGKDNHHQGSHGDGAQVNGI 726
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAfrdlqgqlahaKKQQELQQRYAELCAAAITCTAQCEKLEKIH 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 727 QPEEISRLREEIEELKSQQALLQgQLAEKDSLIENLKssqasgmSEQASATCP----PRDPEQVAELKQELTALKSQLCS 802
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHL-QETRKKAVVLARL-------LELQEEPCPlcgsCIHPNPARQDIDNPGPLTRRMQR 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 803 QSLEITRLQTEN-------CELLQRAETLAKSVPVEGESEHVSAAKTTDVEGRLSALLQETKELKNEIKALSEERtaiQK 875
Cdd:TIGR00618 533 GEQTYAQLETSEedvyhqlTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE---DM 609
|
250 260 270
....*....|....*....|....*....|....*...
gi 2451976109 876 QLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLA 913
Cdd:TIGR00618 610 LACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTA 647
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
658-912 |
2.91e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 658 IREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKvqlgkdnhhqgshgdgaqvngiqpEEISRLREE 737
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE------------------------EELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 738 IEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATcpprdpEQVAELKQELTALKSQLCSQSLEITRLQTENCEL 817
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLE------QQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 818 LQRAETLAKSVPVEGESEHVSAAKTTDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLE 897
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250
....*....|....*
gi 2451976109 898 VTDSKKEQDDLLVLL 912
Cdd:COG4372 243 ELEEDKEELLEEVIL 257
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
658-851 |
3.17e-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: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 658 IREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNHHQgshgdgaQVNGIQPEEISRL--- 734
Cdd:COG3883 39 LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL-------YRSGGSVSYLDVLlgs 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 735 --------------------REEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATcpprdpEQVAELKQELT 794
Cdd:COG3883 112 esfsdfldrlsalskiadadADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE------AQQAEQEALLA 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2451976109 795 ALKSQLCSQSLEITRLQTENCELLQRAETLAKSVPVEGESEHVSAAKTTDVEGRLSA 851
Cdd:COG3883 186 QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
855-929 |
4.29e-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: 4.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2451976109 855 ETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 929
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
659-929 |
5.45e-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: 44.04 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 659 REQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDnhhQGSHGDGAQVNGIQPEEISRLREEI 738
Cdd:pfam10174 49 KEEAARISVLKEQYRVTQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTS---PVDGEDKFSTPELTEENFRRLQSEH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 739 EELKSQQALLQGQLAEKDSLIENLKssQASGMSEQA---------SATCPPRDPEQVAELKQELTALKSQLcsQSLEITr 809
Cdd:pfam10174 126 ERQAKELFLLRKTLEEMELRIETQK--QTLGARDESikkllemlqSKGLPKKSGEEDWERTRRIAEAEMQL--GHLEVL- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 810 LQTENCELLQRAETLAKSVPVEGESEHVSAAKTT--DVEGRLSALLQETKELKNEIKAL-------SEERTAIQKQLDSS 880
Cdd:pfam10174 201 LDQKEKENIHLREELHRRNQLQPDPAKTKALQTVieMKDTKISSLERNIRDLEDEVQMLktngllhTEDREEEIKQMEVY 280
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2451976109 881 NSTIAILQTEKDKLDLEVtdSKKEQDdllvlladqdqkILSLKSKLKDL 929
Cdd:pfam10174 281 KSHSKFMKNKIDQLKQEL--SKKESE------------LLALQTKLETL 315
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
730-913 |
6.74e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 730 EISRLREEIEELKSQQALLQGQLAEKDSLIENLKssqasgmseqasatcpprdpEQVAELKQELTALKSQLCSQSLEITR 809
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELN--------------------EEYNELQAELEALQAEIDKLQAEIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 810 LQTENCELLQRAETLAKSVPVEGESEH-----VSAAKTTDVEGRLSAL----------LQETKELKNEI----KALSEER 870
