|
Name |
Accession |
Description |
Interval |
E-value |
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
573-754 |
1.91e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.49 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 573 YESEISSLKQKLEAKDISAVEEWKKKNEilaDRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRerfNAASSASKVLQ 652
Cdd:TIGR04523 293 LKSEISDLNNQKEQDWNKELKSELKNQE---KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSE---SENSEKQRELE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 653 ERIEEMRTSNKEKD---NTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNTTE 729
Cdd:TIGR04523 367 EKQNEIEKLKKENQsykQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446
|
170 180
....*....|....*....|....*
gi 568937276 730 NKLLDAHTQISDLKRTISKLEAQVK 754
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLK 471
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
575-761 |
2.77e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 57.72 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 575 SEISSLKQKLEAKDISAVEEWKKKNEILADRCGQLdSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQER 654
Cdd:TIGR04523 162 NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL-LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 655 IEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKE-----HGRVKDTLNTTE 729
Cdd:TIGR04523 241 INEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKELKSELKNQE 320
|
170 180 190
....*....|....*....|....*....|..
gi 568937276 730 NKLLDAHTQISDLKRTISKLEAQVKQAEHESM 761
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
551-757 |
3.90e-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: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 551 LSKIRQNLKEKHARHVADLRAYYESEISSLKQKLEAKDiSAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEKN---- 626
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAELQELE-EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqil 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 627 --------NNLLEIEVS---------DLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKL 689
Cdd:TIGR02168 308 rerlanleRQLEELEAQleeleskldELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568937276 690 SDDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNT-----TENKLLDAHTQISDLKRTISKLEAQVKQAE 757
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEllkklEEAELKELQAELEELEEELEELQEELERLE 460
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
551-759 |
8.97e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 8.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 551 LSKIRQNLKEKHARHVADLRAYYESEISSLKQKLEAKdISAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLL 630
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEEL-EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 631 EIEVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGE 710
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568937276 711 YESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHE 759
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
580-759 |
2.35e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 580 LKQKLEAKDIS-AVEEWKKKNEILAdrcgQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQERIEEM 658
Cdd:COG1196 218 LKEELKELEAElLLLKLRELEAELE----ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 659 RTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNTTENKLLDAHTQ 738
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180
....*....|....*....|.
gi 568937276 739 ISDLKRTISKLEAQVKQAEHE 759
Cdd:COG1196 374 LAEAEEELEELAEELLEALRA 394
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
608-759 |
3.31e-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: 52.23 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 608 QLDSALNEATSRVRTLEKnnnlleiEVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAY 687
Cdd:COG1579 14 ELDSELDRLEHRLKELPA-------ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937276 688 KlsddkearlrqeNKMFQDLLGEYESLGKEhgrvkdtLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHE 759
Cdd:COG1579 87 N------------NKEYEALQKEIESLKRR-------ISDLEDEILELMERIEELEEELAELEAELAELEAE 139
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
593-757 |
6.68e-07 |
|
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: 53.53 E-value: 6.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 593 EEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRL 672
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKEL 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 673 KCRLQDLEEAFENAYKLSDDKEARLRQENkmFQDLLGEYESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQ 752
Cdd:TIGR02169 764 EARIEELEEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
....*
gi 568937276 753 VKQAE 757
Cdd:TIGR02169 842 RIDLK 846
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
551-757 |
2.14e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 551 LSKIRQNLKE-----KHARHVADLRAYYEsEISSLKQKLEAKDISAVEEWKKKNEILADRCGQLD---SALNEATSRVRT 622
Cdd:PRK03918 475 ERKLRKELRElekvlKKESELIKLKELAE-QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKgeiKSLKKELEKLEE 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 623 LEKNNNLLEIEVSDLRERF--------NAASSASKVLQERIEEMR----------TSNKEKDNTITRLKCRLQDLEEAFE 684
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELaellkeleELGFESVEELEERLKELEpfyneylelkDAEKELEREEKELKKLEEELDKAFE 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 685 NAYKLSDD---KEARLRQENKMFQD-----LLGEYESLGKEHGRVKDTLNTTENklldahtQISDLKRTISKLEAQVKQA 756
Cdd:PRK03918 634 ELAETEKRleeLRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEK-------RREEIKKTLEKLKEELEER 706
|
.
