|
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 |
9.20e-68 |
|
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: 229.01 E-value: 9.20e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 347 NQDYFASV--------------NAPSNPPRPAIVVLL--MSMVNERQPFVLRCAVLYCFQCFLYKNQKGQGEIVSTLLPS 410
Cdd:pfam04869 2 LQEEFAKIdvpypdpslpsaanAADQPVKVPVIDLLLnwALSANSVHAFDLRVAACYCLKAYFYNNEEIRLHFLQRAIEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 411 TIDATGNSVSAGQLLCGGL-----FSTDSLSNWCAAVALAHALQENATQKEQLLRVQLAT-SIGNPPVSLLQQCTNIL-- 482
Cdd:pfam04869 82 YKSGNDSSSTTANLLEVLLdydpdLKLDPYKLWFASVILMHLLEDNPEAKELARSVTEGDaESGEEVVTLIQTISELLit 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 483 -SQGSKIQTRVGLLMLLCTWLSNCPIAVTHFLHNSANVPFLTGQIAENlGEEEQLVQGLCALLLGISIYFNDNSlESYMK 561
Cdd:pfam04869 162 sLQREDPRIPIGYLMLLIVWLFEDPDAVNDFLSEGSNLQSLLQFLSQS-SDEDVLVQGLCAMLLGIAYEFSTKD-SPIPR 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 586798161 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 |
1.70e-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: 122.80 E-value: 1.70e-33
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 270 SGWSAQKVTNLHLMLQLVRVLVSPTNPPGATSSCQKAMFQCGLLQQLCTILMATGVPADI 329
Cdd:pfam18770 1 SGWSAQKVSNVHCMLQVVRTLVSPNNPSQVTSSCQKAMRACGLLEALCNILMASGVPADI 60
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
659-896 |
8.83e-16 |
|
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: 82.41 E-value: 8.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 659 IREQDLQLEELRQQVSTLKCQNEQLQT---AVTQQVSQIQQHKDQYNLLKIQLGKDN-QHQGSYSEGAQMNGIQPEEIGR 734
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQLeELEAQLEELESKLDELAEELAE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 735 LREEIEELKRNQELLQSQLTEKDSMIENMKSSQTS---GTNEQSSAIVSARdsEQVAELKQELATLKSQLNSQSVEITKL 811
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEEleeQLETLRSKVAQLE--LQIASLNNEIERLEARLERLEDRRERL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 812 QTEKQELLQKTEAFAKSvEVQGETETIIATKtTDVEGRLSALLQETKELKNEIKALSEERTAIKEQLDSSNSTIAILQTE 891
Cdd:TIGR02168 420 QQEIEELLKKLEEAELK-ELQAELEELEEEL-EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
|
....*
gi 586798161 892 KDKLE 896
Cdd:TIGR02168 498 QENLE 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
659-930 |
2.71e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.67 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 659 IREQDLQLEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHKDQYNLLKIQLGKDNQhqgsysegaqmngiqpeEIGRLREE 738
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ-----------------DIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 739 IEELKRNQELLQSQLTEKDSMIENMKSSQTSGTNEQSSAivsardSEQVAELKQELATLKSQLNSQSVEITKLQTEKQEL 818
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEA------EEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 819 LQKTEAFAKSVEVQGETETIIATKTTDVEGRLSALLQETKELKNEIKALSEERTAIKEQLDSSNSTIAILQTEKDKLELE 898
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250 260 270
....*....|....*....|....*....|..
gi 586798161 899 ITDSKKEQDDLLVLLADQDQKILSLKNKLKDL 930
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
661-936 |
9.74e-14 |
|
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: 75.86 E-value: 9.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 661 EQDLQLEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHKDQYNLLKIQLGKDNQHQGSysegaqmngiQPEEIGRLREEIE 740
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA----------LRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 741 ELKRNQELLQSQLTEKDSMIEnmksSQTSGTNEQSSAIvsARDSEQVAELKQELATLKSQLNSQSVEITKLQTEKQELlq 820
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIE----ELEERLEEAEEEL--AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL-- 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 821 KTEAFAKSVEVQGETETIIATKTtdvegRLSALLQETKELKNEIKALSEERTAIKEQLDSSNSTIAILQTEKDKLELEIT 900
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATER-----RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
250 260 270
....*....|....*....|....*....|....*.
gi 586798161 901 DSKKEQDDLLVLLADQDQKILSLKNKLKDLGHPVEE 936
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
659-931 |
1.78e-13 |
|
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: 75.09 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 659 IREQDLQLEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHKDQYNLLKIQLGKDNQHQGSYsegAQMNGIQPEEIGRLREE 738
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL---EERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 739 IEELKRNQELLQSQLTEKDSMIENMKSSQTSGTNE---QSSAIVSARdsEQVAELKQELATLKSQLNSQSVEITKLQTEK 815
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEElkaLREALDELR--AELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 816 QELLQKTEAFAKSVE----VQGETETIIATKTTDVEG----------RLSALLQETKELKNEIKALSEERTAIKEQLDSS 881
Cdd:TIGR02168 841 EDLEEQIEELSEDIEslaaEIEELEELIEELESELEAllnerasleeALALLRSELEELSEELRELESKRSELRRELEEL 920
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 586798161 882 NSTIAILQTEKDKLELEItDSKKEQ---------DDLLVL-------LADQDQKILSLKNKLKDLG 931
Cdd:TIGR02168 921 REKLAQLELRLEGLEVRI-DNLQERlseeysltlEEAEALenkieddEEEARRRLKRLENKIKELG 985
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
659-882 |
3.23e-13 |
|
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: 72.49 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 659 IREQDLQLEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHKDQYNLLKIQLGKDNQhqgsysegaqmngiqpeEIGRLREE 738
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ-----------------ELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 739 IEELKRNQELLQSQLTE-KDSMIENMKSSQTSGTNEQSSAIVSARDS------------------EQVAELKQELATLKS 799
Cdd:COG4942 85 LAELEKEIAELRAELEAqKEELAELLRALYRLGRQPPLALLLSPEDFldavrrlqylkylaparrEQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 800 QLNSQSVEITKLQTEKQELLQKTEAFAKSVEVQGETETIIATKTTDVEGRLSALLQETKELKNEIKALSEERTAIKEQLD 879
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
...
gi 586798161 880 SSN 882
Cdd:COG4942 245 AAG 247
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
657-937 |
1.95e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 657 NMIREQDLqLEELRQQVSTLKCQNEQLQTAvtqqvsqiQQHKDQYNLLKIQLGkdnqhqgsyseGAQMNGIQpEEIGRLR 736
Cdd:COG1196 187 NLERLEDI-LGELERQLEPLERQAEKAERY--------RELKEELKELEAELL-----------LLKLRELE-AELEELE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 737 EEIEELKRNQELLQSQLTEKDSMIENMKSSQTSGTNEQSSAIV----------------------SARDSEQVAELKQEL 794
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAeeyellaelarleqdiarleerRRELEERLEELEEEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 795 ATLKSQLNSQSVEITKLQTEKQELLQKTEAFAKSVEVQGETETIIATKTTDVEGRLSALLQETKELKNEIKALSEERTAI 874
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586798161 875 KEQLDSSNSTIAILQTEKDKLELEITDSKKEQDDLLVLLADQDQKILSLKNKLKDLGHPVEEE 937
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
728-936 |
7.41e-12 |
|
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: 69.71 E-value: 7.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 728 QPEEIGRLREEIEELKRNQELLQSQLTEKDSMIeNMKSSQTSGTNEQSSAIVSARD--SEQVAELKQELATLKSQLNSQS 805
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRL-DELSQELSDASRKIGEIEKEIEqlEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 806 VEITKLQTEKQELL----QKTEAFAKSV----------------EVQGETETI------IATKTTDVEGRLSALLQETKE 859
Cdd:TIGR02169 751 QEIENVKSELKELEarieELEEDLHKLEealndlearlshsripEIQAELSKLeeevsrIEARLREIEQKLNRLTLEKEY 830
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586798161 860 LKNEIKALSEERTAIKEQLDSSNSTIAILQTEKDKLELEITDSKKEQDDLLVLLADQDQKILSLKNKLKDLGHPVEE 936
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
644-939 |
1.54e-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: 68.51 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 644 TLEQHDNIVTHYKNMIREQDLQLEELRQQVSTLKCQNEQLQTAVTQqvSQIQQHKDQYNLLKIQLGKDNQHQgsysegAQ 723
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELK--SELKNQEKKLEEIQNQISQNNKII------SQ 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 724 MNgiqpEEIGRLREEIEELKRNQELLQSQLTEKDSMIENMKSSQTSGTNEQSSAIVSARDSEQVAELKQELATLK-SQLN 802
Cdd:TIGR04523 340 LN----EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKdEQIK 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 803 SQSVEITKLQTEKQELLQKTEAFAKSVEVQGETETIIATKTTDVEGRLSALLQETKELKNEIKALSEERTAIKEQLDSSN 882
Cdd:TIGR04523 416 KLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE 495
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 586798161 883 STIAILQTEKDKLELEITDSKKEQDDLLVLLADQDQKILSLKNKLKDLGHPVEEEDE 939
Cdd:TIGR04523 496 KELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF 552
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
665-909 |
2.50e-11 |
|
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: 67.79 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 665 QLEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHKDQYNLLKIQLGKDNQHQGSYSEGaQMNGIQPE------EIGRLREE 738
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE-EQLRVKEKigeleaEIASLERS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 739 IEELKRNQELLQSQLTEKDSMIENMKSSQTSGTNEQSS-AIVSARDSEQVAELKQELATLKSQLNSQSV----------- 806
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEeRKRRDKLTEEYAELKEELEDLRAELEEVDKefaetrdelkd 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 807 ---EITKLQTEKQELlqKTEAFAKSVEVQGETETI--IATKTTDVEGRLSALLQETKELKNEIKALSEERTAIKEQLDSS 881
Cdd:TIGR02169 390 yreKLEKLKREINEL--KRELDRLQEELQRLSEELadLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY 467
|
250 260
....*....|....*....|....*...
gi 586798161 882 NSTIAILQTEKDKLELEITDSKKEQDDL 909
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQRELAEA 495
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
659-940 |
8.56e-11 |
|
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: 66.24 E-value: 8.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 659 IREQDLQLEELRQQVSTLKCQNE----------------------QLQTAVTQ------QVSQIQQHKDQynlLKIQLGK 710
Cdd:TIGR02169 186 IERLDLIIDEKRQQLERLRREREkaeryqallkekreyegyellkEKEALERQkeaierQLASLEEELEK---LTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 711 DNQHQGSYSE-----GAQMNGIQPEEIGRLREEIEELKRNQELLQSQLTEKDsmiENMKSSQtsgtnEQSSAIVSARDS- 784
Cdd:TIGR02169 263 LEKRLEEIEQlleelNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKE---RELEDAE-----ERLAKLEAEIDKl 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 785 -EQVAELKQELATLKSQLNSQSVEITKLQTEKQELLQKTEAFAKSVEVQGETETIIATKTTDVEGRLSALLQETKELKNE 863
Cdd:TIGR02169 335 lAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586798161 864 IKALSEERTAIKEQLDSSNSTIAILQTEKDKLELEITDSKKEQDDLLVLLADQDQKILSLKNKLKDLghpveeEDEL 940
Cdd:TIGR02169 415 LQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV------EKEL 485
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
657-930 |
1.46e-10 |
|
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: 65.52 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 657 NMIREQ-DLQLEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHK----DQYNLLKIQLGKDNQH-QGSYSEGAQMNgiqpE 730
Cdd:pfam15921 295 NSIQSQlEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKrmyeDKIEELEKQLVLANSElTEARTERDQFS----Q 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 731 EIGRLREEIEEL-----KRNQEL-----------------------LQSQLTEK-------DSMIENMKSSQTSGTNEQS 775
Cdd:pfam15921 371 ESGNLDDQLQKLladlhKREKELslekeqnkrlwdrdtgnsitidhLRRELDDRnmevqrlEALLKAMKSECQGQMERQM 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 776 SAIVSARDS-EQVAELKQELATLKSQLNSQSVEITKlqteKQELLQKTEAFAK--SVEVQGETETIIATKT--TDVEGRL 850
Cdd:pfam15921 451 AAIQGKNESlEKVSSLTAQLESTKEMLRKVVEELTA----KKMTLESSERTVSdlTASLQEKERAIEATNAeiTKLRSRV 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 851 SALLQETKELKNE---IKALSEERTAIKEQLDSSNSTIAIL---------------------QTEKDKLELEITDSKKEQ 906
Cdd:pfam15921 527 DLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILrqqienmtqlvgqhgrtagamQVEKAQLEKEINDRRLEL 606
|
330 340
....*....|....*....|....