Cdd:COG3883 77 AEAEIEERREELGERARALYRSGGSVSyldvlLGSESFSDFLDRLSALskiadadadlLEELKADKAELeakkAELEAKL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2451976109 871 TAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLA 913
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
651-927 |
6.78e-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: 43.63 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 651 VTHYKNMIREQ----DLQLEELKQ-QVSTLKCQNEQLQTA--------VTQQASQIQQHKDQYNLLKVQLGKDNHHQGSH 717
Cdd:pfam01576 329 VTELKKALEEEtrshEAQLQEMRQkHTQALEELTEQLEQAkrnkanleKAKQALESENAELQAELRTLQQAKQDSEHKRK 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 718 GDGAQVNGIQPE--EISRLREEIEELKSQqalLQGQLAEKDSLIENLKSSQASGMSEQASATCPPRDpeqVAELKQELTA 795
Cdd:pfam01576 409 KLEGQLQELQARlsESERQRAELAEKLSK---LQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQD---TQELLQEETR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 796 LKSQLCSQsleITRLQTENCELLQRAEtlaksvpvegesEHVSAAKTtdVEGRLSALLQETKELKNE-------IKALSE 868
Cdd:pfam01576 483 QKLNLSTR---LRQLEDERNSLQEQLE------------EEEEAKRN--VERQLSTLQAQLSDMKKKleedagtLEALEE 545
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2451976109 869 ERTAIQKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLK 927
Cdd:pfam01576 546 GKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQK 604
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
655-929 |
6.97e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 655 KNMIREQDLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLG-----KDNHHqgshgdgaqvngiqpE 729
Cdd:COG1340 21 REEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKelkeeRDELN---------------E 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 730 EISRLREEIEELKSQQALLQGQLAEKDSL---IENLKSsqasgmsEQASATCPPRD----PEQVAELKQELTALKSQLcS 802
Cdd:COG1340 86 KLNELREELDELRKELAELNKAGGSIDKLrkeIERLEW-------RQQTEVLSPEEekelVEKIKELEKELEKAKKAL-E 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 803 QSLEITRLQTENCELLQRAETLAKsvpvegesehvsaakttdvegRLSALLQETKELKNEIKALSEERTAIQKQLDSSNS 882
Cdd:COG1340 158 KNEKLKELRAELKELRKEAEEIHK---------------------KIKELAEEAQELHEEMIELYKEADELRKEADELHK 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2451976109 883 TIAILQTEKDKLdlevtdsKKEQDDLLVLLADQDQKILSLKSKLKDL 929
Cdd:COG1340 217 EIVEAQEKADEL-------HEEIIELQKELRELRKELKKLRKKQRAL 256
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
652-881 |
8.69e-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: 43.52 E-value: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 652 THYKNMIREQDLQLEELKQQVSTLKCQNEQLQTAVTQqaSQIQQHKDQYNLLKVQLgKDNHHQGSHGDGAqVNGIQPEEI 731
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEV-SRIEARLREIEQK-LNRLTLEKE 829
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 732 SrLREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQASATCPPRDPE--------QVAELKQELTALKSQLCSQ 803
Cdd:TIGR02169 830 Y-LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLEsrlgdlkkERDELEAQLRELERKIEEL 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 804 SLEITRLQTENCELLQRAETLA-------------KSVPVEGESEHVSAAKTTDVEGRLSAL----------LQETKELK 860
Cdd:TIGR02169 909 EAQIEKKRKRLSELKAKLEALEeelseiedpkgedEEIPEEELSLEDVQAELQRVEEEIRALepvnmlaiqeYEEVLKRL 988
|
250 260
....*....|....*....|....*
gi 2451976109 861 NEIKA----LSEERTAIQKQLDSSN 881
Cdd:TIGR02169 989 DELKEkrakLEEERKAILERIEEYE 1013
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
678-914 |
1.06e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 678 QNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNHHQGSHGDgaqvngiqpeEISRLREEIEELKSQQALLQGQLAEKDS 757
Cdd:PHA02562 179 LNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQN----------KYDELVEEAKTIKAEIEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 758 LIENLKSSqasgmseqasatcpprdpeqVAELKQELTALKSQL------------------CSQSLE-----ITRLQTEN 814
Cdd:PHA02562 249 DIEDPSAA--------------------LNKLNTAAAKIKSKIeqfqkvikmyekggvcptCTQQISegpdrITKIKDKL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 815 CELLQRAETLAKSVPVEGESEHVSAAKTTDV----------EGRLSALLQETKELKNEIKALSEERTaiqkqldSSNSTI 884
Cdd:PHA02562 309 KELQHSLEKLDTAIDELEEIMDEFNEQSKKLlelknkistnKQSLITLVDKAKKVKAAIEELQAEFV-------DNAEEL 381
|
250 260 270
....*....|....*....|....*....|...
