|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
3-130 |
6.81e-81 |
|
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and similar proteins; SLMAP, also called sarcolemmal-associated protein (SLAP), is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. It is a cardiac membrane protein that plays an important role in E-C coupling and the adrenergic response of the heart. Overexpression of the SLMAP gene has been associated with diabetes and endothelial dysfunction of macro- and micro-blood vessels. SLMAP contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438731 [Multi-domain] Cd Length: 126 Bit Score: 255.66 E-value: 6.81e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 3 SALAVFSCRPNSHPFQERHVYLDEPVKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINS 82
Cdd:cd22679 1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 528494936 83 QRLSRGSEESPPCEVLSGDIIQFGVDVTENTRKVTHGCIVSTIKLFLP 130
Cdd:cd22679 79 QRLSKGSEESEPRELHSGDIVQFGVDVVENSRKVTHGCIVATVTLFLP 126
|
|
| CC1_SLMAP |
cd21911 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal ... |
163-225 |
7.36e-27 |
|
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal membrane-associated protein (SLMAP), also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. SLMAP contains an N-terminal FHA domain followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409287 [Multi-domain] Cd Length: 63 Bit Score: 103.92 E-value: 7.36e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528494936 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLASTQEASESSWQALIDEDRLLSRLEVMGNQLQ 225
Cdd:cd21911 1 QELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQLS 63
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
163-814 |
3.57e-20 |
|
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: 96.28 E-value: 3.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLASTQEASESSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGirKELVA 242
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL--EELEA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 243 LTEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKY-NGAVNEIKDLTEKI 321
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEEL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 322 KLAEDKHEELTQKGLNEKKELQMRIEEMEEKEQALQARIEALQAdndftneRLTALQVRLEQLQEKSIKENNSFDHFLLK 401
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA-------RLDSLERLQENLEGFSEGVKALLKNQSGL 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 402 SGGDCTLIQQyIECQS--VRQLKEAVDSSINKL--SNFDEVIDA--HLQNNQTTVDNSLPsPDRLKENQIDAKECDMsdt 475
Cdd:TIGR02168 519 SGILGVLSEL-ISVDEgyEAAIEAALGGRLQAVvvENLNAAKKAiaFLKQNELGRVTFLP-LDSIKGTEIQGNDREI--- 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 476 lspskeKSSDDTSDGQMEEQELNEPQNRVSLLKEMDRSLEAGDTEQVIpHIHRELQEAQ-------ELANTG----KQKC 544
Cdd:TIGR02168 594 ------LKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNAL-ELAKKLRPGYrivtldgDLVRPGgvitGGSA 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 545 LELQAMLE--EERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQREN---TITTTREELYSAQEEILVLRHAMEAAT 619
Cdd:TIGR02168 667 KTNSSILErrREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQlrkELEELSRQISALRKDLARLEAEVEQLE 746
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 620 AERER---EITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASF-QLQSQHQ---ERASQLQGEVEKLQADCSGLQNEC 692
Cdd:TIGR02168 747 ERIAQlskELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIeQLKEELKalrEALDELRAELTLLNEEAANLRERL 826
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 693 DSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLgsiqDQHQQDASKLKIQLAQAESRTRDLQKE 772
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL----EALLNERASLEEALALLRSELEELSEE 902
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 528494936 773 YDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLKLLQDK 814
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| FHA_DMA-like |
cd22692 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest ... |
27-108 |
1.16e-17 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest protein 1 (DMA1), 2 (DMA2) and similar proteins; DMA1 (also known as checkpoint forkhead associated with RING domains-containing protein 1, or CHF1) and DMA2 (also known as checkpoint forkhead associated with RING domains-containing protein 2, or CHF2) are E3 ubiquitin-protein ligases which function in cell cycle retarding in conjunction with the UBC4 and UBC13/MMS2 complex, two E2 ubiquitin conjugating enzymes. They are involved in nutritional control of the cell cycle and required for proper spindle positioning, likely regulating septin ring deposition at the bud neck. DMA1 targets the degradation of G1 cyclin PCL1. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438744 [Multi-domain] Cd Length: 139 Bit Score: 80.30 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 27 PVKIGRSVARCRPAQNNAT-FDCKVLSRNHALVWfdHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCEVLSGDIIQF 105
Cdd:cd22692 38 QIHIGRYTERVRQAIYHPVvFKSKVVSRTHGCIK--VDEGNWYIKDVKSSSGTFLNHQRLSPASRTSKPYPLRDGDILQL 115
|
...
gi 528494936 106 GVD 108
Cdd:cd22692 116 GMD 118
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
172-814 |
1.53e-17 |
|
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: 87.80 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 172 LQEALHREQMLEQKLATLQRLLASTQEASESSWQALIDEDRllsrlevmgnqlqaySKNQTEDGIRKELVALTEDKHNYE 251
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS---------------ELEEEIEELQKELYALANEISRLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 252 ttakeslrrvlQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEEL 331
Cdd:TIGR02168 302 -----------QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 332 TQKG-----------------LNEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVR--------LEQLQE 386
Cdd:TIGR02168 371 ESRLeeleeqletlrskvaqlELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKelqaeleeLEEELE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 387 KSIKENNSFDHFLLKSGGDCTLIQQYI-----ECQSVRQLKEAVDSSINKLSNFDEVIDAHLQNNQTTVDNSLPSPDRLK 461
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALdaaerELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIS 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 462 enqIDAK-ECDMSDTLSPSKEKSSDDTSDGQMEEQELNEPQNR----VSLLKEMDRSLEAGDTEQVIPHIHRELQEAQEL 536
Cdd:TIGR02168 531 ---VDEGyEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELgrvtFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDL 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 537 ANTGKQKCLELQAML-------------EEERKTNRQQT-------------------EESAKQIRFLQTQLAKLQTDME 584
Cdd:TIGR02168 608 VKFDPKLRKALSYLLggvlvvddldnalELAKKLRPGYRivtldgdlvrpggvitggsAKTNSSILERRREIEELEEKIE 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 585 ALrEQRENTITTTREELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQ 664
Cdd:TIGR02168 688 EL-EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 665 SQH----QERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENK 740
Cdd:TIGR02168 767 EERleeaEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528494936 741 LGSIQDQHQQDA---SKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLKLLQDK 814
Cdd:TIGR02168 847 IEELSEDIESLAaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
506-813 |
5.28e-15 |
|
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: 79.72 E-value: 5.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 506 LLKEMDRSLEagdteqvipHIHRELQEAQ---ELANTGKQKCLELQAMLEEERKTNRQQTEESAKQirfLQTQLAKLQTD 582
Cdd:TIGR02168 194 ILNELERQLK---------SLERQAEKAErykELKAELRELELALLVLRLEELREELEELQEELKE---AEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 583 MEALREQrentITTTREELYSAQEEILVLRHAMEAATAErereITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQ 662
Cdd:TIGR02168 262 LQELEEK----LEELRLEVSELEEEIEELQKELYALANE----ISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 663 LQsqhQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLG 742
Cdd:TIGR02168 334 EL---AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 743 SIQDQHQQ---------------DASKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVN 807
Cdd:TIGR02168 411 RLEDRRERlqqeieellkkleeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
....*.
gi 528494936 808 LKLLQD 813
Cdd:TIGR02168 491 LDSLER 496
|
|
| FHA_VPS64-like |
cd22695 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ... |
6-126 |
7.30e-15 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 64 (VPS64) and similar proteins; This subfamily includes VPS64 (also called factor arrest protein 9 or FAR9) and factor arrest protein 10 (FAR10), which participate in the control of the re-entry into the cell cycle following pheromone treatment. VPS64 is also involved in vacuolar protein sorting. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438747 [Multi-domain] Cd Length: 133 Bit Score: 71.95 E-value: 7.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 6 AVFSCRPNSHPFQERHV---YLDEPVKIGRSVARCRPAQN---------------NATFDCKVLSRNHALVWFDHKTGKF 67
Cdd:cd22695 2 HILVLKSLNATFETKFLvvpFKPDGLKLGRPVTNSVNKNNsgskrdlfsqqvrpdNGNFDSRVLSRNHACLSCDPTTGKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 528494936 68 YLQDTKSSNGTFINSQRLSRGSeesppCEVLSGDIIQFGVDVTEntrKVTHGCIVSTIK 126
Cdd:cd22695 82 YIRDLKSSNGTFVNGQKIRQND-----VELKVGDEVDLGTDIDS---KIEHRKISAYVE 132
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-804 |
1.16e-13 |
|
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: 75.10 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 197 QEASESSWQALIDEDRLLSRLEVMGNQLQAYsknqtedgiRKELVALTEDKHNYETTAKESLRRVLQEKI---EVVRKLS 273
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEE---------RKRRDKLTEEYAELKEELEDLRAELEEVDKefaETRDELK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 274 EVERSLSNTEDECTHLREMNERTQEELRELANkyngavnEIKDLTEKIKLAEDKHEELTQkglnEKKELQMRIEEMEEKE 353
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSE-------ELADLNAAIAGIEAKINELEE----EKEDKALEIKKQEWKL 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 354 QALQA-------RIEALQADNDFTNERLTALQVRLEQLQ-EKSIKENNSFDHF----LLKSGGDCT--LIQQYIECQsvR 419
Cdd:TIGR02169 458 EQLAAdlskyeqELYDLKEEYDRVEKELSKLQRELAEAEaQARASEERVRGGRaveeVLKASIQGVhgTVAQLGSVG--E 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 420 QLKEAVDSSI-NKLSNF----DEVIDAHLQ-----------------NNQTTVDNSLPSPDRLKENQIDAKECD------ 471
Cdd:TIGR02169 536 RYATAIEVAAgNRLNNVvvedDAVAKEAIEllkrrkagratflplnkMRDERRDLSILSEDGVIGFAVDLVEFDpkyepa 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 472 ----MSDTLSPSK---------------------EKS------SDDTSDGQMEEQELNEPQNRVSL-LKEMDRSLEAGDT 519
Cdd:TIGR02169 616 fkyvFGDTLVVEDieaarrlmgkyrmvtlegelfEKSgamtggSRAPRGGILFSRSEPAELQRLRErLEGLKRELSSLQS 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 520 EQviPHIHRELQEAQELANTGKQKCLELQA---MLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALR---EQRENT 593
Cdd:TIGR02169 696 EL--RRIENRLDELSQELSDASRKIGEIEKeieQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEariEELEED 773
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 594 ITTTREELYS-----AQEEILVLRHAMEAATAERER------EITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQ 662
Cdd:TIGR02169 774 LHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRiearlrEIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE 853
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 663 -----LQSQHQERASQL---QGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQ 734
Cdd:TIGR02169 854 keienLNGKKEELEEELeelEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528494936 735 GDLENKLGSIQDQHQQDAS--KLKIQLAQAESRTRDLQ-------KEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQC 804
Cdd:TIGR02169 934 SEIEDPKGEDEEIPEEELSleDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
13-106 |
1.50e-13 |
|
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.
Pssm-ID: 438714 [Multi-domain] Cd Length: 92 Bit Score: 66.92 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 13 NSHPFQERHVYLDEPVKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINSQRLsrgseeS 92
Cdd:cd00060 6 DGDGGGREFPLTKGVVTIGRS------PDCDIVLDDPSVSRRHARIEVDG--GGVYLEDLGSTNGTFVNGKRI------T 71
|
90
....*....|....
gi 528494936 93 PPCEVLSGDIIQFG 106
Cdd:cd00060 72 PPVPLQDGDVIRLG 85
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
28-105 |
2.80e-13 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 65.29 E-value: 2.80e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528494936 28 VKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRLSRgseesPPCEVLSGDIIQF 105
Cdd:pfam00498 1 VTIGRS------PDCDIVLDDPSVSRRHAEIRYD-GGGRFYLEDLGSTNGTFVNGQRLGP-----EPVRLKDGDVIRL 66
|
|
| CC1_SLMAP-like |
cd21868 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ... |
167-204 |
4.55e-13 |
|
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar proteins; The family includes Sarcolemmal membrane-associated protein (SLMAP), its paralog TRAF3-interacting JNK-activating modulator (T3JAM), and similar proteins. SLMAP, also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. T3JAM, also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. SLMAP contains an N-terminal FHA domain, followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409286 [Multi-domain] Cd Length: 38 Bit Score: 63.66 E-value: 4.55e-13
10 20 30
....*....|....*....|....*....|....*...
gi 528494936 167 QLSQYLQEALHREQMLEQKLATLQRLLASTQEASESSW 204
Cdd:cd21868 1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
527-803 |
9.61e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 9.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 527 HRELQEAQELantgkqkcLELQAMLEEERKTNRQQtEESAKQIRFLQTQLAKLQTD---MEALREQRENTITTTREELYS 603
Cdd:COG1196 215 YRELKEELKE--------LEAELLLLKLRELEAEL-EELEAELEELEAELEELEAElaeLEAELEELRLELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 604 AQEEILVLRHAMEAATAERERE---ITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQ-LQSQHQERASQLQGEVE 679
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLeerRRELEERLEELEEELAELEEELEELEEELEELEEELEeAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 680 KLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKsqgdLENKLGSIQDQHQQDASKLKIQL 759
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER----LEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 528494936 760 AQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQ 803
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
14-106 |
1.07e-11 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 61.90 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 14 SHPFQERHVYLDE-PVKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716 8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
|
90
....*....|....
gi 528494936 93 pPCEVLSGDIIQFG 106
Cdd:COG1716 75 -PAPLRDGDVIRLG 87
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
52-106 |
1.29e-11 |
|
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 (AGGF1) and similar proteins; AGGF1, also called angiogenic factor VG5Q, or G patch domain-containing protein 7 (GPATC7), or vasculogenesis gene on 5q protein, is an angiogenic factor involved in vascular development, angiogenesis, specification of hemangioblasts, and differentiation of veins. It promotes angiogenesis and the proliferation of endothelial cells. It inhibits inflammatory effect and preserve vascular integrity in non-nervous system diseases. Mutated AGGF1 causes susceptibility to Klippel-Trenaunay syndrome, a vascular disorder. Increased AGGF1 expression is associated with tumor angiogenesis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438738 [Multi-domain] Cd Length: 123 Bit Score: 62.30 E-value: 1.29e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 528494936 52 SRNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCEVLSGDIIQFG 106
Cdd:cd22686 48 SKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPYPLTHGDELKIG 102
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
531-796 |
2.03e-11 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 67.73 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 531 QEAQELANTgkqkcLeLQAMLEEERKTNRQQTEESakqIRFLQTQLAKLQTDMEALRE-----QRENTITTTREELYSAQ 605
Cdd:COG3206 148 ELAAAVANA-----L-AEAYLEQNLELRREEARKA---LEFLEEQLPELRKELEEAEAaleefRQKNGLVDLSEEAKLLL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 606 EEIlvlrhameaatAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERAsQLQGEVEKLQADc 685
Cdd:COG3206 219 QQL-----------SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLA-ELEAELAELSAR- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 686 sgLQNECDSLRAekstLMQKLNRLEEELDSSRERS-ATLSSNLNALEKSQGDLENKLGSIQDQHQQdasklkiqLAQAES 764
Cdd:COG3206 286 --YTPNHPDVIA----LRAQIAALRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAE--------LPELEA 351
|
250 260 270
....*....|....*....|....*....|..
gi 528494936 765 RTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRS 796
Cdd:COG3206 352 ELRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
515-765 |
1.59e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 515 EAGDTEQVIPHIHRELQEAQELANTGKQKCLELQAMLEEERKTNRQQTEESA---KQIRFLQTQLAKLQTDMEALREQRE 591
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELArleQDIARLEERRRELEERLEELEEELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 592 NT---ITTTREELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQ 668
Cdd:COG1196 327 ELeeeLEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 669 ERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQH 748
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
250
....*....|....*..
gi 528494936 749 QQDASKLKIQLAQAESR 765
Cdd:COG1196 487 AEAAARLLLLLEAEADY 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
528-803 |
2.22e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 528 RELQEAQELAntgkQKCLELQAMLEEERKTNRQQTEesaKQIRFLQTQLAKLQTDMEALREqRENTITTTREELYSAQEE 607
Cdd:COG1196 235 RELEAELEEL----EAELEELEAELEELEAELAELE---AELEELRLELEELELELEEAQA-EEYELLAELARLEQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 608 ILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQADcsg 687
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE--- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 688 LQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESRTR 767
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270
....*....|....*....|....*....|....*.
