|
Name |
Accession |
Description |
Interval |
E-value |
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
25-116 |
9.81e-10 |
|
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.
Pssm-ID: 411060 [Multi-domain] Cd Length: 220 Bit Score: 59.41 E-value: 9.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 25 LTKLNLSYNHINDLSGLMPLHglkyKLRYIDLHSNYIDSIHHLLQCTVGLHFLTNLILEkdgeGNPICLIPGYRAIILQT 104
Cdd:cd21340 122 LRVLNISGNNIDSLEPLAPLR----NLEQLDASNNQISDLEELLDLLSSWPSLRELDLT----GNPVCKKPKYRDKIILA 193
|
90
....*....|..
gi 1907152203 105 LPQLRILDCKNI 116
Cdd:cd21340 194 SKSLEVLDGKEI 205
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
549-929 |
1.19e-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: 62.38 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 549 RRFKDVQDGFEDVATELAKSKHALIWAQRKENESSSLIKDLTCMVKEQKTKLSEVCKLKQEAAANLQNQINTLEILIEDD 628
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 629 KQKSIQIELLKHEKTQLISELAAKESLIYGLRTERKVWGQELACQSSTLSQSRGKLEAQIESLcRENESLRKSHESDCDA 708
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA-ANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 709 LRikcKIIEDQNETIRKLKDSLQEKDGQIKLLQEQIALIEkcsqEQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKEL 788
Cdd:TIGR02168 836 TE---RRLEDLEEQIEELSEDIESLAAEIEELEELIEELE----SELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 789 ELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDKErklkaerdkSLELqkDAMEKLQNMDDAFRRQVDEIVEAH 868
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY---------SLTL--EEAEALENKIEDDEEEARRRLKRL 977
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907152203 869 QAEIMQLANekqkyidcANLKVQQVEDEMRGLLDETCKNKKMMEEKIKQLACAISEIQKEM 929
Cdd:TIGR02168 978 ENKIKELGP--------VNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREA 1030
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
559-914 |
2.30e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 559 EDVATELAKSKHALIWAQRKENESSSLIKDLTCMVKEQKTKLSEVCKLKQEAAANLQNQINTLEILIEDDKQKSIQIELL 638
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 639 KHEKTQLISELAAKESLIyglrterkvwgqelacqsstlsqsrGKLEAQIESLCReneslRKSHESdcdaLRIKCKIIED 718
Cdd:TIGR02169 757 KSELKELEARIEELEEDL-------------------------HKLEEALNDLEA-----RLSHSR----IPEIQAELSK 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 719 QNETIRKLKDSLQEKDGQIKLLQEQIALIEKCSQE---QLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRK 795
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQElqeQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 796 AystlnkkwhdkgelLSHLEMQVKEVKEKF---EDKERKLKAERDKSLELQKDAMEKLQN-------MDDAFRRQVDE-- 863
Cdd:TIGR02169 883 R--------------LGDLKKERDELEAQLrelERKIEELEAQIEKKRKRLSELKAKLEAleeelseIEDPKGEDEEIpe 948
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1907152203 864 ---IVEAHQAEIMQLANEKQKYIDCANLKVQQVEDEMRGLLDETCKNKKMMEEK 914
Cdd:TIGR02169 949 eelSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEER 1002
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
326-913 |
2.95e-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: 61.23 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 326 QLDQEREMRWKAEQTEkkLMDYIDELHKQADEKKDVHSQALITTDRLKDAIFKERHCKAQLEIIVHRLQNEVKKLTIELM 405
Cdd:TIGR02168 333 DELAEELAELEEKLEE--LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 406 KARDQQEDHIRHLRTLERALEKMEkqkaqqqaaqirlIQEVELKASAADREINLLRTSLHQEKQQVQQLHELLALKEQEH 485
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEEAE-------------LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 486 RQeieTRQFFTDAEFQDALTKRLCKEERKHEQEVKEY---QEKIDILNQQYLDL---ENEFRIALTVEARRF------KD 553
Cdd:TIGR02168 478 DA---AERELAQLQARLDSLERLQENLEGFSEGVKALlknQSGLSGILGVLSELisvDEGYEAAIEAALGGRlqavvvEN 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 554 VQDGFEDVATELAKSKHALIWAQRKENESSSLIKDLTCMVKEQKTKLSeVCKLKQEAAANLQNQINTL--EILIEDDKQK 631
Cdd:TIGR02168 555 LNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLG-VAKDLVKFDPKLRKALSYLlgGVLVVDDLDN 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 632 SIQIELLKHEKTQLIS---ELAAKESLIYGLRTERKVWGQELACQSSTLSQSRGKLEAQIESLCRENESLRKSHESDCDA 708
Cdd:TIGR02168 634 ALELAKKLRPGYRIVTldgDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEE 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 709 LRIKCKIIEDQNETIRKLKDSLQEKDGQIKLLQEQIALIEKCSQE----------QLNEKSSQLDSIVEKLERHNERKEK 778
Cdd:TIGR02168 714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleaeieeleeRLEEAEEELAEAEAEIEELEAQIEQ 793
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 779 LKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDKERKLKAERDKSLELQKdAMEKLQNMDDAFR 858
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA-EIEELEELIEELE 872
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1907152203 859 RQVDEIVEAHQAEIMQLANEKQKYIDcANLKVQQVEDEMRGLLDETCKNKKMMEE 913
Cdd:TIGR02168 873 SELEALLNERASLEEALALLRSELEE-LSEELRELESKRSELRRELEELREKLAQ 926
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
447-743 |
3.37e-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: 57.76 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 447 ELKASAADREINLLRTSLHQEKQQVQQLHELLALKEQEHRqEIETRQFFTDAEFQdalTKRLCKEERkhEQEVKEYQEKI 526
Cdd:TIGR02168 217 ELKAELRELELALLVLRLEELREELEELQEELKEAEEELE-ELTAELQELEEKLE---ELRLEVSEL--EEEIEELQKEL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 527 DILNQQYLDLENEFRIAltveARRFKDVQDGFEDVATELAKSKHALIWAQRKENESSSLIKDLTCMVKEQKTKLSEVCKL 606
Cdd:TIGR02168 291 YALANEISRLEQQKQIL----RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 607 KQEaaanLQNQINTLEILIEDDKQKSIQielLKHEKTQLISELAAKESLIYGLRTERKVWGQELACQSSTLSQSRGK-LE 685
Cdd:TIGR02168 367 LEE----LESRLEELEEQLETLRSKVAQ---LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKeLQ 439
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907152203 686 AQIESLCRENESLRKSHESDCDALRIKCKIIEDQNETIRKLKDSLQEKDGQIKLLQEQ 743
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
338-928 |
3.40e-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: 57.34 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 338 EQTEKKLMDYIDELHKQADEKKDVHSQALITTDRLKDAIFKERHCKAQLEiivhRLQNEVKKLTIELMKARDQQEDHIRH 417
Cdd:TIGR04523 50 KNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKIN----KLNSDLSKINSEIKNDKEQKNKLEVE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 418 LRTLERALEKMEKQKAQQQAAQIRLIQEVELKASAADREINLLRTSLHQEKQQVQQLHELLALKEQEHRQEIETRQFFTD 497
Cdd:TIGR04523 126 LNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSN 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 498 AEFQDALTKRLCKEERKHEQEVKEYQEKIDILNQQYLDLENEFrialtvearrfKDVQDGFEDVATELAKSKHALIWAQR 577
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEI-----------SNTQTQLNQLKDEQNKIKKQLSEKQK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 578 KENESSSLIKDLTCMVKEQKTKLSEVCKLKQeaaanlQNQINTLEILIEDDKQKSIQIELLKHEKTQLISELaakESLIY 657
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISDLNNQKE------QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQL---NEQIS 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 658 GLRTERKvwgqELACQSSTLSQSRGKLEAQIESLCRENESLR---KSHESDCDALRIKCKIIEDQN----ETIRKLKDSL 730
Cdd:TIGR04523 346 QLKKELT----NSESENSEKQRELEEKQNEIEKLKKENQSYKqeiKNLESQINDLESKIQNQEKLNqqkdEQIKKLQQEK 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 731 QEKDGQIKLLQEQIALiEKCSQEQLNEKSSQLDSIVEKLERhneRKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGEL 810
Cdd:TIGR04523 422 ELLEKEIERLKETIIK-NNSEIKDLTNQDSVKELIIKNLDN---TRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 811 LSHLEMQVKEVKEKFED----------KERKLKAERDKSLELQKDAMEKLQNMDDAFRR-QVDEIVEAHQAEIMQLANEk 879
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDltkkisslkeKIEKLESEKKEKESKISDLEDELNKDDFELKKeNLEKEIDEKNKEIEELKQT- 576
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1907152203 880 QKYIDCANLKVQQVEDEMRGLLDETCKNKKMMEEKIKQLACAISEIQKE 928
Cdd:TIGR04523 577 QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
320-929 |
5.47e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 320 YRSLVEQLDQEREMRWKAEQTEKKLMDYIDELHKQADEKKD----VHSQALITTDRLKDAIFKERHCKAQLEIIV---HR 392
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLevseLEEEIEELQKELYALANEISRLEQQKQILRerlAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 393 LQNEVKKLTIELMKARDQQEDHIRHLRTLERALEKMEKQKAQQQAAQIRL---IQEVELKASAADREINLLRTSLHQEKQ 469
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELeaeLEELESRLEELEEQLETLRSKVAQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 470 QVQQLhellalkeQEHRQEIETRQFFTDAEFQDALTKRLCKEERKHEQEVKEYQEKIDILNQQYLDLENEFRialtvear 549
Cdd:TIGR02168 394 QIASL--------NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE-------- 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 550 rfkDVQDGFEDVATELAKSKHALIWAQRKENESSSLIKDLTCMVKEQKTKLSEVCKLKQEAAAnLQNQINTLEILIEDDK 629
Cdd:TIGR02168 458 ---RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG-LSGILGVLSELISVDE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 630 QKSIQIELLKHEKTQ--LISELAAKESLIYGLRTERKVWGQELACQSSTLSQSRGKLEAQIESLcRENESLRKSHESDCD 707
Cdd:TIGR02168 534 GYEAAIEAALGGRLQavVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNI-EGFLGVAKDLVKFDP 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 708 ALRI-------KCKIIEDQNETIRKLKDSLQE-----KDGQIKLLQEQIALIEKCSQEQLNEKSSQLDSIVEKLERHNER 775
Cdd:TIGR02168 613 KLRKalsyllgGVLVVDDLDNALELAKKLRPGyrivtLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEK 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 776 KEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEK-----------------FEDKERKLKAERDK 838
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEveqleeriaqlskelteLEAEIEELEERLEE 772
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 839 SLELQKDAMEKLQNMD---DAFRRQVDEIVEAHQAEIMQLANEKQKYIDcANLKVQQVEDEMRGL---LDETCKNKKMME 912
Cdd:TIGR02168 773 AEEELAEAEAEIEELEaqiEQLKEELKALREALDELRAELTLLNEEAAN-LRERLESLERRIAATerrLEDLEEQIEELS 851
|
650
....*....|....*..