gi 586798161 907 DDLLVLLADQDQKILSLKNKLKDL 930
Cdd:pfam15921 607 QEFKILKDKKDAKIRELEARVSDL 630
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
730-940 |
2.54e-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: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 730 EEIGRLREEIEELKRNQELLQSQLTEKDSMIENMKSSQTsgTNEQSSAIVSA-RDSEQVAELKQ------ELATLKSQLN 802
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERE--KAERYQALLKEkREYEGYELLKEkealerQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 803 SQSVEITKLQTEKQEL-------LQKTEAFAKSVEVQGETETI-IATKTTDVEGRLS-------ALLQETKELKNEIKAL 867
Cdd:TIGR02169 248 SLEEELEKLTEEISELekrleeiEQLLEELNKKIKDLGEEEQLrVKEKIGELEAEIAslersiaEKERELEDAEERLAKL 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586798161 868 SEERTAIKEQLDSSNSTIAILQTEKDKLELEITDSKKEQDDLLVLLADQDQKILSLKNKLKDLghpVEEEDEL 940
Cdd:TIGR02169 328 EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY---REKLEKL 397
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
658-937 |
4.64e-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: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 658 MIREQDLQLEELRQQVSTLKCQNEQLQTavtqQVSQIQQHKDQYNLLKIQLGKDNQHQgsysegaqmngiqPEEIGRLRE 737
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEE----DLSSLEQEIENVKSELKELEARIEEL-------------EEDLHKLEE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 738 EIEELKRnqELLQSQLTEKDSMIENMKssqtsgtneqssaivsardsEQVAELKQELATLKSQLNSQSVEITKLQTEKQE 817
Cdd:TIGR02169 780 ALNDLEA--RLSHSRIPEIQAELSKLE--------------------EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 818 LLQKTEAF-AKSVEVQGETEtiiatkttDVEGRLSALLQETKELKNEIKALSEERTAIKEQLDSSNSTIAILQTEKDKLE 896
Cdd:TIGR02169 838 LQEQRIDLkEQIKSIEKEIE--------NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 586798161 897 LEITDSKKEQDDLLVLLADQDQKILSLKNKLKDLGHPVEEE 937
Cdd:TIGR02169 910 AQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEE 950
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
644-905 |
6.76e-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: 63.15 E-value: 6.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 644 TLEQHDNIVTHYKNMIREQDLQLEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHKDQYNLLKIQLGKDNQHQGSYSEGAQ 723
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 724 MngiQPEEIGRLREEIEELKRNQELLQSQLTEKDSMIENMKSSQTSGTNEQSS---AIVSARD-----SEQVAELKQELA 795
Cdd:TIGR02168 835 A---TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASleeALALLRSeleelSEELRELESKRS 911
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 796 TLKSQLNSQSVEITKLQTEKQELLQKTEAFAKSVEVQGETE-TIIATKTTDVEGRLSALLQETKELKNEIKALS------ 868
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTlEEAEALENKIEDDEEEARRRLKRLENKIKELGpvnlaa 991
|
250 260 270
....*....|....*....|....*....|....*...
gi 586798161 869 -EERTAIKEQLDSSNSTIAILQTEKDKLELEITDSKKE 905
Cdd:TIGR02168 992 iEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDRE 1029
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
731-939 |
1.50e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 731 EIGRLREEIEELKRNQELLQSQLTE---KDSMIENMKSSQTSGTNEQSSAIVSARDS------------EQVAELKQELA 795
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAElrkELEELEEELEQLRKELEELSRQISALRKDlarleaeveqleERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 796 TLKSQLNSQSVEITKLQTEKQELLQKTEAFAKSVE-VQGETETIIATKT------TDVEGRLSALLQETKELKNEIKALS 868
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEqLKEELKALREALDelraelTLLNEEAANLRERLESLERRIAATE 837
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 586798161 869 EERTAIKEQLDSSNSTIAILQTEKDKLELEITDSKKEQDDLLVLLADQDQKILSLKNKLKDLGHPVEEEDE 939
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
656-940 |
1.60e-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: 61.96 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 656 KNMIREQDLQLEELRQQVStlkcQNEQLQTAVTQQVSQIQQHKDQYNL----LKIQLG-KDNQHQGSYSEGAQMNgiqpE 730
Cdd:TIGR04523 313 KSELKNQEKKLEEIQNQIS----QNNKIISQLNEQISQLKKELTNSESenseKQRELEeKQNEIEKLKKENQSYK----Q 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 731 EIGRLREEIEELKRNQELLQSQLTEKDSMIENMKSSQTSGTNEQSsaivsaRDSEQVAELKQELATLKSQLNSQSVEITK 810
Cdd:TIGR04523 385 EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE------RLKETIIKNNSEIKDLTNQDSVKELIIKN 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 811 LQTEKQELLQKTEAFAKSVEV----QGETETIIATKT----------TDVEGRLSALLQETKELKNEIKALSEERTAIKE 876
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKikqnLEQKQKELKSKEkelkklneekKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586798161 877 QLDSSNSTI---------AILQTEKDKLELEITDSKKEQDDLLVLLADQDQKILSLKNKLKDLGHPVEEEDEL 940
Cdd:TIGR04523 539 KISDLEDELnkddfelkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKK 611
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
731-928 |
6.17e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.07 E-value: 6.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 731 EIGRLREEIEELKRNQELLQSQLTEKDSMIENMKssqtsgtneqssaivsardsEQVAELKQELATLKSQLNSQSVEITK 810
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELN--------------------EEYNELQAELEALQAEIDKLQAEIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 811 LQTEKQELLQKTEAFAKSVEVQGETETII-----ATKTTDVEGRLSALLQETKELKNEIKALSEERTAIKEQLDSSNSTI 885
Cdd:COG3883 77 AEAEIEERREELGERARALYRSGGSVSYLdvllgSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 586798161 886 AILQTEKDKLEL---EITDSKKEQDDLLVLLADQDQKILSLKNKLK 928
Cdd:COG3883 157 AELEALKAELEAakaELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
842-939 |
8.97e-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: 54.33 E-value: 8.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 842 KTTDVEGRLSALLQETKELKNEIKALS-------EERTAIKEQLDSSNSTIAILQTEKDKLELEI---TDSKKEQDDLLV 911
Cdd:pfam04871 2 KKSELESEASSLKNENTELKAELQELSkqynsleQKESQAKELEAEVKKLEEALKKLKAELSEEKqkeKEKQSELDDLLL 81
|
90 100
....*....|....*....|....*...
gi 586798161 912 LLADQDQKILSLKNKLKDLGHPVEEEDE 939
Cdd:pfam04871 82 LLGDLEEKVEKYKARLKELGEEVLSDDE 109
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
730-879 |
1.72e-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: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 730 EEIGRLREEIEELKRNQELLQSQLTEKDSMIENMKSSQtsgtNEQSSAIVSARdsEQVAELKQELATLKS--QLNSQSVE 807
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI----KRLELEIEEVE--ARIKKYEEQLGNVRNnkEYEALQKE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 586798161 808 ITKLQTEKQEL----LQKTEAFAKSVEVQGETETIIATKTTDVEGRLSALLQETKELKNEIKALSEERTAIKEQLD 879
Cdd:COG1579 98 IESLKRRISDLedeiLELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
728-930 |
1.82e-08 |
|
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: 57.47 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 728 QPEEIGRLREEIEELKRNQELLQSQLTEkdsmIENMKSSQTSGTNEQSSAIVSARdsEQVAELKQELATLKSQLNSQSVE 807
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAA----LKKEEKALLKQLAALERRIAALA--RRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 808 ITKLQTEKQELLQKTEAFAKSVEVQGETETII----ATKTTDVEGRLS-------ALLQETKELKNEIKALSEERTAIKE 876
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQylkylapARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 586798161 877 QLDSSNSTIAILQTEKDKLELEITDSKKEQDDLLVLLADQDQKILSLKNKLKDL 930
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
521-930 |
2.09e-08 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 58.05 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 521 FLTGQIAENLGEEEQLVQGLCALLLGISIYFND-----NSLESYMKEKLKQLIEKRIGKENFIEKLGFISKHELYSRASQ 595
Cdd:COG5185 124 YLYKSEIVALKDELIKVEKLDEIADIEASYGEVetgiiKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGT 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 596 KPQPNFpspEYMIFDheftkLVKELEGVITKAIYKSSEEDKKEEEVKKTLEQHDNIVTHYKNMIRE-QDLQLEELRQQVS 674
Cdd:COG5185 204 VNSIKE---SETGNL-----GSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQnTDLRLEKLGENAE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 675 TLKCQNEQlqtaVTQQVSQIQQHKDQYNLlKIQLGKDNQHQGSYSEGAQMNgiqpeeigRLREEIEELKRNQEllqSQLT 754
Cdd:COG5185 276 SSKRLNEN----ANNLIKQFENTKEKIAE-YTKSIDIKKATESLEEQLAAA--------EAEQELEESKRETE---TGIQ 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 755 EKDSMIENMKSSQTSGTNEQSSAIVSARDSEQVAELKQELATLKSQLNSQsveITKLQTEKQELLQKTEAFAKSVEvqgE 834
Cdd:COG5185 340 NLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIEST---KESLDEIPQNQRGYAQEILATLE---D 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 835 TETIIATKTTDVEGRLSALLQETKELKNEIKALSEERTaiKEQLDSSNSTIAILQTEKDKLELEITDSKKEQDDLLVLLA 914
Cdd:COG5185 414 TLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELN--KVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIE 491
|
410
....*....|....*.