gi 528494936 768 DLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQ 803
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| CC1_T3JAM |
cd21912 |
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ... |
164-204 |
4.28e-10 |
|
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; TRAF3-interacting JNK-activating modulator (T3JAM), also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. The model corresponds to a conserved region that shows high sequence similarity with the first CC (CC1) domain of Sarcolemmal membrane-associated protein (SLMAP), which is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409288 [Multi-domain] Cd Length: 45 Bit Score: 55.43 E-value: 4.28e-10
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 528494936 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLASTQEASESSW 204
Cdd:cd21912 5 EILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
164-812 |
7.49e-10 |
|
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: 62.93 E-value: 7.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLASTQEASESSWQALIDEDRL------------LSRLEVMGNQLQAYSKNQ 231
Cdd:pfam12128 259 RLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGelsaadaavakdRSELEALEDQHGAFLDAD 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 232 TE---------DGIRKEL------VALTEDKHNYETTAKEslRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERT 296
Cdd:pfam12128 339 IEtaaadqeqlPSWQSELenleerLKALTGKHQDVTAKYN--RRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDD 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 297 QEEL-RELANKYNGAVNEIKDLTEKIKLA--EDK---------HEELTQKGLNekkelQMRIEEMEEKEQALQARIEALQ 364
Cdd:pfam12128 417 LQALeSELREQLEAGKLEFNEEEYRLKSRlgELKlrlnqatatPELLLQLENF-----DERIERAREEQEAANAEVERLQ 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 365 ADN--------------DFTNERLTALQVRLEQLQEKSIKENNSFDHFLLKSGGDCTliQQYIECQSVRQL------KEA 424
Cdd:pfam12128 492 SELrqarkrrdqasealRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWE--QSIGKVISPELLhrtdldPEV 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 425 VDSSINKLSNFDEVidaHLQNNQTTVDNSLPSPDRLKEnQIDAKECDMSDTLSPSKEKSSD-DTSDGQMEEQELNEP--- 500
Cdd:pfam12128 570 WDGSVGGELNLYGV---KLDLKRIDVPEWAASEEELRE-RLDKAEEALQSAREKQAAAEEQlVQANGELEKASREETfar 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 501 ----QNRVSL--LKEMDRSLEAGDTEQVIPHIHRELQEAQELANTGKQKCLELQAMLEEERKTNRQQTEESAKQIRFLQ- 573
Cdd:pfam12128 646 talkNARLDLrrLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEg 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 574 ---TQLAKLQTDMEALREQRENTITTTREELYSAqeeiLVLRHAMEAATAEREREITALQGDLSivtaELDKWRQTAAKY 650
Cdd:pfam12128 726 aldAQLALLKAAIAARRSGAKAELKALETWYKRD----LASLGVDPDVIAKLKREIRTLERKIE----RIAVRRQEVLRY 797
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 651 EVeisnlqasfQLQSQHQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRleeELDSSRERSATLSSNLNAL 730
Cdd:pfam12128 798 FD---------WYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEM---ERKASEKQQVRLSENLRGL 865
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 731 EKSQGDL-ENKLGSIQDQHQQDASKLKIQLAQ----AESRTRDLQKEYDDTQSLLSDLR-----QRYEQTEQEKRSINDE 800
Cdd:pfam12128 866 RCEMSKLaTLKEDANSEQAQGSIGERLAQLEDlklkRDYLSESVKKYVEHFKNVIADHSgsglaETWESLREEDHYQNDK 945
|
730
....*....|..
gi 528494936 801 LEQCKVNLKLLQ 812
Cdd:pfam12128 946 GIRLLDYRKLVP 957
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
164-739 |
9.14e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 9.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLAStQEASESSWQALIDEDRL-LSRLEVMGNQLQA--YSKNQTEDGIRKEL 240
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEE-LEAELAELEAELEELRLeLEELELELEEAQAeeYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 241 VALTEDKHNYETT---AKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDL 317
Cdd:COG1196 305 ARLEERRRELEERleeLEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 318 TEKIKLAEDKHEELTQKGLNEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEKSIKENNSFDH 397
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 398 FLLKSGGDCTLIQQYIECQSVRQLKEAVDSSINKLSNFDE-----VIDAHLQNNQTTVDNSLPSPDRLKENQIDAKECDM 472
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 473 SDTLSPSKEKssDDTSDGQMEEQELNEPQNRVSLL---KEMDRSLEAGDTEQVIPHIHRELQEAQELANTGKQKCLELQA 549
Cdd:COG1196 545 AAALQNIVVE--DDEVAAAAIEYLKAAKAGRATFLpldKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 550 MLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQRENTITTTREELYSAQEEILVLRHAMEAATAEREREITAL 629
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 630 QGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQADcsGLQNEcDSLRAEKSTLMQKLNRL 709
Cdd:COG1196 703 EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELP--EPPDL-EELERELERLEREIEAL 779
|
570 580 590
....*....|....*....|....*....|....*..
gi 528494936 710 -------EEELDSSRERSATLSSNLNALEKSQGDLEN 739
Cdd:COG1196 780 gpvnllaIEEYEELEERYDFLSEQREDLEEARETLEE 816
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
526-730 |
9.84e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.63 E-value: 9.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 526 IHRELQEAQElantgKQKCLE-----LQAMLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQRENT---ITTT 597
Cdd:COG4913 240 AHEALEDARE-----QIELLEpirelAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLeaeLERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 598 REELYSAQEEILVLRHAMEAATAER----EREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQlqsqhqERASQ 673
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRleqlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA------ALRAE 388
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 528494936 674 LQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNAL 730
Cdd:COG4913 389 AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
507-750 |
1.17e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.39 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 507 LKEMDRSLEAGDTEqvIPHIHRELQEAQELANTGKQKCLELQAMLEEERKTNRQQTEESA----KQIRFLQTQLAKLQTD 582
Cdd:TIGR02169 232 KEALERQKEAIERQ--LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkEKIGELEAEIASLERS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 583 MEALREQRE-------------NTITTTREELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAK 649
Cdd:TIGR02169 310 IAEKERELEdaeerlakleaeiDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 650 YEVEISNLQ----ASFQLQSQHQERASQLQGEVEKLQADCSG-------LQNECDSLRAEKSTLMQKLNRLEEELDSSRE 718
Cdd:TIGR02169 390 YREKLEKLKreinELKRELDRLQEELQRLSEELADLNAAIAGieakineLEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
250 260 270
....*....|....*....|....*....|..
gi 528494936 719 RSATLSSNLNALEKSQGDLENKLGSIQDQHQQ 750
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARA 501
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
179-817 |
1.18e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.39 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 179 EQMLEQKLATLQRLLASTQEASEssWQALIDEDR------LLSRLEVMGNQLQAYSKNQteDGIRKELVALTE--DKHNY 250
Cdd:TIGR02169 190 DLIIDEKRQQLERLRREREKAER--YQALLKEKReyegyeLLKEKEALERQKEAIERQL--ASLEEELEKLTEeiSELEK 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 251 ETTAKESLRRVLQEKIE---------VVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKI 321
Cdd:TIGR02169 266 RLEEIEQLLEELNKKIKdlgeeeqlrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREI 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 322 KlaedkheelTQKGlnEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEKsikennsfdHFLLK 401
Cdd:TIGR02169 346 E---------EERK--RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE---------INELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 402 SGGDCTLIQQYIECQSVRQLKEAVDSSINKLSNFDEV-------IDAHLQNNQTTVDnslpspDRLKENQ----IDAKEC 470
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEkedkaleIKKQEWKLEQLAA------DLSKYEQelydLKEEYD 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 471 DMSDTLSPSKEKSSDDTSDGQMEEQELNEPQnRVSLLKEMDRSLEAGDTEQVIpHIHRELQEAQELANTGK--------- 541
Cdd:TIGR02169 480 RVEKELSKLQRELAEAEAQARASEERVRGGR-AVEEVLKASIQGVHGTVAQLG-SVGERYATAIEVAAGNRlnnvvvedd 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 542 ---QKCLE--------------LQAMLEEERKTNRQQTE---------------------------------ESAKQI-- 569
Cdd:TIGR02169 558 avaKEAIEllkrrkagratflpLNKMRDERRDLSILSEDgvigfavdlvefdpkyepafkyvfgdtlvvediEAARRLmg 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 570 --------------------------------RFLQTQLAKLQTDMEALREQREntitTTREELYSAQEEILVLRHAMEA 617
Cdd:TIGR02169 638 kyrmvtlegelfeksgamtggsraprggilfsRSEPAELQRLRERLEGLKRELS----SLQSELRRIENRLDELSQELSD 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 618 ATA---EREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQ----LQSQHQERASQLQGEVEKLQADCSG--- 687
Cdd:TIGR02169 714 ASRkigEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKeleaRIEELEEDLHKLEEALNDLEARLSHsri 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 688 --LQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQH---QQDASKLKIQLAQA 762
Cdd:TIGR02169 794 peIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIenlNGKKEELEEELEEL 873
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 528494936 763 ESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLKLLQDKGSN 817
Cdd:TIGR02169 874 EAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
312-633 |
1.31e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 312 NEIKDLTEKIKLAEDKHEELTQkglnEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEKsike 391
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEK----ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER---- 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 392 nnsfdhfllksggdctLIQQYIECQSVRQLKEAVDSSINKLSNFDEVIDAHLQNNQTTVDNSLPSPDRLKEnQIDAKECD 471
Cdd:TIGR02168 749 ----------------IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE-ALDELRAE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 472 MSDT---LSPSKEKSSDDTSDGQMEEQELNEPQNRVSLLKEMDRSLEA--GDTEQVIPHIHRELQEAQELANTGKQKCLE 546
Cdd:TIGR02168 812 LTLLneeAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAeiEELEELIEELESELEALLNERASLEEALAL 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 547 LQAMLEEERKTNR---QQTEESAKQIRFLQTQLAKLQTDMEALREQRENTITTTREELYSAQEEILVLRHAMEAATAERE 623
Cdd:TIGR02168 892 LRSELEELSEELReleSKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR 971
|
330
....*....|
gi 528494936 624 REITALQGDL 633
Cdd:TIGR02168 972 RRLKRLENKI 981
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
275-803 |
1.41e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 275 VERSLSNTEDECTHLREMNERTQEelRELANKYNGAVNEIKDLTEKIKLAEDKHEELTQKglneKKELQMRIEEMEEKEQ 354
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEE--KDLHERLNGLESELAELDEEIERYEEQREQARET----RDEADEVLEEHEERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 355 ALQ---ARIEALQADNDFTNERLTALQVRLEQLQEKSIKENNSFDHFLLKSGGDCTLIqqyiecqsvrqlkEAVDSSINK 431
Cdd:PRK02224 252 ELEtleAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADA-------------EAVEARREE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 432 LSNFDEVIDAHLQNNQTTVDNSLPSPDRLKENQIDAKEcdMSDTLspsKEKSSDDTSDGQMEEQELNEPQNRVSLLKEMD 511
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE--RAEEL---REEAAELESELEEAREAVEDRREEIEELEEEI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 512 RSLEA--GDTEQVIPHIHRELQEAQELANTGKQKCLELQAMLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQ 589
Cdd:PRK02224 394 EELRErfGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEED 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 590 RENtitttREELYSAQEEIlvlrhamEAATAEREREITALQgDLSIVTAELDKWRQTAakyeveisnlQASFQLQSQHQE 669
Cdd:PRK02224 474 RER-----VEELEAELEDL-------EEEVEEVEERLERAE-DLVEAEDRIERLEERR----------EDLEELIAERRE 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 670 RASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQ----------KLNRLEEELDSSRERSATLSSNLNALEksqgDLEN 739
Cdd:PRK02224 531 TIEEKRERAEELRERAAELEAEAEEKREAAAEAEEeaeeareevaELNSKLAELKERIESLERIRTLLAAIA----DAED 606
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528494936 740 KLGSIQDQHQQDASK---LKIQLAQAESRTRDLQKEYDDTQslLSDLRQRYEQTEQEKRSINDELEQ 803
Cdd:PRK02224 607 EIERLREKREALAELndeRRERLAEKRERKRELEAEFDEAR--IEEAREDKERAEEYLEQVEEKLDE 671
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
264-786 |
1.73e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.59 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 264 EKIEVVRKLSEVERSLSNTEDECTHL---REMNERTQEELRELANKYNGAVNEIKDLTEKI-KLAEDKHEELTqkglnEK 339
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYeeqREQARETRDEADEVLEEHEERREELETLEAEIeDLRETIAETER-----ER 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 340 KELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEKSIKENNSFDhfllksggDCTLIQQYIECQSVR 419
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLE--------ECRVAAQAHNEEAES 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 420 QLKEAVD--SSINKLSNFDEVIDAHLQNNQTTVDNSlpspdrlkENQIDAKECDMsDTLSPSKEKSSDDTSDGQMEEQEL 497
Cdd:PRK02224 347 LREDADDleERAEELREEAAELESELEEAREAVEDR--------REEIEELEEEI-EELRERFGDAPVDLGNAEDFLEEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 498 NEPQNRvslLKEMDRSLEAGdteqvIPHIHRELQEAQELANTGK-----------------QKCLELQAMLEEERKTNRQ 560
Cdd:PRK02224 418 REERDE---LREREAELEAT-----LRTARERVEEAEALLEAGKcpecgqpvegsphvetiEEDRERVEELEAELEDLEE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 561 QTE------ESAKQIRFLQTQLAKLQT---DMEALREQRENTITTTREELYSAQEEILVLRHAME----AATAERER--- 624
Cdd:PRK02224 490 EVEeveerlERAEDLVEAEDRIERLEErreDLEELIAERRETIEEKRERAEELRERAAELEAEAEekreAAAEAEEEaee 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 625 ---EITALQGDLSIVTAELDKWRQ------TAAKYEVEISNLQASF-QLQSQHQERASQLQGEVEKLQADCSGLQNE-CD 693
Cdd:PRK02224 570 areEVAELNSKLAELKERIESLERirtllaAIADAEDEIERLREKReALAELNDERRERLAEKRERKRELEAEFDEArIE 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 694 SLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENklgsiqdqhqqdaskLKIQLAQAESRTRDLQKEY 773
Cdd:PRK02224 650 EAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE---------------LRERREALENRVEALEALY 714
|
570 580
....*....|....*....|
gi 528494936 774 DDTQSLLS-------DLRQR 786
Cdd:PRK02224 715 DEAEELESmygdlraELRQR 734
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
179-758 |
2.82e-09 |
|
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: 60.90 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 179 EQMLEQKLATLQRLLAS--------TQEASESSWQAlideDRLLSRLEVmgnqLQAYSKNQTEDGIRkELVALTEDKHNY 250
Cdd:pfam15921 259 ELLLQQHQDRIEQLISEheveitglTEKASSARSQA----NSIQSQLEI----IQEQARNQNSMYMR-QLSDLESTVSQL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 251 ETTAKESlRRVLQEKIEvvrklsEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEE 330
Cdd:pfam15921 330 RSELREA-KRMYEDKIE------ELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKR 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 331 LTQKGLNE-------KKELQMRIEEMEEKEQALQA-----------RIEALQADNDfTNERLTALQVRLEQLQE--KSIK 390
Cdd:pfam15921 403 LWDRDTGNsitidhlRRELDDRNMEVQRLEALLKAmksecqgqmerQMAAIQGKNE-SLEKVSSLTAQLESTKEmlRKVV 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 391 ENNSFDHFLLKSGgDCTLIQQYIECQSVRQLKEAVDSSINKLSNfdeVIDAHLQNNQTTVDNSlpspDRLKENQidaKEC 470
Cdd:pfam15921 482 EELTAKKMTLESS-ERTVSDLTASLQEKERAIEATNAEITKLRS---RVDLKLQELQHLKNEG----DHLRNVQ---TEC 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 471 DMSDTLSPSKEKssddtsdgqMEEQELNEPQNRVSLLKEMDRS-----LEAGDTEQVIPHIHRELQEAQELANTGKQKCL 545
Cdd:pfam15921 551 EALKLQMAEKDK---------VIEILRQQIENMTQLVGQHGRTagamqVEKAQLEKEINDRRLELQEFKILKDKKDAKIR 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 546 ELQAMLEEERKTNRQQTEESAKQIRFLQtqlaklqtDMEALREQRENTITTTREELYSAQEEILVLRHAMEAATAERERE 625
Cdd:pfam15921 622 ELEARVSDLELEKVKLVNAGSERLRAVK--------DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETT 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 626 ITALQGDLSIVTAELDKWRQTAAKYE-VEISNLQASFQLQSQHQERASQ---LQGEVEKLQADCSGLQNECDSLRAEKST 701
Cdd:pfam15921 694 TNKLKMQLKSAQSELEQTRNTLKSMEgSDGHAMKVAMGMQKQITAKRGQidaLQSKIQFLEEAMTNANKEKHFLKEEKNK 773
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528494936 702 LMQKL-------NRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQD---QHQQDASKLKIQ 758
Cdd:pfam15921 774 LSQELstvatekNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDiiqRQEQESVRLKLQ 840
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
205-795 |
2.94e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 205 QALIDEDRLLsRLEVMGNQLQAYSKNQTEDGIRKELVALTEDKHNYETTAKESLRRVLQEKIEVVRK--------LSEVE 276
Cdd:COG1196 216 RELKEELKEL-EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELeleeaqaeEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 277 RSLSNTEDECTHLREMNERTQEELRELANkyngavnEIKDLTEKIKLAEDKHEELTQKGLNEKKELQMRIEEMEEKEQAL 356
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEE-------ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 357 ----QARIEALQADNDFTNERLTALQVRLEQLQEKSIKENNSFDHFLLKSggdcTLIQQYIECQsvRQLKEAVDSSINKL 432
Cdd:COG1196 368 leaeAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE----RLEEELEELE--EALAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 433 SNFDEVIDAHLQNNQTTVDNSLPSPDRLKENQIDAKEcdMSDTLSPSKEKSSDDTSDGQMEEQELNEPQN--RVSLLKEM 510
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA--LAELLEELAEAAARLLLLLEAEADYEGFLEGvkAALLLAGL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 511 DRSLEAGDTEQVIPHIHRELQEAQELANTGK---------QKCLELQAMLEEERKTNRQQTEESAKQIRFLQTQLAKLQT 581
Cdd:COG1196 520 RGLAGAVAVLIGVEAAYEAALEAALAAALQNivveddevaAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGA 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 582 DMEALREQREntittTREELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASF 661
Cdd:COG1196 600 AVDLVASDLR-----EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 662 QLQSQHQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKS----QGDL 737
Cdd:COG1196 675 LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEElleeEALE 754
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528494936 738 ENKLGSIQDQHQQDASKLKIQL--------------AQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKR 795
Cdd:COG1196 755 ELPEPPDLEELERELERLEREIealgpvnllaieeyEELEERYDFLSEQREDLEEARETLEEAIEEIDRETR 826
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
177-801 |
5.13e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.03 E-value: 5.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 177 HREQMLEQKLATLQRLLASTQEASESSWQALIDEDRLLSRLEVMGNQLQAYSK---------NQTEDGIRKELVALTED- 246
Cdd:TIGR04523 33 TEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKdlndklkknKDKINKLNSDLSKINSEi 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 247 --KHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKIKLA 324
Cdd:TIGR04523 113 knDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 325 EDKHEELTQKGLNEK------KELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEKSIKENNSFDHF 398
Cdd:TIGR04523 193 KNKLLKLELLLSNLKkkiqknKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 399 LLKSGGDCTLIQQYIEcqsvrQLKEaVDSSINKLSNF-DEVIDAHLQNNQTTVDNSLpspdRLKENQIDAKE---CDMSD 474
Cdd:TIGR04523 273 QKELEQNNKKIKELEK-----QLNQ-LKSEISDLNNQkEQDWNKELKSELKNQEKKL----EEIQNQISQNNkiiSQLNE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 475 TLSPSKEKSSDDTSDGQMEEQELNEPQNRVSLLKEMDRSL--EAGDTEQVIPHIHRELQEAQELANTGKQKCLELQA--- 549
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYkqEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQeke 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 550 MLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQREntitttreelySAQEEILVLrhameaataerEREITAL 629
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE-----------SLETQLKVL-----------SRSINKI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 630 QGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQeraSQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNR- 708
Cdd:TIGR04523 481 KQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKI---SSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKe 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 709 -LEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESRTRDL---QKEYDDTQSLLSDLR 784
Cdd:TIGR04523 558 nLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELekaKKENEKLSSIIKNIK 637
|
650
....*....|....*..