gi 568937276 757 E 757
Cdd:PRK03918 707 E 707
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
574-759 |
2.65e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 574 ESEISSLKQKLEaKDISAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQE 653
Cdd:TIGR02168 781 EAEIEELEAQIE-QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 654 RIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNTTENKLL 733
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
170 180 190
....*....|....*....|....*....|....
gi 568937276 734 DAHTQIS--------DLKRTISKLEAQVKQAEHE 759
Cdd:TIGR02168 940 NLQERLSeeysltleEAEALENKIEDDEEEARRR 973
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
574-759 |
3.65e-06 |
|
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: 50.79 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 574 ESEISSLKQKLEAKDiSAVEEWKKKNEILADRCGQLDSALNEATS--------------RVRTLEKNNNLLEIEVSDLRE 639
Cdd:TIGR04523 355 ESENSEKQRELEEKQ-NEIEKLKKENQSYKQEIKNLESQINDLESkiqnqeklnqqkdeQIKKLQQEKELLEKEIERLKE 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 640 RFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLgkehg 719
Cdd:TIGR04523 434 TIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEL----- 508
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568937276 720 rvkdtlnttENKLLDAHTQISDLKRTISKLEAQVKQAEHE 759
Cdd:TIGR04523 509 ---------EEKVKDLTKKISSLKEKIEKLESEKKEKESK 539
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
577-749 |
4.52e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.59 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 577 ISSLKQKLEAKDISAvEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQERIE 656
Cdd:pfam10174 326 IEVLKESLTAKEQRA-AILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 657 EMRTSNKEKDNTITRLKCRLQDLEE----------AFENAykLSdDKE---ARLR-QENKMFQDLLGEYESLGKEHGRVK 722
Cdd:pfam10174 405 NLQEQLRDKDKQLAGLKERVKSLQTdssntdtaltTLEEA--LS-EKEriiERLKeQREREDRERLEELESLKKENKDLK 481
|
170 180
....*....|....*....|....*..
gi 568937276 723 DTLNTTENKLLDAHTQISDLKRTISKL 749
Cdd:pfam10174 482 EKVSALQPELTEKESSLIDLKEHASSL 508
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
560-757 |
4.71e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 560 EKHARHVADLRAYYESEISSLKQKLEAKdiSAVEEWKKKNEilaDRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRE 639
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRT--ENIEELIKEKE---KELEEVLREINEISSELPELREELEKLEKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 640 RFnaassaskvlqERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMfQDLLGEYESLGKEHG 719
Cdd:PRK03918 236 LK-----------EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL-KEKAEEYIKLSEFYE 303
|
170 180 190
....*....|....*....|....*....|....*...
gi 568937276 720 RVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAE 757
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE 341
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
576-762 |
4.77e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 576 EISSLKQKLEAKDiSAVEEWKKKNEILAdrcgQLDSALNEATSRVRTLEKNNNLLE--IEVSDLRERFNAASSASKVLQE 653
Cdd:COG4717 72 ELKELEEELKEAE-EKEEEYAELQEELE----ELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 654 RIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQEnkmFQDLLGEYESLGKEHGRVKDTLNTTENKLL 733
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE---LQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180
....*....|....*....|....*....