gi 586798161 915 DQdqkILSLKNKLKDL 930
Cdd:COG5185 492 SR---VSTLKATLEKL 504
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
645-939 |
2.33e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 645 LEQHDNIVTHYKNMIREQDLQLEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHKDQYNLLKIQLGKDNQHQG---SYSEG 721
Cdd:PRK02224 337 AQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGnaeDFLEE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 722 AQmngiqpEEIGRLREEIEELKRNQELLQSQLTEKDSMIENMKSSqTSGTNEQSSAIVSA--RDSEQVAELKQELATLKS 799
Cdd:PRK02224 417 LR------EERDELREREAELEATLRTARERVEEAEALLEAGKCP-ECGQPVEGSPHVETieEDRERVEELEAELEDLEE 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 800 QLNSQSVEITKLqtekqELLQKTEAFAKSVEVQGET-ETIIATKTTDVEG---RLSALLQETKELKNEIKALSEERTAIK 875
Cdd:PRK02224 490 EVEEVEERLERA-----EDLVEAEDRIERLEERREDlEELIAERRETIEEkreRAEELRERAAELEAEAEEKREAAAEAE 564
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 586798161 876 EQLDSSNSTIAILQTEKDKLELEItDSKKEQDDLLVLLADQDQKILSLKNKLKDLGhpvEEEDE 939
Cdd:PRK02224 565 EEAEEAREEVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKREALA---ELNDE 624
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
734-930 |
4.18e-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: 57.37 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 734 RLREEIEELKRNQELL--QSQLTEKDSMIENMKssqtsgtnEQSSAIVSARDSEqvaELKQELATLKSQLNSQSVEITKL 811
Cdd:TIGR02168 190 RLEDILNELERQLKSLerQAEKAERYKELKAEL--------RELELALLVLRLE---ELREELEELQEELKEAEEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 812 QTEKQELLQKTEAF-AKSVEVQGETETIiatkttdvEGRLSALLQETKELKNEIKALSEERTAIKEQLDSSNSTIAILQT 890
Cdd:TIGR02168 259 TAELQELEEKLEELrLEVSELEEEIEEL--------QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 586798161 891 EKDKLELEITDSKKEQDDLLVLLADQDQKILSLKNKLKDL 930
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
662-898 |
4.43e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.95 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 662 QDLQLEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHKDQYNLLkiqlgkdnqhqgSYSEGAQMNGiqpEEIGRLREEIEE 741
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLV------------DLSEEAKLLL---QQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 742 LKRNQELLQSQLTEKDSMIENmkSSQTSGTNEQSSAIVSARdsEQVAELKQELATLKSQLNSQSVEITKLQTEKQELLQk 821
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGS--GPDALPELLQSPVIQQLR--AQLAELEAELAELSARYTPNHPDVIALRAQIAALRA- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 822 teafaksvEVQGETETIIATKTTDVEG---RLSALLQETKELKNEIKALSE---ERTAIKEQLDSSNSTIAILQTEKDKL 895
Cdd:COG3206 306 --------QLQQEAQRILASLEAELEAlqaREASLQAQLAQLEARLAELPEleaELRRLEREVEVARELYESLLQRLEEA 377
|
...
gi 586798161 896 ELE 898
Cdd:COG3206 378 RLA 380
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
656-926 |
2.27e-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: 55.03 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 656 KNMIREQDLQLEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHKDQYNLLKIQL--------GKDNQHQGSYSEGAQMNgi 727
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLeqkqkelkSKEKELKKLNEEKKELE-- 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 728 qpEEIGRLREEIEELKRNQELLQSQLTEKDSMIENMKSSqtsgTNEQSSAIVSARDSEQVAELKQELATLKSQLNSqsve 807
Cdd:TIGR04523 510 --EKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE----LNKDDFELKKENLEKEIDEKNKEIEELKQTQKS---- 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 808 ITKLQTEKQELLQKTEAfaKSVEVQGETETIIATKTTdVEGRLSALLQETKELKNEIKALSEERTAIKEQLDSSNSTIAI 887
Cdd:TIGR04523 580 LKKKQEEKQELIDQKEK--EKKDLIKEIEEKEKKISS-LEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKE 656
|
250 260 270
....*....|....*....|....*....|....*....
gi 586798161 888 LQTEKDKLELEITDSKKEQDDLLVLLADQDQKILSLKNK 926
Cdd:TIGR04523 657 IRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKK 695
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
665-830 |
3.16e-07 |
|
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: 52.62 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 665 QLEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHKDQYNLLKIQLGKDNQHQGSYsEGAQMNGIQPEEIGRLREEIEELKR 744
Cdd:COG1579 25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY-EEQLGNVRNNKEYEALQKEIESLKR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 745 NQELLQSQLTEKDSMIENMKSSQtsgtneqssaivsARDSEQVAELKQELATLKSQLNSqsvEITKLQTEKQELLQKTEA 824
Cdd:COG1579 104 RISDLEDEILELMERIEELEEEL-------------AELEAELAELEAELEEKKAELDE---ELAELEAELEELEAEREE 167
|
....*.
gi 586798161 825 FAKSVE 830
Cdd:COG1579 168 LAAKIP 173
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
785-930 |
6.78e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 6.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 785 EQVAELKQELATLKSQLNSQSVEITKLQTEKQELLQKTEAFAKSVEVQGEtetiiatkttdvegrlsalLQETKELKNEI 864
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWD-------------------EIDVASAEREI 670
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 586798161 865 KALSEERtaikEQLDSSNSTIAILQTEKDKLELEITDSKKEQDDLLVLLADQDQKILSLKNKLKDL 930
Cdd:COG4913 671 AELEAEL----ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL 732
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
666-939 |
8.53e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 8.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 666 LEELRQQVSTLKCQNEQL----QTAVTQQVSQIQQHKDQynllkiqlgkdNQHqgsysegAQMNGIQpEEIGRLREEIEE 741
Cdd:PRK02224 164 LEEYRERASDARLGVERVlsdqRGSLDQLKAQIEEKEEK-----------DLH-------ERLNGLE-SELAELDEEIER 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 742 LKRNQELLQSQLTEKDSMIENMKSSQT---------SGTNEQSSAIVSARD--SEQVAELKQELATLKSQLNS------- 803
Cdd:PRK02224 225 YEEQREQARETRDEADEVLEEHEERREeletleaeiEDLRETIAETEREREelAEEVRDLRERLEELEEERDDllaeagl 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 804 QSVEITKLQTEKQELLQKTEAFAKSVEvqgETETIIATKTTDVEG---RLSALLQETKELKNEIKALSEERTAIKEQLDS 880
Cdd:PRK02224 305 DDADAEAVEARREELEDRDEELRDRLE---ECRVAAQAHNEEAESlreDADDLEERAEELREEAAELESELEEAREAVED 381
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 586798161 881 SNSTIAILQTEKDKLELEITDSKKEQDDLLVLLADQDQKILSLKNKLKDLGHPVEEEDE 939
Cdd:PRK02224 382 RREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARE 440
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
649-940 |
9.19e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.72 E-value: 9.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 649 DNIVTHYKNMIREQDLQLEELRQQVSTLKCQ------------------NEQLQTavtqQVSQIQQHKDQYNLLKIQLGK 710
Cdd:TIGR04523 60 DKNLNKDEEKINNSNNKIKILEQQIKDLNDKlkknkdkinklnsdlskiNSEIKN----DKEQKNKLEVELNKLEKQKKE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 711 DNQHQGSYS-----EGAQMNGIQpEEIGRLREEIEELKRNQELLQSQLTEKDSMIENMKSSQTSgtNEQSSAIVSARDSE 785
Cdd:TIGR04523 136 NKKNIDKFLteikkKEKELEKLN-NKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK--LELLLSNLKKKIQK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 786 ------QVAELKQELATLKSQLNSQSVEITKLQTE----KQELLQ--------KTEAFAKSVEVQgETETIIATKTTDV- 846
Cdd:TIGR04523 213 nkslesQISELKKQNNQLKDNIEKKQQEINEKTTEisntQTQLNQlkdeqnkiKKQLSEKQKELE-QNNKKIKELEKQLn 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 847 --EGRLSALLQE-----TKELKNEIKALSEERTAIKEQLDSSNSTIAILQTEKDKLELEITDS-----------KKEQDD 908
Cdd:TIGR04523 292 qlKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSesensekqrelEEKQNE 371
|
330 340 350
....*....|....*....|....*....|....*
gi 586798161 909 LLVLLADQDQK---ILSLKNKLKDLGHPVEEEDEL 940
Cdd:TIGR04523 372 IEKLKKENQSYkqeIKNLESQINDLESKIQNQEKL 406
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
645-940 |
1.52e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 645 LEQHDNIvthyKNMIREQDLQLEELRQQVSTLKCQNEQLQ---TAVTQQVSQIQQHKDQYNLLKIQLGKDNQHQGSYSEg 721
Cdd:PRK03918 185 IKRTENI----EELIKEKEKELEEVLREINEISSELPELReelEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEE- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 722 aQMNGIQpEEIGRLREEIEELKRNQELLQS--QLTEKDSMIENMKSSQTSGTNEQSSAIvsARDSEQVAELKQELatlkS 799
Cdd:PRK03918 260 -KIRELE-ERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRL--SRLEEEINGIEERI----K 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 800 QLNSQSVEITKLQTEKQELLQKTEAFAKSVE-------VQGETETIIATKTTDVEGRLSALLQETKELKNEIKalsEERT 872
Cdd:PRK03918 332 ELEEKEERLEELKKKLKELEKRLEELEERHElyeeakaKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIE---EEIS 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 873 AIKEQLDSSNSTIAILQ--------------------TEKDKLEL------EITDSKKEqddllvlLADQDQKILSLKNK 926
Cdd:PRK03918 409 KITARIGELKKEIKELKkaieelkkakgkcpvcgrelTEEHRKELleeytaELKRIEKE-------LKEIEEKERKLRKE 481
|
330
....*....|....
gi 586798161 927 LKDLGHPVEEEDEL 940
Cdd:PRK03918 482 LRELEKVLKKESEL 495
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
722-928 |
1.74e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 51.94 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 722 AQMNGIQPEEIGRLREEIEELKRNQELLQSQLTEKDSMIENMKSSQTSGTNEQSSAIVSARDSE-----QVAELKQELAT 796
Cdd:PHA02562 166 SEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAktikaEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 797 LKSQLNSQSVEITKLQTEKQELLQKTEAFAK----------------SVEVQGETETIIATKTTDVEGRLSALL---QET 857
Cdd:PHA02562 246 LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyekggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDtaiDEL 325
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 586798161 858 KELKNEIKALSEERTAIKEQLDSSNSTIAILQTEKDKLELEI---TDSKKEQDDLLVLLADQDQKILSLKNKLK 928
Cdd:PHA02562 326 EEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIeelQAEFVDNAEELAKLQDELDKIVKTKSELV 399
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
663-891 |
1.77e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 663 DLQLEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHKDQYNLLKIQLgKDNQhqgsysegaqmngiqpEEIGRLREEIEEL 742
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL-EALQ----------------AEIDKLQAEIAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 743 KRNQELLQSQLTEkdsmieNMKSSQTSGTN-----------------EQSSAI--VSARDSEQVAELKQELATLKSQLNS 803
Cdd:COG3883 78 EAEIEERREELGE------RARALYRSGGSvsyldvllgsesfsdflDRLSALskIADADADLLEELKADKAELEAKKAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 804 QSVEITKLQTEKQELLQKTEAFAKSVEVQGETETIIATKTTDVEGRLSALLQETKELKNEIKALSEERTAIKEQLDSSNS 883
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
....*...