gi 2451976109 885 AILQTEKDKLDLEVTDSKKEQDDLLV---LLAD 914
Cdd:PHA02562 382 AKLQDELDKIVKTKSELVKEKYHRGIvtdLLKD 414
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
656-908 |
1.15e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 656 NMIREQDLQLEELKQQVSTLKcqneqlqtavtqqaSQIQQHKDQYNLLKVQLGKdnhhqgshgdgaqvngiQPEEISRLR 735
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELR--------------EEIEELKEKRDELNEELKE-----------------LAEKRDELN 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 736 EEIEELKSQqalLQGQLAEKDSLIENLKSSQASgmseqasatcppRDP--EQVAELKQELTALKSQ---LCSQSLEITRL 810
Cdd:COG1340 50 AQVKELREE---AQELREKRDELNEKVKELKEE------------RDElnEKLNELREELDELRKElaeLNKAGGSIDKL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 811 QTENCELLQRAETlaKSVPVEGESEHVSAAKttdvegRLSALLQETK---ELKNEIKALSEERTAIQKQLDSSNSTIAIL 887
Cdd:COG1340 115 RKEIERLEWRQQT--EVLSPEEEKELVEKIK------ELEKELEKAKkalEKNEKLKELRAELKELRKEAEEIHKKIKEL 186
|
250 260
....*....|....*....|.
gi 2451976109 888 QTEKDKLDLEVTDSKKEQDDL 908
Cdd:COG1340 187 AEEAQELHEEMIELYKEADEL 207
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
729-929 |
1.16e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 729 EEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEQA--SAtcpprDPEQVAELKQELTALKSQlCSQSLE 806
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGldDA-----DAEAVEARREELEDRDEE-LRDRLE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 807 ITRLQTEncELLQRAETLAKSVpvegesehvsaaktTDVEGRlsallqeTKELKNEIKALSEERTAIQKQLDSSNSTIAI 886
Cdd:PRK02224 332 ECRVAAQ--AHNEEAESLREDA--------------DDLEER-------AEELREEAAELESELEEAREAVEDRREEIEE 388
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2451976109 887 LQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 929
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEL 431
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
784-929 |
1.17e-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: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 784 EQVAELKQELTALKSQLCSQSLEITRLQTENCELLQRAETLAKSVpvegesehvsaakttdvegRLSALLQETKELKNEI 863
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLA-------------------EYSWDEIDVASAEREI 670
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2451976109 864 KALSEERtaiqKQLDSSNSTIAILQTEKDKLDLEVTDSKKEQDDLLVLLADQDQKILSLKSKLKDL 929
Cdd:COG4913 671 AELEAEL----ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL 732
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
721-927 |
1.26e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 721 AQVNGIQPEEISRLREEIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSE-QA---SATCPPRDPE-QVAELKQELTA 795
Cdd:PHA02562 166 SEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARkQNkydELVEEAKTIKaEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 796 LKSQLCSQSLEITRLQTENCELLQRAETLAKSV--------------PVEGESEHVSAAKT--TDVEGRLSALL---QET 856
Cdd:PHA02562 246 LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIkmyekggvcptctqQISEGPDRITKIKDklKELQHSLEKLDtaiDEL 325
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2451976109 857 KELKNEIKALSEERTAIQKQLDSSNSTIAIL-------QTEKDKLDLEVTDSKKEqddlLVLLADQDQKILSLKSKLK 927
Cdd:PHA02562 326 EEIMDEFNEQSKKLLELKNKISTNKQSLITLvdkakkvKAAIEELQAEFVDNAEE----LAKLQDELDKIVKTKSELV 399
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
659-812 |
1.29e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 659 REQDLQLEELKQQVSTL----KCQNEQLQTAVTQQASQIQQHKDQYNLLKVQL---GKDNHHQGSHGDGAQVNgiqpEEI 731
Cdd:COG4717 359 LEEELQLEELEQEIAALlaeaGVEDEEELRAALEQAEEYQELKEELEELEEQLeelLGELEELLEALDEEELE----EEL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 732 SRLREEIEELKSQQALLQGQLAEKDSLIENLKSSqasgmseqasatcpprdpEQVAELKQELTALKSQLCSQSLEITRLQ 811
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELEQLEED------------------GELAELLQELEELKAELRELAEEWAALK 496
|
.
