|
Name |
Accession |
Description |
Interval |
E-value |
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
260-613 |
1.45e-90 |
|
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.
Pssm-ID: 462869 [Multi-domain] Cd Length: 303 Bit Score: 284.28 E-value: 1.45e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 260 VEERPDKDFAE---------KGSRNMPSLSAATLASLGGTSSRRGSGDTSISMDTEASIREIKelnelkdqiqdvegkym 330
Cdd:pfam09738 30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIK----------------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 331 qglkemkDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQF 410
Cdd:pfam09738 93 -------HELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 411 AEVKEALRQREEMLEeirqlqqkqagfireisdlqetiewkdkkigalerqkeffdsirserddlreetvklkeelkKHG 490
Cdd:pfam09738 166 AELKEQLKQRDELIE--------------------------------------------------------------KHG 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 491 IILNSEIATNGEtsdTVNDVGYQAPTKITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQ--KNNKL 568
Cdd:pfam09738 184 LVIVPDENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKskRNSTR 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 568908290 569 DLLRAEDGILENGTdaHVMDLQRDANRQISDLKFKLAKSEQEITA 613
Cdd:pfam09738 261 SSQSPDGFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
282-663 |
5.21e-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: 59.69 E-value: 5.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 282 ATLASLGGTSSRRGSGDTSISMDTEASI----REIKELNELkdqiqdvegkymqgLKEMKDSLAEVEEKYKKAMVSNAQL 357
Cdd:TIGR02168 645 YRIVTLDGDLVRPGGVITGGSAKTNSSIlerrREIEELEEK--------------IEELEEKIAELEKALAELRKELEEL 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 358 DNEktnfmyqVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQagf 437
Cdd:TIGR02168 711 EEE-------LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA--- 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 438 IREISDLQETIewkdkkigalERQKEFFDSIRSERDDLREETVKLKEELKKHGIILNSEIATNGETSDTVNDVGYQAptK 517
Cdd:TIGR02168 781 EAEIEELEAQI----------EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI--E 848
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 518 ITKEELNALKSAGEgTLDVRLKKLIDERECLLEQIKKLKGQLEGRQKNnkLDLLRAEdgilENGTDAHVMDLQRDANRqi 597
Cdd:TIGR02168 849 ELSEDIESLAAEIE-ELEELIEELESELEALLNERASLEEALALLRSE--LEELSEE----LRELESKRSELRRELEE-- 919
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568908290 598 sdLKFKLAKSEQEITALEQNVIRLESQVT-RYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 663
Cdd:TIGR02168 920 --LREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
357-664 |
7.37e-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: 59.31 E-value: 7.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 357 LDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAG 436
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 437 firEISDLQETIEWKDKKIGALERQ--KEFFDSIRSERDDLREETVKLKEELKKHGIILNSEIATNGETSDTVND-VGYQ 513
Cdd:TIGR02169 766 ---RIEELEEDLHKLEEALNDLEARlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQElQEQR 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 514 APTKITKEELNALKSAGEGTLDvRLKKLIDERECLLEQIKKLKGQLEGRQKNNKLDLLRAEDGILENGTDAHvmdlqrDA 593
Cdd:TIGR02169 843 IDLKEQIKSIEKEIENLNGKKE-ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE------KK 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 594 NRQISDLKFKLAKSEQEITALEQNVIRLES---QVTRYRSAAENAEKIE------------------------DELKAEK 646
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGEDEEipeEELSLEDVQAELQRVEeeiralepvnmlaiqeyeevlkrlDELKEKR 995
|
330
....*....|....*...
gi 568908290 647 RKLQRELRSALDKTEELE 664
Cdd:TIGR02169 996 AKLEEERKAILERIEEYE 1013
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
411-687 |
3.15e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 411 AEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQkefFDSIRSERDDLREETVKLKEELKKhg 490
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER---IAQLSKELTELEAEIEELEERLEE-- 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 491 iiLNSEIATNGETSDTVNDV--GYQAPTKITKEELNALKSAgEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQKNNKl 568
Cdd:TIGR02168 773 --AEEELAEAEAEIEELEAQieQLKEELKALREALDELRAE-LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE- 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 569 dllRAEDGILEngtdahvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRK 648
Cdd:TIGR02168 849 ---ELSEDIES-------------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270
....*....|....*....|....*....|....*....