gi 586798161 884 TIAILQTE 891
Cdd:COG3883 232 AAAAAAAA 239
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
713-936 |
2.10e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 51.66 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 713 QHQGSYSEGAQMNGIQPEEIGRLREEIEELKRNQElLQSQLTEKDSMIENMKSSQTSGTNEQSS-AIVSARDSEQV--AE 789
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVE-RRRKLEEAEKARQAEMDRQAAIYAEQERmAMERERELERIrqEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 790 LKQELATLKSQLNSQSV----EITKLQTEKQE----LLQKTEAFAKSVEVQGETETIIATKTTDVEgRLSALLQETKELk 861
Cdd:pfam17380 358 RKRELERIRQEEIAMEIsrmrELERLQMERQQknerVRQELEAARKVKILEEERQRKIQQQKVEME-QIRAEQEEARQR- 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 862 nEIKALSEERT-----AIKEQLDSSNSTIAILQTEKD----KLELEITDSKK---EQDDLLVL---LADQDQKILSLKNK 926
Cdd:pfam17380 436 -EVRRLEEERAremerVRLEEQERQQQVERLRQQEEErkrkKLELEKEKRDRkraEEQRRKILekeLEERKQAMIEEERK 514
|
250
....*....|
gi 586798161 927 LKDLGHPVEE 936
Cdd:pfam17380 515 RKLLEKEMEE 524
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
660-863 |
2.15e-06 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 50.53 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 660 REQDLQLEELRQ-------QVSTLKCQNEQLQTAVTQQVSQIQQHKDQYNLLKIQLGKDNQHQGSYSEGAQmngiqpEEI 732
Cdd:pfam09787 43 TALTLELEELRQerdllreEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAE------AEL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 733 GRLREEI----EELKRNQELLQSQLTEKDSMIENMKSSQTSGTNEQSSAivsardseqvAELKQELATLKSQLNSQSVEI 808
Cdd:pfam09787 117 ERLQEELryleEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQ----------SELENRLHQLTETLIQKQTML 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 586798161 809 TKLQTEKQELLQKTEAFAKSV-EVQGETETIIATKTTDVEGRLSALLQETKELKNE 863
Cdd:pfam09787 187 EALSTEKNSLVLQLERMEQQIkELQGEGSNGTSINMEGISDGEGTRLRNVPGLFSE 242
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
730-906 |
2.56e-06 |
|
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: 51.66 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 730 EEIGRLREEIEELKRNQ---ELLQSQLTEKDSMIENMKSSQTSGTNeqssaiVSARDSEQVAELKQELATLKSQLNSQSV 806
Cdd:pfam15921 531 QELQHLKNEGDHLRNVQtecEALKLQMAEKDKVIEILRQQIENMTQ------LVGQHGRTAGAMQVEKAQLEKEINDRRL 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 807 EITK---LQTEKQELLQKTEAFAKSVE------VQGETETIIATKttDVEGRLSALLQETKELKNEIKALSEERTAIKEQ 877
Cdd:pfam15921 605 ELQEfkiLKDKKDAKIRELEARVSDLElekvklVNAGSERLRAVK--DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRN 682
|
170 180
....*....|....*....|....*....
gi 586798161 878 LDSSNSTIAiLQTEKDKLELEITDSKKEQ 906
Cdd:pfam15921 683 FRNKSEEME-TTTNKLKMQLKSAQSELEQ 710
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
665-931 |
3.24e-06 |
|
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: 51.20 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 665 QLEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHKDQYNLlkiQLGKDNQHQGSYSEGA-QMNGIQPEE--IGRLREEIEE 741
Cdd:TIGR00606 574 QLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINN---ELESKEEQLSSYEDKLfDVCGSQDEEsdLERLKEEIEK 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 742 LKRNQELLQSQLTEKDSMIENmkssqtSGTNEQSSAIVSARDSEQVAELKQELATLKSQLNSQSVEITKLQTEKQELLQK 821
Cdd:TIGR00606 651 SSKQRAMLAGATAVYSQFITQ------LTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKR 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 822 TEAFAKSVEVQGETETIIATKTTDVEGRLSALLQETKELKNEIK--------ALSEERTA------------IKEQLDSS 881
Cdd:TIGR00606 725 RDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEeqetllgtIMPEEESAkvcltdvtimerFQMELKDV 804
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 586798161 882 NSTIAILQTEKDKLELEIT--------DSKKEQDDLLV--------LLADQDQKILSLKNKLKDLG 931
Cdd:TIGR00606 805 ERKIAQQAAKLQGSDLDRTvqqvnqekQEKQHELDTVVskielnrkLIQDQQEQIQHLKSKTNELK 870
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
663-906 |
3.39e-06 |
|
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: 51.27 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 663 DLQLEELRQqvstLKCQNEQLQTAVTQ-QVSQIQQ-HKDQY-NLLKIQLGKDNQHQGSYSEGA---QMNGIQPE-EIGRL 735
Cdd:pfam15921 527 DLKLQELQH----LKNEGDHLRNVQTEcEALKLQMaEKDKViEILRQQIENMTQLVGQHGRTAgamQVEKAQLEkEINDR 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 736 REEIEELKRNQELLQSQLTEKDSMIENMKSSQTSGTNEQSSAIVSARDSEQVA-ELKQELATLKSQLN------------ 802
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERdQLLNEVKTSRNELNslsedyevlkrn 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 803 ----SQSVEIT----KLQTEK-QELLQKTEAFAKSVEVQGETETIIAT----KTTDVEGRLSALLQETKELKNEIKALSE 869
Cdd:pfam15921 683 frnkSEEMETTtnklKMQLKSaQSELEQTRNTLKSMEGSDGHAMKVAMgmqkQITAKRGQIDALQSKIQFLEEAMTNANK 762
|
250 260 270
....*....|....*....|....*....|....*....
gi 586798161 870 ERTAIKEQLDSSNSTIAILQTEKDKL--ELEITDSKKEQ 906
Cdd:pfam15921 763 EKHFLKEEKNKLSQELSTVATEKNKMagELEVLRSQERR 801
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
665-911 |
3.60e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 665 QLEELRQQVStlkcqneQLQTAVTQQVSQIQQHKDQYNLLKIQLGKDNQHQGsysegaQMNGIQPEEIGRLREEIEElkr 744
Cdd:PRK04863 838 ELRQLNRRRV-------ELERALADHESQEQQQRSQLEQAKEGLSALNRLLP------RLNLLADETLADRVEEIRE--- 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 745 nqELLQSQLTEKDsmienmkSSQTSGTNEQSSAIVSA--RDSEQVAELKQELATLKSQLNSQSVEITKLqtekQELLQKT 822
Cdd:PRK04863 902 --QLDEAEEAKRF-------VQQHGNALAQLEPIVSVlqSDPEQFEQLKQDYQQAQQTQRDAKQQAFAL----TEVVQRR 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 823 EAFAKSVEVQgetetiIATKTTDVEGRLSALLQETKELKNEIKalsEERTAIKEQLDSSNSTIAILQTEKDKLELEITDS 902
Cdd:PRK04863 969 AHFSYEDAAE------MLAKNSDLNEKLRQRLEQAEQERTRAR---EQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQEL 1039
|
....*....
gi 586798161 903 KKEQDDLLV 911
Cdd:PRK04863 1040 KQELQDLGV 1048
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
656-937 |
4.20e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.52 E-value: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 656 KNMIREQDLQLEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHKDQYNllkiqlgkdnqhqgsysegaQMNgiqpEEIGRL 735
Cdd:COG1340 21 REEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRD--------------------ELN----EKVKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 736 REEIEELKRNQELLQSQLTEKDSMIENMKssqtsgtneqssaivsaRDSEQVAELKQELATLksqLNSQSVEITKLQTEK 815
Cdd:COG1340 77 KEERDELNEKLNELREELDELRKELAELN-----------------KAGGSIDKLRKEIERL---EWRQQTEVLSPEEEK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 816 Q------ELLQKTEAFAKSVEVQGETETIIAtKTTDVEGRLSALLQETKELKNEIKALSEERTAIKEQLDSSNSTIAILQ 889
Cdd:COG1340 137 ElvekikELEKELEKAKKALEKNEKLKELRA-ELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELH 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 586798161 890 TEKDKLELEITDSKKEQDDLLVLLADQDQKILSLKNKLKDLGHPVEEE 937
Cdd:COG1340 216 KEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKE 263
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
730-929 |
4.59e-06 |
|
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: 50.82 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 730 EEIGRLREEIEELKRNQELLQSQLTEKDSMIENMKSSQTSGTNEQSSAIVSARDSEQVAELKQELATLKSQLNSQSVE-- 807
Cdd:TIGR00606 744 KEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDrt 823
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 808 ITKLQTEKQE-------LLQKTEAFAKSVEVQGETETIIATKTTDVE----------GRLSALLQETKELKNEIKALSEE 870
Cdd:TIGR00606 824 VQQVNQEKQEkqheldtVVSKIELNRKLIQDQQEQIQHLKSKTNELKseklqigtnlQRRQQFEEQLVELSTEVQSLIRE 903
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586798161 871 RTAIKEQLDSSNSTIAILQTEKDKL-ELEITDSKKEQDDLLVLLADQDQKIL---SLKNKLKD 929
Cdd:TIGR00606 904 IKDAKEQDSPLETFLEKDQQEKEELiSSKETSNKKAQDKVNDIKEKVKNIHGymkDIENKIQD 966
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
785-909 |
7.91e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 7.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 785 EQVAELKQELATLKSQLNSQSVEITKLQTEKQELLQKTEAFAKSVEVQGETETIIATKTTDVEGRLSALLQETKELKNEI 864
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 586798161 865 KALSEERTAIKEQLDSSNSTIAILQTEKDKLELEITDSKKEQDDL 909
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
665-891 |
8.80e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 8.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 665 QLEELRQQVstlkcqnEQLQTAVTQQVSQIQQHKDQYNLLKIQLGKDNQHQGSYSEGAQMNGIQpEEIGRLREEIEELKR 744
Cdd:COG4913 611 KLAALEAEL-------AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE-REIAELEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 745 nqellqsqltekdsmienmkssqtsgtneqssaivsarDSEQVAELKQELATLKSQLNSQSVEITKLQTEKQELLQKTEA 824
Cdd:COG4913 683 --------------------------------------SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ 724
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 586798161 825 FAKSVE-----VQGETETIIATKTTDVEGRLSALLQETKElKNEIKALSEERTAIKEQLDSSNSTIAILQTE 891
Cdd:COG4913 725 AEEELDelqdrLEAAEDLARLELRALLEERFAAALGDAVE-RELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
660-940 |
1.07e-05 |
|
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: 49.44 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 660 REQDLQLEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHKDQYNLLKIQLgkdNQHQGSYSEGAQMNGIQPEEIGRLREEI 739
Cdd:pfam10174 49 KEEAARISVLKEQYRVTQEENQHLQLTIQALQDELRAQRDLNQLLQQDF---TTSPVDGEDKFSTPELTEENFRRLQSEH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 740 EELKRNQELLQSQLTEKDSMIENMKssQTSGTNEQS---------SAIVSARDSEQVAELKQELATLKSQLNSQSVEitk 810
Cdd:pfam10174 126 ERQAKELFLLRKTLEEMELRIETQK--QTLGARDESikkllemlqSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVL--- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 811 LQTEKQELLQKTEAFAKSVEVQGETETIIATKTT--DVEGRLSALLQETKELKNEIKAL-------SEERTA-------- 873
Cdd:pfam10174 201 LDQKEKENIHLREELHRRNQLQPDPAKTKALQTVieMKDTKISSLERNIRDLEDEVQMLktngllhTEDREEeikqmevy 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 874 -------------IKEQLDSSNSTIAILQTEKDKLELEITDSKKEQDDLLVLLADQDQKILSLKNKLKDLGHPVEEEDEL 940
Cdd:pfam10174 281 kshskfmknkidqLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESF 360
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
644-940 |
1.12e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 644 TLEQHDNIVTHYknmireqdlqlEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHKDQYNLLKIQLGkdnqhqgsySEGAQ 723
Cdd:PRK02224 235 TRDEADEVLEEH-----------EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLE---------ELEEE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 724 MNGIQpEEIGRLREEIEELKRNQELLQSQLTEKDSMIENMKSSQTSGTNEQSSAIVSARD-SEQVAELKQELATLKSQLN 802
Cdd:PRK02224 295 RDDLL-AEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDlEERAEELREEAAELESELE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 803 SQSVEITKLQTEKQELLQKTEAFAKSVEVQGETETIIATKTTDVEGRLSALLQETKELKNEIKALsEERTAIKEQL---- 878
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTA-RERVEEAEALleag 452
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586798161 879 ----------DSSN-STIAILQTEKDKLELEITDSKKEQDDLlvlladqDQKIlslkNKLKDLghpVEEEDEL 940
Cdd:PRK02224 453 kcpecgqpveGSPHvETIEEDRERVEELEAELEDLEEEVEEV-------EERL----ERAEDL---VEAEDRI 511
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
730-900 |
1.57e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 730 EEIGRLREEIEELKRNQELLQSQLTEKDSMIENMKSSQTSGTNEQSSAIVSARDSEQVAELkQELATLKSQLNSQSVEIT 809
Cdd:COG4717 95 EELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERL-EELRELEEELEELEAELA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 810 KLQTEKQELLQKTeafakSVEVQGETETIIAtkttdvegRLSALLQETKELKNEIKALSEERTAIKEQLDSSNSTIAILQ 889
Cdd:COG4717 174 ELQEELEELLEQL-----SLATEEELQDLAE--------ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170
....*....|.