gi 568937276 734 DAHTQISDLKRTISKLEAQVKQAEHESML 762
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEARLLL 252
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
551-757 |
5.62e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 5.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 551 LSKIRQNLKEKHARHVADLrAYYESEISSLKQKLEA-KDISAVEEWKKKN---EILADRCGQLDSALNEATSRVRTLEKN 626
Cdd:TIGR02169 749 LEQEIENVKSELKELEARI-EELEEDLHKLEEALNDlEARLSHSRIPEIQaelSKLEEEVSRIEARLREIEQKLNRLTLE 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 627 NNLLEIEVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEafenayKLSDDKEARLRQENKMfqd 706
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES------RLGDLKKERDELEAQL--- 898
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568937276 707 llgeyeslgkehGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAE 757
Cdd:TIGR02169 899 ------------RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
554-778 |
6.07e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 554 IRQNLKEKHARhVADLRAYYESEISSLKQKLEAKDiSAVEEWKKKNEI---------LADRCGQLDSALNEAT------- 617
Cdd:COG3206 162 LEQNLELRREE-ARKALEFLEEQLPELRKELEEAE-AALEEFRQKNGLvdlseeaklLLQQLSELESQLAEARaelaeae 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 618 SRVRTLEKNNNL-----------------------LEIEVSDLRERFNAASSASKVLQERIEEMRTS-NKEKDNTITRLK 673
Cdd:COG3206 240 ARLAALRAQLGSgpdalpellqspviqqlraqlaeLEAELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILASLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 674 CRLQDLEEAfENAYKlsdDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNTTENKLldahtqisdlkrtiskLEAQV 753
Cdd:COG3206 320 AELEALQAR-EASLQ---AQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRL----------------EEARL 379
|
250 260
....*....|....*....|....*
gi 568937276 754 KQAEHESMLSLRNGAKVPERPSRSN 778
Cdd:COG3206 380 AEALTVGNVRVIDPAVVPLKPVSPK 404
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
573-759 |
7.08e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 7.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 573 YESEISSLKQKLEAKD--ISAVEEwkkKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKV 650
Cdd:TIGR02168 244 LQEELKEAEEELEELTaeLQELEE---KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 651 LQERIEemrtsnkEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNTTEN 730
Cdd:TIGR02168 321 LEAQLE-------ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
170 180
....*....|....*....|....*....
gi 568937276 731 KLLDAHTQISDLKRTISKLEAQVKQAEHE 759
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQE 422
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
550-757 |
1.13e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 550 MLSKIRQNLKEKhARHVADLRAYY---ESEISSLKQKLEAKDIsAVEEWKKKNEILADRCGQLDSALNEA-------TSR 619
Cdd:TIGR02168 713 ELEQLRKELEEL-SRQISALRKDLarlEAEVEQLEERIAQLSK-ELTELEAEIEELEERLEEAEEELAEAeaeieelEAQ 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 620 VRTLEKNNNLLEIEVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQ 699
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568937276 700 ENKMFQDLLGEYESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAE 757
Cdd:TIGR02168 871 LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
555-755 |
1.81e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 555 RQNLKEKHARHVADLRAYYESEISSLKQKLEaKDISAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEV 634
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 635 SDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESL 714
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568937276 715 GKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQ 755
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
567-757 |
2.50e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 567 ADLRAYYESEISSLKQKLEAKDISAVEEWKKKNEILADRcGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASS 646
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL-AALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 647 ASKVLQERIEEM-----RTSN------------------------------KEKDNTITRLKCRLQDLEEAFENAYKLSD 691
Cdd:COG4942 98 ELEAQKEELAELlralyRLGRqpplalllspedfldavrrlqylkylaparREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937276 692 DKEARLRQENKMFQDLLGEYESLGKehgRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAE 757
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLA---RLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
569-772 |
3.01e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 569 LRAYYES--EISSLKQKLEaKDISAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASS 646
Cdd:PRK02224 243 LEEHEERreELETLEAEIE-DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELED 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 647 ASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEE--------------AFENAYKLSDDKEARLRQENKMFQDLLGEYE 712
Cdd:PRK02224 322 RDEELRDRLEECRVAAQAHNEEAESLREDADDLEEraeelreeaaelesELEEAREAVEDRREEIEELEEEIEELRERFG 401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 713 SLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEhesmlSLRNGAKVPE 772
Cdd:PRK02224 402 DAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAE-----ALLEAGKCPE 456
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
550-817 |
4.80e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 550 MLSKIRQNLkEKHARHVADLRAYyeSEISSLKQKLEAKDISAveEWKKKNEILADRCGQLDSA---LNEATSRVRTLEKN 626
Cdd:TIGR02169 192 IIDEKRQQL-ERLRREREKAERY--QALLKEKREYEGYELLK--EKEALERQKEAIERQLASLeeeLEKLTEEISELEKR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 627 NNLLEIEVSDLRERFNAASSASKV-LQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQ 705
Cdd:TIGR02169 267 LEEIEQLLEELNKKIKDLGEEEQLrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 706 DLLGEYESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHESMLSLRNGAKVPERPSRsnsvATSDV 785
Cdd:TIGR02169 347 EERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR----LSEEL 422
|
250 260 270
....*....|....*....|....*....|..