gi 1907152203 913 EKIKQLACAISEIQKEM 929
Cdd:TIGR02168 852 EDIESLAAEIEELEELI 868
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
593-845 |
2.70e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 54.25 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 593 VKEQKTKLSEVCKLKQEAAANLQNQINTLEILIEDDKQksiQIELLKHEKTQLISELAAKESLIYGLRTERkvwgqelac 672
Cdd:PHA02562 197 IKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKA---EIEELTDELLNLVMDIEDPSAALNKLNTAA--------- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 673 qsstlsqsrGKLEAQIESLCRENESLRKSHEsdCDAlrikCK-IIEDQNETIRKLKDSLQEKDGQIKLLQEQIaliekcs 751
Cdd:PHA02562 265 ---------AKIKSKIEQFQKVIKMYEKGGV--CPT----CTqQISEGPDRITKIKDKLKELQHSLEKLDTAI------- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 752 qEQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDKERK 831
Cdd:PHA02562 323 -DELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
250
....*....|....
gi 1907152203 832 lKAERDKSLELQKD 845
Cdd:PHA02562 402 -KYHRGIVTDLLKD 414
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
324-897 |
3.02e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 324 VEQLDQERE-----MRWKAEQTEKKLMDYIDELHKQADEKKDVHSQALITTDRLKDAIFKERHCKAQLEiivhRLQNEVK 398
Cdd:COG1196 202 LEPLERQAEkaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE----ELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 399 KLTIELmkaRDQQEDHIRHLRTLERALEKMEKQKAQQQAAQIRLIQEVELKASAADREINLLRTSLHQEKQQVQQLHELL 478
Cdd:COG1196 278 ELELEL---EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 479 ALKEQEHRQEIETRQFFTDAEFQDALTKRLCKEERKHEQEVKEYQEKIDILNQQYLDLENEFRIALTVEARRFKDVQDGF 558
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 559 EDVATELAKSKHALIWAQRKENESSSLIKDLTCMVKEQKTKLSEVCKLKQEAAAnLQNQINTLEILIEDDKQKSIQIELL 638
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE-AAARLLLLLEAEADYEGFLEGVKAA 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 639 KHEKTQ------LISELAAKESLIYGLRTERKVWGQELACQSStlsqsrGKLEAQIESLCRENESLRKSHESDcdalrik 712
Cdd:COG1196 514 LLLAGLrglagaVAVLIGVEAAYEAALEAALAAALQNIVVEDD------EVAAAAIEYLKAAKAGRATFLPLD------- 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 713 ckiIEDQNETIRKLKDSLQEKDGQIKLLQEQIALIEKCSQEQLNEKSSQLDsiVEKLERHNERKEKLKQQLKAKELELEE 792
Cdd:COG1196 581 ---KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLV--AARLEAALRRAVTLAGRLREVTLEGEG 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 793 IRKAYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDKERKLKAERDKSLELQKDAMEKLQNMDDAFRRQVDEIVEAHQAEI 872
Cdd:COG1196 656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
570 580
....*....|....*....|....*
gi 1907152203 873 MQLANEKQKYIDCANLKVQQVEDEM 897
Cdd:COG1196 736 ELLEELLEEEELLEEEALEELPEPP 760
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
751-929 |
3.33e-07 |
|
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: 53.61 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 751 SQEQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDKER 830
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 831 KLKAERDKsLELQKDAMEKL------------QNMDDAFRRQ--VDEIVEAHQAEIMQLANEKQKyIDCANLKVQQVEDE 896
Cdd:COG4942 98 ELEAQKEE-LAELLRALYRLgrqpplalllspEDFLDAVRRLqyLKYLAPARREQAEELRADLAE-LAALRAELEAERAE 175
|
170 180 190
....*....|....*....|....*....|...
gi 1907152203 897 MRGLLDETCKNKKMMEEKIKQLACAISEIQKEM 929
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
370-928 |
5.98e-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: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 370 DRLKDAifKERHCKAQLEIivHRLQNEVKKLTIEL---MKARDQQEDHIRHLRTLERALE-KMEKQKAQQQAAQIRLIQE 445
Cdd:TIGR02169 315 RELEDA--EERLAKLEAEI--DKLLAEIEELEREIeeeRKRRDKLTEEYAELKEELEDLRaELEEVDKEFAETRDELKDY 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 446 VElKASAADREINLLRTSLHQEKQQVQQLHELLAlkeqEHRQEIEtRQFFTDAEFQDALtKRLCKEERKHEQEVKEYQEK 525
Cdd:TIGR02169 391 RE-KLEKLKREINELKRELDRLQEELQRLSEELA----DLNAAIA-GIEAKINELEEEK-EDKALEIKKQEWKLEQLAAD 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 526 IDILNQQYLDLENEFRialtvearrfkDVQDGFEDVATELAKSKHALIWAQRKENESSSLIKDLTCMVKEQKTKLSEVCK 605
Cdd:TIGR02169 464 LSKYEQELYDLKEEYD-----------RVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGS 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 606 LKQEAAANLQ----NQINTleILIEDDKQKSIQIELLKHEK--------------------------------------- 642
Cdd:TIGR02169 533 VGERYATAIEvaagNRLNN--VVVEDDAVAKEAIELLKRRKagratflplnkmrderrdlsilsedgvigfavdlvefdp 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 643 ------------TQLISELAAKESLIYGLR---------------TERKVWGQELACQSSTLSQSRGKLEAQIESLCREN 695
Cdd:TIGR02169 611 kyepafkyvfgdTLVVEDIEAARRLMGKYRmvtlegelfeksgamTGGSRAPRGGILFSRSEPAELQRLRERLEGLKREL 690
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 696 ESLRK---SHESDCDALRIKCKIIEDQNETIRKLKDSLQEKDGQIKLLQEQIAL-IEKCSQEQLNEKSSqLDSIVEKLER 771
Cdd:TIGR02169 691 SSLQSelrRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEdLSSLEQEIENVKSE-LKELEARIEE 769
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 772 HNERKEKLKQQLKAKELEL-----EEIRKAYSTLNKKWHDKGELLSHLE--MQVKEVKEKFEDKERKLKAERDKSLELQK 844
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARLREIEqkLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 845 DAMEKLQNMDDAFRRQVDEIVEAHQAEIMQLANEK---QKYIDCANLKVQQVEDEMRGL---LDETCKNKKMMEEKIKQL 918
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLgdlKKERDELEAQLRELERKIEELeaqIEKKRKRLSELKAKLEAL 929
|
650
....*....|
gi 1907152203 919 ACAISEIQKE 928
Cdd:TIGR02169 930 EEELSEIEDP 939
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
383-928 |
6.19e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.58 E-value: 6.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 383 KAQLEIIVHRLQNEVKKLTIELMKARDQQEDHIRHLRT----LERALEKMEKQKAQQQAAQIRLIQEVELKASAADREIN 458
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQsvidLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 459 LLRTS-------LHQEKQQVQQLHELLaLKEQEHRQEIetRQFFTDaeFQDALTKRLCKEERKHEQEVKEYQEKIDILNQ 531
Cdd:pfam15921 153 ELEAAkclkedmLEDSNTQIEQLRKMM-LSHEGVLQEI--RSILVD--FEEASGKKIYEHDSMSTMHFRSLGSAISKILR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 532 QyLDLENEFrialtVEARRFKdVQDGFEDVATElAKSKHALIWAQRKENessslIKDLTCMVKEQKTKLSEVCKLKQEAA 611
Cdd:pfam15921 228 E-LDTEISY-----LKGRIFP-VEDQLEALKSE-SQNKIELLLQQHQDR-----IEQLISEHEVEITGLTEKASSARSQA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 612 ANLQNQintLEILIEDDKQKSI----QIELLKHEKTQLISELAAKE------------------SLIYGLRTERKVWGQE 669
Cdd:pfam15921 295 NSIQSQ---LEIIQEQARNQNSmymrQLSDLESTVSQLRSELREAKrmyedkieelekqlvlanSELTEARTERDQFSQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 670 LACQSSTLSQSRGKLEAQIESLCRENESLRKSHESDC------DALRikcKIIEDQNETIRKLKDSLQ----EKDGQikl 739
Cdd:pfam15921 372 SGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTgnsitiDHLR---RELDDRNMEVQRLEALLKamksECQGQ--- 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 740 LQEQIALIEKcsqeqLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVK 819
Cdd:pfam15921 446 MERQMAAIQG-----KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEIT 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 820 EVKEKFEdkerkLKAERDKSLELQKDAMEKLQNMDDAFRRQV---DEIVEAHQAEI---MQLANEKQKYIDCANLKVQQV 893
Cdd:pfam15921 521 KLRSRVD-----LKLQELQHLKNEGDHLRNVQTECEALKLQMaekDKVIEILRQQIenmTQLVGQHGRTAGAMQVEKAQL 595
|
570 580 590
....*....|....*....|....*....|....*...