gi 568908290 649 LQRELrsaldktEELEVSNGHLVKRLEKMKANRSALLSQ 687
Cdd:TIGR02168 913 LRREL-------EELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
391-687 |
1.29e-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: 55.07 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 391 EKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKeffDSIRS 470
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL---KELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 471 ERDDLREETVKLKEELkkhgiilnseiatngetsdtvndvgyqaptkitkEELNALKSagegtlDVRLKKLIDERECLLE 550
Cdd:TIGR02169 766 RIEELEEDLHKLEEAL----------------------------------NDLEARLS------HSRIPEIQAELSKLEE 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 551 QIKKLKGQL-EGRQKNNKLDLLRAedgILEngtdahvmDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYR 629
Cdd:TIGR02169 806 EVSRIEARLrEIEQKLNRLTLEKE---YLE--------KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 568908290 630 SAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQ 687
Cdd:TIGR02169 875 AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
415-668 |
4.03e-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: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 415 EALRQREEMLE---EIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFFD----SIRSERDDLREETVKLKEELK 487
Cdd:TIGR02169 288 EQLRVKEKIGEleaEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEreieEERKRRDKLTEEYAELKEELE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 488 KhgiiLNSEIATNGETSDTvndvgyqaptkiTKEELNALKsagegtldVRLKKLIDERECLLEQIKKL---KGQLEGRQK 564
Cdd:TIGR02169 368 D----LRAELEEVDKEFAE------------TRDELKDYR--------EKLEKLKREINELKRELDRLqeeLQRLSEELA 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 565 NNKLDLLRAEDGILENGTDAHVMDLQ-RDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRyrsaaenAEKIEDELK 643
Cdd:TIGR02169 424 DLNAAIAGIEAKINELEEEKEDKALEiKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK-------LQRELAEAE 496
|
250 260
....*....|....*....|....*
gi 568908290 644 AEKRKLQRELRSALDKTEELEVSNG 668
Cdd:TIGR02169 497 AQARASEERVRGGRAVEEVLKASIQ 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
386-664 |
4.75e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 386 QRQYEEKNKEFEREKHAHSILQFQFAEVKEAL----RQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQ 461
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLeelrLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 462 KEFFDSIR----SERDDLREETVKLKEELkkhgiilnseiatngeTSDTVNDVGYQAPTKITKEELNALKSAgEGTLDVR 537
Cdd:TIGR02168 318 LEELEAQLeeleSKLDELAEELAELEEKL----------------EELKEELESLEAELEELEAELEELESR-LEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 538 LKKLIDERECLLEQIKKLKGQLEgRQKNNKLDLLRAEDGILENGTDAhvmdLQRDANRQISDLKFKLAKSEQEITALEQN 617
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIE-RLEARLERLEDRRERLQQEIEEL----LKKLEEAELKELQAELEELEEELEELQEE 455
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 568908290 618 VIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELE 664
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
387-688 |
2.40e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 387 RQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAgfiREISDLQETIEWKDKKIGALERQKEffd 466
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE---LELEEAQAEEYELLAELARLEQDIA--- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 467 SIRSERDDLREETVKLKEELKKhgiiLNSEIATNGETsdtvndvgyqaptkitKEELNALKSAGEGTLDVRLKKLIDERE 546
Cdd:COG1196 306 RLEERRRELEERLEELEEELAE----LEEELEELEEE----------------LEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 547 cLLEQIKKLKGQLEGRQKNNKLDLLRAEDGILEngtdahvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVT 626
Cdd:COG1196 366 -ALLEAEAELAEAEEELEELAEELLEALRAAAE-------------LAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568908290 627 RYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 688
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
411-664 |
2.58e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.91 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 411 AEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETiewKDKKIGALERQKEFFDSIRSERDDLREETVKLKEELKKHG 490
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEK---RDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 491 IILNS---EIATNGETSDTVNDVGYqaPTKITKEELNALksagEGTLDVRLKKLIDEREcLLEQIKKLKGQLEGRQK--- 564
Cdd:COG1340 85 EKLNElreELDELRKELAELNKAGG--SIDKLRKEIERL----EWRQQTEVLSPEEEKE-LVEKIKELEKELEKAKKale 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 565 -NNKLDLLRAE-DGILENGTDAHvMDLQRDANrQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDEL 642
Cdd:COG1340 158 kNEKLKELRAElKELRKEAEEIH-KKIKELAE-EAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIEL 235
|
250 260
....*....|....*....|..
gi 568908290 643 KAEKRKLQRELRSALDKTEELE 664
Cdd:COG1340 236 QKELRELRKELKKLRKKQRALK 257
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
313-664 |
2.88e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.79 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 313 KELNELKDQIQDVEGKYMQGL-KEMKDSLAEVEEKYKkamvsnaQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEE 391
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQKEQDWnKELKSELKNQEKKLE-------EIQNQISQNNKIISQLNEQISQLKKELTNSESENSE 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 392 KNKEFErEKHAhsilqfqfaEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEffdSIRSE 471
Cdd:TIGR04523 361 KQRELE-EKQN---------EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE---LLEKE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 472 RDDLREETVKLKEELKKhgiiLNSEIATNGETSDTVNDVGYQAPTKI--TKEELNALKSAGEGT---------------- 533
Cdd:TIGR04523 428 IERLKETIIKNNSEIKD----LTNQDSVKELIIKNLDNTRESLETQLkvLSRSINKIKQNLEQKqkelkskekelkklne 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 534 ----LDVRLKKLIDERECLLEQIKKLKgqLEGRQKNNKLDLLraEDGILENGTDAHVMDLQ---RDANRQISDLK--FKL 604
Cdd:TIGR04523 504 ekkeLEEKVKDLTKKISSLKEKIEKLE--SEKKEKESKISDL--EDELNKDDFELKKENLEkeiDEKNKEIEELKqtQKS 579
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568908290 605 AKSEQE-----ITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELE 664
Cdd:TIGR04523 580 LKKKQEekqelIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLK 644
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
299-684 |
3.84e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 299 TSISMDTEASIREIKELNELKDQIQDVE---GKYMQGLKEMKDSLAEVEEKYKKAmvsnAQLDNEKTNFMYQVDTLKDML 375
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLDELREIEkrlSRLEEEINGIEERIKELEEKEERL----EELKKKLKELEKRLEELEERH 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 376 LE--LEEQLAESQRQYEEKNKEFEREKHAhsilqfqfAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEW--- 450
Cdd:PRK03918 362 ELyeEAKAKKEELERLKKRLTGLTPEKLE--------KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkk 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 451 -------------KDKKIGALERQKEFFDSIRSERDDLREETVKLKEELKKHGIILN--SEIATNGETSDTVNDVgYQAP 515
Cdd:PRK03918 434 akgkcpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkeSELIKLKELAEQLKEL-EEKL 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 516 TKITKEELNALKSAGEGTLDvRLKKLIDERECLLEQIKKLKGqLEGRQK--NNKLDLLRAE----DGILENGTDAHVMDL 589
Cdd:PRK03918 513 KKYNLEELEKKAEEYEKLKE-KLIKLKGEIKSLKKELEKLEE-LKKKLAelEKKLDELEEElaelLKELEELGFESVEEL 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 590 Q----------------RDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDE-----LKAEKRK 648
Cdd:PRK03918 591 EerlkelepfyneylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEeeyeeLREEYLE 670
|
410 420 430
....*....|....*....|....*....|....*.