gi 528494936 785 QRYEQTEQEKRSINDEL 801
Cdd:TIGR04523 638 SKKNKLKQEVKQIKETI 654
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
565-798 |
9.04e-09 |
|
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: 58.24 E-value: 9.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 565 SAKQIRFLQTQLAKLQTDMEALREQRENT---ITTTREELYSAQEEILVLR---HAMEAATAEREREITALQGDLSIVTA 638
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALkkeEKALLKQLAALERRIAALArriRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 639 ELDKWRQTAAKYeveisnLQASFQLQSQ-------HQERASQLQGEVEKLQADCSGLQNECDSLRAEKstlmQKLNRLEE 711
Cdd:COG4942 98 ELEAQKEELAEL------LRALYRLGRQpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADL----AELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 712 ELDSSRERsatlssnLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTE 791
Cdd:COG4942 168 ELEAERAE-------LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
....*..
gi 528494936 792 QEKRSIN 798
Cdd:COG4942 241 ERTPAAG 247
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
550-808 |
1.08e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 550 MLEEerktnrQQTEESAKQIRFLQTQLAKLQTDMEALREQRE--NTITTTREELYSAQEEILVLRHAMEAATAEREREit 627
Cdd:COG4913 217 MLEE------PDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAQR-- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 628 alqgdlsivtaELDKWRQTAAKYEVEISNLQASfqlQSQHQERASQLQGEVEKLQADCSGLQNEcdslraEKSTLMQKLN 707
Cdd:COG4913 289 -----------RLELLEAELEELRAELARLEAE---LERLEARLDALREELDELEAQIRGNGGD------RLEQLEREIE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 708 RLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQdasklkiQLAQAESRTRDLQKEYDDTQSLLSDLRQRY 787
Cdd:COG4913 349 RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA-------LLEALEEELEALEEALAEAEAALRDLRREL 421
|
250 260
....*....|....*....|.
gi 528494936 788 EQTEQEKRSindeLEQCKVNL 808
Cdd:COG4913 422 RELEAEIAS----LERRKSNI 438
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
256-715 |
1.98e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.99 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 256 ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERtQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEELTQkg 335
Cdd:PRK01156 315 SNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQ-ILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSA-- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 336 lnekkELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEKsiKENNSFDHFLLKSGGDCTLIQQYIEC 415
Cdd:PRK01156 392 -----FISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALREN--LDELSRNMEMLNGQSVCPVCGTTLGE 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 416 QSVRQLKEAVDssiNKLSNFDEVIDaHLQNNQTTVDNSLPSPDRLKEnQIDAKECDMSDTLSPSKEKSSDDTSDGQMEEQ 495
Cdd:PRK01156 465 EKSNHIINHYN---EKKSRLEEKIR-EIEIEVKDIDEKIVDLKKRKE-YLESEEINKSINEYNKIESARADLEDIKIKIN 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 496 ELNEPQNRVSLLKEMDRSLEAGDTEQviphihrelqeaqelANTGKQKCLELQAMLEEErkTNRQQTEESAKQIRFLQTQ 575
Cdd:PRK01156 540 ELKDKHDKYEEIKNRYKSLKLEDLDS---------------KRTSWLNALAVISLIDIE--TNRSRSNEIKKQLNDLESR 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 576 LAKLQTDMEALREQRENTITTTREELYSAQEEILVLRhameaataEREREITALQGDLSivtaelDKWRQTAAKYEVEIS 655
Cdd:PRK01156 603 LQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQ--------ENKILIEKLRGKID------NYKKQIAEIDSIIPD 668
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 656 NLQASFQLqSQHQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDS 715
Cdd:PRK01156 669 LKEITSRI-NDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLES 727
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
301-803 |
2.41e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 301 RELANKYNGAVNEIKDLTEKIKLAEDKHEELTQKGLNEK-KELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQV 379
Cdd:COG1196 209 AEKAERYRELKEELKELEAELLLLKLRELEAELEELEAElEELEAELEELEAELAELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 380 RLEQLQEKSIKENNSFDHFLLKSGGDCTLIQQYIECQSV-----RQLKEAVDSSINKLSNFDEVIDAhLQNNQTTVDNSL 454
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAEleeelEELEEELEELEEELEEAEEELEE-AEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 455 PSPDRLKENQIDAKECDMSDTLSPSKEKSSDDTSDGQMEEQELNEPQNRVSLLKEM-DRSLEAGDTEQVIPHIHRELQEA 533
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELeELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 534 QELANTGKQKCLELQAMLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQRENTITTTREELYSAQEEILVLRH 613
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 614 AMEAATAEREREI-TALQGDLSIVTAELDKWRQTAAKYEVEISNLQASF-QLQSQHQERASQLQGEVEKLQADCSGLQNE 691
Cdd:COG1196 528 VLIGVEAAYEAALeAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFlPLDKIRARAALAAALARGAIGAAVDLVASD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 692 CDSLRAEKSTLMQKL---NRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESRTRD 768
Cdd:COG1196 608 LREADARYYVLGDTLlgrTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER 687
|
490 500 510
....*....|....*....|....*....|....*
gi 528494936 769 LQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQ 803
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELE 722
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
28-85 |
2.50e-08 |
|
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.
Pssm-ID: 214578 [Multi-domain] Cd Length: 52 Bit Score: 50.64 E-value: 2.50e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 528494936 28 VKIGRSvarcrPAQNNATFDCKVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRL 85
Cdd:smart00240 1 VTIGRS-----SEDCDIQLDGPSISRRHAVIVYD-GGGRFYLIDLGSTNGTFVNGKRI 52
|
|
| FHA_TCF19 |
cd22685 |
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ... |
28-119 |
2.67e-08 |
|
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar proteins; TCF-19, also called transcription factor SC1, was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It also functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. TCF-19 contains an N-terminal fork head association domain (FHA), a proline rich region, and a C-terminal plant homeodomain (PHD) finger. The FHA domain may serve as a nuclear signaling domain or as a phosphoprotein binding domain. The proline rich region is a common characteristic of trans-activating factors. The PHD finger may allow TCF-19 to interact with chromatin via methylated histone H3.
Pssm-ID: 438737 [Multi-domain] Cd Length: 130 Bit Score: 53.19 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 28 VKIGRSVARCRPAQNNATFDcKVLSRNHALVW---FDHKTGKFYLQDTkSSNGTFINSQRLSRGSEEsppcEVLSGDIIQ 104
Cdd:cd22685 30 YRIGRNPEVCDVFLCSSQHP-NLISREHAEIHaerDGNGNWKVLIEDR-STNGTYVNDVRLQDGQRR----ELSDGDTIT 103
|
90
....*....|....*..
gi 528494936 105 FG--VDVTENTRKVTHG 119
Cdd:cd22685 104 FGhkNGRRVKQWPYQKS 120
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
162-387 |
3.32e-08 |
|
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: 57.39 E-value: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 162 SQELFQLSQY--LQEALHREQMLEQKLATLQRLLASTQEASESSWQALIDEDRLLSRLEVMGNQLQAYSKNQTE--DGIR 237
Cdd:TIGR02169 664 GGILFSRSEPaeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKErlEELE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 238 KELVALTEDKHNYETTAKEsLRRVLQEKIEvvrKLSEVERSLSNTEDECTHlremnertqEELRELANKYNGAVNEIKDL 317
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKE-LEARIEELEE---DLHKLEEALNDLEARLSH---------SRIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528494936 318 TEKIKLAEDKHEELTQKGL---NEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEK 387
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEyleKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
616-803 |
3.78e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 616 EAATAEREREitaLQGDLSIVTAEL--DKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQADCSGLQNECD 693
Cdd:COG1196 208 QAEKAERYRE---LKEELKELEAELllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 694 SLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLgsiqDQHQQDASKLKIQLAQAESRTRDLQKEY 773
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL----EELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190
....*....|....*....|....*....|
gi 528494936 774 DDTQSLLSDLRQRYEQTEQEKRSINDELEQ 803
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLE 390
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
14-110 |
2.39e-07 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine/threonine-protein kinase MEK1 and similar proteins; MEK1 (EC 2.7.11.1), also known as MRE4, is a meiosis-specific protein kinase required for chromosome synapsis and meiotic recombination. The recruitment and activation of MEK1 require the phosphorylation of the chromosome axis protein Hop1 at Thr318 (pT318), which is necessary for recognition by the MEK1 FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438722 [Multi-domain] Cd Length: 105 Bit Score: 49.53 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 14 SHPFQERHV---YLDEPVKIGRSvARCRPAQNNATfdckvLSRNHALVW---FDHKTG-KFYLQDTkSSNGTFINSQRLS 86
Cdd:cd22670 7 SSPGSTDIVlpiYKNQVITIGRS-PSCDIVINDPF-----VSRTHCRIYsvqFDESSApLVYVEDL-SSNGTYLNGKLIG 79
|
90 100
....*....|....*....|....*
gi 528494936 87 RGseespPCEVLS-GDIIQFGVDVT 110
Cdd:cd22670 80 RN-----NTVLLSdGDVIEIAHSAT 99
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
25-114 |
3.11e-07 |
|
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. Specially, RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438715 [Multi-domain] Cd Length: 110 Bit Score: 49.66 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 25 DEPVKIGRSVArcrpAQNNATFDC-KVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRLsrgsEESPPCEVLSGDII 103
Cdd:cd22663 20 GKEVTVGRGLG----VTYQLVSTCpLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERI----EPLKPYPLNEGDLI 90
|
90
....*....|.
gi 528494936 104 QFGVDVTENTR 114
Cdd:cd22663 91 QLGVPPENKEP 101
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
182-698 |
3.51e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 182 LEQKLATLQRLLASTQEASESSWQALIDEDRLLSRLEvmgnqlqaySKNQTEDGIRKELVALTEDKHNYETTaKESLRRV 261
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHE---------ERREELETLEAEIEDLRETIAETERE-REELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 262 LQEKIEVVRKLSE------VERSLSNTEDECTHLR-----EMNERTQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEE 330
Cdd:PRK02224 281 VRDLRERLEELEEerddllAEAGLDDADAEAVEARreeleDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 331 LTQKGLNEKKELQ----------MRIEEMEEKEQALQARI--------------EALQADNDFTNERLTALQVRLEQLQE 386
Cdd:PRK02224 361 LREEAAELESELEeareavedrrEEIEELEEEIEELRERFgdapvdlgnaedflEELREERDELREREAELEATLRTARE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 387 kSIKENNSfdhflLKSGGDCTLIQQYIECQSVRQLKEAVDSSINKLSnfDEVIDAHLQnnQTTVDNSLPSPDRLKEnqid 466
Cdd:PRK02224 441 -RVEEAEA-----LLEAGKCPECGQPVEGSPHVETIEEDRERVEELE--AELEDLEEE--VEEVEERLERAEDLVE---- 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 467 akecdMSDTLSPSKEKSSDDTSDGQMEEQELNEPQNRVSLLKEMDRSLEAGDTEQviphiHRELQEAQELAntgkQKCLE 546
Cdd:PRK02224 507 -----AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEK-----REAAAEAEEEA----EEARE 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 547 LQAMLEEERKTNRQQTEESAKqIRFLQTQLAKLQTDMEALREQRENTI---TTTREELYSAQEEILVLR-----HAMEAA 618
Cdd:PRK02224 573 EVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERLREKREALAelnDERRERLAEKRERKRELEaefdeARIEEA 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 619 TAEREREITALQGdlsiVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQA---DCSGLQNECDSL 695
Cdd:PRK02224 652 REDKERAEEYLEQ----VEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEALEAlydEAEELESMYGDL 727
|
...