gi 586798161 890 TEKDKLELEIT 900
Cdd:COG4717 241 LEERLKEARLL 251
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
652-937 |
2.01e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.63 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 652 VTHYKNMIREQ----DLQLEELRQQvstlkcQNEQLQTaVTQQVSQIQQHKDQYNLLKIQLGKDNQH--------QGSYS 719
Cdd:pfam01576 329 VTELKKALEEEtrshEAQLQEMRQK------HTQALEE-LTEQLEQAKRNKANLEKAKQALESENAElqaelrtlQQAKQ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 720 EGAQMNGIQPEEIGRLREEIEELKRNQELLQSQLTEKDSMIENMKS--SQTSGTNEQSSAIVSARDSE--QVAELKQELA 795
Cdd:pfam01576 402 DSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSllNEAEGKNIKLSKDVSSLESQlqDTQELLQEET 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 796 TLKSQLNSQSVEITKLQTEKQELLQKTEAFAKSVEVQGETETIiatkttdvegRLSALLQETKELKNEIKALSEERTAIK 875
Cdd:pfam01576 482 RQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQA----------QLSDMKKKLEEDAGTLEALEEGKKRLQ 551
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 586798161 876 EQLDSSNSTIAILQTEKDKLELEITDSKKEQDDLLVLLADQDQKILSLKNKLKDLGHPVEEE 937
Cdd:pfam01576 552 RELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEE 613
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
660-875 |
3.74e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 660 REQDLQLEELRQQVSTLKCQNEQLQTAVT---QQVSQIQQHKDQYNLLKIQLgKDNQHQGSYSEGAQMNGIQPEEigRLR 736
Cdd:COG4717 312 ALEELEEEELEELLAALGLPPDLSPEELLellDRIEELQELLREAEELEEEL-QLEELEQEIAALLAEAGVEDEE--ELR 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 737 EEIEELKRNQELLQsQLTEKDSMIEnmkssqtsgtnEQSSAIVSARDSEQVAELKQELATLKSQLNSQSVEITKLQTEKQ 816
Cdd:COG4717 389 AALEQAEEYQELKE-ELEELEEQLE-----------ELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELA 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 586798161 817 ELLQKTEAFAKSvevqgetetiiatkttdveGRLSALLQETKELKNEIKALSEERTAIK 875
Cdd:COG4717 457 ELEAELEQLEED-------------------GELAELLQELEELKAELRELAEEWAALK 496
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
785-937 |
4.31e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 785 EQVAELKQELATLKSQLNSQSVEITKLQTEKQELLQKTEAF-AKSVEVQGETETIIATKttdvegRLSALLQETKELKNE 863
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVeARIKKYEEQLGNVRNNK------EYEALQKEIESLKRR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 586798161 864 IKALSEERTAIKEQLDSSNSTIAILQTEKDKLELEITDSKKEQDDllvLLADQDQKILSLKNKLKDLGHPVEEE 937
Cdd:COG1579 105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE---ELAELEAELEELEAEREELAAKIPPE 175
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
665-838 |
4.63e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 665 QLEELRQQVSTLKCQNEQLQTAVTQQVS---QIQQHKDQYNLLKIQLGKDNQHQGSYSEGAQMNGIQpEEIGRLREEIEE 741
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEEleeELEELEAELEELREELEKLEKLLQLLPLYQELEALE-AELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 742 LKRNQELLQSQLTEKDSMIENMKSSQTSGTNEQSSaiVSARDSEQVAELKQELATLKSQLNSQSVEITKLQTEKQELLQK 821
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQ--LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170
....*....|....*..
gi 586798161 822 TEAFAKSVEVQGETETI 838
Cdd:COG4717 229 LEQLENELEAAALEERL 245
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
730-930 |
5.86e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.27 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 730 EEIGRLREEIEELKRNQELLQSQLTEKDSMIENMKSSQtsgtNEQSSAIVSARDSEQVAELKQELATLKSQL--NSQSVE 807
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKL----QELKLKEQAKKALEYYQLKEKLELEEEYLLylDYLKLN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 808 ITKLQTEKQELLQKTEAFAKSVEVQGETETIIAT--KTTDVEGRLSALLQET-KELKNEIKALSEERTAIKEQLDSSNST 884
Cdd:pfam02463 236 EERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQvlKENKEEEKEKKLQEEElKLLAKEEEELKSELLKLERRKVDDEEK 315
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 586798161 885 IAILQTEKDKLELEITDSKKEQDDLLVLLADQDQKILSLKNKLKDL 930
Cdd:pfam02463 316 LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEL 361
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
655-927 |
6.81e-05 |
|
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: 46.94 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 655 YKNMIREQDLQLEELRQQVSTLKCQNEQ-------LQTAVTQQVSQIQQHKDQYNLLKIQL------GKDNQHQ------ 715
Cdd:TIGR04523 24 YKNIANKQDTEEKQLEKKLKTIKNELKNkekelknLDKNLNKDEEKINNSNNKIKILEQQIkdlndkLKKNKDKinklns 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 716 -------GSYSEGAQMNgIQPEEIGRLREEIEELKRNQELLQSQLTEKDSMIENmKSSQTSGTNEQSSAIVSARD--SEQ 786
Cdd:TIGR04523 104 dlskinsEIKNDKEQKN-KLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEK-LNNKYNDLKKQKEELENELNllEKE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 787 VAELKQELATLKSQLNSQSVEITKLQTEKQELLQKTEAFAKSVEVQGETETIIATKTTDvegrLSALLQETKELKNEIKA 866
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQE----INEKTTEISNTQTQLNQ 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586798161 867 LSEERTAIKEQLDSSNSTI-----AILQTEKD----KLELEITDSKKEQD---DLLVLLADQDQKILSLKNKL 927
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELeqnnkKIKELEKQlnqlKSEISDLNNQKEQDwnkELKSELKNQEKKLEEIQNQI 330
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
659-930 |
7.13e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 7.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 659 IREQDLQLEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHKDQYNLLKIQLGKDNQHQGSYSEG-----AQMNGIQpEEIG 733
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAElaqaqEELESLQ-EEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 734 RLREEIEELKRNQELLQSQLTEKDSMIENMKSSQTSGTNEQSSAivsardSEQVAELKQELATLKSQLNSQSV-----EI 808
Cdd:COG4372 112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL------EEQLESLQEELAALEQELQALSEaeaeqAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 809 TKLQTEKQELLQKTEAFAKSVEVQGETETIIATKTTDVEGRLSALLQETKELKNEIKALSEERTAIKEQLDSSNSTIAIL 888
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 586798161 889 QTEKDKLELEITDSKKEQDDLLVLLADQDQKILSLKNKLKDL 930
Cdd:COG4372 266 AILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAAL 307
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
645-925 |
7.32e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.97 E-value: 7.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 645 LEQHDNIVTHYKNMireqdlqlEELRQQVStLKCQNEQLQTAVTQQVSQIQQHKD----QYNLLKIQLGKDNQHQgsYSE 720
Cdd:TIGR01612 1432 LSEESNIDTYFKNA--------DENNENVL-LLFKNIEMADNKSQHILKIKKDNAtndhDFNINELKEHIDKSKG--CKD 1500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 721 GAQMNGIQPEeigRLREEIEELKRNQELLQSQLTEKDsmIENmKSSQTSGTNEQssaIVsardsEQVAELKQELaTLKSQ 800
Cdd:TIGR01612 1501 EADKNAKAIE---KNKELFEQYKKDVTELLNKYSALA--IKN-KFAKTKKDSEI---II-----KEIKDAHKKF-ILEAE 1565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 801 LNSQSV-EITKLQTEKQELLQKTEAFAKS-VEVQGETETIIAT--KTTDVEGRLSALLQETKELKNEIKALS--EERTAI 874
Cdd:TIGR01612 1566 KSEQKIkEIKKEKFRIEDDAAKNDKSNKAaIDIQLSLENFENKflKISDIKKKINDCLKETESIEKKISSFSidSQDTEL 1645
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 586798161 875 KEQLDSSNSTIAILQTEKDKlELEITDSKKEQDDLlvlladqDQKILSLKN 925
Cdd:TIGR01612 1646 KENGDNLNSLQEFLESLKDQ-KKNIEDKKKELDEL-------DSEIEKIEI 1688
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
730-909 |
1.08e-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: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 730 EEIGRLREEIEELKRNQELLQ---------SQLTEKDSMIENMKSSQTSGTNEQSSAIVSARdseqVAELKQELATLKSQ 800
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEpirelaeryAAARERLAELEYLRAALRLWFAQRRLELLEAE----LEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 801 LNSQSVEITKLQTEKQEL--------LQKTEAFAKSVEVQGETETIIATKTTDVEGRLSALlqeTKELKNEIKALSEERT 872
Cdd:COG4913 311 LERLEARLDALREELDELeaqirgngGDRLEQLEREIERLERELEERERRRARLEALLAAL---GLPLPASAEEFAALRA 387
|
170 180 190
....*....|....*....|....*....|....*..
gi 586798161 873 AIKEQLDSSNSTIAILQTEKDKLELEITDSKKEQDDL 909
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRRELREL 424
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
730-818 |
1.55e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.62 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 730 EEIGRLREEIEELKRNQELLQSQLTEKDSMIENMKSSQTSgtnEQSSAIVSARDSEQVAELKQELATLKSQLNSQSVEIT 809
Cdd:COG2433 413 EEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSE---ARSEERREIRKDREISRLDREIERLERELEEERERIE 489
|
....*....