gi 568908290 649 LQRELRSALDKTEELEVSNGHLVKRLEKMKANRSAL 684
Cdd:PRK03918 671 LSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
312-679 |
1.46e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 312 IKELNELKDQIQDV---EGKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEqlaeSQRQ 388
Cdd:PRK03918 171 IKEIKRRIERLEKFikrTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE----LEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 389 YEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWK---DKKIGALERQKEFF 465
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELreiEKRLSRLEEEINGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 466 DSIRSERDDLREETVKLKEELKKhgiiLNSEIATNGETSDTVNDVgyqaptKITKEELNALKSAGEGTLDVRLKKLIDE- 544
Cdd:PRK03918 327 EERIKELEEKEERLEELKKKLKE----LEKRLEELEERHELYEEA------KAKKEELERLKKRLTGLTPEKLEKELEEl 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 545 ---RECLLEQIKKL---KGQLEGRQKNNKLDL--LRAEDGIL----ENGTDAHVMDLQRDANRQISDLKFKLAKSEQEIT 612
Cdd:PRK03918 397 ekaKEEIEEEISKItarIGELKKEIKELKKAIeeLKKAKGKCpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKER 476
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568908290 613 ALEQNVIRLE------SQVTRYRSAAENAEKIEDELKA----EKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 679
Cdd:PRK03918 477 KLRKELRELEkvlkkeSELIKLKELAEQLKELEEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
304-644 |
3.60e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 304 DTEASIREI--------KELNELKDQIQDVEgkymQGLKEMKDSLAEVEEKYKKaMVSNAQLdnektnfmyqvdTLKDML 375
Cdd:TIGR02169 234 ALERQKEAIerqlasleEELEKLTEEISELE----KRLEEIEQLLEELNKKIKD-LGEEEQL------------RVKEKI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 376 LELEEQLAESQRQYEEKNKEFERekhAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKI 455
Cdd:TIGR02169 297 GELEAEIASLERSIAEKERELED---AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 456 GALERQkefFDSIRSERDDLREETVKLKEELKKhgiiLNSEIATNGETSdtvndvgyqaptKITKEELNALKSAGEGTLD 535
Cdd:TIGR02169 374 EEVDKE---FAETRDELKDYREKLEKLKREINE----LKRELDRLQEEL------------QRLSEELADLNAAIAGIEA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 536 vRLKKLIDERECLLEQIKKLKGQLEGRQKNNKldllraedgilengtdahvmdlqrDANRQISDLKFKLAKSEQEITALE 615
Cdd:TIGR02169 435 -KINELEEEKEDKALEIKKQEWKLEQLAADLS------------------------KYEQELYDLKEEYDRVEKELSKLQ 489
|
330 340
....*....|....*....|....*....
gi 568908290 616 QNVIRLESQVTRYRSAAENAEKIEDELKA 644
Cdd:TIGR02169 490 RELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
412-643 |
1.22e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 412 EVKEALRQREeMLEEIRQLQQKQAGFIREISDLQETIEWkdkkiGALERQKEFFDSIRSERDDLREETVKLKEELKKHgi 491
Cdd:COG4913 243 ALEDAREQIE-LLEPIRELAERYAAARERLAELEYLRAA-----LRLWFAQRRLELLEAELEELRAELARLEAELERL-- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 492 ilnseiatngetsdtvndvgyQAPTKITKEELNALK----SAGEGTLDvRLKKLIDERECLLEQIKKLKGQLEGRQKNNK 567
Cdd:COG4913 315 ---------------------EARLDALREELDELEaqirGNGGDRLE-QLEREIERLERELEERERRRARLEALLAALG 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 568 LDLLRAEDGILENGTDAH------------VMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSA-AEN 634
Cdd:COG4913 373 LPLPASAEEFAALRAEAAallealeeeleaLEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAlAEA 452
|
....*....
gi 568908290 635 AEKIEDELK 643
Cdd:COG4913 453 LGLDEAELP 461
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
306-580 |
1.56e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 306 EASIREIKELNELKDQIQdvegkymQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES 385
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 386 QRQYEEKNKEFEREKhahsilqfqfAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEff 465
Cdd:TIGR02168 343 EEKLEELKEELESLE----------AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE-- 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 466 dSIRSERDDLREETVKLKEELKKHGIilnSEIATNGETsdtvndvgyqaptkiTKEELNALKSAGEgTLDVRLKKLIDER 545
Cdd:TIGR02168 411 -RLEDRRERLQQEIEELLKKLEEAEL---KELQAELEE---------------LEEELEELQEELE-RLEEALEELREEL 470
|
250 260 270
....*....|....*....|....*....|....*
gi 568908290 546 ECLLEQIKKLKGQLEgrQKNNKLDLLRAEDGILEN 580
Cdd:TIGR02168 471 EEAEQALDAAERELA--QLQARLDSLERLQENLEG 503
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
313-681 |
1.59e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 313 KELNELKDQIQDVE-GKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLE--------LEEQLA 383
Cdd:PRK03918 372 EELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelTEEHRK 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 384 ESQRQYEEKNKEFEREKhahsilqfqfAEVKEALRQREEMLEEIRQLQQKQAGFI--REISDLQETIEWKDKKIGA--LE 459
Cdd:PRK03918 452 ELLEEYTAELKRIEKEL----------KEIEEKERKLRKELRELEKVLKKESELIklKELAEQLKELEEKLKKYNLeeLE 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 460 RQKEFFDSIRSERDDLREETVKLKEELKKhGIILNSEIATNGETSDTVNdvgyqaptKITKEELNALKSAGEGT---LDV 536
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGEIKSLKKELEK-LEELKKKLAELEKKLDELE--------EELAELLKELEELGFESveeLEE 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 537 RLKKL--IDERECLLEQIKKLKGQLEGRQKNNKLDLLRAEDGILENGTDAhvmdlqRDANRQISDLKFKLakSEQEITAL 614
Cdd:PRK03918 593 RLKELepFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL------EELRKELEELEKKY--SEEEYEEL 664
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568908290 615 EQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVsnghLVKRLEKMKANR 681
Cdd:PRK03918 665 REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK----LEKALERVEELR 727
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
311-658 |
1.74e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 311 EIKELNELKDQIQDVEGKymqgLKEMKDSLAEVEEKYKKAMVSNAQLDNEktnfmyqVDTLKDMLLELEEQLAESQRQYE 390
Cdd:COG1196 223 KELEAELLLLKLRELEAE----LEELEAELEELEAELEELEAELAELEAE-------LEELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 391 EKNKEFEREKHAHSILQfqfAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFFDSIRS 470
Cdd:COG1196 292 ELLAELARLEQDIARLE---ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 471 ERDDLREETVKLKEELKKHgiilnseiatngetsdtvndvgYQAPTKITKEELNALKSAGEgtldvRLKKLIDERECLLE 550
Cdd:COG1196 369 EAEAELAEAEEELEELAEE----------------------LLEALRAAAELAAQLEELEE-----AEEALLERLERLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 551 QIKKLKGQLEgRQKNNKLDLLRAEDGILEngTDAHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRS 630
Cdd:COG1196 422 ELEELEEALA-ELEEEEEEEEEALEEAAE--EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
330 340
....*....|....*....|....*....