gi 1907152203 894 EDEM---RGLLDETCKNKKMMEEKIKQLACAISEIQKE 928
Cdd:pfam15921 596 EKEIndrRLELQEFKILKDKKDAKIRELEARVSDLELE 633
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
275-887 |
1.03e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 275 RKMRQPYLRDLYVRSSLVNCNNLRDLDEQKTGVIKVDKNFSDNSTYRSLVEQLDQEREMRWKAEQTEKKLMDY---IDEL 351
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkkADAA 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 352 HKQADEKKDVHSQALITTDRLKDAIFKERHCKAQLEIIVHRLQ---NEVKKLTIELMKA----RDQQEDHIRHLRTLERA 424
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKkkaDAAKKKAEEKKKAdeakKKAEEDKKKADELKKAA 1414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 425 LEKMEKQKAQQQAAQIRLIQEVELKASAADREINLLRTSlhQEKQQVQQLHEllalKEQEHRQEIETRQFFTDAEFQDAL 504
Cdd:PTZ00121 1415 AAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKA--EEAKKAEEAKK----KAEEAKKADEAKKKAEEAKKADEA 1488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 505 TKRLCKEERKHEQEVKEYQEKIDILNQQYLDLENEFRIALTVEARRFKDVQDGFEDV--ATELAKSKHALIWAQRKENES 582
Cdd:PTZ00121 1489 KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKkkADELKKAEELKKAEEKKKAEE 1568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 583 SSLIKDLtcmvKEQKTKLSEVCKLKQEAAANLQNQINTLEILIEDDKQKSIQIELLKHEKTQLISELAAKESLIYGLRTE 662
Cdd:PTZ00121 1569 AKKAEED----KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 663 RKVWGQELACQSSTLSQSRGKLEAQIESLCRENESLRKSHESDCDALRIKCKIIEDQN--ETIRKLKDSLQEKDGQIKLL 740
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKkaEELKKKEAEEKKKAEELKKA 1724
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 741 QEqialIEKCSQEQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMqvke 820
Cdd:PTZ00121 1725 EE----ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEV---- 1796
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907152203 821 vkekfedkERKLKAERDKSLELQKDAMEKLQNMDDAFRRQVDEIVEAHQAEIMQL--ANEKQKYIDCAN 887
Cdd:PTZ00121 1797 --------DKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLeeADAFEKHKFNKN 1857
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
410-795 |
1.21e-06 |
|
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: 52.20 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 410 QQEDHIRHLRTLERALEKMEKQKAQQQAAQIRLIQEVELKASAADREINLLRTSLHQEKQQVQQLhellalkeqEHRQEI 489
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEEL---------EEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 490 ETRQFFTDAEFQDALTKrlckEERKHEQEVKEYQEKIDILNQQYLDLENEF-RIALTVE--ARRFKDVQDGFEDVATELa 566
Cdd:pfam07888 106 LSASSEELSEEKDALLA----QRAAHEARIRELEEDIKTLTQRVLERETELeRMKERAKkaGAQRKEEEAERKQLQAKL- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 567 kskhaliwaQRKENESSSLIKDLtcmvKEQKTKLSEvcklKQEAAANLQNQINTLEILIEDDKQKSIQIELLKHEKTQLI 646
Cdd:pfam07888 181 ---------QQTEEELRSLSKEF----QELRNSLAQ----RDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 647 SELAAKESLIYGLRTERKVWGQ--------------ELACQSSTLSQSRGKLEAQIESLCRENESLRKSHESDCDAlrik 712
Cdd:pfam07888 244 ERLNASERKVEGLGEELSSMAAqrdrtqaelhqarlQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDR---- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 713 ckiIEDQNETIRKLKDSLQEKDGQIKLLQEQIALIEKCSQEQLNEKSSQLDSIVEKLERhnERKEKLKQQLKAKELeLEE 792
Cdd:pfam07888 320 ---IEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRV--AQKEKEQLQAEKQEL-LEY 393
|
...
gi 1907152203 793 IRK 795
Cdd:pfam07888 394 IRQ 396
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
716-928 |
2.33e-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: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 716 IEDQNETIRKLKDSLQEKDGQIKLLQEQ----IALIEKCSQE----------QLNEKSSQLDSIVEKLERHNERKEKLKQ 781
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQaekaERYKELKAELrelelallvlRLEELREELEELQEELKEAEEELEELTA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 782 QLKAKELELEEIRKAYSTLNKK-------WHDKGELLSHLEMQVKEVKEKFEDKERKLK------AERDKSLELQKDAME 848
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEieelqkeLYALANEISRLEQQKQILRERLANLERQLEeleaqlEELESKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 849 KLQNMDDAFRRQVDEIVEAHQAEIMQLANEKQKYIDCanlkvQQVEDEMRGLLDETCKNKKMMEEKIKQLACAISEIQKE 928
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEEL-----EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
716-894 |
2.77e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 716 IEDQNETIRKLKDSLQEKDGQIKLLQEQIALIekcsQEQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEE-IR 794
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEEL----NEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 795 KAYST----------LNKKwhDKGELLSHLEM-------------QVKEVKEKFEDKERKLKAERD------KSLELQKD 845
Cdd:COG3883 94 ALYRSggsvsyldvlLGSE--SFSDFLDRLSAlskiadadadlleELKADKAELEAKKAELEAKLAelealkAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907152203 846 AMEKLQNMDDAFRRQVDEIVEAHQAEIMQLANEKQKYIDCANLKVQQVE 894
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
348-878 |
5.61e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 348 IDELHKQADE-KKDVHSQALITTDRLKDAIFKERHCKAQLEIIvHRLQNEVKKLTIELMKARDQQEDHIRHLRTLERALE 426
Cdd:COG4717 48 LERLEKEADElFKPQGRKPELNLKELKELEEELKEAEEKEEEY-AELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 427 KMEKQKAQQQAAqiRLIQEVELKASAADREINLLRTSLHQEKQQVQQLHELlalkEQEHRQEIETRQFFTDAEFQDALTK 506
Cdd:COG4717 127 LLPLYQELEALE--AELAELPERLEELEERLEELRELEEELEELEAELAEL----QEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 507 --RLCKEERKHEQEVKEYQEKIDILNQQYLDLENEFRIALTVEARRFKDVQDGFEDVATELAKSKHALIWAQRKENESSS 584
Cdd:COG4717 201 leELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 585 LIKDLTCMVKEQKTKlSEVCKLKQEAAANLQNQINTLEiliedDKQKSIQIELLKHEKTQLISELAAKESLIYGLRTERK 664
Cdd:COG4717 281 LVLGLLALLFLLLAR-EKASLGKEAEELQALPALEELE-----EEELEELLAALGLPPDLSPEELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 665 VWGQElacqsstlsqsrgKLEAQIESLCRENESL-RKSHESDCDALRIKCKIIEDQNETIRKLKDSLQEKDGQIKLLQEQ 743
Cdd:COG4717 355 EAEEL-------------EEELQLEELEQEIAALlAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEL 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 744 IALIEKCS-QEQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKEleleeirkaystlnkkwhdKGELLSHLEMQVKEVK 822
Cdd:COG4717 422 LEALDEEElEEELEELEEELEELEEELEELREELAELEAELEQLE-------------------EDGELAELLQELEELK 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907152203 823 EKFEDkerklKAERDKSLELQKDAMEKLQnmddafrrqvDEIVEAHQAEIMQLANE 878
Cdd:COG4717 483 AELRE-----LAEEWAALKLALELLEEAR----------EEYREERLPPVLERASE 523
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
592-929 |
6.51e-06 |
|
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: 49.96 E-value: 6.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 592 MVKEQKTKLSEVCKLKQEAAANLQNQINTLEILIEDD---KQKSIQ----IELLKHEKTQLISELAAKESLIYGLRTERK 664
Cdd:COG5185 184 LTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTlleKAKEIInieeALKGFQDPESELEDLAQTSDKLEKLVEQNT 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 665 VWGQELACQSSTLSQsrgKLEAQIESLCRENESLRKSHESDCDALRIKCKIIEDQNETIR-----KLKDSLQEKDGQIKL 739
Cdd:COG5185 264 DLRLEKLGENAESSK---RLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAaeaeqELEESKRETETGIQN 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 740 LQEQIALIEKCSQEQLNEKSSQLDSIVEKlerhnERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKG-ELLSHLEMQV 818
Cdd:COG5185 341 LTAEIEQGQESLTENLEAIKEEIENIVGE-----VELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAqEILATLEDTL 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 819 KEVKEKFEDKERKLKAERDKSLELQKDAMEKLQNMDDAFRRQVDEIVEAHQAEIMQLANEKQKYIDCANLKVQQVEDEMR 898
Cdd:COG5185 416 KAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVS 495
|
330 340 350
....*....|....*....|....*....|.
gi 1907152203 899 GLLDETCKNKKMMEEKIKQLACAISEIQKEM 929
Cdd:COG5185 496 TLKATLEKLRAKLERQLEGVRSKLDQVAESL 526
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
683-882 |
7.69e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 7.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 683 KLEAQIESLCRENESLRKSHESDCDALRIKCKIIEDQNETIRKLKDSLQEKDGQIKLLQEQIaliekcsqEQLNEKSSQL 762
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAEL--------EELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 763 DSIVEKLERHNERKEkLKQQLKAKELELEEIRKAYstlnKKWHDKGELLSHLEMQVKEVKEKFEDKERKLKAERDKSLEL 842
Cdd:COG4717 122 EKLLQLLPLYQELEA-LEAELAELPERLEELEERL----EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD 196
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907152203 843 QKDAMEKLQnmddAFRRQVDEIVEAHQAEIMQLANEKQKY 882
Cdd:COG4717 197 LAEELEELQ----QRLAELEEELEEAQEELEELEEELEQL 232
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
323-864 |
1.06e-05 |
|
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: 49.58 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 323 LVEQLDQEREMRWKAEQTEKKLMDYIDELHKQADEKKDVHSQALITTDRLKDAIFKERHCKAQLEIIVHRLQ--NEVKKL 400
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQklQSLCKE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 401 TIELMKARDQQEDHIRHLRTLER---ALEKMEKQKAQQQAAQIRLIQEVELKASAADREINLLRTSLHQEKQQ---VQQL 474
Cdd:TIGR00618 402 LDILQREQATIDTRTSAFRDLQGqlaHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQlqtKEQI 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 475 HELLALKEQEH---------------RQEIETRQFFTDAEFQDALTKRLCKEERKHEQEVKE----YQEKIDILNQQYLD 535
Cdd:TIGR00618 482 HLQETRKKAVVlarllelqeepcplcGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSeedvYHQLTSERKQRASL 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 536 LENEFRI-----ALTVEARRFKDVQDGFEDVATELAKSKHALIWAQRKEN-ESSSLIKDLTCMVKEQKTKLSEVCKLKQE 609
Cdd:TIGR00618 562 KEQMQEIqqsfsILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAcEQHALLRKLQPEQDLQDVRLHLQQCSQEL 641
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 610 AAANLQNQINTLEILIEDDKQKSIQIELLKHEKTQLI-SELAAKESLIYGLRTERKVWGQELACQSStLSQSRGKLEAQI 688
Cdd:TIGR00618 642 ALKLTALHALQLTLTQERVREHALSIRVLPKELLASRqLALQKMQSEKEQLTYWKEMLAQCQTLLRE-LETHIEEYDREF 720
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 689 ESLCRENESLRKSHESDCDALRIKCKIIEDQNETIRKLKDSLQEKDGQIKLLQEQIALIEKCSQEQLNEKSSQLDSIVEK 768
Cdd:TIGR00618 721 NEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHL 800
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 769 L-ERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDKERKLKAERDKSLELQK-DA 846
Cdd:TIGR00618 801 LkTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKlNG 880
|
570 580
....*....|....*....|
gi 1907152203 847 MEKLQNM--DDAFRRQVDEI 864
Cdd:TIGR00618 881 INQIKIQfdGDALIKFLHEI 900
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
734-928 |
1.06e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 734 DGQIKLLQEQIALIekcsQEQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKaystlnkkwhdkgellsh 813
Cdd:COG3883 15 DPQIQAKQKELSEL----QAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA------------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 814 lemQVKEVKEKFEDKERKLKaERDKSLELQKDAMEKL------QNMDDAFRRQ--VDEIVEAhQAEIMQLANEKQKYIDC 885
Cdd:COG3883 73 ---EIAEAEAEIEERREELG-ERARALYRSGGSVSYLdvllgsESFSDFLDRLsaLSKIADA-DADLLEELKADKAELEA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907152203 886 ANLKVQQVEDEMRGLLDETCKNKKMMEEKIKQLACAISEIQKE 928
Cdd:COG3883 148 KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
289-843 |
1.09e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.35 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 289 SSLVNCNNLRDLDEQKTGVIkvdknfsDNSTYRSLVEQLDQEREMRWKAEQTeKKLMD-------YIDELHKQADEKKdv 361
Cdd:pfam15921 356 SELTEARTERDQFSQESGNL-------DDQLQKLLADLHKREKELSLEKEQN-KRLWDrdtgnsiTIDHLRRELDDRN-- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 362 hsqalITTDRLkDAIFK--ERHCKAQLEIIVHRLQ------NEVKKLTIELMKARDQQEDHIRHLRTLERALEKMEKQKA 433
Cdd:pfam15921 426 -----MEVQRL-EALLKamKSECQGQMERQMAAIQgkneslEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVS 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 434 QQQAAqirlIQEVELKASAADREINLLRTSLHQEKQQVQQLHellalKEQEHRQEIETRQfftdaefqDALTKRLCKEER 513
Cdd:pfam15921 500 DLTAS----LQEKERAIEATNAEITKLRSRVDLKLQELQHLK-----NEGDHLRNVQTEC--------EALKLQMAEKDK 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 514 KheqevkeyqekIDILNQQyldLENEFRIAltvearrfkdVQDGFEDVATELAKSKhaliwAQRKENESSSLIKDLTCMV 593
Cdd:pfam15921 563 V-----------IEILRQQ---IENMTQLV----------GQHGRTAGAMQVEKAQ-----LEKEINDRRLELQEFKILK 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 594 KEQKTKLSEvcklkqeaaanLQNQINTLEI----LIEDDKQKSIQIELLKHEKTQLISELAAKESLIYGLRTERKVWGQE 669
Cdd:pfam15921 614 DKKDAKIRE-----------LEARVSDLELekvkLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRN 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 670 LACQSSTLSQSRGKLEAQIESLCRENESLR---KSHE-SDCDALRIKCkiiedqnetirKLKDSLQEKDGQIKLLQEQIA 745
Cdd:pfam15921 683 FRNKSEEMETTTNKLKMQLKSAQSELEQTRntlKSMEgSDGHAMKVAM-----------GMQKQITAKRGQIDALQSKIQ 751
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 746 LIEKCSQEQLNEKSSQldsiveklerhNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEKF 825
Cdd:pfam15921 752 FLEEAMTNANKEKHFL-----------KEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQF 820
|
570
....*....|....*...