gi 568937276 786 SRRKWLIPGAEysiftGQPLDPRDRKLDKQLE 817
Cdd:TIGR02169 423 ADLNAAIAGIE-----AKINELEEEKEDKALE 449
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
602-773 |
7.51e-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: 45.30 E-value: 7.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 602 LADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQERIEEMR------TSNKEKDN---TITRL 672
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlgnvRNNKEYEAlqkEIESL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 673 KCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKEhgrvkdtlnttenklLDAhtQISDLKRTISKLEAQ 752
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---------------LDE--ELAELEAELEELEAE 164
|
170 180
....*....|....*....|.
gi 568937276 753 VKQAEhesmlslrngAKVPER 773
Cdd:COG1579 165 REELA----------AKIPPE 175
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
552-757 |
8.35e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 8.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 552 SKIRQNLKEKHARHVADLRAYyeSEISSLKQKLEAKdISAVEEWKKKNEILADRcgqldsaLNEATSRVRTLEKNNNLLE 631
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREI--NEISSELPELREE-LEKLEKEVKELEELKEE-------IEELEKELESLEGSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 632 IEVSDLRERFNAASSASKVLQERI----------EEMRTSNKEKDNT---ITRLKCRLQDLEEAFENAYKLSDD---KEA 695
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVkelkelkekaEEYIKLSEFYEEYldeLREIEKRLSRLEEEINGIEERIKEleeKEE 338
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937276 696 RLRQENKMFQDLLGEYESLGKEHgRVKDTLNTTENKLLDAHTQISDLkrTISKLEAQVKQAE 757
Cdd:PRK03918 339 RLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGL--TPEKLEKELEELE 397
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
551-759 |
8.90e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 551 LSKIRQNLKEKHARHVADLRAYyESEISSLKQKLEAKDIsAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLL 630
Cdd:COG1196 244 LEAELEELEAELEELEAELAEL-EAELEELRLELEELEL-ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 631 EIEVSDLRERFNAassaskvLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGE 710
Cdd:COG1196 322 EEELAELEEELEE-------LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568937276 711 YESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHE 759
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
551-714 |
9.61e-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: 44.92 E-value: 9.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 551 LSKIRQNLKEkHARHVADLrayyESEISSLKQKLEA--KDISAVEEWKKKNEILADrcgQLDSALNEATSRVRTLEKNNN 628
Cdd:COG1579 19 LDRLEHRLKE-LPAELAEL----EDELAALEARLEAakTELEDLEKEIKRLELEIE---EVEARIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 629 L--LEIEVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQE-----N 701
Cdd:COG1579 91 YeaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEreelaA 170
|
170
....*....|...
gi 568937276 702 KMFQDLLGEYESL 714
Cdd:COG1579 171 KIPPELLALYERI 183
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
574-760 |
1.55e-04 |
|
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: 43.74 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 574 ESEISSLKQKLEakdisaveEWKKKNEILADRCGQLDSALNeatsrvRTLEKNNNLLEI------EVSDLRERFnaassa 647
Cdd:pfam15619 17 QNELAELQSKLE--------ELRKENRLLKRLQKRQEKALG------KYEGTESELPQLiarhneEVRVLRERL------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 648 sKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEeafenayKLSDDK---------------EARLRQENKMFQDLLGEYE 712
Cdd:pfam15619 77 -RRLQEKERDLERKLKEKEAELLRLRDQLKRLE-------KLSEDKnlaereelqkkleqlEAKLEDKDEKIQDLERKLE 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568937276 713 SLGKEHGRvkdTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHES 760
Cdd:pfam15619 149 LENKSFRR---QLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
566-755 |
2.07e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 566 VADLRAYYESEISSLKQK---LEAkDISAVEEWKKKNEILAD-----RCGQ--LDS----ALNEATSRVRTLEKNNNLLE 631
Cdd:PRK02224 410 AEDFLEELREERDELREReaeLEA-TLRTARERVEEAEALLEagkcpECGQpvEGSphveTIEEDRERVEELEAELEDLE 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 632 IEVSDLRERFNAASSASKV-------------LQERIEEMRTSNKEKDNTITRLKCRLQDLEEAfenayklSDDKEARLR 698
Cdd:PRK02224 489 EEVEEVEERLERAEDLVEAedrierleerredLEELIAERRETIEEKRERAEELRERAAELEAE-------AEEKREAAA 561
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568937276 699 QENKMFQDLLGEYESLGKEHGRVKDTLNTTeNKLLDAHTQISDLKRTISKLEAQVKQ 755
Cdd:PRK02224 562 EAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREA 617
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
633-759 |
2.27e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 633 EVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQEN-------KMFQ 705
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQeeaeelqEELE 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 568937276 706 DLLGEYESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHE 759
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
594-765 |
2.73e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 44.24 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 594 EWKKKneILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQERIEEMrtsNKEKDNTITRLK 673
Cdd:smart00787 136 EWRMK--LLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDEL---EDCDPTELDRAK 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 674 CRLQDLEEAFENAYKLSDDKEARLRQenkmfqdllgeyeslgkehgrVKDTLNTTENKLLDAHTQISDLKRT-------- 745
Cdd:smart00787 211 EKLKKLLQEIMIKVKKLEELEEELQE---------------------LESKIEDLTNKKSELNTEIAEAEKKleqcrgft 269
|
170 180
....*....|....*....|...