gi 568908290 631 AAENAE-KIEDELKAEKRKLQRELRSALD 658
Cdd:COG1196 499 AEADYEgFLEGVKAALLLAGLRGLAGAVA 527
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
309-663 |
2.13e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 309 IREIKELNELKDQIQDVEGKYmqglKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES--Q 386
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAelP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 387 RQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQ-AGFIREISDLQETIEWKDKKIGALERQKEff 465
Cdd:COG4717 146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELE-- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 466 dSIRSERDDLREETV--KLKEELKKHGIILNSEIAtngetsdTVNDVGYQAPTKITKEELNALKSAGEGTLDVRLKKLID 543
Cdd:COG4717 224 -ELEEELEQLENELEaaALEERLKEARLLLLIAAA-------LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 544 ERECLLEQIKKLKGQLEGRQ-KNNKLDLLRAEDGILENGTDAHVMDLQrdanRQISDLKFKLAKSEQEITALEQNVIRLE 622
Cdd:COG4717 296 EKASLGKEAEELQALPALEElEEEELEELLAALGLPPDLSPEELLELL----DRIEELQELLREAEELEEELQLEELEQE 371
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 568908290 623 SQ----------VTRYRSAAENAEKIEdELKAEKRKLQRELRSALDKTEEL 663
Cdd:COG4717 372 IAallaeagvedEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEEL 421
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
386-682 |
3.45e-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: 44.19 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 386 QRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQagfirEISDLQETIEWKDKKIGALERQKEFF 465
Cdd:pfam02463 210 LEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQ-----EIEKEEEKLAQVLKENKEEEKEKKLQ 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 466 DSIRSERDDLREEtVKLKEELKKHGIILNSEIATNGETSDTVNDVGYQAPTKITKEELNALKSAGEGTLdvRLKKLIDER 545
Cdd:pfam02463 285 EEELKLLAKEEEE-LKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKRE--AEEEEEEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 546 ECLLEQIKKLKGQLEGRQKNNKLDLLRAEDGILENGTDAHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQV 625
Cdd:pfam02463 362 EKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIEL 441
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 568908290 626 TRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRS 682
Cdd:pfam02463 442 KQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER 498
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
439-687 |
3.63e-04 |
|
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: 43.21 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 439 REISDLQETIEWKDKKIGALERQKEffdSIRSERDDLREETVKLKEELKKhgiilnseiatngetsdtvndvgyqaptki 518
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEK---ALLKQLAALERRIAALARRIRA------------------------------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 519 TKEELNALKSagegtldvRLKKLIDERECLLEQIKKLKGQLEGR----QKNNKLDLLRaedgILENGTDAhvmdlqRDAN 594
Cdd:COG4942 74 LEQELAALEA--------ELAELEKEIAELRAELEAQKEELAELlralYRLGRQPPLA----LLLSPEDF------LDAV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 595 RQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRL 674
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
250
....*....|...