gi 528494936 696 RAE 698
Cdd:PRK02224 728 RAE 730
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
27-106 |
3.65e-07 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 (FKH1), 2 (FKH2) and similar proteins; This family includes FKH1 and FKH2, as well as pre-rRNA-processing protein FHL1. FKH1 and FKH2 are forkhead transcription factors that regulate the expression of the CLB2 cluster of genes during the G2/M phase of the mitotic cell cycle. The CLB2 cluster of genes includes mitotic regulators such as CLB1, CLB2, CDC5 and CDC20, as well as SWI5 and ACE2. FKH1 and FKH2 are involved in HMRa silencing. They associate with the coding regions of active genes and influence, in opposing ways, transcriptional elongation and termination, and coordinate early transcription elongation and pre-mRNA processing. Both FKH1 and FKH2 play a role as regulators of lifespan in collaboration with the anaphase-promoting complex (APC), likely through combined regulation of stress response, genomic stability, and cell cycle regulation. They also function in controlling yeast cell morphology by preventing pseudohyphal growth and act as rate-limiting replication origin activators via their interaction with the origin recognition complex (ORC). FHL1 is a forkhead protein that controls the pre-rRNA processing machinery in conjunction with IFH1. It might act as a transcriptional regulator of genes specifically involved in that process. IFH1 convert FHL1 from a repressor to an activator. This family also includes AtFHA1 and AtFHA2, which may play a role in the control of plant organ development. AtFHA2 is specifically involved in the regulation of stamen development. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438753 [Multi-domain] Cd Length: 106 Bit Score: 49.16 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 27 PVKIGRSVARcRPAQNNATFDC-----KVLSRNHALVWFDHKTGKFYLQdTKSSNGTFINSQRLSRGseeSPPCEVLSGD 101
Cdd:cd22701 18 EVVLGRNSKN-SSSTAADSVDIdlgpsKKISRRHARIFYDFTTQCFELS-VLGRNGVKVDGILVKPG---SPPVPLRSGS 92
|
....*
gi 528494936 102 IIQFG 106
Cdd:cd22701 93 LIQIG 97
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
633-800 |
3.73e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 633 LSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKL--QADCSGLQNECDSLRAEKSTLMQKLNRLE 710
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 711 EELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQT 790
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170
....*....|
gi 528494936 791 EQEKRSINDE 800
Cdd:COG4717 233 ENELEAAALE 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
623-804 |
1.30e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 623 EREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQgEVEKLQADCSGLQNECDSLRAEKSTL 702
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-DVASAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 703 M---QKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESRTRDLQKEYDDTQSL 779
Cdd:COG4913 688 AaleEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
|
170 180
....*....|....*....|....*
gi 528494936 780 LSDLRQRYEQTEQEKRSINDELEQC 804
Cdd:COG4913 768 RENLEERIDALRARLNRAEEELERA 792
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
526-724 |
1.34e-06 |
|
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: 51.30 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 526 IHRELQEAQELANTGKQKclelQAMLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQR---ENTITTTREEL- 601
Cdd:COG4942 32 LQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIaelRAELEAQKEELa 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 602 --------YSAQEEILVLRHA------------MEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQAS- 660
Cdd:COG4942 108 ellralyrLGRQPPLALLLSPedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEEr 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528494936 661 FQLQSQHQERASQLQgeveKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLS 724
Cdd:COG4942 188 AALEALKAERQKLLA----RLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
276-803 |
1.48e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 52.10 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 276 ERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKIKLAED---KHEELTQKGLNEKKELQMRIEEMEEK 352
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETElcaEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 353 EQALQARIEALQADNDFTNERLTALQvrlEQLQEKSIKEnnsfdhfllksggdctliqqyiecQSVRQLKEAVDSSINKL 432
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLE---EQLDEEEAAR------------------------QKLQLEKVTTEAKIKKL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 433 SnfDEVIDAHLQNNQTTVDNSLPSpDRLKENQID-AKECDMSDTLSPSKEKSSDDTSDgqMEEQELNEPQNRVSLLKeMD 511
Cdd:pfam01576 137 E--EDILLLEDQNSKLSKERKLLE-ERISEFTSNlAEEEEKAKSLSKLKNKHEAMISD--LEERLKKEEKGRQELEK-AK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 512 RSLEaGDTEQVIPHIHRELQEAQELANTGKQKCLELQAMLEEERKTNRQQTEeSAKQIRFLQTQLAKLQTDMEALREQRE 591
Cdd:pfam01576 211 RKLE-GESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNN-ALKKIRELEAQISELQEDLESERAARN 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 592 NTITTTR------EELYSAQEEILVLRHAMEAATAEREREITALQGDLsivtaELDKWRQTAAKYEVEISNLQASFQLQS 665
Cdd:pfam01576 289 KAEKQRRdlgeelEALKTELEDTLDTTAAQQELRSKREQEVTELKKAL-----EEETRSHEAQLQEMRQKHTQALEELTE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 666 QhQERASQLQGEVEK----LQADCSGLQNECDSLRAEKSTLMQKLNRLEEELdssrersATLSSNLNALEKSQGDLENKL 741
Cdd:pfam01576 364 Q-LEQAKRNKANLEKakqaLESENAELQAELRTLQQAKQDSEHKRKKLEGQL-------QELQARLSESERQRAELAEKL 435
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528494936 742 GSIQDQHQQDASklkiQLAQAESRTRDLQKEYD-------DTQSLLSD-------LRQRYEQTEQEKRSINDELEQ 803
Cdd:pfam01576 436 SKLQSELESVSS----LLNEAEGKNIKLSKDVSslesqlqDTQELLQEetrqklnLSTRLRQLEDERNSLQEQLEE 507
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
234-814 |
1.81e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 234 DGIRKELVALTEDKHNYETTAKEsLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREmNERTQEELRELANKY---NGA 310
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKE-LESLEGSKRKLEEKIRELEERIEELKKEIEELEE-KVKELKELKEKAEEYiklSEF 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 311 VNEIKDLTEKIKLAEDKHEEL---TQKGLNEKKELQMRIEEMEEKEQALQARIEALQADNDfTNERLTALQVRLEQLQEK 387
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEingIEERIKELEEKEERLEELKKKLKELEKRLEELEERHE-LYEEAKAKKEELERLKKR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 388 SikennsfdhfllksgGDCTLIQQYIECQSVRQLKEAVDSSINKLsnfdevidahlqnnqttvdnslpspdRLKENQIDA 467
Cdd:PRK03918 381 L---------------TGLTPEKLEKELEELEKAKEEIEEEISKI--------------------------TARIGELKK 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 468 KECDMSDTLSPSKEKSSDDTSDGQmeeqELNEpQNRVSLLKEMDRSLEagdteqvipHIHRELQEAQELANTGKQKCLEL 547
Cdd:PRK03918 420 EIKELKKAIEELKKAKGKCPVCGR----ELTE-EHRKELLEEYTAELK---------RIEKELKEIEEKERKLRKELREL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 548 QAMLEEERKTNRQqtEESAKQIRFLQTQLAKLqtDMEALrEQRENTITTTREELYSAQEEILVLrhameaatAEREREIT 627
Cdd:PRK03918 486 EKVLKKESELIKL--KELAEQLKELEEKLKKY--NLEEL-EKKAEEYEKLKEKLIKLKGEIKSL--------KKELEKLE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 628 ALQGDLSIVTAELDKWRQTAAKYEVEISNLQAsfqlqsqhqERASQLQGEVEKLQAdcsgLQNECDSLRAEKSTLMQKLN 707
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAELLKELEELGF---------ESVEELEERLKELEP----FYNEYLELKDAEKELEREEK 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 708 RLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDAS----KLKIQLAQAESRTRDLQKEYDDTQSLLSDL 783
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELReeylELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
570 580 590
....*....|....*....|....*....|.
gi 528494936 784 RQRYEQTEQEKRSINDeLEQCKVNLKLLQDK 814
Cdd:PRK03918 700 KEELEEREKAKKELEK-LEKALERVEELREK 729
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
55-108 |
3.64e-06 |
|
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) family; The Cep170 family includes Cep170 and Cep170B. Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438756 [Multi-domain] Cd Length: 102 Bit Score: 46.16 E-value: 3.64e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 528494936 55 HALVWFDHKTGKFYLQDTKSSNGTFINSQRLSrgseESPPCEVLSGDIIQFGVD 108
Cdd:cd22704 39 HAVITYDQIDNEFKIKDLGSLNGTFVNDSRIP----EQTYITLKLGDSIRFGYD 88
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
258-807 |
3.95e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 258 LRRVLQ-EKIE-VVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEELtQKG 335
Cdd:PRK03918 151 VRQILGlDDYEnAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKL-EKE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 336 LNEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEKsIKEnnsfdhfllksggdctliqqyiec 415
Cdd:PRK03918 230 VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK-VKE------------------------ 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 416 qsVRQLKEAVDSSInKLSNFDEVIDAHLQNNQTTVDNSlpspdrlkENQIDAKECDMSDTLSPSKEKssddtsdGQMEEq 495
Cdd:PRK03918 285 --LKELKEKAEEYI-KLSEFYEEYLDELREIEKRLSRL--------EEEINGIEERIKELEEKEERL-------EELKK- 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 496 ELNEPQNRVSLLKEMDRSLEagdteqvipHIHRELQEAQELANTGKQKCLE-LQAMLEEERKTNRQQTEESAK---QIRF 571
Cdd:PRK03918 346 KLKELEKRLEELEERHELYE---------EAKAKKEELERLKKRLTGLTPEkLEKELEELEKAKEEIEEEISKitaRIGE 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 572 LQTQLAKLQTDMEALREQRENTITTTREELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYe 651
Cdd:PRK03918 417 LKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEL- 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 652 veISNLQASFQLQSQHQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEeldsSRERSATLSSNLNALE 731
Cdd:PRK03918 496 --IKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE----LKKKLAELEKKLDELE 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 732 KSQGDLENKLGSIQ-DQHQQDASKLK---------IQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDEL 801
Cdd:PRK03918 570 EELAELLKELEELGfESVEELEERLKelepfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL 649
|
....*.
gi 528494936 802 EQCKVN 807
Cdd:PRK03918 650 EELEKK 655
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
30-106 |
4.05e-06 |
|
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438750 [Multi-domain] Cd Length: 93 Bit Score: 45.87 E-value: 4.05e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528494936 30 IGRSVArcrpaqNNATFDCKVLSRNHALVwfDHKTGKFYLQDTKSSNGTFINSQRLSRGseesppcEVLSGDIIQFG 106
Cdd:cd22698 25 IGRSSN------NDIRLNDHSVSRHHARI--VRQGDKCNLTDLGSTNGTFLNGIRVGTH-------ELKHGDRIQLG 86
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
603-773 |
4.95e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 603 SAQEEILVLRHAMEAATAER---EREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERAS------- 672
Cdd:COG4913 607 DNRAKLAALEAELAELEEELaeaEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERldassdd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 673 --QLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGD-------LENKLGS 743
Cdd:COG4913 687 laALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEerfaaalGDAVERE 766
|
170 180 190
....*....|....*....|....*....|
gi 528494936 744 IQDQHQQDASKLKIQLAQAESRTRDLQKEY 773
Cdd:COG4913 767 LRENLEERIDALRARLNRAEEELERAMRAF 796
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
671-814 |
5.43e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 671 ASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGS-IQDQHQ 749
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErARALYR 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528494936 750 QDASKLKI-QLAQAES------RTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLKLLQDK 814
Cdd:COG3883 98 SGGSVSYLdVLLGSESfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
51-106 |
5.77e-06 |
|
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also called human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP), is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438729 [Multi-domain] Cd Length: 106 Bit Score: 45.62 E-value: 5.77e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528494936 51 LSRNHALVWF----DHKTGKFYLQDTKSSNGTFINSQRLsrgseesPP---CEVLSGDIIQFG 106
Cdd:cd22677 41 ISRYHAVLQYrgdaDDHDGGFYLYDLGSTHGTFLNKQRI-------PPkqyYRLRVGHVLKFG 96
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
267-809 |
6.61e-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: 50.02 E-value: 6.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 267 EVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEELTQKGLNEKKELQMRI 346
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 347 EEMEEKEQalqaRIEALQADNDFTNERLTALQVRLEQLQEKSIKENNSFDhfllksggdcTLIQQyiecqsVRQLKEAVD 426
Cdd:TIGR04523 117 EQKNKLEV----ELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYN----------DLKKQ------KEELENELN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 427 SSINKLSNFDEVIDahLQNNQTTVDNSLPSPDRLKENQIDAKECDMSDtlspSKEKSSDDTSDGQMEEQELNEPQNRVSL 506
Cdd:TIGR04523 177 LLEKEKLNIQKNID--KIKNKLLKLELLLSNLKKKIQKNKSLESQISE----LKKQNNQLKDNIEKKQQEINEKTTEISN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 507 LKEmdrslEAGDTEQVIPHIHRELQEAQELANTGKQKCLELQAMLEE-ERKTNRQQTEESAKQIRFLQTQLAKLQTDMEA 585
Cdd:TIGR04523 251 TQT-----QLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQlKSEISDLNNQKEQDWNKELKSELKNQEKKLEE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 586 LREQ---RENTITTTREELYSAQEEILVLrhamEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQ 662
Cdd:TIGR04523 326 IQNQisqNNKIISQLNEQISQLKKELTNS----ESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 663 LQsqhQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEE----------LDSSRErsaTLSSNLNALEK 732
Cdd:TIGR04523 402 NQ---EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkeliiknLDNTRE---SLETQLKVLSR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 733 SQGDLENKLGSIQ---DQHQQDASKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLK 809
Cdd:TIGR04523 476 SINKIKQNLEQKQkelKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK 555
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
52-106 |
7.88e-06 |
|
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 (PPP1R8) and similar proteins; PPP1R8, also called nuclear inhibitor of protein phosphatase 1 (NIPP-1), is an inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. It may also be involved in pre-mRNA splicing and binds DNA and might act as a transcriptional repressor. PPP1R8 seems to be required for cell proliferation. PPP1R8 contains an FHA domain that mediates interactions with threonine-phosphorylated maternal embryonic leucine zipper kinase (MELK). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438726 [Multi-domain] Cd Length: 108 Bit Score: 45.33 E-value: 7.88e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 528494936 52 SRNH-ALVWfdHK-TGKFYLQDTKSSNGTFINSQRLsrgsEESPPCEVLSGDIIQFG 106
Cdd:cd22674 48 SRVHaALVY--HKhLNRVFLIDLGSTHGTFVGGIRL----EPHKPQQLPIDSTLRFG 98
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
152-625 |
8.80e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 8.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 152 KVSANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLASTQEASEsswqaliDEDRLLSRLEVMGNQLQAYSKNQ 231
Cdd:COG4717 60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA-------ELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 232 TEDGIRKELVALTEdkhnyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDEC-THLREMNERTQEELRELANKYNGA 310
Cdd:COG4717 133 ELEALEAELAELPE--------RLEELEERLEELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 311 VNEIKDLTEKIKLAEDKHEELTQkglnEKKELQMRIEEMEEKEQALQARIEALqadndftnerLTALQVRLEQLqeksik 390
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEE----ELEQLENELEAAALEERLKEARLLLL----------IAAALLALLGL------ 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 391 eNNSFDHFLLKSGGDCTLIQQYIECQSVRQLKEAVDSsinklsnfdevidahlqNNQTTVDNSLPSPDRLKENQID--AK 468
Cdd:COG4717 265 -GGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL-----------------GKEAEELQALPALEELEEEELEelLA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 469 ECDMSDTLSPSK-EKSSDDTSDGQMEEQELNEPQNRV---SLLKEMDRSLEAG--DTEQVIPHIHRELQEAQELantgKQ 542
Cdd:COG4717 327 ALGLPPDLSPEElLELLDRIEELQELLREAEELEEELqleELEQEIAALLAEAgvEDEEELRAALEQAEEYQEL----KE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 543 KCLELQAMLEEERKTNRQQTEESAKQirFLQTQLAKLQTDMEALREQRENtittTREELYSAQEEILVLRHAMEAATAER 622
Cdd:COG4717 403 ELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEE----LREELAELEAELEQLEEDGELAELLQ 476
|
...
gi 528494936 623 ERE 625
Cdd:COG4717 477 ELE 479
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
585-804 |
1.04e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.57 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 585 ALREQRENTITTTREELYSAQEEILVLRHAMEAATAEREREIT-----ALQGDLSivtAELDKWRQTAAKYEVEISNLQA 659
Cdd:COG3096 781 AAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGghlavAFAPDPE---AELAALRQRRSELERELAQHRA 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 660 SFQlqsQHQERASQLQGEVEKLQadcsGLQNECDSLRAEksTLMQKLNRLEEELDSSRERSATLSSNLNALEKsqgdLEN 739
Cdd:COG3096 858 QEQ---QLRQQLDQLKEQLQLLN----KLLPQANLLADE--TLADRLEELREELDAAQEAQAFIQQHGKALAQ----LEP 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 740 KLGSIQDQHQQDASkLKIQLAQAESRTRDLQKE---------------YDDTQSLLSD-------LRQRYEQTEQEKRSI 797
Cdd:COG3096 925 LVAVLQSDPEQFEQ-LQADYLQAKEQQRRLKQQifalsevvqrrphfsYEDAVGLLGEnsdlnekLRARLEQAEEARREA 1003
|
....*..