gi 568937276 746 ---ISKLEAQVKQAEHESMLSLR 765
Cdd:smart00787 270 fkeIEKLKEQLKLLQSLTGWKIT 292
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
557-759 |
2.95e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 557 NLKEKHARHVADLRAYYESEISSLKQKLEAKDISaVEEWKKKNEILADrcgQLDSALNEATSRVRTLEKNNNLLEIEVSD 636
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI-IKNLDNTRESLET---QLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 637 LRERFNAASSAS---KVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFEnayKLSDDK-----EARLRQENKMFQDLL 708
Cdd:TIGR04523 498 LKKLNEEKKELEekvKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN---KDDFELkkenlEKEIDEKNKEIEELK 574
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568937276 709 GEYESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHE 759
Cdd:TIGR04523 575 QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
592-766 |
3.30e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 592 VEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERfnaASSASKVLQERIEEMRTSNKEKDNTITR 671
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREE---AQELREKRDELNEKVKELKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 672 LKCRLQDLEEAFENAYKLSDDK------EARLRQENKMFQ----------DLLGEYESLGKEHGRVKDtLNTTENKLLDA 735
Cdd:COG1340 87 LNELREELDELRKELAELNKAGgsidklRKEIERLEWRQQtevlspeeekELVEKIKELEKELEKAKK-ALEKNEKLKEL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 568937276 736 HTQISDLKRTISKLEAQVK------QAEHESMLSLRN 766
Cdd:COG1340 166 RAELKELRKEAEEIHKKIKelaeeaQELHEEMIELYK 202
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
566-756 |
3.34e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 566 VADLRAYYESEISSLKQKLEAKDISA-------------VEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEI 632
Cdd:PRK02224 312 VEARREELEDRDEELRDRLEECRVAAqahneeaeslredADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 633 EVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAyklsddkeARLRQENK---MFQDLLG 709
Cdd:PRK02224 392 EIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEA--------EALLEAGKcpeCGQPVEG 463
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568937276 710 EYESLGKEHGRVKdtLNTTENKLLDAHTQISDLKRTISKLEAQVKQA 756
Cdd:PRK02224 464 SPHVETIEEDRER--VEELEAELEDLEEEVEEVEERLERAEDLVEAE 508
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
563-763 |
4.46e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 563 ARHVADLRAYYESEISSLKQKLEAKDISAVEEWKKkneiLADRCGQLDSALNEATSRVRTLEKNNnlLEIEVSDLRERFN 642
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLE----LLDRIEELQELLREAEELEEELQLEE--LEQEIAALLAEAG 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 643 AASSASkvLQERIEEMRtsnkekdntitrlkcRLQDLEEAFENAyklsddkEARLRQENKMFQDLLgeyESLGKEhgRVK 722
Cdd:COG4717 381 VEDEEE--LRAALEQAE---------------EYQELKEELEEL-------EEQLEELLGELEELL---EALDEE--ELE 431
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568937276 723 DTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHESMLS 763
Cdd:COG4717 432 EELEELEEELEELEEELEELREELAELEAELEQLEEDGELA 472
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
619-700 |
4.63e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.37 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 619 RVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQER-IEEMRtsNKEKDNTITRLKCRLQ--DLEEAFENaYKLSDDKEA 695
Cdd:pfam00038 19 KVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKeIEDLR--RQLDTLTVERARLQLEldNLRLAAED-FRQKYEDEL 95
|
....*
gi 568937276 696 RLRQE 700
Cdd:pfam00038 96 NLRTS 100
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
551-711 |
7.42e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 551 LSKIRQNLKEKHARHVADLrayyESEISSL----KQKLEAKDI-SAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEK 625
Cdd:PRK03918 572 LAELLKELEELGFESVEEL----EERLKELepfyNEYLELKDAeKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 626 NNNLLEIEVSD-----LRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKE--ARLR 698
Cdd:PRK03918 648 ELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALErvEELR 727
|
170
....*....|...