gi 568908290 675 EKMKANRSALLSQ 687
Cdd:COG4942 216 AELQQEAEELEAL 228
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
533-662 |
3.66e-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: 42.60 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 533 TLDVRLKKLIDERECLLEQIKKLKGQLEGRQK-----NNKLDLLRAEDGILENGTDAHVMDLQRD--------ANRQISD 599
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEArleaaKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrNNKEYEA 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568908290 600 LKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEE 662
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
409-688 |
5.00e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 409 QFAEVKEALRQRE--EMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEffdSIRSERDDLREETVKLKEEL 486
Cdd:COG1196 214 RYRELKEELKELEaeLLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 487 kkhgiilnseiatngetsdtvndvgyqaptkitkEELNALKSAGEGTLDVRLKKLIDEREcLLEQIKKLKGQLEGRQKNN 566
Cdd:COG1196 291 ----------------------------------YELLAELARLEQDIARLEERRRELEE-RLEELEEELAELEEELEEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 567 KLDLLRAEDgilengtdahvmdlqrdanrqisdlkfKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEK 646
Cdd:COG1196 336 EEELEELEE---------------------------ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 568908290 647 RKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 688
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
307-687 |
5.16e-04 |
|
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: 43.57 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 307 ASIREIKELneLKDQIQDVEGKYM---QGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMlleleeqla 383
Cdd:pfam15921 468 AQLESTKEM--LRKVVEELTAKKMtleSSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL--------- 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 384 esqRQYEEKNKEFEREKHAhsiLQFQFAE---VKEALRQR-EEMLEEIRQ-------LQQKQAGFIREISD----LQETI 448
Cdd:pfam15921 537 ---KNEGDHLRNVQTECEA---LKLQMAEkdkVIEILRQQiENMTQLVGQhgrtagaMQVEKAQLEKEINDrrleLQEFK 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 449 EWKDKKIGALERqkeffdsIRSERDDLREETVKLKEELKKHgiiLNSEIATNGETSDTVNDVgyqaptKITKEELNALKS 528
Cdd:pfam15921 611 ILKDKKDAKIRE-------LEARVSDLELEKVKLVNAGSER---LRAVKDIKQERDQLLNEV------KTSRNELNSLSE 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 529 AGEgtldVRLKKLIDERECLLEQIKKLKGQLEGRQknNKLDLLRAEDGILEnGTDAHVMDLQRDANRQISdlkfklAKSE 608
Cdd:pfam15921 675 DYE----VLKRNFRNKSEEMETTTNKLKMQLKSAQ--SELEQTRNTLKSME-GSDGHAMKVAMGMQKQIT------AKRG 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 609 QeITALEQNVIRLESQVTryrsaaeNAEKIEDELKAEKRKLQRELRS-ALDKTE---ELEVSNGHlVKRLEKMKANRSAL 684
Cdd:pfam15921 742 Q-IDALQSKIQFLEEAMT-------NANKEKHFLKEEKNKLSQELSTvATEKNKmagELEVLRSQ-ERRLKEKVANMEVA 812
|
...
gi 568908290 685 LSQ 687
Cdd:pfam15921 813 LDK 815
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
390-497 |
5.34e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 390 EEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRqlqqkqagfiREISDLQETIEWKDKKIGALERQKEFFDSIR 469
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457
|
90 100
....*....|....*....|....*...
gi 568908290 470 SERDDLREETVKLKEELKKhgiiLNSEI 497
Cdd:COG2433 458 RREIRKDREISRLDREIER----LEREL 481
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
311-688 |
6.73e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.09 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 311 EIKELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYE 390
Cdd:TIGR04523 219 QISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 391 EKNKEFEREKHahsilqfqfAEVKEALRQREemlEEIRQLQQKQAGFIREISDLQETIEwkdkkigalerqkeffdSIRS 470
Cdd:TIGR04523 299 DLNNQKEQDWN---------KELKSELKNQE---KKLEEIQNQISQNNKIISQLNEQIS-----------------QLKK 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 471 ERDDLREETVKLKEELKKHGIILNSEIATNGETSDTVNDVGYQA---PTKITK-EELNALKsagegtlDVRLKKLIDERE 546
Cdd:TIGR04523 350 ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIndlESKIQNqEKLNQQK-------DEQIKKLQQEKE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 547 CLLEQIKKLKGQLEgrQKNNKLDLLRAEDGILENGTDAH----------VMDLQRDANRQISDLKFK---LAKSEQEITA 613
Cdd:TIGR04523 423 LLEKEIERLKETII--KNNSEIKDLTNQDSVKELIIKNLdntresletqLKVLSRSINKIKQNLEQKqkeLKSKEKELKK 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 614 LEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALD---------KTEELEVSNGHLVKRLEKMKANRSAL 684
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDelnkddfelKKENLEKEIDEKNKEIEELKQTQKSL 580
|
....
gi 568908290 685 LSQQ 688
Cdd:TIGR04523 581 KKKQ 584
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
390-580 |
7.52e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 390 EEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFFDSIR 469
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 470 sERDDLREETVKLKEELKKhgiiLNSEIATNGETSDTVNDVGYQAptKITKEELNALKSAGEGTLDVRLKKLIDERECLL 549
Cdd:COG4717 133 -ELEALEAELAELPERLEE----LEERLEELRELEEELEELEAEL--AELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190
....*....|....*....|....*....|.
gi 568908290 550 EQIKKLKGQLEgrQKNNKLDLLRAEDGILEN 580
Cdd:COG4717 206 QRLAELEEELE--EAQEELEELEEELEQLEN 234
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
312-688 |
9.89e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.73 E-value: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 312 IKELNELKDQIQDVE---GKYMQGLKEMkDSLAEVEEKYKKAMVSNAQLDNEKTNF----------MYQVDTLKDMLLEL 378
Cdd:TIGR01612 1249 IEDLDEIKEKSPEIEnemGIEMDIKAEM-ETFNISHDDDKDHHIISKKHDENISDIrekslkiiedFSEESDINDIKKEL 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 379 EEQLAESQRQYEEKNKEFEREKHAHSILQFQ-----FAEVKEALRQREEMLEEIRQLQQKQAGFIREISD---------- 443
Cdd:TIGR01612 1328 QKNLLDAQKHNSDINLYLNEIANIYNILKLNkikkiIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDdinleecksk 1407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 444 LQETIEWKDKKiGALERQKEFFDSIRSERDDLREETVKLKEELKKHGIILNS-EIATNG-------ETSDTVNDVGYQap 515
Cdd:TIGR01612 1408 IESTLDDKDID-ECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNiEMADNKsqhilkiKKDNATNDHDFN-- 1484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 516 tkITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEgrqknNKLDLLRAEDGILENGTDAH-VMDLQRDAN 594
Cdd:TIGR01612 1485 --INELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELL-----NKYSALAIKNKFAKTKKDSEiIIKEIKDAH 1557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 595 RQISdlkFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKL------QRELRSALDKTEELE--VS 666
Cdd:TIGR01612 1558 KKFI---LEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFlkisdiKKKINDCLKETESIEkkIS 1634
|
410 420
....*....|....*....|..