gi 528494936 798 NDELEQC 804
Cdd:COG3096 1004 REQLRQA 1010
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
212-822 |
1.32e-05 |
|
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: 49.27 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 212 RLLSRLEVMGNQLQAYSKNQTEDGIRKELVALTEDKHNYETTAKESLRRVLQEKIEvvrkLSEVERSlSNTEDECTHLRE 291
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE----LDGFERG-PFSERQIKNFHT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 292 MNERTQEELRELANKyngavnEIKDLTEKIKLAEDKHEELTQKGLNEKKELQMRIEEMEEKEQALQARIEALQADNDFTN 371
Cdd:TIGR00606 398 LVIERQEDEAKTAAQ------LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 372 ERLTALQVRLEQLQEKSIKENNSFdhfllksggdctliqqyIECQSVRQLkeavdssinklsnfdevidaHLQNNQTTVD 451
Cdd:TIGR00606 472 RILELDQELRKAERELSKAEKNSL-----------------TETLKKEVK--------------------SLQNEKADLD 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 452 NSLPSPDRlKENQIDAKECDMSDTLSPSKEKSsddTSDGQMEEQELNEPQNRVSLLKEMDRSLEAGDTeqviphIHRELQ 531
Cdd:TIGR00606 515 RKLRKLDQ-EMEQLNHHTTTRTQMEMLTKDKM---DKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDW------LHSKSK 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 532 EAQELANTGKQKCLELQAMLEEERKTNrqqteesaKQIRFLQTQLAKLQTDMEAL--REQRENTITTTREELYSAQEEil 609
Cdd:TIGR00606 585 EINQTRDRLAKLNKELASLEQNKNHIN--------NELESKEEQLSSYEDKLFDVcgSQDEESDLERLKEEIEKSSKQ-- 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 610 vlRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQADCSGL- 688
Cdd:TIGR00606 655 --RAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLa 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 689 ---QNECDSLRAEKSTL---MQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQD-QHQQDASKLKIQLAQ 761
Cdd:TIGR00606 733 pgrQSIIDLKEKEIPELrnkLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERfQMELKDVERKIAQQA 812
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528494936 762 AESRTRDLQKEYddtqsllSDLRQRYEQTEQEKRSINDELEQckvNLKLLQDKGSNPSILQ 822
Cdd:TIGR00606 813 AKLQGSDLDRTV-------QQVNQEKQEKQHELDTVVSKIEL---NRKLIQDQQEQIQHLK 863
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
613-814 |
1.62e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 613 HAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQAsfqlqsqhqeRASQLQGEVEKLQADCSGLQNEC 692
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER----------RIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 693 DSLRAEKSTLMQKLNRLEEELdSSRERSATLSSNLNALE--KSQGDLENK------LGSIQDQHQQDASKLKIQLAQAES 764
Cdd:COG4942 86 AELEKEIAELRAELEAQKEEL-AELLRALYRLGRQPPLAllLSPEDFLDAvrrlqyLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 528494936 765 RTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLKLLQDK 814
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
617-803 |
1.96e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 617 AATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQAsfQLQSQhQERASQLQGEVEKLQADCSGLQNECDSLR 696
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK--QLAAL-ERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 697 AEKSTLMQKLNRLEEELdSSRERSATLSSNLNALE--KSQGDLENK------LGSIQDQHQQDASKLKIQLAQAESRTRD 768
Cdd:COG4942 90 KEIAELRAELEAQKEEL-AELLRALYRLGRQPPLAllLSPEDFLDAvrrlqyLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 528494936 769 LQKEYDDTQSLLSDL---RQRYEQTEQEKRSINDELEQ 803
Cdd:COG4942 169 LEAERAELEALLAELeeeRAALEALKAERQKLLARLEK 206
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
552-767 |
2.01e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 552 EEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQRENT---ITTTREELYSAQEEILVLRHAMEAATAEREREITA 628
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELqaeLEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 629 LQ---GDLSIVTAELDkwrqtAAKYEVEISNLQASFQLQSQHQErasqlqgEVEKLQADCSGLQNECDSLRAEKSTLMQK 705
Cdd:COG3883 95 LYrsgGSVSYLDVLLG-----SESFSDFLDRLSALSKIADADAD-------LLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528494936 706 LNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESRTR 767
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
28-106 |
2.41e-05 |
|
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438732 [Multi-domain] Cd Length: 96 Bit Score: 43.87 E-value: 2.41e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528494936 28 VKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDhkTGKFYLQDTKSSNGTFINSQRlsrgsEESPPCEVLSGDIIQFG 106
Cdd:cd22680 23 VSIGRDP------ENVIVIPDPFVSRNHARITVD--SNEIYIEDLGSTNGTFVNDFK-----RIKGPAKLHPNDIIKLG 88
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
471-837 |
2.41e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.41 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 471 DMSDTLSPSKEKSSDDTSDGQMEEQELNEPQNRVSLLKEMDRSLEAGDteqviphihrELQEAQELANtgkqkclELQAM 550
Cdd:COG3096 310 EMARELEELSARESDLEQDYQAASDHLNLVQTALRQQEKIERYQEDLE----------ELTERLEEQE-------EVVEE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 551 LEEERKTNRQQTEESAKQIRFLQTQLAKLQTDME--------------ALREQR-------------ENTITTTREELYS 603
Cdd:COG3096 373 AAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDvqqtraiqyqqavqALEKARalcglpdltpenaEDYLAAFRAKEQQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 604 AQEEILVLRHAMEAATAEREREITALQGDLSIV--TAELDKW---RQTAAKYEVEISNLQASFQLQSQHQE--RASQLQG 676
Cdd:COG3096 453 ATEEVLELEQKLSVADAARRQFEKAYELVCKIAgeVERSQAWqtaRELLRRYRSQQALAQRLQQLRAQLAEleQRLRQQQ 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 677 EVEKLQADCSGLQNEC----DSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLEnKLGSIQDQHQQDA 752
Cdd:COG3096 533 NAERLLEEFCQRIGQQldaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELA-ARAPAWLAAQDAL 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 753 SKLKIQLAQAESRTRDLQkeyDDTQSLLSDLRQRY---EQTEQEKRSINDELEQckvnlkLLQDKGSNPSILQPVQAIFI 829
Cdd:COG3096 612 ERLREQSGEALADSQEVT---AAMQQLLEREREATverDELAARKQALESQIER------LSQPGGAEDPRLLALAERLG 682
|
....*...
gi 528494936 830 GLFLALLY 837
Cdd:COG3096 683 GVLLSEIY 690
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
27-117 |
2.48e-05 |
|
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 (AtPP2C70) and similar proteins; AtPP2C70, also called kinase-associated protein phosphatase, or protein ROOT ATTENUATED GROWTH 1, dephosphorylates the serine/threonine receptor-like kinase RLK5. It may function as a signaling component in a pathway involving RLK5. It acts as a negative regulator of the CLAVATA1 signaling in plant development by binding and dephosphorylating CLAVATA1. It is also a component of a signaling pathway which mediates adaptation to NaCl stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438730 [Multi-domain] Cd Length: 102 Bit Score: 43.89 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 27 PVKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLsrgSEESPPCEVLSGDIIQFG 106
Cdd:cd22678 24 PLTIGRIQ------RGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESI---SPNGRPVVLSSGDVITLG 94
|
90
....*....|.
gi 528494936 107 vdvTENTRKVT 117
Cdd:cd22678 95 ---SETKILVR 102
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
657-814 |
2.81e-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: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 657 LQASFQLQSQHQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGD 736
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 737 LENKLGSIQDQHQQ------------------------DASKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQ 792
Cdd:COG4942 95 LRAELEAQKEELAEllralyrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180
....*....|....*....|..
gi 528494936 793 EKRSINDELEQCKVNLKLLQDK 814
Cdd:COG4942 175 ELEALLAELEEERAALEALKAE 196
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
289-796 |
3.23e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 289 LREMNERTQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEELTQKgLNEKKELQMRIEEMEEKEQALQARIEALQADND 368
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 369 F---------TNERLTALQVRLEQLQEKsikennsfdhfllksggdctlIQQYiecqsvRQLKEAVDSSINKLSNFDEVI 439
Cdd:COG4717 127 LlplyqeleaLEAELAELPERLEELEER---------------------LEEL------RELEEELEELEAELAELQEEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 440 DAHLQnnqttvDNSLPSPDRLKENQIDAKECDmsdtlspskekssddtSDGQMEEQELNEPQNRVSLLKEmdrSLEAGDT 519
Cdd:COG4717 180 EELLE------QLSLATEEELQDLAEELEELQ----------------QRLAELEEELEEAQEELEELEE---ELEQLEN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 520 EQVIPHIHRELQEAQELANTGKQKCLeLQAMLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQRENTITTTRE 599
Cdd:COG4717 235 ELEAAALEERLKEARLLLLIAAALLA-LLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 600 ELYSAQE--EILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTA--AKYEVEISNLQASFQLQS--------QH 667
Cdd:COG4717 314 EELEEEEleELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqlEELEQEIAALLAEAGVEDeeelraalEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 668 QERASQLQGEVEKLQADCSGLQNECDSLRA--EKSTLMQKLNRLEEELDSSRERsatlssnLNALEKSQGDLENKLGSIQ 745
Cdd:COG4717 394 AEEYQELKEELEELEEQLEELLGELEELLEalDEEELEEELEELEEELEELEEE-------LEELREELAELEAELEQLE 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 528494936 746 DQHqqDASKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRS 796
Cdd:COG4717 467 EDG--ELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLP 515
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
18-86 |
3.68e-05 |
|
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the first FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438746 [Multi-domain] Cd Length: 93 Bit Score: 43.09 E-value: 3.68e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528494936 18 QERHVYLDEPVKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhkTGKFYLQDTKSSNGTFINSQRLS 86
Cdd:cd22694 8 GELRFDPGSSVRIGRD------PDADVRLDDPRVSRRHALLEFD--GDGWVYTDLGSRNGTYLNGRRVQ 68
|
|
| FHA_CHFR |
cd22672 |
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ... |
49-105 |
4.08e-05 |
|
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains protein (CHFR); CHFR, also called RING finger protein 196 (RNF196), is a checkpoint protein that delays entry into mitosis in response to stress. It functions as an E3 ubiquitin ligase that ubiquitinates and degrades its target proteins, such as Aurora-A, Plk1, Kif22 and PARP-1, which are critical for proper mitotic transitions. It also plays an important role in cell cycle progression and tumor suppression and is negatively regulated by SUMOylation-mediated proteasomal ubiquitylation. Moreover, CHFR is involved in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation. CHFR contains a fork head associated-(FHA) domain and a RING-HC finger. The CHFR FHA domain has been crystallized as a segment-swapped dimer. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438724 [Multi-domain] Cd Length: 108 Bit Score: 43.43 E-value: 4.08e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 528494936 49 KVLSRNHALVWFDHKtGKFYLQDTkSSNGTFINSQRLSRGSEesppCEVLSGDIIQF 105
Cdd:cd22672 39 KLVSGDHCKIIRDEK-GQVWLEDT-STNGTLVNKVKVVKGQK----VELKHGDVIYL 89
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
25-108 |
4.49e-05 |
|
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar proteins; ZEP, also called protein ABA DEFICIENT 1, ABA1, protein IMPAIRED IN BABA-INDUCED STERILITY 3, protein LOW EXPRESSION OF OSMOTIC STRESS-RESPONSIVE GENES 6, or protein NON-PHOTOCHEMICAL QUENCHING 2, plays an important role in the xanthophyll cycle and abscisic acid (ABA) biosynthesis. It converts zeaxanthin into antheraxanthin and subsequently violaxanthin. ZEP is required for resistance to osmotic and drought stresses, ABA-dependent stomatal closure, seed development and dormancy, modulation of defense gene expression, and disease resistance and non-photochemical quencing (NPQ). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438754 [Multi-domain] Cd Length: 123 Bit Score: 43.57 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 25 DEPVKIGRsvarcRPAQNNAT----FDCKVLSRNHALVWFdhKTGKFYLQDTKSSNGTFINSQRLSR-GSEESPPCEVLS 99
Cdd:cd22702 31 KQPCIIGS-----DPHQAISGisvvIPSPQVSELHARITC--KNGAFFLTDLGSEHGTWINDNEGRRyRAPPNFPVRLHP 103
|
....*....
gi 528494936 100 GDIIQFGVD 108
Cdd:cd22702 104 SDVIEFGSD 112
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
679-808 |
4.75e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 679 EKLQAdcsgLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLS--SNLNALEKSQGDLENKLGSIQDQHQQ-DASKl 755
Cdd:COG4913 610 AKLAA----LEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERlDASS- 684
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 528494936 756 kIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNL 808
Cdd:COG4913 685 -DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
256-386 |
4.76e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.16 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 256 ESLRRVLQEKIEvvrklSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEELTQKg 335
Cdd:COG2433 376 LSIEEALEELIE-----KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERE- 449
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 528494936 336 LNEKKElQMRIEEMEEKE-QALQARIEALQADNDFTNERLTALQVRLEQLQE 386
Cdd:COG2433 450 LSEARS-EERREIRKDREiSRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
494-684 |
6.90e-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: 45.91 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 494 EQELNEPQNRVSLLKEMDRSLEAG--DTEQVIPHIHRELQEAQELANTGKQKCLELQAMLEEERKTNRQQTEESAKQIRF 571
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQlaALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 572 LQ-----------------TQLAKLQTDMEAL---REQRENTITTTREELYSAQEEILVLRHAMEAATAEREREITALQG 631
Cdd:COG4942 113 LYrlgrqpplalllspedfLDAVRRLQYLKYLapaRREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 528494936 632 DLSIVTAELDKWRQTAAKYEVEISNLQASfqlqsqhqerASQLQGEVEKLQAD 684
Cdd:COG4942 193 LKAERQKLLARLEKELAELAAELAELQQE----------AEELEALIARLEAE 235
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
600-774 |
7.39e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 600 ELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQAsfqlqsqHQERASQLQGEVE 679
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA-------RIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 680 K---LQAdcsgLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLK 756
Cdd:COG1579 87 NnkeYEA----LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|....*....
gi 528494936 757 IQLAQAESRT-RDLQKEYD 774
Cdd:COG1579 163 AEREELAAKIpPELLALYE 181
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
704-814 |
8.11e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 704 QKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQ------------DQHQQDASKLKIQLAQAESRTRD--- 768
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlaeyswdeidvASAEREIAELEAELERLDASSDDlaa 689
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 528494936 769 LQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLKLLQDK 814
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
549-751 |
8.46e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 8.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 549 AMLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALReqrentittTREELYSAQEEILVLRHAMEAATAEREReITA 628
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQ---------RLAEYSWDEIDVASAEREIAELEAELER-LDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 629 LQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQADCSGLQNECDSLRAEKstlmqklnR 708
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE--------R 754
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 528494936 709 LEEELDSSRER--SATLSSNLNALEKSQGDLENKLGSIQDQHQQD 751
Cdd:COG4913 755 FAAALGDAVERelRENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
638-803 |
8.50e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 8.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 638 AELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQADCSGLQNEcdslraeksTLMQKLNRLEEELDSSR 717
Cdd:PRK04863 837 AELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADE---------TLADRVEEIREQLDEAE 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 718 ERSATLSSNLNALEKsqgdLENKLGSIQdQHQQDASKLKIQLAQAESRTRDLQKE---------------YDDTQSLLSD 782
Cdd:PRK04863 908 EAKRFVQQHGNALAQ----LEPIVSVLQ-SDPEQFEQLKQDYQQAQQTQRDAKQQafaltevvqrrahfsYEDAAEMLAK 982
|
170 180
....*....|....*....|....*...
gi 528494936 783 -------LRQRYEQTEQEKRSINDELEQ 803
Cdd:PRK04863 983 nsdlnekLRQRLEQAEQERTRAREQLRQ 1010
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
225-827 |
9.49e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 9.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 225 QAYSKNQTEDGIRKELVALTEDKHNYETTAK-ESLRRV--LQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELR 301
Cdd:PTZ00121 1195 KAEDARKAEAARKAEEERKAEEARKAEDAKKaEAVKKAeeAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA 1274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 302 ELANKyngaVNEIKDLTEKIKLAE-------DKHEELTQKGLNEKK--ELQMRIEEMEEKEQALQARIEALQADNDFTNE 372
Cdd:PTZ00121 1275 EEARK----ADELKKAEEKKKADEakkaeekKKADEAKKKAEEAKKadEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKA 1350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 373 RLTALQVRLEQLQEKsiKENNSFDHFLLKSGGDctliQQYIECQSVRQLKEAVDSSINKLSNFDEVIDAHLQNNQTtvdn 452
Cdd:PTZ00121 1351 EAEAAADEAEAAEEK--AEAAEKKKEEAKKKAD----AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKA---- 1420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 453 slpspDRLKENQIDAKECDmsDTLSPSKEKSSDDTSDGQMEEQELNEPQNRVSLLKEMDRSLEAGDTEQviphihRELQE 532
Cdd:PTZ00121 1421 -----DEAKKKAEEKKKAD--EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEA------KKADE 1487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 533 AQELANTGKQKCLELQAMLEEERKTNR-QQTEESAKQIRFLQTQLAKLQTDMEALREQRENTITTTREELYSAQEeilvl 611
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKADEaKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEE----- 1562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 612 RHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQADCSGLQNE 691
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE 1642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 692 CDSLR-AEKSTLMQKLNRLE-EELDSSRERSATLSSNLNALEKSQGDLENKLGSiQDQHQQDASKLKIQLAQAESRTRDL 769
Cdd:PTZ00121 1643 AEEKKkAEELKKAEEENKIKaAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK-EAEEAKKAEELKKKEAEEKKKAEEL 1721
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 528494936 770 QKEYDDTQSLLSDLRQRYEQTEQEKRSIN-DELEQCKVNLKLLQDKGSNPSILQPVQAI 827
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKKAEEAKkDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
238-771 |
1.09e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 238 KELVALTEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQE----------ELRELANKY 307
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEElekeleslegSKRKLEEKI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 308 NGAVNEIKDLTEKIKLAEDKHEELTQ----------------KGLNEKKELQMRIEEMEEKEQALQARIEALQADNDFTN 371
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKElkekaeeyiklsefyeEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 372 E---RLTALQVRLEQLQEK-----SIKENNSFDHFLLKSGGDCTLIQQYIECQSVRQLKEAVDSSINKLSNFDEVIDAHL 443
Cdd:PRK03918 342 ElkkKLKELEKRLEELEERhelyeEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEI 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 444 QNNQTTVdnslpspDRLKENQIDAKECDMSDTLSPSKEKSSDDTSDGQMEEQELNEPQNRVSLLKEMDRSLEAGDTEQvi 523
Cdd:PRK03918 422 KELKKAI-------EELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE-- 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 524 phihRELQEAQELANtgkqkclELQAMLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQRENTitttrEELYS 603
Cdd:PRK03918 493 ----SELIKLKELAE-------QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL-----EELKK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 604 AQEEILVLRHAMEAATAEREREITALqGDLSIvtAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQA 683
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEEL-GFESV--EELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFE 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 684 DCSGLQNECDSLRAEKSTLMQKLNrlEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIqdqhQQDASKLKIQLAQAE 763
Cdd:PRK03918 634 ELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEI----KKTLEKLKEELEERE 707
|
....*...
gi 528494936 764 SRTRDLQK 771
Cdd:PRK03918 708 KAKKELEK 715
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
30-106 |
1.13e-04 |
|
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.