gi 2451976109 812 T 812
Cdd:COG4717 497 L 497
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
644-903 |
1.60e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 644 LEQHDNIvthyKNMIREQDLQLEELKQQVSTLKCQNEQLQ---TAVTQQASQIQQHKDQYNLLKVQLGKDNHHQGshGDG 720
Cdd:PRK03918 185 IKRTENI----EELIKEKEKELEEVLREINEISSELPELReelEKLEKEVKELEELKEEIEELEKELESLEGSKR--KLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 721 AQVNGIQpEEISRLREEIEELKSQQALLQG--QLAEKDSLIENLKSSQASGMSE-QASATCPPRDPEQVAELKQELTALK 797
Cdd:PRK03918 259 EKIRELE-ERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREiEKRLSRLEEEINGIEERIKELEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 798 SQLCSQSLEITRLQTENCELLQRAETLAKSVPVEGESEHVSAAKTTdvegrlsallQETKELKNEIKALSEERTAIQKQL 877
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTG----------LTPEKLEKELEELEKAKEEIEEEI 407
|
250 260
....*....|....*....|....*.
gi 2451976109 878 DSSNSTIAILQTEKDKLDLEVTDSKK 903
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKK 433
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
662-906 |
1.84e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 662 DLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKvqlgkdnhhqgshgdgaqvngiqpEEISRLREEIEEL 741
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQ------------------------AELEALQAEIDKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 742 KSQQALLQGQLAEK-DSLIENLKSSQASGMSEQAsatcpprdpeqvaelkqeLTALksqLCSQSLEitrlqtencELLQR 820
Cdd:COG3883 71 QAEIAEAEAEIEERrEELGERARALYRSGGSVSY------------------LDVL---LGSESFS---------DFLDR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 821 AETLAKSVPVEGES-EHVSAAKTtDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTEKDKLDLEVT 899
Cdd:COG3883 121 LSALSKIADADADLlEELKADKA-ELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
....*..
gi 2451976109 900 DSKKEQD 906
Cdd:COG3883 200 ELEAELA 206
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
730-924 |
2.99e-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: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 730 EISRLREEIEELK-----SQQAL--LQGQLAEKDSLIENLKssqasgmsEQASATCPPRdPEQVAELKQELTALKSQLCS 802
Cdd:pfam10174 416 QLAGLKERVKSLQtdssnTDTALttLEEALSEKERIIERLK--------EQREREDRER-LEELESLKKENKDLKEKVSA 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 803 QSLEITRLQTENCELLQRAETLAKSvPVEGESehvsaaKTTDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNS 882
Cdd:pfam10174 487 LQPELTEKESSLIDLKEHASSLASS-GLKKDS------KLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDR 559
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2451976109 883 tIAILQTEKDKLDLEVTDSKKEQDDLLVLL-------ADQDQKILSLKS 924
Cdd:pfam10174 560 -IRLLEQEVARYKEESGKAQAEVERLLGILrevenekNDKDKKIAELES 607
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
744-909 |
3.33e-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: 40.29 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 744 QQALLQgqLAEKDSLIENLKSSQASGMSEQASATcpprdpEQVAELKQELTALKSQLCSQSLEITRLQTENCELLQRAET 823
Cdd:COG1579 6 LRALLD--LQELDSELDRLEHRLKELPAELAELE------DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 824 LaksvpvEGESEHVSAAKT-TDVEGRLSALLQETKELKNEIKALSEERTAIQKQLDSSNSTIAILQTE----KDKLDLEV 898
Cdd:COG1579 78 Y------EEQLGNVRNNKEyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEleekKAELDEEL 151
|
170
....*....|.