gi 568937276 699 QENKMFQDLLGEY 711
Cdd:PRK03918 728 EKVKKYKALLKER 740
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
610-744 |
8.74e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.65 E-value: 8.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 610 DSALNEATSRVR------TLEKNNNL-LEIEVSDLRERFNAASSaskvLQERIEEMRTsnkEKDNTITRLKCRLQDLEEA 682
Cdd:PRK09039 52 DSALDRLNSQIAeladllSLERQGNQdLQDSVANLRASLSAAEA----ERSRLQALLA---ELAGAGAAAEGRAGELAQE 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568937276 683 FENAYKLSDDKEARLrqenkmfqDLLGE-YESLGKEHGRVKDTLNTTENKLLDAHTQISDLKR 744
Cdd:PRK09039 125 LDSEKQVSARALAQV--------ELLNQqIAALRRQLAALEAALDASEKRDRESQAKIADLGR 179
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
651-759 |
1.28e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 651 LQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMF-------QDLLGEYESLGKEHGRVKD 723
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLarleaevEQLEERIAQLSKELTELEA 761
|
90 100 110
....*....|....*....|....*....|....*.
gi 568937276 724 TLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHE 759
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
567-738 |
1.28e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 567 ADLRAYYESEISSLKQKLEA--KDISAVEEWKKKNEILADRCGQLDsALNEATSRVRTLEKnnnllEI-EVSDLRERFNA 643
Cdd:COG4913 609 RAKLAALEAELAELEEELAEaeERLEALEAELDALQERREALQRLA-EYSWDEIDVASAER-----EIaELEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 644 ASSASKVLQERIE----EMRTSNKEKD---NTITRLKCRLQDLEEAFENAYKLSDDKEARLRQE-----NKMFQDLLGE- 710
Cdd:COG4913 683 SSDDLAALEEQLEeleaELEELEEELDelkGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElrallEERFAAALGDa 762
|
170 180 190
....*....|....*....|....*....|...
gi 568937276 711 -----YESLGKEHGRVKDTLNTTENKLLDAHTQ 738
Cdd:COG4913 763 verelRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
541-757 |
1.98e-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: 42.26 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 541 SLASLEDPVMLSKIRQNlKEKHARHVADLRAYYESEISSLKQKLEAKDISAVEEWKKKNEILadrcgqldsalNEATSRV 620
Cdd:TIGR00618 664 ALSIRVLPKELLASRQL-ALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIE-----------NASSSLG 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 621 RTLEKNNNLLEIEVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQE 700
Cdd:TIGR00618 732 SDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQE 811
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568937276 701 NKMFQD-LLGEYESLGKEhgrvkdtLNTTENKLLDAHTQISDLKRTISKLEAQVKQAE 757
Cdd:TIGR00618 812 IPSDEDiLNLQCETLVQE-------EEQFLSRLEEKSATLGEITHQLLKYEECSKQLA 862
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
576-759 |
2.39e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 576 EISSLKQKLEAKDISAVEEWKKKNEILADRCGQLDSALNEAtsrvRTLEKNNNLLEIEVSDL-RERFNAASSASKVLQER 654
Cdd:PHA02562 189 KIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEA----KTIKAEIEELTDELLNLvMDIEDPSAALNKLNTAA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 655 IE---EMRTSNKE----KDNTItrlkCR--LQDLEEAFENAYKLSDdKEARLRQENKMFQDLLGEYESLgkehgrvKDTL 725
Cdd:PHA02562 265 AKiksKIEQFQKVikmyEKGGV----CPtcTQQISEGPDRITKIKD-KLKELQHSLEKLDTAIDELEEI-------MDEF 332
|
170 180 190
....*....|....*....|....*....|....