gi 1907152203 826 EDKERKLKAERDKSLELQ 843
Cdd:pfam15921 821 AECQDIIQRQEQESVRLK 838
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
707-928 |
1.76e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 707 DALRIKCKIIEDQNETIRKLKDSLQEKDGQIKLLQEqIALIEKCSQEQLNEKS-SQLDSIVEKLERHnerKEKLKQQLKA 785
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRREREKAERYQALLKEKRE-YEGYELLKEKEALERQkEAIERQLASLEEE---LEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 786 KELELEEIRKAYSTLNKKWHDKGEllsHLEMQVKEVKEKFEDKERKLKAERDKSLELQKDAMEKLQNMDDAFRRQVDEI- 864
Cdd:TIGR02169 263 LEKRLEEIEQLLEELNKKIKDLGE---EEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIe 339
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907152203 865 -----VEAHQAEIMQLANEKQKYIDCANLKVQQVEDEMRGlLDETCKNKKMMEEKIKQLACAISEIQKE 928
Cdd:TIGR02169 340 elereIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE-FAETRDELKDYREKLEKLKREINELKRE 407
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
712-918 |
2.49e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.09 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 712 KCKIIEDQNETIRKLKDSLQEkdgQIKLLQEQIALIEKCSQEQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELE 791
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQ---QIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 792 EIRKAYSTLNK----------------KWHDKGELLSHLEMQVKEVKEKFEDKERKLKaERDKSLELQKDAMEKLQNMDD 855
Cdd:PHA02562 252 DPSAALNKLNTaaakikskieqfqkviKMYEKGGVCPTCTQQISEGPDRITKIKDKLK-ELQHSLEKLDTAIDELEEIMD 330
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907152203 856 AFRRQVDEIVEAHQaeimQLANEKQKYIDCANlKVQQVEDEMRGLLDETCKNKKMMEEKIKQL 918
Cdd:PHA02562 331 EFNEQSKKLLELKN----KISTNKQSLITLVD-KAKKVKAAIEELQAEFVDNAEELAKLQDEL 388
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
677-881 |
2.85e-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: 47.45 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 677 LSQSRGKLEAQIESLCRENESLRKSHESDCDALRIKCKIIEDQNETIRKLKDSLQEKDGQIKLLQEQIALIEKCSQEQLN 756
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 757 EKSSQLDSIvEKLERHNERKEKLKQQlkaKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDKERKLKAER 836
Cdd:COG4942 105 ELAELLRAL-YRLGRQPPLALLLSPE---DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907152203 837 DKsLELQKDAMEKLQNMDDAFRRQVDEIVEAHQAEIMQLANEKQK 881
Cdd:COG4942 181 AE-LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
683-877 |
3.33e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 683 KLEAQIESLcrenESLRKSHEsDCDALRIKCKIIEDQNETIRKLKDS--LQEKDGQIKLLQEQIALIEkcsqEQLNEKSS 760
Cdd:COG4913 246 DAREQIELL----EPIRELAE-RYAAARERLAELEYLRAALRLWFAQrrLELLEAELEELRAELARLE----AELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 761 QLDSIVEKLERHNERKEKLK-QQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDKERKLKAERDKS 839
Cdd:COG4913 317 RLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL 396
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907152203 840 LELQKDAMEKLQNMDDAFRRQVDEIvEAHQAEIMQLAN 877
Cdd:COG4913 397 EEELEALEEALAEAEAALRDLRREL-RELEAEIASLER 433
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
320-884 |
7.13e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 7.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 320 YRSLVEQLDQEREMRWKAEQTEKKLMDYIDELHKQ-----------------ADEKKDVHSQALITTDRLKDAI------ 376
Cdd:PRK04863 416 YQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKeqeateellsleqklsvAQAAHSQFEQAYQLVRKIAGEVsrseaw 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 377 --FKE--------RHCKAQLEIIVHRLQnevkkltiELMKARDQQEDHIRHLRTLERALEKMEKQKAQQQAAQIRLIQEV 446
Cdd:PRK04863 496 dvAREllrrlreqRHLAEQLQQLRMRLS--------ELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARL 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 447 ElKASAADREINLLRTSLHQEKQQVQQLHELLALKEQEHR--QEIETR---QF---FTDAEFQDALTKRLCKEERKHEQE 518
Cdd:PRK04863 568 E-SLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLaaQDALARlreQSgeeFEDSQDVTEYMQQLLERERELTVE 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 519 VKEYQEKIDILNQQYLDL---ENEFRIALTVEARRFKDV--QDGFEDVATE--------LAKSKHALiwaqrkenesssL 585
Cdd:PRK04863 647 RDELAARKQALDEEIERLsqpGGSEDPRLNALAERFGGVllSEIYDDVSLEdapyfsalYGPARHAI------------V 714
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 586 IKDLtCMVKEQktklsevcklkqeaaanLQNQINTLE--ILIEDDKQK----SIQIELLKHEKTQLISEL---------- 649
Cdd:PRK04863 715 VPDL-SDAAEQ-----------------LAGLEDCPEdlYLIEGDPDSfddsVFSVEELEKAVVVKIADRqwrysrfpev 776
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 650 -----AAKESLIYGLRTERkvwgQELACQSSTLSQSRGKLEAQIESLCRE-NESLRKSHESDCDALrikckiIEDQNETI 723
Cdd:PRK04863 777 plfgrAAREKRIEQLRAER----EELAERYATLSFDVQKLQRLHQAFSRFiGSHLAVAFEADPEAE------LRQLNRRR 846
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 724 RKLKDSLQEKDG-------QIKLLQEQIALIEKCS-----------QEQLNEKSSQLDSIVEK---LERHNERKEKLKQQ 782
Cdd:PRK04863 847 VELERALADHESqeqqqrsQLEQAKEGLSALNRLLprlnlladetlADRVEEIREQLDEAEEAkrfVQQHGNALAQLEPI 926
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 783 ---LKAKELELEEIRKAYSTLNKKWHDkgellshLEMQVKEVKE--------KFEDKERKLKAERDKSLELQKDaMEKLQ 851
Cdd:PRK04863 927 vsvLQSDPEQFEQLKQDYQQAQQTQRD-------AKQQAFALTEvvqrrahfSYEDAAEMLAKNSDLNEKLRQR-LEQAE 998
|
650 660 670
....*....|....*....|....*....|...