Pssm-ID: 438734 [Multi-domain] Cd Length: 96 Bit Score: 41.74 E-value: 1.13e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528494936 30 IGRSVarcrpaQNNATFDCKVLSRNHALvwFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEesppCEVLSGDIIQFG 106
Cdd:cd22682 24 IGRSV------ESQVQIDDDSVSRYHAK--LAVNPSAVSIIDLGSTNGTIVNGKKIPKLAS----CDLQNGDQIKIG 88
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
5-110 |
1.52e-04 |
|
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also called nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438717 [Multi-domain] Cd Length: 97 Bit Score: 41.45 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 5 LAVFSCRPnshpFQERHVYLDE-PVKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTgkFYLQDTKSSNGTFINSQ 83
Cdd:cd22665 3 LKVFSQAH----GPEKDFPLYEgENVIGRD------PSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNK 70
|
90 100
....*....|....*....|....*....
gi 528494936 84 RLSrgseeSPPC--EVLSGDIIQFGvDVT 110
Cdd:cd22665 71 VRL-----KPNVryELIDGDLLLFG-DVK 93
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
256-808 |
1.60e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 256 ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQE---ELRELANKYNGAVNEIKDLTEKIKLAEDKHEELT 332
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETElcaEAEEMRARLAARKQELEEILHELESRLEEEEERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 333 QKGLNEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEKSIKENNSFDhfllksggdcTLIQQY 412
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERK----------LLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 413 IECQSVRQLKEAVDSSINKLSNFDEVIDAHLQnnqttvdnslpspDRLKenqidaKECDMSDTLSPSKEKSSDDTSDGQm 492
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLE-------------ERLK------KEEKGRQELEKAKRKLEGESTDLQ- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 493 eeQELNEPQNRVSLLKemdrsLEAGDTEQVIPHIHRELQEAQELANTGKQKCLELQAM---LEEERKTNRQQTEESAKQI 569
Cdd:pfam01576 222 --EQIAELQAQIAELR-----AQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQiseLQEDLESERAARNKAEKQR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 570 RFLQTQLAKLQTDME----------ALREQRENTIT-------------------------TTREELYSAQEEILVLRHA 614
Cdd:pfam01576 295 RDLGEELEALKTELEdtldttaaqqELRSKREQEVTelkkaleeetrsheaqlqemrqkhtQALEELTEQLEQAKRNKAN 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 615 MEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQ----LQSQHQERASQLQGEVEKLQADCSGLQN 690
Cdd:pfam01576 375 LEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSeserQRAELAEKLSKLQSELESVSSLLNEAEG 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 691 ECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQ---QDASKLKIQLA------- 760
Cdd:pfam01576 455 KNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRnveRQLSTLQAQLSdmkkkle 534
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 528494936 761 -------QAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNL 808
Cdd:pfam01576 535 edagtleALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDL 589
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
52-107 |
1.67e-04 |
|
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also called cell cycle regulatory protein p95, or Nijmegen breakage syndrome protein 1 (NBS1), is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. Nibrin modulates the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-dependent protein kinase catalytic subunit (DNA-PKcs) to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. Nibrin also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. Nibrin is a major player in the control of intra-S-phase checkpoint. This subfamily also includes Schizosaccharomyces pombe DNA repair and telomere maintenance protein Nbs1 and Arabidopsis thaliana AtNbs1. SpNbs1 is an FHA domain-containing protein required for DNA damage repair and S-phase DNA damage checkpoint. It is involved in telomere length maintenance and maintenance of chromatin structure. AtNbs1 is a component of MRN complex. It also functions in the very early stages of meiosis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438719 [Multi-domain] Cd Length: 108 Bit Score: 41.54 E-value: 1.67e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528494936 52 SRNHALVWFDHKTG---------KFYLQDTkSSNGTFINSQRLSRGSEesppCEVLSGDIIQFGV 107
Cdd:cd22667 40 SRKHATLTVLHPEAnlsdpdtrpELTLKDL-SKYGTFVNGEKLKGGSE----VTLKDGDVITFGV 99
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
258-387 |
1.79e-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: 43.76 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 258 LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEEL-TQKGL 336
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrNNKEY 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 528494936 337 N----EKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEK 387
Cdd:COG1579 92 EalqkEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
234-387 |
1.82e-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: 43.76 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 234 DGIRKELVALTEdkhnyETTAKESLRRVLQEKIEVVRK-LSEVERSLSNTEDECTHLREMNERTQEELRELAN--KYNGA 310
Cdd:COG1579 20 DRLEHRLKELPA-----ELAELEDELAALEARLEAAKTeLEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEAL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528494936 311 VNEIKDLTEKIKLAEDKHEELtqkgLNEKKELQMRIEEMEEKEQALQARIEALQADNDftnERLTALQVRLEQLQEK 387
Cdd:COG1579 95 QKEIESLKRRISDLEDEILEL----MERIEELEEELAELEAELAELEAELEEKKAELD---EELAELEAELEELEAE 164
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
599-809 |
1.87e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 599 EELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQtaakyevEISNLQASFQLQSQHQERASQLQGEV 678
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEK-------EVKELEELKEEIEELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 679 EKLQADCSGLQNECDSLRAEKSTLMQKLNRLeEELDSSRERSATLS-------SNLNALEKSQGDLENKLGSIQDQHQQD 751
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSefyeeylDELREIEKRLSRLEEEINGIEERIKEL 333
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 528494936 752 ASKlkiqlaqaESRTRDLQKEYDDTQSLLSDLRQRyEQTEQEKRSINDELEQCKVNLK 809
Cdd:PRK03918 334 EEK--------EERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLT 382
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
1-106 |
2.21e-04 |
|
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442679 [Multi-domain] Cd Length: 402 Bit Score: 44.37 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 1 MPSALAVFSCRPNSHPFQERHVYLDEPVKIGRSvARC-----RPAQnnatfdckVLSRNHALVWFDHktGKFYLQDTkSS 75
Cdd:COG3456 1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRS-ADCdwvlpDPDR--------SVSRRHAEIRFRD--GAFCLTDL-ST 68
|
90 100 110
....*....|....*....|....*....|....
gi 528494936 76 NGTFIN--SQRLSRGSEesppcEVLS-GDIIQFG 106
Cdd:COG3456 69 NGTFLNgsDHPLGPGRP-----VRLRdGDRLRIG 97
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
162-388 |
2.52e-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: 44.37 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 162 SQELFQLSQYLQEALHREQMLEQKLATLQRLLASTQEASESSWQALIDEDRLLSRLEVMGNQLQAySKNQTEDGIRKELV 241
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA-ELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 242 ALTEDKHNYETTAKESLRRVLQEKIEVV---RKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLT 318
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLlspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 319 EKIKLAEDKHEELTQkglnEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEKS 388
Cdd:COG4942 178 ALLAELEEERAALEA----LKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
167-386 |
3.61e-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: 44.29 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 167 QLSQYLQEALHREQMLEQKLATLQRLLASTQEASESSWQALIDEDRLLSRLEVMGNQLQAYSKNQTE-----DGIRKELV 241
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvkselKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 242 ALTEDKHNYETTAKESLRRVLQEKI-EVVRKLSEVERSLSNTE-------------------------------DECTHL 289
Cdd:TIGR02169 769 ELEEDLHKLEEALNDLEARLSHSRIpEIQAELSKLEEEVSRIEarlreieqklnrltlekeylekeiqelqeqrIDLKEQ 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 290 REMNERTQEEL----RELANKYNGAVNEIKDLTEkiklaedkheeltqkglnEKKELQMRIEEMEEKEQALQARIEALQA 365
Cdd:TIGR02169 849 IKSIEKEIENLngkkEELEEELEELEAALRDLES------------------RLGDLKKERDELEAQLRELERKIEELEA 910
|
250 260
....*....|....*....|.
gi 528494936 366 DNDFTNERLTALQVRLEQLQE 386
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLEALEE 931
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
253-803 |
3.63e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 253 TAKESLRR------VLQEKIEVVRKLSEVERSLSNtedecthlremNERTQEELRELANKYNGAVNEIKDLTEKIKLAED 326
Cdd:COG3096 496 TARELLRRyrsqqaLAQRLQQLRAQLAELEQRLRQ-----------QQNAERLLEEFCQRIGQQLDAAEELEELLAELEA 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 327 KHEELTQKgLNEKKELQMrieEMEEKEQALQARIEALQAdndfTNERLTALQVRLEQLQEKSIKEnnsfdhflLKSGGDC 406
Cdd:COG3096 565 QLEELEEQ-AAEAVEQRS---ELRQQLEQLRARIKELAA----RAPAWLAAQDALERLREQSGEA--------LADSQEV 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 407 TLIQQY---------IECQSVRQLKEAVDSSINKLSNFDEVIDAHLQN--------------NQTTVDNS---------- 453
Cdd:COG3096 629 TAAMQQllerereatVERDELAARKQALESQIERLSQPGGAEDPRLLAlaerlggvllseiyDDVTLEDApyfsalygpa 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 454 -----LPSPDRLKEnQIDAKECDMSDTLSPSKEKSSDDTSDGQMEEQE------LNEPQNRVSLLKEMDRSLEAGdTEQV 522
Cdd:COG3096 709 rhaivVPDLSAVKE-QLAGLEDCPEDLYLIEGDPDSFDDSVFDAEELEdavvvkLSDRQWRYSRFPEVPLFGRAA-REKR 786
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 523 IPHIHRELQE-AQELANT--GKQKCLELQAMLEEERKTNRQQTEES--AKQIRFLQTQLAKLQTDMEALREQrentITTT 597
Cdd:COG3096 787 LEELRAERDElAEQYAKAsfDVQKLQRLHQAFSQFVGGHLAVAFAPdpEAELAALRQRRSELERELAQHRAQ----EQQL 862
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 598 REELYSAQEEILVLR------HAMEAAT-AEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQER 670
Cdd:COG3096 863 RQQLDQLKEQLQLLNkllpqaNLLADETlADRLEELREELDAAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQAD 942
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 671 ASQLQGEVEKLQA------------------DCSGLQNECDSLrAEKstLMQKLNRLEEELDSSRERSATLSSNLNALEK 732
Cdd:COG3096 943 YLQAKEQQRRLKQqifalsevvqrrphfsyeDAVGLLGENSDL-NEK--LRARLEQAEEARREAREQLRQAQAQYSQYNQ 1019
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528494936 733 SQGDLENKLGSIQDQHQ---QDASKLKIQL-AQAESRTRDlqkEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQ 803
Cdd:COG3096 1020 VLASLKSSRDAKQQTLQeleQELEELGVQAdAEAEERARI---RRDELHEELSQNRSRRSQLEKQLTRCEAEMDS 1091
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
666-803 |
4.46e-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: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 666 QHQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALeKSQGDLENKLGSIQ 745
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNNKEYEALQKEIE 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 528494936 746 DQhQQDASKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQ 803
Cdd:COG1579 100 SL-KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
553-814 |
4.51e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 553 EERKTNRQQTEESAKQIRFLQTQLAKLQTDmealREQRENTITTTREELYSAQEEILVLRHAMEAATAEREREITALQGD 632
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 633 LSIVTAELDKWRQTAAKYEVEISNLQAsfQLQSQHQERASQLQGEVEKLQADcsglQNECDSLRAEKSTLMQKLNRLEEE 712
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELNK--KIKDLGEEEQLRVKEKIGELEAE----IASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 713 LDSSRErsatlssnlnaleKSQGDLENKLGSIQDQhqqdasklKIQLAQAESRTRDLQKEYDDtqsllsdLRQRYEQTEQ 792
Cdd:TIGR02169 327 LEAEID-------------KLLAEIEELEREIEEE--------RKRRDKLTEEYAELKEELED-------LRAELEEVDK 378
|
250 260
....*....|....*....|..
gi 528494936 793 EKRSINDELEQCKVNLKLLQDK 814
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKRE 400
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
490-811 |
4.52e-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: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 490 GQMEEQELNEPQNRVSLLKEMDRSLEAGDTEQVIPHIHRELQEAQELANTGKQKCLELQAMLEEERKTNRQQtEESAKQI 569
Cdd:pfam02463 142 GKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYY-QLKEKLE 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 570 RFLQTQLAKLQTDMEALREQRENTITTTREELYSAQEEILVLRHAMEAATAEREREITALQGDLSivtaelDKWRQTAAK 649
Cdd:pfam02463 221 LEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE------EELKLLAKE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 650 YEVEISNLQASFQLQSQHQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNA 729
Cdd:pfam02463 295 EEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 730 LEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLK 809
Cdd:pfam02463 375 LLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELE 454
|
..
gi 528494936 810 LL 811
Cdd:pfam02463 455 KQ 456
|
|
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
53-106 |
5.06e-04 |
|
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 (FHAD1) and similar proteins; FHAD1, also called FHA domain-containing protein 1, is an uncharacterized FHA domain-containing protein. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438752 [Multi-domain] Cd Length: 96 Bit Score: 39.93 E-value: 5.06e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 528494936 53 RNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPcevlsGDIIQFG 106
Cdd:cd22700 36 EQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAP-----GDVLRFG 84
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
16-111 |
5.67e-04 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaB and similar proteins; FhaB, also called FtsZ-interacting protein A (FipA), is a putative virulence factor involved in regulating cell shape. It can interact with polyketide-associated protein PapA5, a putative membrane protein involved in the biosynthesis of virulence enhancing lipids. FhaB regulates growth and cell division. It is probably required for divisomal protein assembly under oxidative stress. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438745 [Multi-domain] Cd Length: 91 Bit Score: 39.59 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 16 PFQERHVYLD-EPVKIGRSvarcrpAQNNATFDCKVLSRNHALVWFdhKTGKFYLQDTKSSNGTFINSQRLSRgseespP 94
Cdd:cd22693 7 TLQGQTFPIDkSGITIGRA------DDNDLVLSDDFVSSRHARIYL--QGSSWYLEDLGSTNGTFVNGNRVTQ------P 72
|
90
....*....|....*..
gi 528494936 95 CEVLSGDIIQFGVDVTE 111
Cdd:cd22693 73 VVVQPGDTIRIGATVFE 89
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
494-813 |
5.73e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 494 EQELNEPQNRVSLLKEMDRSLEagDTEQVIPHIHRELQEAQELANtgkQKCLELQAMLEEERKTNRQQTEESAKQIRFLQ 573
Cdd:COG4717 138 EAELAELPERLEELEERLEELR--ELEEELEELEAELAELQEELE---ELLEQLSLATEEELQDLAEELEELQQRLAELE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 574 TQLAKLQTDMEALREQRENT----------------------------ITTTREELYSAQEEI-------------LVLR 612
Cdd:COG4717 213 EELEEAQEELEELEEELEQLeneleaaaleerlkearlllliaaallaLLGLGGSLLSLILTIagvlflvlgllalLFLL 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 613 HAMEAATAEREREITALQGDLSIVTAEldKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQAdcsglQNEC 692
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEE--ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE-----ELQL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 693 DSLRAEKSTLMQKLN-RLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQ--------DQHQQDASKLKIQLAQAE 763
Cdd:COG4717 366 EELEQEIAALLAEAGvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEellealdeEELEEELEELEEELEELE 445
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 528494936 764 SRTRDLQKEYDDTQS---------LLSDLRQRYEQTEQEKRSINDELEQCKVNLKLLQD 813
Cdd:COG4717 446 EELEELREELAELEAeleqleedgELAELLQELEELKAELRELAEEWAALKLALELLEE 504
|
|
| FHA_RAD53-like_rpt2 |
cd22690 |
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
12-103 |
6.14e-04 |
|
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine/threonine-protein kinase RAD53 and similar proteins; RAD53, also called CHEK2 homolog, or serine-protein kinase 1 (Spk1), is a nuclear protein kinase that phosphorylates proteins on serine, threonine, and tyrosine. It controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints and prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. It may be involved in the phosphorylation of RPH1. RAD53 contains two FHA domains. This model corresponds to the second one. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438742 [Multi-domain] Cd Length: 105 Bit Score: 39.97 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 12 PNSHPfqerHVYL-DEPVKIGRSvarcrpAQNNATFDCKVLSRNHALVWFD-HKTGK--FYLQDTkSSNGTFINSQRLSR 87
Cdd:cd22690 8 NPSYP----DIELtQNTTFIGRS------KDCDEEITDPRISKHHCIITRKrSGKGLddVYVTDT-STNGTFINNNRLGK 76
|
90
....*....|....*.