gi 568937276 726 NTTENKLLDAHTQISDLKRTISKLEAQVKQAEHE 759
Cdd:PHA02562 333 NEQSKKLLELKNKISTNKQSLITLVDKAKKVKAA 366
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
551-759 |
2.55e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 551 LSKIRQNLKEKHAR---HVADLRAYyESEISSLKQKLEAKDISAVEEwKKKNEILADRCGQLDSALNEATSRVRTLEKNN 627
Cdd:COG1196 276 LEELELELEEAQAEeyeLLAELARL-EQDIARLEERRRELEERLEEL-EEELAELEEELEELEEELEELEEELEEAEEEL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 628 NLLEIEVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAyklsDDKEARLRQENKMFQD- 706
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL----LERLERLEEELEELEEa 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568937276 707 ---LLGEYESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHE 759
Cdd:COG1196 430 laeLEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
556-773 |
2.58e-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: 41.42 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 556 QNLKEKHARHVADL-RAYYESEISSLKQKLEAKdiSAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEV 634
Cdd:pfam07888 33 QNRLEECLQERAELlQAQEAANRQREKEKERYK--RDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 635 SDLRERFNAASSASKVLQERIEEMRTSNK-------EKDNTITRLKCRLQDL------EEAFENAYKLS-DDKEARLRQE 700
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKtltqrvlERETELERMKERAKKAgaqrkeEEAERKQLQAKlQQTEEELRSL 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568937276 701 NKMFQDLLGEYESLGKEHGRVKDTLNTTENKLLDAHTQISDLkrtiskleaqvkQAEHESMLSLRNGAKVPER 773
Cdd:pfam07888 191 SKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEN------------EALLEELRSLQERLNASER 251
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
567-752 |
3.13e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 567 ADLRAY--YESEISSLKQKLEAK-DISAVeewkkKNEILAdrcGQ-LDSALNEATSRVRTLEKNNNLL-----EIEVSDL 637
Cdd:COG2433 340 AALKAYdaYKNKFERVEKKVPPDvDRDEV-----KARVIR---GLsIEEALEELIEKELPEEEPEAERekeheERELTEE 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 638 RERFnaassasKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEafenayKLsddKEARLRQENKMFQDllGEYESLGKE 717
Cdd:COG2433 412 EEEI-------RRLEEQVERLEAEVEELEAELEEKDERIERLER------EL---SEARSEERREIRKD--REISRLDRE 473
|
170 180 190
....*....|....*....|....*....|....*
gi 568937276 718 HGRVKDTLNTTENKLLDAHTQISDLKRTIsKLEAQ 752
Cdd:COG2433 474 IERLERELEEERERIEELKRKLERLKELW-KLEHS 507
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
526-661 |
3.52e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 526 QSQLPGTANSVPECIS----------LASLEdpVMLSKIRQNLKEKHARhVADLRAyyesEISSLKQKLEAKDISAVEEW 595
Cdd:COG3206 246 RAQLGSGPDALPELLQspviqqlraqLAELE--AELAELSARYTPNHPD-VIALRA----QIAALRAQLQQEAQRILASL 318
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937276 596 KKKNEILADRCGQLDSALNEATSRVRTLeknnNLLEIEVSDLRERFNAASSASKVLQERIEEMRTS 661
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAEL----PELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
605-757 |
4.10e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 605 RCGQLDSALNEATSRVRTLEK----------NNNLLEI--EVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRL 672
Cdd:PRK03918 133 RQGEIDAILESDESREKVVRQilglddyenaYKNLGEVikEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 673 KCRLQDLEEAFENayklsddkearLRQENKMFQDLLGEYESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQ 752
Cdd:PRK03918 213 SSELPELREELEK-----------LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK 281
|
....*
gi 568937276 753 VKQAE 757
Cdd:PRK03918 282 VKELK 286
|
|
| cdk7 |
TIGR00570 |
CDK-activating kinase assembly factor MAT1; All proteins in this family for which functions ... |
656-807 |
4.36e-03 |
|