gi 1907152203 852 NMddafRRQVDEIVEAHQAeimQLANEKQKYID 884
Cdd:PRK04863 999 QE----RTRAREQLRQAQA---QLAQYNQVLAS 1024
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
370-669 |
7.21e-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: 46.98 E-value: 7.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 370 DRLKdaifKERHCKAQLEIIVHRLQN-EVKKLTIELMKARDQQEDHIRHLRTLERALEKMEKQKAQQQA---AQIRLIQE 445
Cdd:TIGR02169 201 ERLR----REREKAERYQALLKEKREyEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKrleEIEQLLEE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 446 VELKASA-ADREINLLRTSLHQEKQQVQQLHELLALKEQEHRQEIETRQfFTDAEFQ------DALTKRLCKEERKHEQ- 517
Cdd:TIGR02169 277 LNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA-KLEAEIDkllaeiEELEREIEEERKRRDKl 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 518 --EVKEYQEKIDILNQQYLDLENEFRIALtveaRRFKDVQDGFEDVATELAKSKHALIWAQRKENESSSLIKDLTCMVKE 595
Cdd:TIGR02169 356 teEYAELKEELEDLRAELEEVDKEFAETR----DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAG 431
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907152203 596 QKTKLSEVCKLKQEAAANLQNQINTLEILIEDDKQKSIQIELLKHEKTQLISELAAKESLIYGLRTERKVWGQE 669
Cdd:TIGR02169 432 IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
19-220 |
7.98e-05 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 46.08 E-value: 7.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 19 LEALVNLTKLNLSYNHINDLSglMPLHGLKyKLRYIDLHSNYIDSIHHLLQctvGLHFLTNLILekdgEGNPICLIPGyr 98
Cdd:COG4886 178 LGNLTNLKELDLSNNQITDLP--EPLGNLT-NLEELDLSGNQLTDLPEPLA---NLTNLETLDL----SNNQLTDLPE-- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 99 aiiLQTLPQLRILDCKN-------IFGEPVSLEEINSSHLQ----CLEGLLDNLVSSDSPLNISEDEVNDDVSAPPMDVL 167
Cdd:COG4886 246 ---LGNLTNLEELDLSNnqltdlpPLANLTNLKTLDLSNNQltdlKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTT 322
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907152203 168 PSLKEFKSTPEDNVLASLLSVCPSSEPEKINQENDFQNETNNSLIDNVPEKDL 220
Cdd:COG4886 323 LLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLL 375
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
631-914 |
8.28e-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: 46.59 E-value: 8.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 631 KSIQIELLKHEKTQLISELAAKESLIYGLRTERKvwgqelacqsstlsqsrgKLEAQIESLCRENESLRKSHESDCDALR 710
Cdd:TIGR02168 223 RELELALLVLRLEELREELEELQEELKEAEEELE------------------ELTAELQELEEKLEELRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 711 IKCKIIEDQNETIRKLKDSLQEKDGQIKLLQEQIALIEkcsqEQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELEL 790
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRERLANLERQLEELE----AQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 791 EEIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEKFED--------KERK--LKAERDKSLELQKDAMEKLQNMD-DAFRR 859
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIASlnneierlEARLerLEDRRERLQQEIEELLKKLEEAElKELQA 440
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907152203 860 QVDEI------VEAHQAEIMQLANEKQKYIDCANLKVQQVEDEMRGLLDETCKNKKMMEEK 914
Cdd:TIGR02168 441 ELEELeeeleeLQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
445-928 |
8.86e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 8.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 445 EVELKASAADREINLLRTSLHQEKQQVQQLHELLALKEqEHRQEIETrqffTDAEFQDaLTKRLCKEERKHEqevkEYQE 524
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHE-ERREELET----LEAEIED-LRETIAETERERE----ELAE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 525 KIDILNQQYLDLENEFRIAL-----------TVEARRfKDVQDGFEDVATELAKSKHAliwAQRKENESSSL---IKDLT 590
Cdd:PRK02224 280 EVRDLRERLEELEEERDDLLaeaglddadaeAVEARR-EELEDRDEELRDRLEECRVA---AQAHNEEAESLredADDLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 591 CMVKEQKTKLSEVCKLKQEAAANLQNQINTLEILIEddkqksiQIELLKHEKTQLISELAAKESLIYGLRTERKVWGQEL 670
Cdd:PRK02224 356 ERAEELREEAAELESELEEAREAVEDRREEIEELEE-------EIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 671 ACQSSTLSQSRGKLEaqieslcrENESLRKshESDC--------DALRIKckIIEDQNETIRKLKDSLQEKDGQIKLLQE 742
Cdd:PRK02224 429 AELEATLRTARERVE--------EAEALLE--AGKCpecgqpveGSPHVE--TIEEDRERVEELEAELEDLEEEVEEVEE 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 743 QIAliekcSQEQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVK 822
Cdd:PRK02224 497 RLE-----RAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAR 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 823 EKFEDKERKLkAERDKSLELQKDAMEKLQNMDDAfRRQVDEIVEaHQAEIMQLANEKQKYIDCANLKVQQVEDEMRGLLD 902
Cdd:PRK02224 572 EEVAELNSKL-AELKERIESLERIRTLLAAIADA-EDEIERLRE-KREALAELNDERRERLAEKRERKRELEAEFDEARI 648
|
490 500 510
....*....|....*....|....*....|....
gi 1907152203 903 ETCKNKKM--------MEEKIKQLACAISEIQKE 928
Cdd:PRK02224 649 EEAREDKEraeeyleqVEEKLDELREERDDLQAE 682
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
410-833 |
1.18e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 410 QQEDHIRHLRTLERALEKMEKQKAQQQAAQIRLIQEVELKASAADREINLLR---TSLHQEKQQVQQLHELLALKEQEHR 486
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEkeiEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 487 QEIETRqfftdaefqdaltkrlcKEERKH-EQEVKEYQEKIDILNQQYLDLENEFRialtveARRFKDVQDGFEDVATEL 565
Cdd:TIGR02169 751 QEIENV-----------------KSELKElEARIEELEEDLHKLEEALNDLEARLS------HSRIPEIQAELSKLEEEV 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 566 AKSKHALIWAQRKENESSSLIKDLtcmvkeqktklsevcklkQEAAANLQNQINTLEILIEDDKQksiQIELLKHEKTQL 645
Cdd:TIGR02169 808 SRIEARLREIEQKLNRLTLEKEYL------------------EKEIQELQEQRIDLKEQIKSIEK---EIENLNGKKEEL 866
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 646 ISELAAKESLIYGLRTERKvwgqelacqssTLSQSRGKLEAQIESLCREneslrkshesdcdalrikckiIEDQNETIRK 725
Cdd:TIGR02169 867 EEELEELEAALRDLESRLG-----------DLKKERDELEAQLRELERK---------------------IEELEAQIEK 914
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 726 LKDSLQEKDGQIKLLQEQIALIEKCSQEQLNEKSSQLD--SIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKK 803
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSleDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEK 994
|
410 420 430
....*....|....*....|....*....|
gi 1907152203 804 whdkgelLSHLEMQVKEVKEKFEDKERKLK 833
Cdd:TIGR02169 995 -------RAKLEEERKAILERIEEYEKKKR 1017
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
348-794 |
1.65e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 348 IDELHKQADEKKDVHSQALITTDRLKDAIfkERHCKAQLEIivHRLQNEVKKLTIELMKARDQQEDHIRHLRTLERALEK 427
Cdd:PRK02224 215 LAELDEEIERYEEQREQARETRDEADEVL--EEHEERREEL--ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 428 MEKQKAQqqaaqirLIQEVELKaSAADREINLLRTSLHQEKQQVQQLHELLALKEQEHRQEIET-RQFFTDAEfQDALTK 506
Cdd:PRK02224 291 LEEERDD-------LLAEAGLD-DADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESlREDADDLE-ERAEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 507 R-----LCKEERKHEQEVKEYQEKIDILNQQYLDLENEFRIALTvearRFKDVQDGFEDVATELAK-------------- 567
Cdd:PRK02224 362 ReeaaeLESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV----DLGNAEDFLEELREERDElrereaeleatlrt 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 568 --------------------------SKHALIWAQRKEN--ESSSLIKDLTCMVKEQKTKLSEVCKLKQEAA--ANLQNQ 617
Cdd:PRK02224 438 arerveeaealleagkcpecgqpvegSPHVETIEEDRERveELEAELEDLEEEVEEVEERLERAEDLVEAEDriERLEER 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 618 INTLEILIEDDK----QKSIQIELLKHEKTQLISELAAKESLIYGLRTErkvwGQELACQSSTLSQSRGKLEAQIESLCR 693
Cdd:PRK02224 518 REDLEELIAERRetieEKRERAEELRERAAELEAEAEEKREAAAEAEEE----AEEAREEVAELNSKLAELKERIESLER 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 694 ENESL--RKSHESDCDALRIKCKIIEDQNETIRklkDSLQEKDGQIKLLQEQI--ALIEKcSQEQLNEKSSQLDSIVEKL 769
Cdd:PRK02224 594 IRTLLaaIADAEDEIERLREKREALAELNDERR---ERLAEKRERKRELEAEFdeARIEE-AREDKERAEEYLEQVEEKL 669
|
490 500
....*....|....*....|....*
gi 1907152203 770 ERHNERKEKLKQQLKAKELELEEIR 794
Cdd:PRK02224 670 DELREERDDLQAEIGAVENELEELE 694
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
703-856 |
2.18e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 703 ESDCDALRIKCKIIEDQ--NETIRKLKDSLQEKDGQIKLLQEQIALIEkcsQEQLNEKSSQLDSIVEKLERHNERkekLK 780
Cdd:COG2433 360 PPDVDRDEVKARVIRGLsiEEALEELIEKELPEEEPEAEREKEHEERE---LTEEEEEIRRLEEQVERLEAEVEE---LE 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 781 QQLKAKELELE----EIRKAYSTLNKKwHDKGELLSHLEMQVKEVKEKFEDKERKLKAERDKSLELQKdaMEKLQNMDDA 856
Cdd:COG2433 434 AELEEKDERIErlerELSEARSEERRE-IRKDREISRLDREIERLERELEEERERIEELKRKLERLKE--LWKLEHSGEL 510
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
506-878 |
2.30e-04 |
|
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: 45.04 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 506 KRLCKEERKHEQEVKEYQEKIDILNQQYLDLENEFrialtVEARRFKDVQDGFEDVATELAKSKHALIWAQRKENESSSL 585
Cdd:TIGR00606 594 AKLNKELASLEQNKNHINNELESKEEQLSSYEDKL-----FDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQF 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 586 IKDLTcmvkEQKTKLSEVCKLKQEAAANLQNQINTLE--ILIEDDKQKSIQIELLKHEKTQLI---------SELAAKES 654
Cdd:TIGR00606 669 ITQLT----DENQSCCPVCQRVFQTEAELQEFISDLQskLRLAPDKLKSTESELKKKEKRRDEmlglapgrqSIIDLKEK 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 655 LIYGLRTERKVWGQELACQSSTLSQSRGKLE----------------AQIESLCRENESLRKSHESDCDALRIKckiieD 718
Cdd:TIGR00606 745 EIPELRNKLQKVNRDIQRLKNDIEEQETLLGtimpeeesakvcltdvTIMERFQMELKDVERKIAQQAAKLQGS-----D 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 719 QNETIRKLKDSLQEKDGQIKLLQEQIALIEKCSQEQlNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYS 798
Cdd:TIGR00606 820 LDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQ-QEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQ 898