gi 528494936 88 GSEesppCEVLSGDII 103
Cdd:cd22690 77 GSQ----SLLQDGDEI 88
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
324-802 |
7.99e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 324 AEDKHEELTQKGLNEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEKSIKENNSfdhfllksg 403
Cdd:TIGR00618 185 EFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQ--------- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 404 gdctlIQQYIECQSVRQLKEAVDSSINKLSNFDEVID---------------AHLQNNQTTVDNSLPSPDRLKENQIDAK 468
Cdd:TIGR00618 256 -----LKKQQLLKQLRARIEELRAQEAVLEETQERINrarkaaplaahikavTQIEQQAQRIHTELQSKMRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 469 ECDMSDTLSPSKEKSSDDTsdgQMEEQELNEPQNRVSLLKEMDRSLEAGDTEqvipHIHRElqeaQELANTGKQKCLELQ 548
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQT---LHSQEIHIRDAHEVATSIREISCQQHTLTQ----HIHTL----QQQKTTLTQKLQSLC 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 549 AMLEEERKTNRQQTEESAKQiRFLQTQLAKLQTDMEALREQRENTITTTREElysAQEEILVLRHAMEAATAEREREitA 628
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAF-RDLQGQLAHAKKQQELQQRYAELCAAAITCT---AQCEKLEKIHLQESAQSLKERE--Q 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 629 LQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQADCSGLQNEC-------DSLRAEKST 701
Cdd:TIGR00618 474 QLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYaqletseEDVYHQLTS 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 702 LMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDaSKLKIQLAQAESRTRDLQKEYDDTQSLLS 781
Cdd:TIGR00618 554 ERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKL-SEAEDMLACEQHALLRKLQPEQDLQDVRL 632
|
490 500
....*....|....*....|.
gi 528494936 782 DLRQRYEQTEQEKRSINDELE 802
Cdd:TIGR00618 633 HLQQCSQELALKLTALHALQL 653
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
172-624 |
8.24e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 43.20 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 172 LQEALHREqmLEQKLATLQRLLASTQEASESSWQALIDE----DRLLSRLEVM-GNQLQAYSKNQTEDGIRKELVALTED 246
Cdd:pfam07111 134 LEEGSQRE--LEEIQRLHQEQLSSLTQAHEEALSSLTSKaeglEKSLNSLETKrAGEAKQLAEAQKEAELLRKQLSKTQE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 247 KHNYETTAKESLRRVLQEKI--EVVRKLSEVERSlsNTEDECTHLREMNERTQEELRELANKYNGAVNEI----KDLTEK 320
Cdd:pfam07111 212 ELEAQVTLVESLRKYVGEQVppEVHSQTWELERQ--ELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLalqeEELTRK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 321 IKLAEDKHEELTQKglnekkeLQMRIEEMEEKEQALQARIEALQADNdftNERLTALQVRLEQLQEKSIKEnnSFDHFLL 400
Cdd:pfam07111 290 IQPSDSLEPEFPKK-------CRSLLNRWREKVFALMVQLKAQDLEH---RDSVKQLRGQVAELQEQVTSQ--SQEQAIL 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 401 KSGGDCTLIQQYIECQSVRQLKEAVDSSINKLSNFDEVIDAHLQNNQTTVDNSLPSPDRL-----KENQIDAKECDMSDT 475
Cdd:pfam07111 358 QRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLettmtRVEQAVARIPSLSNR 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 476 LS---------------------------PSKEKSSDDTSDGQMEEQELNEPQNRVS---------LLKEMDRSLEAGDT 519
Cdd:pfam07111 438 LSyavrkvhtikglmarkvalaqlrqescPPPPPAPPVDADLSLELEQLREERNRLDaelqlsahlIQQEVGRAREQGEA 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 520 E-----QVIPHIHRELQEAQE-LANTGKQKCLELQAMLE--EERKTNRQQ-TEESAKQIRFLQTQLAKLQTdmeALREQR 590
Cdd:pfam07111 518 ErqqlsEVAQQLEQELQRAQEsLASVGQQLEVARQGQQEstEEAASLRQElTQQQEIYGQALQEKVAEVET---RLREQL 594
|
490 500 510
....*....|....*....|....*....|....
gi 528494936 591 ENTITTTREELYSAQEEILVLRHAMEAATAERER 624
Cdd:pfam07111 595 SDTKRRLNEARREQAKAVVSLRQIQHRATQEKER 628
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
49-112 |
8.24e-04 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 (PML1) and similar proteins; PML1 is an FHA domain-containing protein required for efficient splicing and pre-mRNA nuclear retention. It is a component of the pre-mRNA retention and splicing (RES) complex composed of at least BUD13, IST3, and PML1. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438733 [Multi-domain] Cd Length: 129 Bit Score: 40.12 E-value: 8.24e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528494936 49 KVLSRNHALVWFDHKTG--KFYLQDTKSSNGTFINsqrlsrgSEESPPC---EVLSGDIIQFGVDVTEN 112
Cdd:cd22681 64 ETCSKQHCVIQFRNVKGilKPYIMDLDSSNGTCLN-------DNVIPSSryvELRSGDVITFSKSNDYE 125
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
528-808 |
8.58e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 8.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 528 RELQEAQELANTGKQKCL----ELQAMLEEERKTNRQQT------------------------EESAKQIRFLQTQLAKL 579
Cdd:pfam01576 731 RDLQARDEQGEEKRRQLVkqvrELEAELEDERKQRAQAVaakkkleldlkeleaqidaankgrEEAVKQLKKLQAQMKDL 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 580 QTDMEALREQRENTITTTRE----------ELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAK 649
Cdd:pfam01576 811 QRELEEARASRDEILAQSKEsekklknleaELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEAR 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 650 ---YEVEISNLQASFQLQSQHQERASQlqgEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELdssRERSATLSSN 726
Cdd:pfam01576 891 iaqLEEELEEEQSNTELLNDRLRKSTL---QVEQLTTELAAERSTSQKSESARQQLERQNKELKAKL---QEMEGTVKSK 964
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 727 LNAlekSQGDLENKLGSIQDQHQQDASklkiQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKV 806
Cdd:pfam01576 965 FKS---SIAALEAKIAQLEEQLEQESR----ERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKR 1037
|
..
gi 528494936 807 NL 808
Cdd:pfam01576 1038 QL 1039
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
172-383 |
1.08e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.55 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 172 LQEALHREQMLEQKLATLQRLLASTQEASESSwqalidEDRLLSRLEvmgNQLQAYSKNQTEDGIRKELvaltEDKHNYE 251
Cdd:pfam00261 24 LEEAEKRAEKAEAEVAALNRRIQLLEEELERT------EERLAEALE---KLEEAEKAADESERGRKVL----ENRALKD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 252 TTAKESLRRVLQEKIEVV----RKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDL---TEKIKLA 324
Cdd:pfam00261 91 EEKMEILEAQLKEAKEIAeeadRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLeasEEKASER 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 325 EDKHEElTQKGLNEK-KELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQ 383
Cdd:pfam00261 171 EDKYEE-QIRFLTEKlKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQ 229
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
556-821 |
1.13e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 556 KTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQRENTITTTREELYSAQEEILvlrhAMEAATAEREREITALQGDLSI 635
Cdd:PHA02562 177 RELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAK----TIKAEIEELTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 636 VTAELDKWRQTAAKYEVEISNLQASFQLQSQHQER---ASQLQGEVEKLQadcsglqnecdSLRAEKSTLMQKLNRLEEE 712
Cdd:PHA02562 253 PSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGVCptcTQQISEGPDRIT-----------KIKDKLKELQHSLEKLDTA 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 713 LDSSRERSatlsSNLNALEKSQGDLENKLgsiqDQHQQDASKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQ 792
Cdd:PHA02562 322 IDELEEIM----DEFNEQSKKLLELKNKI----STNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVK 393
|
250 260
....*....|....*....|....*....
gi 528494936 793 EKRSINDELEQCKVNLKLLQDKGSNPSIL 821
Cdd:PHA02562 394 TKSELVKEKYHRGIVTDLLKDSGIKASII 422
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
163-366 |
1.27e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.37 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 163 QELFQLSQYLQEALHREQMLEQKLATLQRLlastqEASESSWQALIDEDRLLSRLEVMGNQLQ-AYSK-NQTEDGI---- 236
Cdd:COG0497 172 KELEELRADEAERARELDLLRFQLEELEAA-----ALQPGEEEELEEERRRLSNAEKLREALQeALEAlSGGEGGAldll 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 237 ---RKELVALTEDKHNYETTAkESLRRVLQEKIEVVRklsEVERSLSNTEDECTHLREMNERtQEELRELANKYNGAVNE 313
Cdd:COG0497 247 gqaLRALERLAEYDPSLAELA-ERLESALIELEEAAS---ELRRYLDSLEFDPERLEEVEER-LALLRRLARKYGVTVEE 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 528494936 314 IKDLTEKIKlaedkhEELTQkglnekkelqmrIEEMEEKEQALQARIEALQAD 366
Cdd:COG0497 322 LLAYAEELR------AELAE------------LENSDERLEELEAELAEAEAE 356
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
688-814 |
1.36e-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: 41.06 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 688 LQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLgsiqDQHQQDASKLKIQLAQAESrtr 767
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI----EEVEARIKKYEEQLGNVRN--- 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 528494936 768 dlQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLKLLQDK 814
Cdd:COG1579 88 --NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE 132
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
686-806 |
1.83e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.16 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 686 SGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESR 765
Cdd:smart00787 147 EGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKK 226
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 528494936 766 TRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKV 806
Cdd:smart00787 227 LEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
271-813 |
2.33e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 271 KLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEELTQKGLNEKKELQ--MRIEE 348
Cdd:PRK01156 170 KLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNelSSLED 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 349 MEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEKSI--KENNSFDHFLLKSggdctliqqyiECQSVRQLKEAVD 426
Cdd:PRK01156 250 MKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVykNRNYINDYFKYKN-----------DIENKKQILSNID 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 427 SSINKlsnFDEVID--AHLQNNQTTVDNSLPSPDRLKeNQIDAKECDMSDTLSPSK------------EKSSDDTSDGQM 492
Cdd:PRK01156 319 AEINK---YHAIIKklSVLQKDYNDYIKKKSRYDDLN-NQILELEGYEMDYNSYLKsieslkkkieeySKNIERMSAFIS 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 493 EEQELNE--PQNRVSLLKEMDRSL-----EAGDTEQVIPHIHRELQEAQELAN--TGKQKCLELQAMLEEErKTNRQQTE 563
Cdd:PRK01156 395 EILKIQEidPDAIKKELNEINVKLqdissKVSSLNQRIRALRENLDELSRNMEmlNGQSVCPVCGTTLGEE-KSNHIINH 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 564 ESAKQIRfLQTQLAKLQTDMEALREQRENTItttREELYSAQEEILVLRhAMEAATAEREREITALQGDLSIVTAELDKW 643
Cdd:PRK01156 474 YNEKKSR-LEEKIREIEIEVKDIDEKIVDLK---KRKEYLESEEINKSI-NEYNKIESARADLEDIKIKINELKDKHDKY 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 644 RQTAAKYE-VEISNLQASFQ----------------LQSQHQERASQLQGEVEKLQADCSGLQNEcdslraeKSTLMQKL 706
Cdd:PRK01156 549 EEIKNRYKsLKLEDLDSKRTswlnalavislidietNRSRSNEIKKQLNDLESRLQEIEIGFPDD-------KSYIDKSI 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 707 NRLEEELDSSRERSATLSSNLNALEKSQGDLEN--KLGSIQDQHQQDASKLKIQLAQAESRTRDLQKEYDDTQSLLSD-- 782
Cdd:PRK01156 622 REIENEANNLNNKYNEIQENKILIEKLRGKIDNykKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARle 701
|
570 580 590
....*....|....*....|....*....|....*.
gi 528494936 783 -----LRQRYEQTEQEKRSINDELEQCKVNLKLLQD 813
Cdd:PRK01156 702 stieiLRTRINELSDRINDINETLESMKKIKKAIGD 737
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-730 |
2.55e-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: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 263 QEKIEVVRKLSEVERSLSNTEDEcthLREMnERTQEELR---ELANKYNGAVNEIKDLtEKIKLAEDKHEELtqkglNEK 339
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDI---LNEL-ERQLKSLErqaEKAERYKELKAELREL-ELALLVLRLEELR-----EEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 340 KELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEKsikennsfdhfllksggdctLIQQYIECQSVR 419
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE--------------------LYALANEISRLE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 420 QLKEAVDSSINKLSNFDEVIDAHLQNNQTtvdnslpspdrlkenqidakecdmsdtlspSKEKSSDDTSDGQMEEQELNE 499
Cdd:TIGR02168 302 QQKQILRERLANLERQLEELEAQLEELES------------------------------KLDELAEELAELEEKLEELKE 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 500 pqNRVSLLKEMDRSleagdtEQVIPHIHRELQEAQELANTGKQKCLELqamleeerktnRQQTEESAKQIRFLQTQLakl 579
Cdd:TIGR02168 352 --ELESLEAELEEL------EAELEELESRLEELEEQLETLRSKVAQL-----------ELQIASLNNEIERLEARL--- 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 580 qtdmEALREQRENTITTTREELYSAQEeilVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEveisnlQA 659
Cdd:TIGR02168 410 ----ERLEDRRERLQQEIEELLKKLEE---AELKELQAELEELEEELEELQEELERLEEALEELREELEEAE------QA 476
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528494936 660 SFQLQSQHQERASQLQGeVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEE--ELDSSRER--SATLSSNLNAL 730
Cdd:TIGR02168 477 LDAAERELAQLQARLDS-LERLQENLEGFSEGVKALLKNQSGLSGILGVLSEliSVDEGYEAaiEAALGGRLQAV 550
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
493-837 |
2.79e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 493 EEQELNEPQNRVSLLKEMDRSLEAgDTEQVIPHIHReLQEAQELANTGKQ---KCLELQAMLE----------EERKTNR 559
Cdd:PRK04863 305 EQYRLVEMARELAELNEAESDLEQ-DYQAASDHLNL-VQTALRQQEKIERyqaDLEELEERLEeqnevveeadEQQEENE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 560 QQTEESAKQIRFLQTQLAKLQTDME--------------ALREQR-------------ENTITTTREELYSAQEEILVLR 612
Cdd:PRK04863 383 ARAEAAEEEVDELKSQLADYQQALDvqqtraiqyqqavqALERAKqlcglpdltadnaEDWLEEFQAKEQEATEELLSLE 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 613 HAMEAATAEREREITALQGDLSIV--TAELDKWRQ------TAAKYEVEISNLQasfQLQSQHQ--ERASQLQGEVEKLQ 682
Cdd:PRK04863 463 QKLSVAQAAHSQFEQAYQLVRKIAgeVSRSEAWDVarellrRLREQRHLAEQLQ---QLRMRLSelEQRLRQQQRAERLL 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 683 ADC-----SGLQNEcDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSnlnaleksqgdlenklgsIQDQHQQDASKLK- 756
Cdd:PRK04863 540 AEFckrlgKNLDDE-DELEQLQEELEARLESLSESVSEARERRMALRQ------------------QLEQLQARIQRLAa 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 757 -----IQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNL-----KLLQDKGSNPSILQPVQA 826
Cdd:PRK04863 601 rapawLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALdeeieRLSQPGGSEDPRLNALAE 680
|
410
....*....|.