gi 568908290 667 NGHLVKRLEKMKANRSALLSQQ 688
Cdd:TIGR01612 1635 SFSIDSQDTELKENGDNLNSLQ 1656
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
404-580 |
1.22e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.22 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 404 SILQFQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQ--ETIEWKDKKIGALERQKEFFDSIRSErddlreetvk 481
Cdd:PRK05771 86 ELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYVSVFVGTVPED---------- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 482 LKEELKKHGIILNSEIATNGETSDTVNDVGYQAPTKITKEELN-----ALKSAGEGTLDVRLKKLIDERECLLEQIKKLK 556
Cdd:PRK05771 156 KLEELKLESDVENVEYISTDKGYVYVVVVVLKELSDEVEEELKklgfeRLELEEEGTPSELIREIKEELEEIEKERESLL 235
|
170 180
....*....|....*....|....*
gi 568908290 557 GQLEgrQKNNKL-DLLRAEDGILEN 580
Cdd:PRK05771 236 EELK--ELAKKYlEELLALYEYLEI 258
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
414-688 |
1.49e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.96 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 414 KEALRQREEMLEEIRQLQQKQAgfireISDLQETIEWKDKKIGALERQKEFFDSIrserDDLREETVKLKEELKKHgiil 493
Cdd:PRK10929 25 EKQITQELEQAKAAKTPAQAEI-----VEALQSALNWLEERKGSLERAKQYQQVI----DNFPKLSAELRQQLNNE---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 494 nseiatngetSDTVNDVgyqaPTKITKEELNalksagEGTLDVRLKKLIDERECLLEQ-----IKKLKGQLEGRQKNNKL 568
Cdd:PRK10929 92 ----------RDEPRSV----PPNMSTDALE------QEILQVSSQLLEKSRQAQQEQdrareISDSLSQLPQQQTEARR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 569 DLLRAEDGILENGTDAHVMDLQRDANRQISDLKFKLAKSEQEITAL----EQNVIRLESQVTRYRSaaenaEKIEDELKA 644
Cdd:PRK10929 152 QLNEIERRLQTLGTPNTPLAQAQLTALQAESAALKALVDELELAQLsannRQELARLRSELAKKRS-----QQLDAYLQA 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 568908290 645 EKRKL----QRELRSALDKTEELEVSNGHLVKRL-EKMKANR--SALLSQQ 688
Cdd:PRK10929 227 LRNQLnsqrQREAERALESTELLAEQSGDLPKSIvAQFKINRelSQALNQQ 277
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
384-637 |
1.82e-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: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 384 ESQRQYEEKNKEFEREKhahsilqfqfaevkealRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKE 463
Cdd:COG4942 31 QLQQEIAELEKELAALK-----------------KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 464 ffdSIRSERDDLREETVKLKEELKKHGIILNSEIATNGET-SDTVNDVGY-QAPTKITKEELNALKSAGEgtldvRLKKL 541
Cdd:COG4942 94 ---ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDfLDAVRRLQYlKYLAPARREQAEELRADLA-----ELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 542 IDERECLLEQIKKLKGQLEGRQKnnKLDLLRAEdgilengtdahvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRL 621
Cdd:COG4942 166 RAELEAERAELEALLAELEEERA--ALEALKAE------------------RQKLLARLEKELAELAAELAELQQEAEEL 225
|
250
....*....|....*.
gi 568908290 622 ESQVTRYRSAAENAEK 637
Cdd:COG4942 226 EALIARLEAEAAAAAE 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
388-679 |
1.99e-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: 41.58 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 388 QYEEKNKEFEREKHAHSILQFQFAEvkealRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEffdS 467
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRLEELR-----EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE---E 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 468 IRSERDDLREETVKLKEELKkhgiilnseiatngetsdtvndvgyqaptkITKEELNALKSAGEgTLDVRLKKLIDEREC 547
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQ------------------------------ILRERLANLERQLE-ELEAQLEELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 548 LLEQIKKLKGQLEGRQKN-----NKLDLLRAEDGILENGtdahvmdlQRDANRQISDLKFKLAKSEQEITALEQNVIRLE 622
Cdd:TIGR02168 335 LAEELAELEEKLEELKEElesleAELEELEAELEELESR--------LEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568908290 623 SQVT-----RYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 679
Cdd:TIGR02168 407 ARLErledrRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
452-666 |
2.94e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 452 DKKIGALERQKEFFDS-IRSERDDLREETVKLKEELKKHGII-LNSEIATNGETSDTVND--VGYQAPTKITKEELNALK 527
Cdd:COG3206 167 ELRREEARKALEFLEEqLPELRKELEEAEAALEEFRQKNGLVdLSEEAKLLLQQLSELESqlAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 528 SAGEGTLDVRLKKLIDEreclleQIKKLKGQLegrqknnkLDLLRAEDGILENGTDAH--VMDLQR---DANRQISD-LK 601
Cdd:COG3206 247 AQLGSGPDALPELLQSP------VIQQLRAQL--------AELEAELAELSARYTPNHpdVIALRAqiaALRAQLQQeAQ 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568908290 602 FKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELkaekRKLQRELRSA-------LDKTEELEVS 666
Cdd:COG3206 313 RILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL----RRLEREVEVArelyeslLQRLEEARLA 380
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
315-662 |
3.13e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 315 LNELKDQIQDVEGK--------YMQGLKEMKDSLAEVEEKYKKAMVSNAQLD---NEKTNFMYQVDTLKDMLLELEEQLA 383
Cdd:PRK02224 189 LDQLKAQIEEKEEKdlherlngLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDLRETIA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 384 esqrqyeeknkEFEREKHAHSilqfqfAEVKEALRQREEMLEEIRQ--------------LQQKQAGFIREISDLQETIE 449
Cdd:PRK02224 269 -----------ETEREREELA------EEVRDLRERLEELEEERDDllaeaglddadaeaVEARREELEDRDEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 450 WKDKKIGALERQKEffdSIRSERDDLREETVKLKEELKKhgiiLNSEIATNGETSDTvndvgYQAPTKITKEELNALKSA 529
Cdd:PRK02224 332 ECRVAAQAHNEEAE---SLREDADDLEERAEELREEAAE----LESELEEAREAVED-----RREEIEELEEEIEELRER 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 530 GEGTlDVRLKKLIDERECLLEQikklKGQLEGRQKNNKLDLLRAEDGILENGT---------------DAHVMDLQRDAN 594
Cdd:PRK02224 400 FGDA-PVDLGNAEDFLEELREE----RDELREREAELEATLRTARERVEEAEAlleagkcpecgqpveGSPHVETIEEDR 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 595 RQISDLKFKLAKSEQEITALEQNVIRL------ESQVTRYRSAAENAEKI---------EDELKAE-KRKLQRELRSALD 658
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLERAedlveaEDRIERLEERREDLEELiaerretieEKRERAEeLRERAAELEAEAE 554
|
....