gi 586798161 810 KLQTEKQEL 818
Cdd:COG2433 490 ELKRKLERL 498
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
856-930 |
1.59e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 1.59e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 586798161 856 ETKELKNEIKALSEERTAIKEQLDSSNSTIAILQTEKDKLELEITDSKKEQDDLLVLLADQDQKILSLKNKLKDL 930
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
644-905 |
1.76e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.48 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 644 TLEQHDNIVTH-YKNMIREQDLQLEELRQQ-------VSTLKCQNEQLQTAVTQQVSQIQQHKDQYNLLKIQLGKDNQHQ 715
Cdd:pfam05483 314 ALEEDLQIATKtICQLTEEKEAQMEELNKAkaahsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 716 gsysegaqmngiqpeeigrlrEEIEELKRNQEL----LQSQLTEKDSMIENMK-----SSQTSGTNEQSSAIVSARDSEq 786
Cdd:pfam05483 394 ---------------------EEMTKFKNNKEVeleeLKKILAEDEKLLDEKKqfekiAEELKGKEQELIFLLQAREKE- 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 787 VAELKQELATLKSQLNSQSVEITKLQTE-KQELLQKTEAFAKSVEVQGETETiiatkttdvegrlsaLLQETKELKNEIK 865
Cdd:pfam05483 452 IHDLEIQLTAIKTSEEHYLKEVEDLKTElEKEKLKNIELTAHCDKLLLENKE---------------LTQEASDMTLELK 516
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 586798161 866 ALSEERTAIKEQLDSSNSTIAILQTEKDKLELEITDSKKE 905
Cdd:pfam05483 517 KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREE 556
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
773-909 |
1.89e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 44.67 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 773 EQSSAIVSARDSEQVAELKQelaTLKSQLNSQSVEITKLQTEKQELLQKTEAFAKSVEVQGET----ETIIATKTTDVEG 848
Cdd:cd22656 98 ELIDDLADATDDEELEEAKK---TIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAletlEKALKDLLTDEGG 174
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 586798161 849 RLSAllQETKELKNEIKALSEE-RTAIKEQLDSSNSTIAILQTEKDKLELEITDSKKEQDDL 909
Cdd:cd22656 175 AIAR--KEIKDLQKELEKLNEEyAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDL 234
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
652-910 |
2.02e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.48 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 652 VTHYKNmirEQDLQLEELRQ---QVSTLKCQN-------EQLQTAVTQQVSQIQQHKDQYNLLKIQLGKDNQHQGSYSEg 721
Cdd:pfam05483 396 MTKFKN---NKEVELEELKKilaEDEKLLDEKkqfekiaEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLK- 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 722 aqmngiqpeEIGRLREEIEelkrNQELLQSQLTEKDSMI--ENMKSSQTSG------TNEQSSAIVSARDSE----QVAE 789
Cdd:pfam05483 472 ---------EVEDLKTELE----KEKLKNIELTAHCDKLllENKELTQEASdmtlelKKHQEDIINCKKQEErmlkQIEN 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 790 LKQELATLKSQLNSQSVEITKLQTEKQELLQKTEAFAKSVEVQ----GETETIIATKTTDVEGRLSALLQETKELKNEIK 865
Cdd:pfam05483 539 LEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEvlkkEKQMKILENKCNNLKKQIENKNKNIEELHQENK 618
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 586798161 866 ALSEERTAIKEQLDssnstiaILQTEKDKLELEITDSKKEQDDLL 910
Cdd:pfam05483 619 ALKKKGSAENKQLN-------AYEIKVNKLELELASAKQKFEEII 656
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
662-916 |
2.42e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.29 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 662 QDLQ--LEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHKdqyNLLKIqlGKDNQHQGSYSEGAQMNGIQPEEIGRLREEI 739
Cdd:PRK11281 138 QNAQndLAEYNSQLVSLQTQPERAQAALYANSQRLQQIR---NLLKG--GKVGGKALRPSQRVLLQAEQALLNAQNDLQR 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 740 EELKRN---QELLQSQLTEKdsmienmkssqtsgtneqssaivsardSEQVAELKQELATLKSQLNSQSVEITKLQTEKQ 816
Cdd:PRK11281 213 KSLEGNtqlQDLLQKQRDYL---------------------------TARIQRLEHQLQLLQEAINSKRLTLSEKTVQEA 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 817 ELLQKTEAFAKSVEVQGETET--------IIATKttdvegRLSALLQETKELKNEIKALSEERTAIKEQLDSSNSTIA-- 886
Cdd:PRK11281 266 QSQDEAARIQANPLVAQELEInlqlsqrlLKATE------KLNTLTQQNLRVKNWLDRLTQSERNIKEQISVLKGSLLls 339
|
250 260 270
....*....|....*....|....*....|.
gi 586798161 887 -ILQTEKDKLeleitdskkEQDDLLVLLADQ 916
Cdd:PRK11281 340 rILYQQQQAL---------PSADLIEGLADR 361
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
660-828 |
2.52e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 660 REQDLQLEELRQQVSTL----KCQNEQLQTAVTQQVSQIQQHKDQYNLLKIQLGKDNQHQGSYSEGAQMNGIQpEEIGRL 735
Cdd:COG4717 359 LEEELQLEELEQEIAALlaeaGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE-EELEEL 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 736 REEIEELKRNQELLQSQLTEKDSMIENMKSSQTsgtneqssaivsardseqVAELKQELATLKSQLNSQSVEITKLQTEk 815
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEEDGE------------------LAELLQELEELKAELRELAEEWAALKLA- 498
|
170
....*....|...
gi 586798161 816 QELLQKTEAFAKS 828
Cdd:COG4717 499 LELLEEAREEYRE 511
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
730-938 |
2.94e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 730 EEIGRLREEIEELKRNQELL------QSQLTEKDSMIENMKS--SQTSGTNEQSSAivsaRDSEQVAELKQELATLKSQL 801
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELekvlkkESELIKLKELAEQLKEleEKLKKYNLEELE----KKAEEYEKLKEKLIKLKGEI 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 802 NSQSVEITKLQTEKQELlqkteafaksvevqgeteTIIATKTTDVEGRLSALLQETKELKNE-IKALSEERTAIKE---- 876
Cdd:PRK03918 542 KSLKKELEKLEELKKKL------------------AELEKKLDELEEELAELLKELEELGFEsVEELEERLKELEPfyne 603
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 586798161 877 --QLDSSNSTIAILQTEKDKLELEITDSKKEqddllvlLADQDQKILSLKNKLKDLGHPVEEED 938
Cdd:PRK03918 604 ylELKDAEKELEREEKELKKLEEELDKAFEE-------LAETEKRLEELRKELEELEKKYSEEE 660
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
644-812 |
3.71e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 644 TLEQHDNIVTHYKNMIREQDLQ--LEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHKDQYNllkiqlgkdnqhqgsYSEG 721
Cdd:COG4913 273 ELEYLRAALRLWFAQRRLELLEaeLEELRAELARLEAELERLEARLDALREELDELEAQIR---------------GNGG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 722 AQMNGIQpEEIGRLREEIEELKRNQELLQSQL---------TEKD--SMIENMKSSQTSGTNEQSSAivsardSEQVAEL 790
Cdd:COG4913 338 DRLEQLE-REIERLERELEERERRRARLEALLaalglplpaSAEEfaALRAEAAALLEALEEELEAL------EEALAEA 410
|
170 180
....*....|....*....|..
gi 586798161 791 KQELATLKSQLNSQSVEITKLQ 812
Cdd:COG4913 411 EAALRDLRRELRELEAEIASLE 432
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
659-939 |
3.92e-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: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 659 IREQDLQLEELRQQvstLKCQNEQLQTAVTQ-QVSQIQQHKDQYNLLKIQLGKDNQHQGSYSEGAQMNGIQP------EE 731
Cdd:pfam01576 224 IAELQAQIAELRAQ---LAKKEEELQAALARlEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKqrrdlgEE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 732 IGRLREEIE----------EL--KRNQEL------LQSQLTEKDSMIENMKSSQTSGTNEQSSAIVSARDS--------- 784
Cdd:pfam01576 301 LEALKTELEdtldttaaqqELrsKREQEVtelkkaLEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNkanlekakq 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 785 ---EQVAELKQELATLKSQLNSQSVEITKLQTEKQELL--------QKTEAFAKSVEVQGETETiIATKTTDVEGR---- 849
Cdd:pfam01576 381 aleSENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQarlseserQRAELAEKLSKLQSELES-VSSLLNEAEGKnikl 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 850 ------LSALLQETKELKNE-----------IKALSEERTAIKEQLDSSNSTIAILQTEKDKLELEITDSKK--EQDDLL 910
Cdd:pfam01576 460 skdvssLESQLQDTQELLQEetrqklnlstrLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKklEEDAGT 539
|
330 340
....*....|....*....|....*....
gi 586798161 911 VLLADQDQKilSLKNKLKDLGHPVEEEDE 939
Cdd:pfam01576 540 LEALEEGKK--RLQRELEALTQQLEEKAA 566
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
727-939 |
4.16e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 727 IQPEEIGRLREEIEELKRNQEllqsQLTEKDSMIENMKSSQTSGTNEQSSAIVSARDSEQV-----AELKQElaTLKSQL 801
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKE----EIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEE--HRKELL 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 802 NSQSVEITKLQTEKQELLQKTEAFAKSVEvqgETETIIATkttdvEGRLSALLQETKELKN-----------EIKALSEE 870
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELR---ELEKVLKK-----ESELIKLKELAEQLKEleeklkkynleELEKKAEE 526
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586798161 871 RTAIKEQLDSSNSTIAILQTEKDKLEleitDSKKEQDDLLVLLADQDQKILSLKNKLKDLGHPVEEEDE 939
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKLE----ELKKKLAELEKKLDELEEELAELLKELEELGFESVEELE 591
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
841-916 |
4.71e-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: 4.71e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 586798161 841 TKTTDVEGRLSALLQETKELKNEIKALSEERTAIKEQLDSSNSTIAILQTEKDKLELEITDSKKEQDDLLVLLADQ 916
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
660-877 |
5.05e-04 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 43.09 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 660 REQDLQL-----EELRQQVSTLKCQNEQLQTavtqqvsQIQQHKDQYNLLKIQLGKDNQHQGSYSEGAQMNGIQPEEIGR 734
Cdd:pfam04849 78 KERDLELaarigQSLLKQNSVLTERNEALEE-------QLGSAREEILQLRHELSKKDDLLQIYSNDAEESETESSCSTP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 735 LREEIEELKRNQ----ELLQSQLteKDSMIENMK--------SSQTSGTNEQSSAIVS------ARDSEQVAELKQELAT 796
Cdd:pfam04849 151 LRRNESFSSLHGcvqlDALQEKL--RGLEEENLKlrseashlKTETDTYEEKEQQLMSdcveqlSEANQQMAELSEELAR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 797 LKSQLNSQSVEITKLQTEKQELLQKTEAFAksVEVQGETETIIATKttDVEGRLSALLQETKELKNEIKA-LSEERTAIK 875
Cdd:pfam04849 229 KMEENLRQQEEITSLLAQIVDLQHKCKELG--IENEELQQHLQASK--EAQRQLTSELQELQDRYAECLGmLHEAQEELK 304
|
..