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 799 TLNKKWHDKGELLSHLEMQVKEVKEKFEDKERKLKAERDKSLELQKDAMEKLQNMDDAFRRQVDEIVEAHQAEIMQLANE 878
Cdd:TIGR00606 899 SLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETE 978
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
24-91 |
2.99e-04 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 39.82 E-value: 2.99e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907152203 24 NLTKLNLSYNHINDLSGLMpLHGLKyKLRYIDLHSNYIDSIHhlLQCTVGLHFLTNLILekdgEGNPI 91
Cdd:pfam13855 2 NLRSLDLSNNRLTSLDDGA-FKGLS-NLKVLDLSNNLLTTLS--PGAFSGLPSLRYLDL----SGNRL 61
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
594-796 |
3.13e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 594 KEQKTKLSEVCKLKQEAAANLQNQINTLEILIEDDKQKSIQIELLKHEKTQLISELAAKESLIYGLRTERKVWGQELACQ 673
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 674 SSTLSQSRGKLEAQ-IESLCRENESLRKSHESDCDALRikcKIIEDQNEtIRKLKDSLQEKDGQIKLLQEQIALIEKCSQ 752
Cdd:COG3883 99 GGSVSYLDVLLGSEsFSDFLDRLSALSKIADADADLLE---ELKADKAE-LEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907152203 753 EQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKA 796
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
328-866 |
3.63e-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: 44.33 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 328 DQEREMRWKAEQTEKKLMDYIDELHKQADEKKDVHSQA----LITTDRLKDAIFKERHCKAQLEIIVHRLQNEVKKLTIE 403
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAenarLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 404 LMKARDQQEDHIRhlrTLERALEKMEKQKAQQQAAQIRLIQEVElKASAADREINLLRTSLHQEKQQVQQLHELLalkeq 483
Cdd:pfam05483 249 ITEKENKMKDLTF---LLEESRDKANQLEEKTKLQDENLKELIE-KKDHLTKELEDIKMSLQRSMSTQKALEEDL----- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 484 ehrqEIETRQFFTDAEFQDALTKRLCKEERKHEQEVKEYQEKIDILNQqyldlenefriALTVEARRFKDVQDGFEDVAT 563
Cdd:pfam05483 320 ----QIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE-----------LLRTEQQRLEKNEDQLKIITM 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 564 ELAKSKHALIWAQRKENESSSLIKDLTCMVKEQKTKLSE---VCKLKQEAAANLQNQINTLEILIEDDKQKSIQIELLKH 640
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEkkqFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKT 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 641 EKTQLISELaakESLIYGLRTErKVWGQELACQSSTLSQSRGKLEAQIESLCRENESLRKSHESDCDALRIKCKIIEDQN 720
Cdd:pfam05483 465 SEEHYLKEV---EDLKTELEKE-KLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 721 ETIRKLKDSLQEKDGQIKLLQEQIalieKCSQEQLNEKSSQLDSIVEKLERHNERKEK----LKQQLKAKELELEEIRKA 796
Cdd:pfam05483 541 EKEMNLRDELESVREEFIQKGDEV----KCKLDKSEENARSIEYEVLKKEKQMKILENkcnnLKKQIENKNKNIEELHQE 616
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907152203 797 YSTLNKKWHDKGELLSHLEMQVKEVKEKFEDKERKLKAERD---KSLELQKDAMEKLQNMDDAFRRQVDEIVE 866
Cdd:pfam05483 617 NKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDnyqKEIEDKKISEEKLLEEVEKAKAIADEAVK 689
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
336-841 |
3.76e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 336 KAEQTEKKLMDYIDELHKQADEKKDVHSQALITTDRLKDAifkerhcKAQLEIIVHrlqnEVKKLTIELMKARDQQEDHI 415
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEK-------EKELEEVLR----EINEISSELPELREELEKLE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 416 RHLRTLERALEKMEKQKAQQQAAQIRLiQEVELKASAADREINLLRTSLHQEKQQVQQLHELLALKEQ------------ 483
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESLEGSK-RKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiklsefyeeyl 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 484 EHRQEIETRqfFTDAEFQDALTKRLCKEERKHEQEVKEYQEKIDILNQQYLDLENEFRI-----ALTVEARRFKDVQDGF 558
Cdd:PRK03918 307 DELREIEKR--LSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyeeakAKKEELERLKKRLTGL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 559 --EDVATELAKSKHALIWAQRKENESSSLIKDLTCMVKEQKTKLSE---------VCK--LKQEAAANLQNQInTLEIL- 624
Cdd:PRK03918 385 tpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpVCGreLTEEHRKELLEEY-TAELKr 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 625 IEDDKQKSI-QIELLKHEKTQLISELAAKESLIyglrTERKVWGQELACQSSTLSQSRGKLEAQIESLCRENESLRKshe 703
Cdd:PRK03918 464 IEKELKEIEeKERKLRKELRELEKVLKKESELI----KLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIK--- 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 704 sdcdaLRIKCKIIEDQNETIRKLKDSLQEKDGQIKLLQEQIALIEKCSQEQLNEKSSQLDSIVEKLERHNERKEKLKQQL 783
Cdd:PRK03918 537 -----LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAE 611
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907152203 784 KAKELELEEIRKAYSTLNKKWHDKGELLSHLEM---QVKEVKEKFEDKERKLKAERDKSLE 841
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEElrkELEELEKKYSEEEYEELREEYLELS 672
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
316-883 |
3.84e-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: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 316 DNSTYRSLVEQLDQEREMR--WKAEQTEKKLMDYIDELHKQADEKKDVHSQALITTDRLKDAIFKERHCKAQleiivhRL 393
Cdd:COG4913 260 LAERYAAARERLAELEYLRaaLRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ------IR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 394 QN---EVKKLTIELMKARDQQEDHIRHLRTLERALEKMEKQKAQQQAAQIRLIQEVELKASAADREINLLRTSLHQEKQQ 470
Cdd:COG4913 334 GNggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAA 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 471 VQQLHELLALKEQEhRQEIETRQFFTDAEFQDALtKRLCKEERKHEQEVKEYQEKIDILNQQ---------YLdleNEFR 541
Cdd:COG4913 414 LRDLRRELRELEAE-IASLERRKSNIPARLLALR-DALAEALGLDEAELPFVGELIEVRPEEerwrgaierVL---GGFA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 542 IALTVEARRFKDVQDGFEDVATELA----KSKHALIWAQRKENESSSLIKDLTcmVKEQktklsevcklkqEAAANLQNQ 617
Cdd:COG4913 489 LTLLVPPEHYAAALRWVNRLHLRGRlvyeRVRTGLPDPERPRLDPDSLAGKLD--FKPH------------PFRAWLEAE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 618 IN---------TLEILieDDKQKSIQIE-LLKHEKT--QLISELAAKESLIYGLRTERKVwgqelacqsSTLSQSRGKLE 685
Cdd:COG4913 555 LGrrfdyvcvdSPEEL--RRHPRAITRAgQVKGNGTrhEKDDRRRIRSRYVLGFDNRAKL---------AALEAELAELE 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 686 AQIESLCRENESLRKSHESdcdalrikckiIEDQNETIRKLKDsLQEKDGQIKLLQEQIAliekcsqeQLNEKSSQLDSI 765
Cdd:COG4913 624 EELAEAEERLEALEAELDA-----------LQERREALQRLAE-YSWDEIDVASAEREIA--------ELEAELERLDAS 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 766 VEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVkEKFEDKERKLKAERDKSLELQKD 845
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA-EDLARLELRALLEERFAAALGDA 762
|
570 580 590
....*....|....*....|....*....|....*...
gi 1907152203 846 AMEKLQnmdDAFRRQVDEIVEAHQAEIMQLANEKQKYI 883
Cdd:COG4913 763 VERELR---ENLEERIDALRARLNRAEEELERAMRAFN 797
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
768-924 |
4.32e-04 |
|
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: 42.99 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 768 KLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDKERKLKAERD----KSLELQ 843
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkeyEALQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 844 KDAMEKLQNMDDAFRRQVDEIVEAHQAEIMQLANEKQKYIDcanlKVQQVEDEMRGLLDETCKNKKMMEEKIKQLACAIS 923
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA----ELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
.
gi 1907152203 924 E 924
Cdd:COG1579 174 P 174
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
309-928 |
6.40e-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: 43.81 E-value: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 309 KVDKNFSDNSTYRSLVEQLDQEREMRWKAEQTEKKLMDYIDELHKQADEKKDVHSQALITTDRLKDAIF----KERHCKA 384
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEyyqlKEKLELE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 385 QLEIIVHRLQNEVKKLTIELMKARDQQEDHIRHLRTLERALEKMEKQKAQQQAAQIRLIQEVELKASAADREINLLRTSL 464
Cdd:pfam02463 223 EEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSEL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 465 HQEKQQVQQLHELLAL-KEQEHRQEIETRQFFTDAEFQDALTKRLCKEERKHEQEVKEYQEKIDILNQQYLDLENEFRIA 543
Cdd:pfam02463 303 LKLERRKVDDEEKLKEsEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 544 LTVEARRFKDVQDGFEDVATELAKSKHALIWAQRKENESSSLIKDLTCMVKEQKTKLSEVCKLKQEAAANLQNQINTLEI 623
Cdd:pfam02463 383 SERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 624 LIEDDKQKSIQIELLKHEKTQLISELAAKESL-----------IYGLRTERKVWGQELACQSSTLSQSRGKLEAQIESLC 692
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKleersqkeskaRSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 693 RENESLRKSHESDCDALRIKCKIIEDQNETIRKLKDSLQEKDGQIKLLQEQIALIEKCSQEQLNEKSSQLDSIVEKLERH 772
Cdd:pfam02463 543 VAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRA 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 773 NERKEKLKQQLKAKELELEEIRKaySTLNKKWHDKGELLSHLEMQVKEVKEKFEDKERKLKAERDKSLELQKDAMEKLQN 852
Cdd:pfam02463 623 KVVEGILKDTELTKLKESAKAKE--SGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLE 700
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907152203 853 MDDAFRRQVDEIVEAHQAEIMQLANEKQKYIDCANlkvQQVEDEMRGLLDETCKNKKMMEEKIKQLACAISEIQKE 928
Cdd:pfam02463 701 IKKKEQREKEELKKLKLEAEELLADRVQEAQDKIN---EELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKE 773
|
|
| TIGR03545 |
TIGR03545 |
TIGR03545 family protein; This model represents a relatively rare but broadly distributed ... |
752-916 |
6.83e-04 |
|
TIGR03545 family protein; This model represents a relatively rare but broadly distributed uncharacterized protein family, distributed in 1-2 percent of bacterial genomes, all of which have outer membranes. In many of these genomes, it is part of a two-gene pair.