gi 568908290 659 KTEE 662
Cdd:PRK02224 555 EKRE 558
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
312-688 |
3.22e-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: 40.77 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 312 IKELNELKDQIQDVEGKymqgLKEMKDSLAEVEEKYKKamvSNAQLDNEKTnfmyQVDTLKDMLLELEEQLAESQRQYEE 391
Cdd:TIGR04523 39 EKKLKTIKNELKNKEKE----LKNLDKNLNKDEEKINN---SNNKIKILEQ----QIKDLNDKLKKNKDKINKLNSDLSK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 392 KNKEFEREKHAHSILQFQFAEVKEALRQREE----MLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQK----E 463
Cdd:TIGR04523 108 INSEIKNDKEQKNKLEVELNKLEKQKKENKKnidkFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKlniqK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 464 FFDSIRSERDDLREETVKLKEELKKHGIiLNSEIATNGETSDTVND---------VGYQAPTKITKEELNALKSAGEGTL 534
Cdd:TIGR04523 188 NIDKIKNKLLKLELLLSNLKKKIQKNKS-LESQISELKKQNNQLKDniekkqqeiNEKTTEISNTQTQLNQLKDEQNKIK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 535 D---------VRLKKLIDEREcllEQIKKLKGQLEGRQKNNKLDLLRAEDGILENgTDAHVMDLQ---RDANRQISDLKF 602
Cdd:TIGR04523 267 KqlsekqkelEQNNKKIKELE---KQLNQLKSEISDLNNQKEQDWNKELKSELKN-QEKKLEEIQnqiSQNNKIISQLNE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 603 KLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRS 682
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE 422
|
....*.
gi 568908290 683 ALLSQQ 688
Cdd:TIGR04523 423 LLEKEI 428
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
356-679 |
3.91e-03 |
|
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: 40.49 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 356 QLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREkhahsiLQFQFAEVKEALRQREEMLEEI----RQLQ 431
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQ------LVLANSELTEARTERDQFSQESgnldDQLQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 432 QKQAGFIREISDLQETIEwKDKKIGALERQKEF-FDSIRSERDDLREETVKLKEELKkhgiilnseiatngetsdtvndv 510
Cdd:pfam15921 381 KLLADLHKREKELSLEKE-QNKRLWDRDTGNSItIDHLRRELDDRNMEVQRLEALLK----------------------- 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 511 gyqaptkitkeelnALKSAGEGTLDVRLKKLIDEREClLEQIKKLKGQLEGRQknnklDLLRAedgILENGTdAHVMDLQ 590
Cdd:pfam15921 437 --------------AMKSECQGQMERQMAAIQGKNES-LEKVSSLTAQLESTK-----EMLRK---VVEELT-AKKMTLE 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 591 rDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELK-------------AEKRKLQRELRSAL 657
Cdd:pfam15921 493 -SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRnvqtecealklqmAEKDKVIEILRQQI 571
|
330 340
....*....|....*....|..
gi 568908290 658 DKTEELEVSNGHLVKRLEKMKA 679
Cdd:pfam15921 572 ENMTQLVGQHGRTAGAMQVEKA 593
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
284-477 |
3.93e-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: 40.43 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 284 LASLGGTSSRRGSGDTSISMDTEASIREIKELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTN 363
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 364 FMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEM-LEEIRQLQQKQAGFIREIS 442
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtLEEAEALENKIEDDEEEAR 971
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568908290 443 DLQETIEWKDKKIGA--------LERQKEFFDSIRSERDDLRE 477
Cdd:TIGR02168 972 RRLKRLENKIKELGPvnlaaieeYEELKERYDFLTAQKEDLTE 1014
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
404-657 |
4.40e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 404 SILQFQFAEVKEALRQREEMLEeiRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFFDSIRSERDDLREETVKLK 483
Cdd:COG4717 38 TLLAFIRAMLLERLEKEADELF--KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 484 EELKKHGIILNseiatngetsdtvndvgyQAPTKITKEELNALKSAGEGTLDvRLKKLIDERECLLEQIKKLKGQLEgrQ 563
Cdd:COG4717 116 EELEKLEKLLQ------------------LLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELA--E 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 564 KNNKLDLLRAEDGIlengtdahvmdlqrDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKiEDELK 643
Cdd:COG4717 175 LQEELEELLEQLSL--------------ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-ELEAA 239
|
250
....*....|....