gi 2451976109 899 TDSKKEQDDLL 909
Cdd:COG1579 152 AELEAELEELE 162
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
664-831 |
6.90e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 664 QLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQynllkvqlgkdnhhQGSHGDgaqvngiqPEEISRLREEIEELKS 743
Cdd:COG1579 46 RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ--------------LGNVRN--------NKEYEALQKEIESLKR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 744 QQALLQGQLAEKDSLIENLKssqasgmSEQASATcpprdpEQVAELKQELTALKSQLCSqslEITRLQTENCELLQRAET 823
Cdd:COG1579 104 RISDLEDEILELMERIEELE-------EELAELE------AELAELEAELEEKKAELDE---ELAELEAELEELEAEREE 167
|
....*...
gi 2451976109 824 LAKSVPVE 831
Cdd:COG1579 168 LAAKIPPE 175
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
662-859 |
8.04e-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: 39.66 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 662 DLQLEELKQQVSTLKCQNEQLQTAVTQQASQIQQHKDQYNLLKVQLGKDNHHQGSHGD-GAQVNGIQpEEISRLREEIEE 740
Cdd:pfam15742 185 DQNVNELQQQVRSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKSNQElSEKLSSLQ-QEKEALQEELQQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 741 LKSQQALLQGQLAEKDSLIENlKSSQASGMSEQASATcppRDpEQVAELKQELTALKSQLCSQSLEITRLQTENCELLQR 820
Cdd:pfam15742 264 VLKQLDVHVRKYNEKHHHHKA-KLRRAKDRLVHEVEQ---RD-ERIKQLENEIGILQQQSEKEKAFQKQVTAQNEILLLE 338
|
170 180 190
....*....|....*....|....*....|....*....
gi 2451976109 821 AETLAKSVPVEGESEHVSAAKTTDVEGRLSALLQETKEL 859
Cdd:pfam15742 339 KRKLLEQLTEQEELIKNNKRTISSVQNRVNFLDEENKQL 377
|
|
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
737-893 |
9.88e-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: 38.44 E-value: 9.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 737 EIEELKSQQALLQGQLAEKDSLIENLKSSQASGMSEqasatcpprdpeqVAELKQELTALKSQLCSQSLEITRLQTENCE 816
Cdd:pfam06818 32 EIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLE-------------LEVCENELQRKKNEAELLREKVGKLEEEVSG 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2451976109 817 LlQRAETLAKSVPVEGESEHVSAAKTTDVEGRLSALLQETKELKNEikaLSEERTAIQKQLDSSNSTIAILQTEKDK 893
Cdd:pfam06818 99 L-REALSDVSPSGYESVYESDEAKEQRQEEADLGSLRREVERLRAE---LREERQRRERQASSFEQERRTWQEEKEK 171
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
668-860 |
9.91e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.18 E-value: 9.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 668 LKQQVSTlkcQNEQLQtavtQQASQIQQHKDQYNLLKvqlgkdnhhQGSHGDGAQVNGIQPE------EISRLREEIEEL 741
Cdd:PRK09039 44 LSREISG---KDSALD----RLNSQIAELADLLSLER---------QGNQDLQDSVANLRASlsaaeaERSRLQALLAEL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451976109 742 KSQQALLQGQLAEKDSLIENLKssqasGMSEQASAtcpprdpeQVAELKQELTALKSQLcsQSLEitrlqtencELLQRA 821
Cdd:PRK09039 108 AGAGAAAEGRAGELAQELDSEK-----QVSARALA--------QVELLNQQIAALRRQL--AALE---------AALDAS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2451976109 822 ETLAKSvpvegesehvSAAKTTDVEGRL-SALLQETKELK 860
Cdd:PRK09039 164 EKRDRE----------SQAKIADLGRRLnVALAQRVQELN 193
|
|
| |