CDK-activating kinase assembly factor MAT1; All proteins in this family for which functions are known are cyclin dependent protein kinases that are components of TFIIH, a complex that is involved in nucleotide excision repair and transcription initiation. Also known as MAT1 (menage a trois 1). 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: 129661 [Multi-domain] Cd Length: 309 Bit Score: 40.17 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 656 EEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKL-SDDKEARLRQENKMFQDllgeyESLGKEHGRvKDTLNTTENKLLD 734
Cdd:TIGR00570 120 KKIETYQKENKDVIQKNKEKSTREQEELEEALEFeKEEEEQRRLLLQKEEEE-----QQMNKRKNK-QALLDELETSTLP 193
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568937276 735 AHTQISDLKRTISKLEAQVKQAEHESMLSLRNGAKVPERPSRSNsvatsdvsrrkwlIPGAEYSIFTGQPLDP 807
Cdd:TIGR00570 194 AAELIAQHKKNSVKLEMQVEKPKPEKPNTFSTGIKMGYQISLVP-------------VQKSEEALYPYQPLNI 253
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
542-735 |
5.39e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 39.35 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 542 LASLEDPVMLSKIrQNLKEKHARHVADLRAYYE--SEISSLKQKLEAKDISAVEEWKKKNEILADRCGQLdsaLNEATSR 619
Cdd:cd00176 23 LSSTDYGDDLESV-EALLKKHEALEAELAAHEErvEALNELGEQLIEEGHPDAEEIQERLEELNQRWEEL---RELAEER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 620 VRTLEknnnlleiEVSDLRERFNAASSASKVLQERIEEMRTSNKEKD-NTITRLKCRLQDLEEAFENayklsddKEARLR 698
Cdd:cd00176 99 RQRLE--------EALDLQQFFRDADDLEQWLEEKEAALASEDLGKDlESVEELLKKHKELEEELEA-------HEPRLK 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 568937276 699 QENKMFQDLLGEYESLGKEHGRVK-DTLNTTENKLLDA 735
Cdd:cd00176 164 SLNELAEELLEEGHPDADEEIEEKlEELNERWEELLEL 201
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
558-770 |
5.62e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.48 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 558 LKEKHARhVADLRAYYESEISSLKQKLEAKDISAVEEWKKKNEiladrcgqLDSALNEATSRVRTLEKNNNLLEIEVSDL 637
Cdd:pfam05483 217 LKEDHEK-IQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKD--------LTFLLEESRDKANQLEEKTKLQDENLKEL 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 638 RERFNAassaskvLQERIEEMRTSNKEKDNTITRLKcrlQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKE 717
Cdd:pfam05483 288 IEKKDH-------LTKELEDIKMSLQRSMSTQKALE---EDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEAT 357
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568937276 718 HGRVKDTLNTTENKLLDAHTQISdlkrtISKLEAQVKQAEHESMLSLRNGAKV 770
Cdd:pfam05483 358 TCSLEELLRTEQQRLEKNEDQLK-----IITMELQKKSSELEEMTKFKNNKEV 405
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
602-766 |
6.03e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 602 LADRCGQLDSALNEATSRVR-----TLEKNNNLLEIEVSD---------------------LRERFNAASSASKVLQERI 655
Cdd:COG3206 105 LDEDPLGEEASREAAIERLRknltvEPVKGSNVIEISYTSpdpelaaavanalaeayleqnLELRREEARKALEFLEEQL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 656 EEMRTSNKEKDNTIT--RLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNTtenklL 733
Cdd:COG3206 185 PELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE-----L 259
|
170 180 190
....*....|....*....|....*....|....*....
gi 568937276 734 DAHTQISDLKRTISKLEAQVKQ------AEHESMLSLRN 766
Cdd:COG3206 260 LQSPVIQQLRAQLAELEAELAElsarytPNHPDVIALRA 298
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
550-748 |
8.37e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 550 MLSKIRQNLKEKharhVADLrayyESEISSLKQKLEAKDIsavEEWKKKNEIladrcGQLDSALNEATSrvrtlEKNNNL 629
Cdd:TIGR04523 500 KLNEEKKELEEK----VKDL----TKKISSLKEKIEKLES---EKKEKESKI-----SDLEDELNKDDF-----ELKKEN 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937276 630 LEIEVSDLRERFNAassaskvLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARL---RQENK---- 702
Cdd:TIGR04523 559 LEKEIDEKNKEIEE-------LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELekaKKENEklss 631
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568937276 703 MFQDLLGEYESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISK 748
Cdd:TIGR04523 632 IIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| |