gi 568908290 644 AEKRKLQRELRSAL 657
Cdd:COG4717 240 ALEERLKEARLLLL 253
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
416-614 |
5.21e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 416 ALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFF------DSIRSERDDLREETVKLKEElkkh 489
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvASAEREIAELEAELERLDAS---- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 490 giilNSEIATNGETSDTVndvgyqaptkitKEELNALKSAgEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQKNNKLD 569
Cdd:COG4913 684 ----SDDLAALEEQLEEL------------EAELEELEEE-LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568908290 570 L-LRAEDGILENGTDAHVMDLQRDANRQISDLKFKLAKSEQEITAL 614
Cdd:COG4913 747 LrALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERA 792
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
524-688 |
5.24e-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: 40.04 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 524 NALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEG--RQKNN---KLDLLRAEDGILENGTDAHVMDL------QRD 592
Cdd:TIGR02168 220 AELRELELALLVLRLEELREELEELQEELKEAEEELEEltAELQEleeKLEELRLEVSELEEEIEELQKELyalaneISR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 593 ANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVK 672
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
170
....*....|....*.
gi 568908290 673 RLEKMKANRSALLSQQ 688
Cdd:TIGR02168 380 QLETLRSKVAQLELQI 395
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
311-676 |
5.43e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.09 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 311 EIKELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKAmvsNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYE 390
Cdd:pfam05483 255 KMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHL---TKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 391 EKNKEFE---REKHAHSILQFQF----AEVKEALRQREEMLEEIR-QLQQKQAGFIREISDLQETIEWKDKKIGALERQK 462
Cdd:pfam05483 332 EKEAQMEelnKAKAAHSFVVTEFeattCSLEELLRTEQQRLEKNEdQLKIITMELQKKSSELEEMTKFKNNKEVELEELK 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 463 EFFDSIRSERDDlREETVKLKEELKKhgiilnseiatngetsdtvndvgyqaptkiTKEELNALKSAGEGT---LDVRLK 539
Cdd:pfam05483 412 KILAEDEKLLDE-KKQFEKIAEELKG------------------------------KEQELIFLLQAREKEihdLEIQLT 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 540 KLIDERECLLEQIKKLKGQLEGRQKNNKLDLLRAEDGILENgtdahvmdlqRDANRQISDLKFKLAKSEQEITALEQNVI 619
Cdd:pfam05483 461 AIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLEN----------KELTQEASDMTLELKKHQEDIINCKKQEE 530
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 620 RLESQVtryRSAAENAEKIEDELKAEKRKLQR---ELRSALDKTEELEVSNGHLVKRLEK 676
Cdd:pfam05483 531 RMLKQI---ENLEEKEMNLRDELESVREEFIQkgdEVKCKLDKSEENARSIEYEVLKKEK 587
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
410-687 |
7.10e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.82 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 410 FAEVKEALRQREEMLEEIRQLQQ-KQAGFIREISDLQETIEWKDKKI--------GALERQKEFFDSIRSERDdlreetv 480
Cdd:pfam12128 595 WAASEEELRERLDKAEEALQSAReKQAAAEEQLVQANGELEKASREEtfartalkNARLDLRRLFDEKQSEKD------- 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 481 KLKEELKKHGIILNSEIaTNGETSDTVNDVGYQAPTKITKEEL-------NALKSAGEGTLDVRLKKLIDERECLLEQik 553
Cdd:pfam12128 668 KKNKALAERKDSANERL-NSLEAQLKQLDKKHQAWLEEQKEQKreartekQAYWQVVEGALDAQLALLKAAIAARRSG-- 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 554 kLKGQLEGRQKNNKLDLL-RAEDGILENGTDAHVMDLQRDANR---------------------QISDLKFKLAKSEQEI 611
Cdd:pfam12128 745 -AKAELKALETWYKRDLAsLGVDPDVIAKLKREIRTLERKIERiavrrqevlryfdwyqetwlqRRPRLATQLSNIERAI 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 612 TALEQNVIRLESQVTRYRSAAEN----AEKIEDELKAEKRKLQRELRS----ALDKT-EELEVSNGHLVKRLEKMKANRS 682
Cdd:pfam12128 824 SELQQQLARLIADTKLRRAKLEMerkaSEKQQVRLSENLRGLRCEMSKlatlKEDANsEQAQGSIGERLAQLEDLKLKRD 903
|
....*
gi 568908290 683 ALLSQ 687
Cdd:pfam12128 904 YLSES 908
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
629-688 |
7.93e-03 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 38.37 E-value: 7.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 629 RSAAENAEKIeDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 688
Cdd:pfam11932 27 AAAAQSQKKI-DKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQI 85
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
313-667 |
8.10e-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: 39.62 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 313 KELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKamvsNAQLDNEKTNFMYQVDTLKDmlleleeqlaesqrQYEEK 392
Cdd:TIGR04523 124 VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNK----YNDLKKQKEELENELNLLEK--------------EKLNI 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 393 NKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQagfireiSDLQETIEWKDKKIGALERQkefFDSIRSER 472
Cdd:TIGR04523 186 QKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQN-------NQLKDNIEKKQQEINEKTTE---ISNTQTQL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 473 DDLREETVKLKEELKKHGIILNSEIATNGETSDTVNDVgyqaptkitKEELNALKSAGEGTLDVRLKKLIDEREcllEQI 552
Cdd:TIGR04523 256 NQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQL---------KSEISDLNNQKEQDWNKELKSELKNQE---KKL 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908290 553 KKLKGQLegRQKNNKLDLLRAEDGILENgtdaHVMDLQRD---ANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYR 629
Cdd:TIGR04523 324 EEIQNQI--SQNNKIISQLNEQISQLKK----ELTNSESEnseKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLE 397
|
330 340 350
....*....|....*....|....*....|....*...
gi 568908290 630 SAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSN 667
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETI 435
|
|
| |