Pssm-ID: 274640 Cd Length: 555 Bit Score: 43.17 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 752 QEQLNEKSSQLDSIVEKLERHNerkeklkqqLKAKELeLEEIRKAYSTLNKKWHDK------GELLSHLEMQVKEVKEK- 824
Cdd:TIGR03545 138 SSELKKVDSQLPDPRALLKGED---------LKTVET-AEEIEKSLKAMQQKWKKRkkdlpnKQDLEEYKKRLEAIKKKd 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 825 -------FEDKER--KLKAERDKSLELQKDAMEKLQNMDDAFRRQVDEIVEAHQAEIMQLANEKQ-KYIDCANLKVQQVE 894
Cdd:TIGR03545 208 iknplelQKIKEEfdKLKKEGKADKQKIKSAKNDLQNDKKQLKADLAELKKAPQNDLKRLENKYAiKSGDLKNFAVDLFG 287
|
170 180
....*....|....*....|..
gi 1907152203 895 DEMRGLLDETCKNKKMMEEKIK 916
Cdd:TIGR03545 288 PEIRKYLQKFLKYYDQAEPLLN 309
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
19-115 |
7.64e-04 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 43.00 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 19 LEALVNLTKLNLSYNHINDLSGlmPLHGLKyKLRYIDLHSNYIDSIHHLLQctvGLHFLTNLILekdgEGNPICLIPGyr 98
Cdd:COG4886 132 LANLTNLKELDLSNNQLTDLPE--PLGNLT-NLKSLDLSNNQLTDLPEELG---NLTNLKELDL----SNNQITDLPE-- 199
|
90
....*....|....*..
gi 1907152203 99 aiILQTLPQLRILDCKN 115
Cdd:COG4886 200 --PLGNLTNLEELDLSG 214
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
684-864 |
1.47e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.42 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 684 LEAQIESLCRENESLRKSHESDCDALRIKCKIIEDQNETIRklkDSLQEKDGQIKLLQEQIALIEKCSQEQ--------- 754
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRES---DRNQELQKRIRLLEKREAEAEEALREQaelnrlkkk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 755 --------LNEKSSQL-------DSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVK 819
Cdd:pfam05557 84 ylealnkkLNEKESQLadareviSCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907152203 820 EVKE---KFEDKERKLKAERDKSLELQ--KDAMEKLQNMDDAFRRQVDEI 864
Cdd:pfam05557 164 SLAEaeqRIKELEFEIQSQEQDSEIVKnsKSELARIPELEKELERLREHN 213
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
638-928 |
1.69e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.12 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 638 LKHEKTQLISELAAKESLIYGLRTERkvwgQELACQSS-------TLSQSRGKLEAQIESLCRENESLRKSHESDCDALR 710
Cdd:pfam10174 287 MKNKIDQLKQELSKKESELLALQTKL----ETLTNQNSdckqhieVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLN 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 711 IKCKIIEDQNE-------TIRKLKDSLQEKDGQIKLLQEQIALIekcsQEQLNEKSSQLDSIVEK--------------- 768
Cdd:pfam10174 363 KKTKQLQDLTEekstlagEIRDLKDMLDVKERKINVLQKKIENL----QEQLRDKDKQLAGLKERvkslqtdssntdtal 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 769 --LERHNERKEKLKQQLK-AKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDkeRKLKAERDKSLELQKD 845
Cdd:pfam10174 439 ttLEEALSEKERIIERLKeQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLID--LKEHASSLASSGLKKD 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 846 AmeKLQNMDDAFRRQVDEIV-------EAHQAE------------IMQLANEKQKYIDCANlKVQQVEDEMRGLLDETCK 906
Cdd:pfam10174 517 S--KLKSLEIAVEQKKEECSklenqlkKAHNAEeavrtnpeindrIRLLEQEVARYKEESG-KAQAEVERLLGILREVEN 593
|
330 340
....*....|....*....|..
gi 1907152203 907 NKKMMEEKIKQLACAISEIQKE 928
Cdd:pfam10174 594 EKNDKDKKIAELESLTLRQMKE 615
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
348-916 |
1.78e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 348 IDELHKQADEKKDVHSQALITTDRLKDAIFK-ERHCKAQLEIIVHRLQNEVKKLTIELMKARDqqedhIRHLRTLERALE 426
Cdd:PTZ00121 1226 AEAVKKAEEAKKDAEEAKKAEEERNNEEIRKfEEARMAHFARRQAAIKAEEARKADELKKAEE-----KKKADEAKKAEE 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 427 KMEKQKAQQQAAQIRLIQEVELKASAADREINLLRTSLHQEKQQVqqlhELLALKEQEHRQEIETrqfftdAEFQDALTK 506
Cdd:PTZ00121 1301 KKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA----EAAKAEAEAAADEAEA------AEEKAEAAE 1370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 507 RLCKEERKHEQEVKEYQEKIDilnqqyldlenefrialtvEARRFKDVQDGFEDVATELAKSKHALIWAQRKENESSSLI 586
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKK-------------------KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK 1431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 587 KDLTCMVKEQKTKLSEVCKLKQEAAANLQNQINTLEILIEDDKQKSIQIELLKHEKTQLISELAAKESLIYGLRTERKVW 666
Cdd:PTZ00121 1432 KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK 1511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 667 GQELacqsSTLSQSRGKLEAQIESLCRENESLRKSHE-SDCDALRIKCKIieDQNETIRKLKDSLQEKDGQIKLLQEqiA 745
Cdd:PTZ00121 1512 ADEA----KKAEEAKKADEAKKAEEAKKADEAKKAEEkKKADELKKAEEL--KKAEEKKKAEEAKKAEEDKNMALRK--A 1583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 746 LIEKCSQEQLNEKSSQLDSIVEKLERHNERKEKlKQQLKAKEL-ELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEK 824
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE-EAKIKAEELkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK 1662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 825 FEDKERKLKAERDKSLELQKDAMEKlQNMDDAFRRQVDEIVEAHQ-----AEIMQLANEKQKYIDCANLKVQQVEDEMRG 899
Cdd:PTZ00121 1663 AAEEAKKAEEDKKKAEEAKKAEEDE-KKAAEALKKEAEEAKKAEElkkkeAEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
|
570
....*....|....*..
gi 1907152203 900 LLDETCKNKKMMEEKIK 916
Cdd:PTZ00121 1742 DKKKAEEAKKDEEEKKK 1758
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
452-883 |
2.12e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.73 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 452 AADREINLLRTSLHQEKQQVQQLHELLALKEQEHRQEIETRQFF-TDAEFQDALTKRLCKEERKHEQEVKEYQEKIDILN 530
Cdd:pfam10174 237 MKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYkSHSKFMKNKIDQLKQELSKKESELLALQTKLETLT 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 531 QQYLDLENEFRI---ALTVEARRFKDVQD-------GFEDVATELAKSKHALiwaQRKENESSSL---IKDLTCM--VKE 595
Cdd:pfam10174 317 NQNSDCKQHIEVlkeSLTAKEQRAAILQTevdalrlRLEEKESFLNKKTKQL---QDLTEEKSTLageIRDLKDMldVKE 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 596 QKT--------KLSEVCKLKQEAAANLQNQINTLE-----------ILIEDDKQKSIQIELLKHEKT------------- 643
Cdd:pfam10174 394 RKInvlqkkieNLQEQLRDKDKQLAGLKERVKSLQtdssntdtaltTLEEALSEKERIIERLKEQREredrerleelesl 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 644 -QLISELAAKESLIYGLRTERKVWGQELACQSSTLSQSRGKLEAQIESLcrenESLRKSHESDCDALRIKCKIIEDQNET 722
Cdd:pfam10174 474 kKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSL----EIAVEQKKEECSKLENQLKKAHNAEEA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 723 IRKLKDSLQekdgQIKLLQEQIAL-IEKCSQEQL-------------NEKSSQlDSIVEKLERHNER--KEKLKQQLKAK 786
Cdd:pfam10174 550 VRTNPEIND----RIRLLEQEVARyKEESGKAQAeverllgilreveNEKNDK-DKKIAELESLTLRqmKEQNKKVANIK 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 787 ELELEEIRKAYSTLNKKWHDKGELL-SHLEMQVKEVKEKFEDKERKLKAERDKSLELQKDAMEK---LQNMDDAFRRQVD 862
Cdd:pfam10174 625 HGQQEMKKKGAQLLEEARRREDNLAdNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKdghLTNLRAERRKQLE 704
|
490 500
....*....|....*....|.
gi 1907152203 863 EIVEAHQAEIMQLANEKQKYI 883
Cdd:pfam10174 705 EILEMKQEALLAAISEKDANI 725
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
608-834 |
2.17e-03 |
|
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: 41.29 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 608 QEAAANLQNQINTLEILIEDDKQksiQIELLKHEKTQLISELAAKESLIYGLRTERKVWGQELACQSSTLSQSRGKLEAQ 687
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEK---ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 688 IESLCRENESLR-------KSHESDCDALRIKCKIIEDQNETIRKLKDSLQEKDGQIKLLQEQIALIEKcSQEQLNEKSS 760
Cdd:COG4942 96 RAELEAQKEELAellralyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA-LRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907152203 761 QLDSIVEKLErhnERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDKERKLKA 834
Cdd:COG4942 175 ELEALLAELE---EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
714-863 |
2.26e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 714 KIIEDQNETIRKLKDSLQEKDGQIKLLQEQIALIEKcsqeQLNEKSSQLDSIVEKLERHNERKEKLK--QQLKAKELELE 791
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEK----EIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907152203 792 EIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDKERKL---KAERDKSLELQKDAMEKLQNMDDAFRRQVDE 863
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELeekKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
681-795 |
2.32e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 681 RGKLEAQIESLCRENESLRKshESDCDALRIKCKIIEDQNETIRKLKDSLQ----EKDGQIKLLQEQiaLIEKcsQEQLN 756
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEkelrERRNELQKLEKR--LLQK--EENLD 99
|
90 100 110
....*....|....*....|....*....|....*....