gi 586798161 876 EQ 877
Cdd:pfam04849 305 EL 306
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
663-860 |
6.49e-04 |
|
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: 43.13 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 663 DLQLEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHKDQYNLLKIQLGKDNQHQGSYSEGAqmngiqpEEIGRLREEIEEL 742
Cdd:pfam15742 185 DQNVNELQQQVRSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKSNQELS-------EKLSSLQQEKEAL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 743 krnQELLQSQLTEKDSMIENMKSSQTSGTNEQSSA------IVSARDsEQVAELKQELATLKSQLNSQSVEITKLQTEKQ 816
Cdd:pfam15742 258 ---QEELQQVLKQLDVHVRKYNEKHHHHKAKLRRAkdrlvhEVEQRD-ERIKQLENEIGILQQQSEKEKAFQKQVTAQNE 333
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 586798161 817 ELLQKTEAFAKSVEVQGETETIIATKTTDVEGRLSALLQETKEL 860
Cdd:pfam15742 334 ILLLEKRKLLEQLTEQEELIKNNKRTISSVQNRVNFLDEENKQL 377
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
728-895 |
7.15e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 728 QPEEIGRLREEIEELKRNQELLqsqltekdsmienmKSSQTSGTNEQSSAIvsardSEQVAELKQELATLKSQLNSQSVE 807
Cdd:COG0542 409 KPEELDELERRLEQLEIEKEAL--------------KKEQDEASFERLAEL-----RDELAELEEELEALKARWEAEKEL 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 808 ITKLQTEKQELLQKteafaksvevqgetetiiatkttdvEGRLSALLQETKELKneiKALSEERTAIKEQLDSSNstIA- 886
Cdd:COG0542 470 IEEIQELKEELEQR-------------------------YGKIPELEKELAELE---EELAELAPLLREEVTEED--IAe 519
|
170 180
....*....|....*....|.
gi 586798161 887 ------------ILQTEKDKL 895
Cdd:COG0542 520 vvsrwtgipvgkLLEGEREKL 540
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
639-930 |
8.83e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.42 E-value: 8.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 639 EEVKKTLEQHDNivthykNMIREQDLQLEELRQQVST-------LKCQNEQLQTAVTQQ---VSQIQQHKDQYNLLKIQL 708
Cdd:pfam02463 172 KEALKKLIEETE------NLAELIIDLEELKLQELKLkeqakkaLEYYQLKEKLELEEEyllYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 709 GKDNQHQGSYSEGAQMNGIqpEEIGRLREEIEELKRNQELLQSQLTEKDSMIENMKSSQTsgTNEQSSAIvsarDSEQVA 788
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEE--EKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL--KLERRKVD----DEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 789 ELKQELATLKSQLNSQSVEITKLQTEKQELLQKTEAFAKSVEvqgETETIIATKTTDVEGRLSALLQETKELKNEIKALS 868
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE---ELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 586798161 869 EERTAIKEQLDSSNSTIAILQTEKDKLELEITDSKKEQDDLLVLLADQDQKILSLKNKLKDL 930
Cdd:pfam02463 395 EELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQ 456
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
659-909 |
9.28e-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: 43.27 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 659 IREQDLQLEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHKDQYNLLKIQLGKDNQHQGsysegaqmngiqpEEIGRLREE 738
Cdd:pfam10174 410 LRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERL-------------EELESLKKE 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 739 IEELKRNQELLQSQLTEKDSMIENMK---SSQTSGTNEQSSAIVSARDSEQVAelKQELATLKSQL-NSQSVEIT----- 809
Cdd:pfam10174 477 NKDLKEKVSALQPELTEKESSLIDLKehaSSLASSGLKKDSKLKSLEIAVEQK--KEECSKLENQLkKAHNAEEAvrtnp 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 810 ----KLQTEKQELLQKTEAFAKSvevQGETEtiiatkttdvegRLSALLQETKELKN----EIKAL-SEERTAIKEQLDS 880
Cdd:pfam10174 555 eindRIRLLEQEVARYKEESGKA---QAEVE------------RLLGILREVENEKNdkdkKIAELeSLTLRQMKEQNKK 619
|
250 260
....*....|....*....|....*....
gi 586798161 881 SNSTIAILQTEKDKLELEITDSKKEQDDL 909
Cdd:pfam10174 620 VANIKHGQQEMKKKGAQLLEEARRREDNL 648
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
665-931 |
1.53e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.19 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 665 QLEELRQQvstlkcQNEQLQTavtQQVSQIQQHKDQYNLLKIQLGKDNQHQGSYSEGAQMNgiqpEEIGRLREEIEELKR 744
Cdd:pfam07888 35 RLEECLQE------RAELLQA---QEAANRQREKEKERYKRDREQWERQRRELESRVAELK----EELRQSREKHEELEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 745 NQELLQsqltekdsmienmkSSQTSGTNEQSSAIVSARDSEQ-VAELKQELATLKSQLNSQSVEITKL-QTEKQELLQKT 822
Cdd:pfam07888 102 KYKELS--------------ASSEELSEEKDALLAQRAAHEArIRELEEDIKTLTQRVLERETELERMkERAKKAGAQRK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 823 EAFAKSVEVQGETETiiatkttdVEGRLSALLQETKELKNEIkalsEERTAIKEQLDSSNSTIAILQTEKDKLELEITDS 902
Cdd:pfam07888 168 EEEAERKQLQAKLQQ--------TEEELRSLSKEFQELRNSL----AQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
|
250 260
....*....|....*....|....*....
gi 586798161 903 KKEQDDLLVLLADQDQKILSLKNKLKDLG 931
Cdd:pfam07888 236 LEELRSLQERLNASERKVEGLGEELSSMA 264
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
730-940 |
1.58e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 730 EEIGRLREEIEELKRNQELLQSQLTEKDSMIENMKssqtsgtneqssaivsardsEQVAELKQELATLKSQLNSQSVEIT 809
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKE--------------------KELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 810 KLQTEKQELLQKTEAFAKSVEVQGETETIIATkttdVEGRLSALLQETKELKNEIKALSEERTAIKEqldssnstIAILQ 889
Cdd:PRK03918 225 KLEKEVKELEELKEEIEELEKELESLEGSKRK----LEEKIRELEERIEELKKEIEELEEKVKELKE--------LKEKA 292
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 586798161 890 TEKDKLELEITDSKKEQDDLLVLLADQDQKILSLKNKLKDLGHPVEEEDEL 940
Cdd:PRK03918 293 EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
664-865 |
2.19e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 40.27 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 664 LQLEELRQQVSTLKCQNEQLQTavTQQVSQIQQHKdqynllkiQLGKDNQHQGSYSEGAQMNGIQPEEIGRLREEIEELK 743
Cdd:pfam15619 11 HKIKELQNELAELQSKLEELRK--ENRLLKRLQKR--------QEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 744 RNQELLQSQLTEKDSMIEnmkssQTSGTNEQSSAIVSARDSEQVAELKQELATLKSQLNSQSVEITKLQtEKQELLQKTE 823
Cdd:pfam15619 81 EKERDLERKLKEKEAELL-----RLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLE-RKLELENKSF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 586798161 824 AFAKSVEVQgetetiiatKTTDVEGRLSALLQETKELKNEIK 865
Cdd:pfam15619 155 RRQLAAEKK---------KHKEAQEEVKILQEEIERLQQKLK 187
|
|
| Seryl_tRNA_N |
pfam02403 |
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ... |
807-885 |
2.22e-03 |
|
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA synthetase class II domain (pfam00587) and represents the N-terminal domain of seryl-tRNA synthetase.
Pssm-ID: 426757 [Multi-domain] Cd Length: 108 Bit Score: 38.72 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 807 EITKLQTEKQELLQKTEAF-AKSVEVQGEtetiIATKTTDVEGRlSALLQETKELKNEIKALSEERTAIKEQLDSSNSTI 885
Cdd:pfam02403 30 ELLELDEKRRELQVELEELqAERNELSKE----IGQAKKKKEDA-DALIAEVKELKDELKALEAELKELEAELDKLLLTI 104
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
661-927 |
2.35e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.75 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 661 EQDLQLEELRQQVSTLKCQNEQLQTAVTQQV-SQIQQHKDQYNLLKIQLG--KDNQHQGSYSEGAQMN-GIQPEEIGRLR 736
Cdd:pfam12128 398 KLAKIREARDRQLAVAEDDLQALESELREQLeAGKLEFNEEEYRLKSRLGelKLRLNQATATPELLLQlENFDERIERAR 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 737 EEIEELKRNQELLQSQLTEKDSMIENmkssqtsgtneqssAIVSARDSEQ-VAELKQELATLKSQLNSQSVEITK-LQTE 814
Cdd:pfam12128 478 EEQEAANAEVERLQSELRQARKRRDQ--------------ASEALRQASRrLEERQSALDELELQLFPQAGTLLHfLRKE 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 815 KQ------------ELLQKTEAFAKSVEVQGETETIIATKTTDVEgRLSA--LLQETKELKNEIKALSEERTAIKEQLDS 880
Cdd:pfam12128 544 APdweqsigkvispELLHRTDLDPEVWDGSVGGELNLYGVKLDLK-RIDVpeWAASEEELRERLDKAEEALQSAREKQAA 622
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 586798161 881 SNSTIAILQTEKDKLELEITDSK---KEQDDLLVLLADQDQkilSLKNKL 927
Cdd:pfam12128 623 AEEQLVQANGELEKASREETFARtalKNARLDLRRLFDEKQ---SEKDKK 669
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
789-879 |
2.57e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 41.21 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 789 ELKQELATLKSQLNSQSVEITKLQTEKQELlqkteafaksvevqgetetiiatkttdvegrlSALLQETKELKNEIKALS 868
Cdd:PRK05431 39 ELQTELEELQAERNALSKEIGQAKRKGEDA--------------------------------EALIAEVKELKEEIKALE 86
|
90
....*....|.
gi 586798161 869 EERTAIKEQLD 879
Cdd:PRK05431 87 AELDELEAELE 97
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
735-930 |
2.71e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 735 LREEIEELKRNQELLQSQLTEKDSMieNMKSSQTSGTNEQSSAIVSARDSEQVA---ELKQELATLKSQLNSQSVEITKL 811
Cdd:PRK01156 351 LNNQILELEGYEMDYNSYLKSIESL--KKKIEEYSKNIERMSAFISEILKIQEIdpdAIKKELNEINVKLQDISSKVSSL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 812 QTEKQELLQKTEAFAKSVEV-QGETETIIATKTTDVEG----------RLSALLQETKELKNEIKALSEERTAIKEQLDS 880
Cdd:PRK01156 429 NQRIRALRENLDELSRNMEMlNGQSVCPVCGTTLGEEKsnhiinhyneKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEY 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 586798161 881 SNS-TIAILQTEKDKLELEITDSKKEQDDlLVLLADQDQKILSLKNKLKDL 930
Cdd:PRK01156 509 LESeEINKSINEYNKIESARADLEDIKIK-INELKDKHDKYEEIKNRYKSL 558
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
779-939 |
3.33e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 779 VSARDSE--QVAELKQELATLKSQLNSQSVEITKLQTEKQELLQ-KTEAFAKSVEVQG-------ETETIIatktTDVEG 848
Cdd:pfam01576 7 MQAKEEElqKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQaETELCAEAEEMRArlaarkqELEEIL----HELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 849 RLSALLQETKELKNEIKALSEERTAIKEQLDSSNSTIAILQTEKDKLELEItdsKKEQDDLLvLLADQDQKILS----LK 924
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKI---KKLEEDIL-LLEDQNSKLSKerklLE 158
|
170
....*....|....*
gi 586798161 925 NKLKDLGHPVEEEDE 939
Cdd:pfam01576 159 ERISEFTSNLAEEEE 173
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
666-889 |
3.48e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.48 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 666 LEELRQQVStlkcqneQLQTAVTQQVSQIQQHKDQYNLLKIQLGKDNQHQGsysegaQMNGIQPEEIGRLREEIEElkrn 745
Cdd:COG3096 838 LAALRQRRS-------ELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLP------QANLLADETLADRLEELRE---- 900
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 746 qELLQSQltekdsmiENMKSSQTSG-TNEQSSAIVSA--RDSEQVAELKQELATLKSQLNSQSVEITKLqtekQELLQKT 822
Cdd:COG3096 901 -ELDAAQ--------EAQAFIQQHGkALAQLEPLVAVlqSDPEQFEQLQADYLQAKEQQRRLKQQIFAL----SEVVQRR 967
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586798161 823 EAFAKSVEVQgetetiIATKTTDVEGRLSALLQETKElkneikALSEERTAIKEQLDSSNSTIAILQ 889
Cdd:COG3096 968 PHFSYEDAVG------LLGENSDLNEKLRARLEQAEE------ARREAREQLRQAQAQYSQYNQVLA 1022
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
665-930 |
3.97e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 665 QLEELRQQVSTLKCQNEQLQTAVtQQVSQIQQHKDQYNLLKiqlgKDNQHQGSYSEGAQMNGIQPEEIGRLREEIEELKR 744
Cdd:COG4717 96 ELEELEEELEELEAELEELREEL-EKLEKLLQLLPLYQELE----ALEAELAELPERLEELEERLEELRELEEELEELEA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 745 NQELLQSQLTEKDSMIENMKSSQTSGTNEQSSAIvsardSEQVAELKQELATLKSQLNSQSVEITKLQTEK--------- 815
Cdd:COG4717 171 ELAELQEELEELLEQLSLATEEELQDLAEELEEL-----QQRLAELEEELEEAQEELEELEEELEQLENELeaaaleerl 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 816 QELLQKTEAFAKSVEVQGETETIIATKTTDVE---GRLSALLQETKELKNEIKALSEERTAIKEQLDSSNSTIAILQTEK 892
Cdd:COG4717 246 KEARLLLLIAAALLALLGLGGSLLSLILTIAGvlfLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELL 325
|
250 260 270
....*....|....*....|....*....|....*...