gi 528494936 827 IFIGLFLALLY 837
Cdd:PRK04863 681 RFGGVLLSEIY 691
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
253-624 |
2.82e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 253 TAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRelankyngavneikdLTEKIKLAEDKHEELT 332
Cdd:PRK04863 297 TSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALR---------------QQEKIERYQADLEELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 333 QKgLNEKKELqmrIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEKSI------------KENNSFDHFLL 400
Cdd:PRK04863 362 ER-LEEQNEV---VEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIqyqqavqaleraKQLCGLPDLTA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 401 KSGGDctLIQQYIecQSVRQLKEAVDSSINKLSNFDEVIDAHLQNNQtTVDNSLPSPDRlKENQIDAKEcdmsdTLSPSK 480
Cdd:PRK04863 438 DNAED--WLEEFQ--AKEQEATEELLSLEQKLSVAQAAHSQFEQAYQ-LVRKIAGEVSR-SEAWDVARE-----LLRRLR 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 481 EKSSDDTSDGQME------EQELNEPQNRVSLLKEMDRSLEAG-DTEQVIPHIHRELQEAQELANTGKQKCLELQAMLEE 553
Cdd:PRK04863 507 EQRHLAEQLQQLRmrlselEQRLRQQQRAERLLAEFCKRLGKNlDDEDELEQLQEELEARLESLSESVSEARERRMALRQ 586
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528494936 554 ERKTNRQQTEESAKQI---RFLQTQLAKLQT---DMEALREQRENTITTTREELYSAQEEILVLRHAMEAATAERER 624
Cdd:PRK04863 587 QLEQLQARIQRLAARApawLAAQDALARLREqsgEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIER 663
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
181-670 |
3.36e-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: 41.25 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 181 MLEQKLATLQRLLASTQEASESSWQALIDEDRLLSRLEVMGNQLQAYSKNQT--EDGIR---KELVALTEDKHNY---ET 252
Cdd:pfam05483 262 LLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKalEEDLQiatKTICQLTEEKEAQmeeLN 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 253 TAKESLRRVLQEKIEVVRKLSEVERS----LSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLteKIKLAEDkh 328
Cdd:pfam05483 342 KAKAAHSFVVTEFEATTCSLEELLRTeqqrLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEEL--KKILAED-- 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 329 eeltQKGLNEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTAL----QVRLEQLQE-KSIKENNSFDHFLLKSG 403
Cdd:pfam05483 418 ----EKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIktseEHYLKEVEDlKTELEKEKLKNIELTAH 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 404 GDCTLIQQYIECQS----VRQLKEAVDSSINKLSNFDEVIDA--HLQNNQTTVDNSLPSPDRLKENQIDAKECdmsdTLS 477
Cdd:pfam05483 494 CDKLLLENKELTQEasdmTLELKKHQEDIINCKKQEERMLKQieNLEEKEMNLRDELESVREEFIQKGDEVKC----KLD 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 478 PSKEKSSDDTSDGQMEEQELNEPQNRVSLLKEM--DRSLEAGDTEQVIPHIHRELQEAQELANTGKQKCLELQAMLEEER 555
Cdd:pfam05483 570 KSEENARSIEYEVLKKEKQMKILENKCNNLKKQieNKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAK 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 556 KTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQRENTITTTREELYSAQEEILVLRHAMEAATAEREREITALQGDLSI 635
Cdd:pfam05483 650 QKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGL 729
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 528494936 636 VTAELDKWRQTAAKYEVEISNLQASF-----QLQSQHQER 670
Cdd:pfam05483 730 YKNKEQEQSSAKAALEIELSNIKAELlslkkQLEIEKEEK 769
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
552-659 |
3.36e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 552 EEERKTNRQQTEESAKQIRFLQTQLAKLQ---TDMEALREQRENTITTTREELYSAQEEilvlrhamEAATAEREREITA 628
Cdd:COG2433 398 EREKEHEERELTEEEEEIRRLEEQVERLEaevEELEAELEEKDERIERLERELSEARSE--------ERREIRKDREISR 469
|
90 100 110
....*....|....*....|....*....|.
gi 528494936 629 LQGDLSIVTAELDKWRQTAAKYEVEISNLQA 659
Cdd:COG2433 470 LDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
289-800 |
3.39e-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: 41.25 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 289 LREMNERTQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEELTqkglnekkelqMRIEEMEEKEQALQARIealqadnd 368
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLT-----------FLLEESRDKANQLEEKT-------- 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 369 ftnerltalqvrleQLQEKSIKENNSFDHFLLKSGGDCTL-IQQYIECQsvRQLKEAVDSSINKLSNFDEVIDAHLQNNq 447
Cdd:pfam05483 278 --------------KLQDENLKELIEKKDHLTKELEDIKMsLQRSMSTQ--KALEEDLQIATKTICQLTEEKEAQMEEL- 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 448 ttvdNSLPSPDRLKENQIDAKECDMSDTLSPSKEKssddtsdgqmeeQELNEPQNRVSLLKEMDRSleagdteqviphih 527
Cdd:pfam05483 341 ----NKAKAAHSFVVTEFEATTCSLEELLRTEQQR------------LEKNEDQLKIITMELQKKS-------------- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 528 RELQEAQELANTGKQKCLELQAMLEEERKT--NRQQTEESAKQIRFLQTQLAK-LQTDMEALRE-QRENTITTTREELYS 603
Cdd:pfam05483 391 SELEEMTKFKNNKEVELEELKKILAEDEKLldEKKQFEKIAEELKGKEQELIFlLQAREKEIHDlEIQLTAIKTSEEHYL 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 604 AQEEilvlrhAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERasqLQGEVEKLQA 683
Cdd:pfam05483 471 KEVE------DLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEER---MLKQIENLEE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 684 DCSGLQNECDSLRAEkstLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQ-----------HQQDA 752
Cdd:pfam05483 542 KEMNLRDELESVREE---FIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQienknknieelHQENK 618
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 528494936 753 SKLK------IQLAQAESRTRDLQKEYDDTQSLLSDLRQRYeQTEQEKRSINDE 800
Cdd:pfam05483 619 ALKKkgsaenKQLNAYEIKVNKLELELASAKQKFEEIIDNY-QKEIEDKKISEE 671
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
704-824 |
3.45e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 704 QKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESRTRDLQKEYDDTQSLLSDL 783
Cdd:PHA02562 181 QQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKL 260
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 528494936 784 RQRYEQteqekrsINDELEQCKVNLKLLQDKGSNPSILQPV 824
Cdd:PHA02562 261 NTAAAK-------IKSKIEQFQKVIKMYEKGGVCPTCTQQI 294
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
256-393 |
3.56e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 256 ESLRRVLQEKI-EVVRKLSEVERSLSNTEDEcthLREMNERTQEELRELANKYNGAVNE--------IKDLTEKIKL--A 324
Cdd:PRK00409 526 EELERELEQKAeEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLEEAEKEAQQAIKEakkeadeiIKELRQLQKGgyA 602
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528494936 325 EDKHEELTQKglneKKELQMRIEEMEEKEQALQARIEALQAdndftNERltalqVRLEQLQEK----SIKENN 393
Cdd:PRK00409 603 SVKAHELIEA----RKRLNKANEKKEKKKKKQKEKQEELKV-----GDE-----VKYLSLGQKgevlSIPDDK 661
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
667-797 |
3.66e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 667 HQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNL---NALEKSQGDLENKlgS 743
Cdd:PRK04863 284 HLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALrqqEKIERYQADLEEL--E 361
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 528494936 744 IQDQHQQDASKL-KIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEqtEQEKRSI 797
Cdd:PRK04863 362 ERLEEQNEVVEEaDEQQEENEARAEAAEEEVDELKSQLADYQQALD--VQQTRAI 414
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
168-352 |
3.76e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 168 LSQYLQEALHREQMLEQKLATLQRLLASTQEaSESSWQALIDEDRLlsRLEVMGNQLQAYSKNQTEdgIRKELVALTEDK 247
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKE-QIKSIEKEIENLNG--KKEELEEELEELEAALRD--LESRLGDLKKER 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 248 HNYETTAKESLRRVLQEKIEVVRK---LSEVERSLSNTEDECTH--------------------LREMNERTQEELRELA 304
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKrkrLSELKAKLEALEEELSEiedpkgedeeipeeelsledVQAELQRVEEEIRALE 971
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 528494936 305 NKYNGAVNEIKDLTEKIKLAEDKHEELTQkglnEKKELQMRIEEMEEK 352
Cdd:TIGR02169 972 PVNMLAIQEYEEVLKRLDELKEKRAKLEE----ERKAILERIEEYEKK 1015
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
537-794 |
3.88e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.45 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 537 ANTGKQKCLELQAMLEEERKTNRQQteesakqirflQTQLAKLQtdmEALREQrENTITTTREELYSAQeeilvlrhame 616
Cdd:PRK11637 42 ASDNRDQLKSIQQDIAAKEKSVRQQ-----------QQQRASLL---AQLKKQ-EEAISQASRKLRETQ----------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 617 aataereREITALQGDLSIVTAELDKWRQTAAKYEVEIS-NLQASFQlQSQHQERASQLQGE----VEKLQA-------- 683
Cdd:PRK11637 96 -------NTLNQLNKQIDELNASIAKLEQQQAAQERLLAaQLDAAFR-QGEHTGLQLILSGEesqrGERILAyfgylnqa 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 684 ---DCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGsiQDQHQ-----QDASKL 755
Cdd:PRK11637 168 rqeTIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQ--KDQQQlselrANESRL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 528494936 756 KIQLAQAE--------------SRTRDLQKEYDDTQSllsdlrqRYEQTEQEK 794
Cdd:PRK11637 246 RDSIARAEreakaraereareaARVRDKQKQAKRKGS-------TYKPTESER 291
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
173-366 |
4.01e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 173 QEALHREQMLEQKLATLQRLLASTQEasesswqalidedrllsRLEVMGNQLQAYSKNQTEdgIRKELVALTEDKHNYET 252
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLKELPA-----------------ELAELEDELAALEARLEA--AKTELEDLEKEIKRLEL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 253 TAKESLRRV--LQEKIEVVRKlsevERSLSNTEDECTHLREMNERTQEELRELankyngaVNEIKDLTEKIKLAEDKHEE 330
Cdd:COG1579 67 EIEEVEARIkkYEEQLGNVRN----NKEYEALQKEIESLKRRISDLEDEILEL-------MERIEELEEELAELEAELAE 135
|
170 180 190
....*....|....*....|....*....|....*.
gi 528494936 331 LTQKGLNEKKELQMRIEEMEEKEQALQARIEALQAD 366
Cdd:COG1579 136 LEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
733-808 |
4.34e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 733 SQGDLENKLGSIQ--DQHQQDASKLKIQLAQAESRTRDLQKEYDD-TQSLLSDLRQRYE-----QTEQEKRSINDELEQC 804
Cdd:PRK11281 61 VQQDLEQTLALLDkiDRQKEETEQLKQQLAQAPAKLRQAQAELEAlKDDNDEETRETLStlslrQLESRLAQTLDQLQNA 140
|
....
gi 528494936 805 KVNL 808
Cdd:PRK11281 141 QNDL 144
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
213-416 |
6.07e-03 |
|
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: 40.42 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 213 LLSRLEVMGNQLQAYSKNQTEDGIRKELVALTEDKHNYETTAKEslrrvlqeKIEVVRKLSEVERSlsntedecthlREM 292
Cdd:TIGR01612 1455 LFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSKGC--------KDEADKNAKAIEKN-----------KEL 1515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 293 NERTQEELRELANKY----------------NGAVNEIKDLTEKIKLAEDKHEeltQKgLNEKKELQMRIEEmeekeqal 356
Cdd:TIGR01612 1516 FEQYKKDVTELLNKYsalaiknkfaktkkdsEIIIKEIKDAHKKFILEAEKSE---QK-IKEIKKEKFRIED-------- 1583
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 357 qariEAlqADNDFTNERLTALQVRLEQLQEKSIKENNsfdhfLLKSGGDCTLIQQYIECQ 416
Cdd:TIGR01612 1584 ----DA--AKNDKSNKAAIDIQLSLENFENKFLKISD-----IKKKINDCLKETESIEKK 1632
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
313-757 |
6.64e-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: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 313 EIKDLTEKIKLAEDKHeeltQKGLNEK-KELQMRIEEMEEKEQALQARIEALQADNDFTNErltaLQVRlEQLQEKSIKE 391
Cdd:pfam05483 216 KLKEDHEKIQHLEEEY----KKEINDKeKQVSLLLIQITEKENKMKDLTFLLEESRDKANQ----LEEK-TKLQDENLKE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 392 NNSFDHFLLKSGGDCTL-IQQYIECQsvRQLKEAVDSSINKLSNFDEVIDAHLQNNqttvdNSLPSPDRLKENQIDAKEC 470
Cdd:pfam05483 287 LIEKKDHLTKELEDIKMsLQRSMSTQ--KALEEDLQIATKTICQLTEEKEAQMEEL-----NKAKAAHSFVVTEFEATTC 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 471 DMSDTLSPSKEKSSDDTSDGQMEEQELnepQNRVSLLKEM-----DRSLEAGDTEQVIPHIHRELQE-------AQELAN 538
Cdd:pfam05483 360 SLEELLRTEQQRLEKNEDQLKIITMEL---QKKSSELEEMtkfknNKEVELEELKKILAEDEKLLDEkkqfekiAEELKG 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 539 TGKQKCLELQAMLEEERKTNRQQTEESAKQIRFLQtQLAKLQTDMEalREQRENTITTTREELYSAQEEILVLRHA-MEA 617
Cdd:pfam05483 437 KEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLK-EVEDLKTELE--KEKLKNIELTAHCDKLLLENKELTQEASdMTL 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 618 ATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQ--------SQHQERASQLQGEVEKLQADCSGLQ 689
Cdd:pfam05483 514 ELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKgdevkcklDKSEENARSIEYEVLKKEKQMKILE 593
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528494936 690 NECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLE-------NKLGSIQDQHQQDASKLKI 757
Cdd:pfam05483 594 NKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLElelasakQKFEEIIDNYQKEIEDKKI 668
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
229-608 |
7.22e-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: 40.00 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 229 KNQTEDGIRKELVALTEDKHNYETTAKESLRRVLQekievvrKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYN 308
Cdd:TIGR04523 301 NNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNK-------IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 309 GAVNEIKDLTEKIKLAEDKHEELTQKGLNEKK---ELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQ 385
Cdd:TIGR04523 374 KLKKENQSYKQEIKNLESQINDLESKIQNQEKlnqQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 386 EKSIKENNSFDHflLKSGGDCTLIQQYIECQSVRQLKEAVDSSINKLSNFDEVIDAHLQNNQTTVDN--SLPSPDRLKEN 463
Cdd:TIGR04523 454 LIIKNLDNTRES--LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKisSLKEKIEKLES 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 464 QIDAKECDMSDTLSPSKEKSSDDTSDGQmeEQELNEPQNRVSLLKEMDRSLEAGDTEqviphIHRELQE-AQELANTGKQ 542
Cdd:TIGR04523 532 EKKEKESKISDLEDELNKDDFELKKENL--EKEIDEKNKEIEELKQTQKSLKKKQEE-----KQELIDQkEKEKKDLIKE 604
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528494936 543 --KCLELQAMLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQRENTITTTREELYSAQEEI 608
Cdd:TIGR04523 605 ieEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESK 672
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
310-387 |
7.50e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 7.50e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528494936 310 AVNEIKDLTEKIKLAEDKHEELtqkgLNEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEK 387
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAA----QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
233-391 |
8.12e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 233 EDGIRKELVALTEDKHNYETTAKESLRRVLQEKI----EVVRKLSEVER------SLSNTEDECTHLREMNERTQEELRE 302
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEELAELLKELEELGFesveELEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDK 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 303 LANKYNGAVNEIKDLTEKIKLAEDKHEELTQKGLNEKK-ELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRL 381
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYlELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAK 710
|
170
....*....|..
gi 528494936 382 EQLQ--EKSIKE 391
Cdd:PRK03918 711 KELEklEKALER 722
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
662-827 |
8.14e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 8.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 662 QLQSQHQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKL 741
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 742 GSIQDQhqqdASKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLKLLQDKGSNPSIL 821
Cdd:COG4372 104 ESLQEE----AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179
|
....*.
gi 528494936 822 QPVQAI 827
Cdd:COG4372 180 EAEQAL 185
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
525-794 |
8.62e-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: 39.72 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 525 HIHRELQEAQelantgkQKCLELQAMLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEAL----------REQRENTI 594
Cdd:pfam15921 75 HIERVLEEYS-------HQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMadirrresqsQEDLRNQL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 595 TTTREELYSAQ-----------EEILVLRHAM-----------------EAATAEREREI------------TALQGDLS 634
Cdd:pfam15921 148 QNTVHELEAAKclkedmledsnTQIEQLRKMMlshegvlqeirsilvdfEEASGKKIYEHdsmstmhfrslgSAISKILR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 635 IVTAELDKWRQTAAKYEVEISNLQASFQ-----LQSQHQERASQLQGEVEklqADCSGLQNECDSLRAEKSTLMQKLNRL 709
Cdd:pfam15921 228 ELDTEISYLKGRIFPVEDQLEALKSESQnkielLLQQHQDRIEQLISEHE---VEITGLTEKASSARSQANSIQSQLEII 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 710 EEEldsSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESRTRDLQKEY-----------DDTQS 778
Cdd:pfam15921 305 QEQ---ARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERdqfsqesgnldDQLQK 381
|
330
....*....|....*.
gi 528494936 779 LLSDLRQRYEQTEQEK 794
Cdd:pfam15921 382 LLADLHKREKELSLEK 397
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
501-722 |
9.92e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 39.65 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 501 QNRVSLLKEMDRSLE-AGDTEQVI---PHIHRELQeaQELANTG---------------KQKCLELQA-MLEEERKTnrQ 560
Cdd:PRK10929 51 QSALNWLEERKGSLErAKQYQQVIdnfPKLSAELR--QQLNNERdeprsvppnmstdalEQEILQVSSqLLEKSRQA--Q 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 561 QTEESAKQIRFLQTQLAKLQTdmEALR-----EQRENTITTTREELYSAQeeiLVLRHAMEAATAER--EREITALQG-- 631
Cdd:PRK10929 127 QEQDRAREISDSLSQLPQQQT--EARRqlneiERRLQTLGTPNTPLAQAQ---LTALQAESAALKALvdELELAQLSAnn 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494936 632 --DLSIVTAELDKWRqtAAKYEVEISNLQAsfQLQSQHQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRL 709
Cdd:PRK10929 202 rqELARLRSELAKKR--SQQLDAYLQALRN--QLNSQRQREAERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQ 277
|
250
....*....|....*
gi 528494936 710 EEELD--SSRERSAT 722
Cdd:PRK10929 278 AQRMDliASQQRQAA 292
|
|
| |