gi 1907152203 757 EKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRK 795
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIE 138
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
325-541 |
2.50e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 325 EQLDQEREMRWKAEQTEKKLMDYIDELHKQADEKKDVHSQALITTDRLKDAIFKERHCKAQLEIIVHRLQNEVKKLTIEL 404
Cdd:TIGR02168 775 EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 405 MKARDQQEDHIRHLRTLERALEKMEKQKAQQQAAQIRL----------IQEVELKASAADREINLLRTSLHQEKQQVQQL 474
Cdd:TIGR02168 855 ESLAAEIEELEELIEELESELEALLNERASLEEALALLrseleelseeLRELESKRSELRRELEELREKLAQLELRLEGL 934
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907152203 475 HELLAlkeqeHRQEIETRQFFTDAEFQDALTKRLCKEERKHEQEVKEYQEKIDILNQQYLDLENEFR 541
Cdd:TIGR02168 935 EVRID-----NLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYE 996
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
640-832 |
2.63e-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: 39.89 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 640 HEKTQLISELAAKESLIYGLRTERKVWGQELACQSSTLSQSRGKlEAQIESLCReneslrkSHESDCDALRIKCKIIEDQ 719
Cdd:pfam15619 11 HKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGT-ESELPQLIA-------RHNEEVRVLRERLRRLQEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 720 NetiRKLKDSLQEKDGQIKLLQEQIALIEKCSQEQ-LNEK---SSQLDSIVEKLERHNERKEKLKQQLkakELELEEIRK 795
Cdd:pfam15619 83 E---RDLERKLKEKEAELLRLRDQLKRLEKLSEDKnLAEReelQKKLEQLEAKLEDKDEKIQDLERKL---ELENKSFRR 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907152203 796 AYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDKERKL 832
Cdd:pfam15619 157 QLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
714-896 |
2.64e-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: 40.27 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 714 KIIEDQNETIRKLKDSLQEKDGQIKLLQEQIALIEKCSQeQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEEI 793
Cdd:pfam13851 19 DITRNNLELIKSLKEEIAELKKKEERNEKLMSEIQQENK-RLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLKARLKVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 794 RKAYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDK--ERKLKAErDKSLELQKdameKLQNMDDafrrqVDEIVEAHQAE 871
Cdd:pfam13851 98 EKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAiqDVQQKTG-LKNLLLEK----KLQALGE-----TLEKKEAQLNE 167
|
170 180
....*....|....*....|....*
gi 1907152203 872 IMQLANEKQKYIDCANLKVQQVEDE 896
Cdd:pfam13851 168 VLAAANLDPDALQAVTEKLEDVLES 192
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
16-127 |
3.20e-03 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 41.07 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 16 CTGLEALVNLTKLNLSYNHINDLSGlmPLHGLKyKLRYIDLHSNYIDSIHHLLQctvGLHFLTNLILekdgEGNPICLIP 95
Cdd:COG4886 106 NEELSNLTNLESLDLSGNQLTDLPE--ELANLT-NLKELDLSNNQLTDLPEPLG---NLTNLKSLDL----SNNQLTDLP 175
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1907152203 96 GyraiILQTLPQLRILDCKN--------IFGEPVSLEEIN 127
Cdd:COG4886 176 E----ELGNLTNLKELDLSNnqitdlpePLGNLTNLEELD 211
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
295-495 |
3.77e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 295 NNLRDLDEQKTgviKVDKNFSDNSTYRSLVEQLDQEREMRWKAEQTEKKLMDYIDELHKQAdekkdvhsqalittdRLKD 374
Cdd:COG4717 68 LNLKELKELEE---ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL---------------QLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 375 AIFKERHCKAQLEIIVHRLQNEVKKLT--IELMKARDQQEDHIRHLRT-LERALEKMEKQKAQQQAAQIRLIQEVELKAS 451
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEelRELEEELEELEAELAELQEeLEELLEQLSLATEEELQDLAEELEELQQRLA 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907152203 452 AADREINLLRTSLHQEKQQVQQLHELLALKEQEHRQEIETRQFF 495
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL 253
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
22-61 |
4.30e-03 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 36.35 E-value: 4.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1907152203 22 LVNLTKLNLSYNHINDLSGLMpLHGLKyKLRYIDLHSNYI 61
Cdd:pfam13855 24 LSNLKVLDLSNNLLTTLSPGA-FSGLP-SLRYLDLSGNRL 61
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
716-929 |
4.56e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 716 IEDQNETIRKLKDSLQEKDGQIKLLQEQI-ALIEKCSQ--EQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEE 792
Cdd:COG1340 17 IEELREEIEELKEKRDELNEELKELAEKRdELNAQVKElrEEAQELREKRDELNEKVKELKEERDELNEKLNELREELDE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 793 IRKAYSTLNKKWHDKGEL---LSHLEMQV----------KEVKEKFEDKERKLKaERDKSLELQKDAMEKLQNMDDaFRR 859
Cdd:COG1340 97 LRKELAELNKAGGSIDKLrkeIERLEWRQqtevlspeeeKELVEKIKELEKELE-KAKKALEKNEKLKELRAELKE-LRK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907152203 860 QVDEIVEahqaEIMQLANEKQKYIDCANLKVQQVE------DEMRGLLDETCKNKKMMEEKIKQLACAISEIQKEM 929
Cdd:COG1340 175 EAEEIHK----KIKELAEEAQELHEEMIELYKEADelrkeaDELHKEIVEAQEKADELHEEIIELQKELRELRKEL 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
594-803 |
6.69e-03 |
|
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: 39.75 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 594 KEQKTKLSEVCKLKQEAAANLQNQINTLEILIEDDKQKSIQIELLKHEKTQLISELAAKESLIYGLRTERKVWGQELAcq 673
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 674 sstlsQSRGKLEAQIESLCRENE----SLRKSHESDCDALRIKC---KIIEDQNETIRKLKDSLQEKDGQIKLLQEQIAL 746
Cdd:COG4942 101 -----AQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQylkYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 747 IEKCSQEQLNEKSSQLDSIVEK---LERHNERKEKLKQQLKAKELELEEIRKAYSTLNKK 803
Cdd:COG4942 176 LEALLAELEEERAALEALKAERqklLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
575-928 |
6.89e-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: 40.39 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 575 AQRKENESSSLIKDLTCMVKEQKTK------LSEVCKLKQEAAANLQNQINTLEILIED----DKQKSIQIELLKHEKTQ 644
Cdd:TIGR04523 28 ANKQDTEEKQLEKKLKTIKNELKNKekelknLDKNLNKDEEKINNSNNKIKILEQQIKDlndkLKKNKDKINKLNSDLSK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 645 LISELAAKESLIYGLRTERKVWGQELACQSSTLSQSRG---KLEAQIESLCRENESLRKSHESDCDALRIKCKIIEDQNE 721
Cdd:TIGR04523 108 INSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTeikKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 722 TIRKLKD----------SLQEKDGQIKLLQEQIALIEKCS----------QEQLNEKSSQLDSIVEKLERHNERKEKLKQ 781
Cdd:TIGR04523 188 NIDKIKNkllklelllsNLKKKIQKNKSLESQISELKKQNnqlkdniekkQQEINEKTTEISNTQTQLNQLKDEQNKIKK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 782 QLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQ-----VKEVKEKFEDKERKLKAERDK---------SLELQKDAM 847
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIQNQisqnnkiisQLNEQISQL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 848 EKLQNMDDAFRRQVDEIVEAHQAEIMQLANEKQKYIDcANLKVQQVEDEMRGLLDETCKNKKMMEEKIKQLACAISEIQK 927
Cdd:TIGR04523 348 KKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQ-EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
.
gi 1907152203 928 E 928
Cdd:TIGR04523 427 E 427
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
19-165 |
7.22e-03 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 39.92 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 19 LEALVNLTKLNLSYNHINDLSGLMPLHglkyKLRYIDLHSNYIDSIHhlLQCTVGLHFLTNLILEKDGEGNPICLIPGYR 98
Cdd:COG4886 246 LGNLTNLEELDLSNNQLTDLPPLANLT----NLKTLDLSNNQLTDLK--LKELELLLGLNSLLLLLLLLNLLELLILLLL 319
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907152203 99 AIILQTLPQLRILDCKNIFGEPVSLEEINSSHLQCLEGLLDNLVSSDSPLNISEDEVNDDVSAPPMD 165
Cdd:COG4886 320 LTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLL 386
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
443-705 |
7.35e-03 |
|
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: 39.75 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 443 IQEVELKASAADREINLLRTSLHQEKQQVQQLHELLalkeQEHRQEIETRQfftdaefqdaltkrlcKEERKHEQEVKEY 522
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL----AALERRIAALA----------------RRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 523 QEKIDILNQQYLDLENEFRIALTVEARRFKDVQD-GFEDVATELAKSKHALIWAQRkenesSSLIKDLTCMVKEQKTKLS 601
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYRlGRQPPLALLLSPEDFLDAVRR-----LQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 602 EVCKLKQEAAANLQNQINTLEILIEDDKQKSIQIELLKHEKTQLISELAAKEsliyglrterkvwgQELACQSSTLSQSR 681
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL--------------AELAAELAELQQEA 222
|
250 260
....*....|....*....|....
gi 1907152203 682 GKLEAQIESLCRENESLRKSHESD 705
Cdd:COG4942 223 EELEALIARLEAEAAAAAERTPAA 246
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
580-834 |
8.68e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 580 NESSSLIKDLTCMVKEQKTKLSEVCKLKQEAAANLQNQINTLEILIEDDKQKSIQIELLKHEKTQLISELaaKESLIYGL 659
Cdd:PRK01156 486 REIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRY--KSLKLEDL 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 660 RTERKVWGQELACQSSTlsqsrgKLEAqIESLCRENESLRKSHESDCDALRIKCKIIEDQNE-TIRKLKDSLQEKDGQIK 738
Cdd:PRK01156 564 DSKRTSWLNALAVISLI------DIET-NRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDkSIREIENEANNLNNKYN 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 739 LLQEQIALIEKCSQ--EQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEM 816
Cdd:PRK01156 637 EIQENKILIEKLRGkiDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSD 716
|
250
....*....|....*...
gi 1907152203 817 QVKEVKEKFEDKERKLKA 834
Cdd:PRK01156 717 RINDINETLESMKKIKKA 734
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
754-867 |
8.86e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.06 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 754 QLNEKSSQLDSIVEKLERHNERKEKLKQ------QLKAKEL--ELEEIRKAYSTLNKKWHDKGELLSH------------ 813
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKeqdeasFERLAELrdELAELEEELEALKARWEAEKELIEEiqelkeeleqry 484
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907152203 814 -----LEMQVKEVKEKFEDKERKLKAERDKSL--------------ELQKDAMEKLQNMDDAFRRQV---DEIVEA 867
Cdd:COG0542 485 gkipeLEKELAELEEELAELAPLLREEVTEEDiaevvsrwtgipvgKLLEGEREKLLNLEEELHERVigqDEAVEA 560
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
752-903 |
9.24e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 752 QEQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAkeleLEEIRKAYSTL-NKKWHD-------------KGEL------- 810
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDA----LQERREALQRLaEYSWDEidvasaereiaelEAELerldass 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152203 811 --LSHLEMQVKEVKEKFED----------KERKLKAERDKSLELQKDAMEKLQNMDDAFRRQVDEIVEAHQAEIMQLANE 878
Cdd:COG4913 685 ddLAALEEQLEELEAELEEleeeldelkgEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVE 764
|
170 180 190
....*....|....*....|....*....|.
gi 1907152203 879 K------QKYIDCANLKVQQVEDEMRGLLDE 903
Cdd:COG4913 765 RelrenlEERIDALRARLNRAEEELERAMRA 795
|
|
| |