gi 586798161 893 DKLELEITDSKKEQDDLLVLLADQDQKILSLKNKLKDL 930
Cdd:COG4717 326 AALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
730-839 |
4.44e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.09 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 730 EEIGRLREEIEELKRNQELLQSQLtekdsmienmksSQTSGTNEQSSAIVSARDSEQvAELKQELATLKSQLNSQSVEit 809
Cdd:PRK11448 149 QEVLTLKQQLELQAREKAQSQALA------------EAQQQELVALEGLAAELEEKQ-QELEAQLEQLQEKAAETSQE-- 213
|
90 100 110
....*....|....*....|....*....|.
gi 586798161 810 klqtEKQELLQKTEAFAKSVEV-QGETETII 839
Cdd:PRK11448 214 ----RKQKRKEITDQAAKRLELsEEETRILI 240
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
665-962 |
4.62e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 665 QLEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHKDQYNLLKIQLGKdnqhqgsysegaqmngiQPEEIGRLREEIEELKR 744
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ-----------------LEEELEELNEQLQAAQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 745 NQELLQSQLTEKDSMIENMKSSQTSGTNEQSSAIvsardsEQVAELKQELATLKSQLNSQSVEITKLQTEKQELLQKTEA 824
Cdd:COG4372 95 ELAQAQEELESLQEEAEELQEELEELQKERQDLE------QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 825 FAKSVEVQGETETIIATKTTDVEGRLSALLQETKELKNEIKALSEERTAIKEQLDSSNSTIAILQTE---KDKLELEITD 901
Cdd:COG4372 169 LEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALsalLDALELEEDK 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 586798161 902 SKKEQDDLLVLLADQDQKILSLKNKLKDLGHPVEEEDELESGDQEDEDDESEDPGKDLDHI 962
Cdd:COG4372 249 EELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSL 309
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
669-821 |
4.72e-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: 39.14 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 669 LRQQVSTLKCQNEQLQTAVTQQVSQIQQHKdqynllkIQLGKDNQHQGSYSEgaqmngiqpEEIGRLREEIEELKRNQEL 748
Cdd:pfam08614 12 LLDRTALLEAENAKLQSEPESVLPSTSSSK-------LSKASPQSASIQSLE---------QLLAQLREELAELYRSRGE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 749 LQSQLTEKDSMIENM--KSSQTSGTNEQSSAIVSA-------RDSE------QVAELKQELATLKSQLNSQSVEITKLQT 813
Cdd:pfam08614 76 LAQRLVDLNEELQELekKLREDERRLAALEAERAQleeklkdREEElrekrkLNQDLQDELVALQLQLNMAEEKLRKLEK 155
|
....*...
gi 586798161 814 EKQELLQK 821
Cdd:pfam08614 156 ENRELVER 163
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
659-906 |
5.60e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 659 IREQDLQLEELRQQVSTLkcqnEQLQTAVTQQVSQIQQHKDQYNLLKiqlgkdnqhqgsysegaqmngiqpEEIGRLREE 738
Cdd:COG4913 670 IAELEAELERLDASSDDL----AALEEQLEELEAELEELEEELDELK------------------------GEIGRLEKE 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 739 IEELKRNQELLQSQLTEKDSMIENMKSSQTSGTNEQssAIVSARDSEQVAELKQELATLKSQLNSQSVEITKLQTE-KQE 817
Cdd:COG4913 722 LEQAEEELDELQDRLEAAEDLARLELRALLEERFAA--ALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfNRE 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 818 LLQKTEAFAKSVEVQGETETIIATKTTDV----EGRLSALL--QETKELKNEIKALSEERTAIKEQLDSSNstiAILQT- 890
Cdd:COG4913 800 WPAETADLDADLESLPEYLALLDRLEEDGlpeyEERFKELLneNSIEFVADLLSKLRRAIREIKERIDPLN---DSLKRi 876
|
250
....*....|....*....
gi 586798161 891 ---EKDKLELEITDSKKEQ 906
Cdd:COG4913 877 pfgPGRYLRLEARPRPDPE 895
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
646-882 |
7.02e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 646 EQHDNIVTHY---KNMIREQDLQLEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHKDQYNLLKIQLGKDNQhqgsysega 722
Cdd:TIGR02169 791 SRIPEIQAELsklEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG--------- 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 723 qmngiqpeEIGRLREEIEELKRNQELLQSQLTEKDSMIENMK---SSQTSGTNEQSSAIVSARDseQVAELKQELATLKS 799
Cdd:TIGR02169 862 --------KKEELEEELEELEAALRDLESRLGDLKKERDELEaqlRELERKIEELEAQIEKKRK--RLSELKAKLEALEE 931
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 800 QLNS------QSVEIT-------KLQTEKQELLQKTEAFaKSVEVQGETETiiatktTDVEGRLsallqetKELKNEIKA 866
Cdd:TIGR02169 932 ELSEiedpkgEDEEIPeeelsleDVQAELQRVEEEIRAL-EPVNMLAIQEY------EEVLKRL-------DELKEKRAK 997
|
250
....*....|....*.
gi 586798161 867 LSEERTAIKEQLDSSN 882
Cdd:TIGR02169 998 LEEERKAILERIEEYE 1013
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
659-939 |
7.81e-03 |
|
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: 40.34 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 659 IREQDLQLEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHKDqynlLKIQLgkdnqhqgsysegaqmngiqpeeiGRLREE 738
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRD----LQGQL------------------------AHAKKQ 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 739 IEELKRNQELLQSQLTEKdsmienmkssqtsgTNEQSSAIVSARDSEQ-VAELKQELATLKsQLNSQSVEITKLQTEKQE 817
Cdd:TIGR00618 433 QELQQRYAELCAAAITCT--------------AQCEKLEKIHLQESAQsLKEREQQLQTKE-QIHLQETRKKAVVLARLL 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 818 LLQKTEAFAKSVEVQGETETIIATKTTDVEGRLSALLQETKELKNEIKALSEERTAIKEQLDSSNSTIAILQTEKDKLEL 897
Cdd:TIGR00618 498 ELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQ 577
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 586798161 898 EITDSKKEQDDL---LVLLADQDQKILSLKNKLKDLGHPVEEEDE 939
Cdd:TIGR00618 578 CDNRSKEDIPNLqniTVRLQDLTEKLSEAEDMLACEQHALLRKLQ 622
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
694-888 |
7.95e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 38.73 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 694 IQQHKDQYNLLKIQLGKDNQHqgsYSEGAQMNGIQPEEIGRLREEIEELKRNqelLQSQltEKDSMI-ENMKSsqtsgtn 772
Cdd:pfam13851 28 IKSLKEEIAELKKKEERNEKL---MSEIQQENKRLTEPLQKAQEEVEELRKQ---LENY--EKDKQSlKNLKA------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 773 eqssaivsardseQVAELKQELATLKSQLNSQSVEITKLQTEKQELLQKteaFAKSV-EVQGET-------ETIIATKTT 844
Cdd:pfam13851 93 -------------RLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDK---FEAAIqDVQQKTglknlllEKKLQALGE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 586798161 845 DVEGRlSALLQETKELKN-EIKALSEERTAIKEQLDSSNSTIAIL 888
Cdd:pfam13851 157 TLEKK-EAQLNEVLAAANlDPDALQAVTEKLEDVLESKNQLIKDL 200
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
646-915 |
8.49e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 646 EQHDNIVTHYKNMIreqdlqlEELRQQVSTLKCQNEQLQTAVTQQVSQIQQHKDqynllkiQLGKDNQhqgsysegaqmn 725
Cdd:PHA02562 209 KKNGENIARKQNKY-------DELVEEAKTIKAEIEELTDELLNLVMDIEDPSA-------ALNKLNT------------ 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 726 giqpeEIGRLREEIEELKRNQELLQ---------SQLTEKDSMIENMKSSQTSGTNEQssaivsardsEQVAELKQELAT 796
Cdd:PHA02562 263 -----AAAKIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRITKIKDKLKELQHSL----------EKLDTAIDELEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 797 LKSQLNSQSVEITKLQTEkqellqkteafaksvevqgetetiIATKTTDvegrLSALLQETKELKNEIKALSEERTAIKE 876
Cdd:PHA02562 328 IMDEFNEQSKKLLELKNK------------------------ISTNKQS----LITLVDKAKKVKAAIEELQAEFVDNAE 379
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 586798161 877 QldssnstIAILQTEKDKLELEITDSKKEQDDLLV---LLAD 915
Cdd:PHA02562 380 E-------LAKLQDELDKIVKTKSELVKEKYHRGIvtdLLKD 414
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
730-895 |
8.85e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 39.63 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 730 EEIGRLREEIEELKRNQELLQS--QLTEKDS-----MIENMkssQTSGTNEQSSA------IVSARDSEQVAELKqelaT 796
Cdd:pfam05701 70 EELESTKRLIEELKLNLERAQTeeAQAKQDSelaklRVEEM---EQGIADEASVAakaqleVAKARHAAAVAELK----S 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586798161 797 LKSQLNSQSVEITKLQTEKQELLQKT-EAFAKSVE----VQGETETIIATK-------TTDVEG---RLSALL---QETK 858
Cdd:pfam05701 143 VKEELESLRKEYASLVSERDIAIKRAeEAVSASKEiektVEELTIELIATKeslesahAAHLEAeehRIGAALareQDKL 222
|
170 180 190
....*....|....*....|....*....|....*..
gi 586798161 859 ELKNEIKALSEERTAIKEQLDSSNSTIAILQTEKDKL 895
Cdd:pfam05701 223 NWEKELKQAEEELQRLNQQLLSAKDLKSKLETASALL 259
|
|
| |
