|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
3-132 |
2.10e-79 |
|
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: 252.57 E-value: 2.10e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 3 SALAIFTCRPNSHPFQERHVYLDEPVKIGRSVARCRPAQNNATFDCKVLSRNHALIWFDHktGKFYLQDTKSSNGTFINS 82
Cdd:cd22679 1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1952581426 83 QRLSRGSEESPPCELLSGDIIQFGVDVTENTRkgKVTHGCIVSTVKLFMP 132
Cdd:cd22679 79 QRLSKGSEESEPRELHSGDIVQFGVDVVENSR--KVTHGCIVATVTLFLP 126
|
|
| CC1_SLMAP |
cd21911 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal ... |
165-227 |
9.38e-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: 103.53 E-value: 9.38e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952581426 165 QELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQ 227
Cdd:cd21911 1 QELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQLS 63
|
|
| FHA_DMA-like |
cd22692 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest ... |
27-108 |
1.46e-18 |
|
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: 83.00 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 27 PVKIGRSVARCRPAQNNAT-FDCKVLSRNHALIWfdHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCELLSGDIIQF 105
Cdd:cd22692 38 QIHIGRYTERVRQAIYHPVvFKSKVVSRTHGCIK--VDEGNWYIKDVKSSSGTFLNHQRLSPASRTSKPYPLRDGDILQL 115
|
...
gi 1952581426 106 GVD 108
Cdd:cd22692 116 GMD 118
|
|
| FHA_VPS64-like |
cd22695 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ... |
6-128 |
7.03e-16 |
|
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: 75.03 E-value: 7.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 6 AIFTCRPNSHPFQERHV---YLDEPVKIGRSVARCRPAQN---------------NATFDCKVLSRNHALIWFDHKTGKF 67
Cdd:cd22695 2 HILVLKSLNATFETKFLvvpFKPDGLKLGRPVTNSVNKNNsgskrdlfsqqvrpdNGNFDSRVLSRNHACLSCDPTTGKV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952581426 68 YLQDTKSSNGTFINSQRLSRGSeesppCELLSGDIIQFGVDVTEntrkgKVTHGCIVSTVK 128
Cdd:cd22695 82 YIRDLKSSNGTFVNGQKIRQND-----VELKVGDEVDLGTDIDS-----KIEHRKISAYVE 132
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
13-106 |
5.31e-15 |
|
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: 71.15 E-value: 5.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 13 NSHPFQERHVYLDEPVKIGRSvarcrpAQNNATFDCKVLSRNHALIWFDHktGKFYLQDTKSSNGTFINSQRLsrgseeS 92
Cdd:cd00060 6 DGDGGGREFPLTKGVVTIGRS------PDCDIVLDDPSVSRRHARIEVDG--GGVYLEDLGSTNGTFVNGKRI------T 71
|
90
....*....|....
gi 1952581426 93 PPCELLSGDIIQFG 106
Cdd:cd00060 72 PPVPLQDGDVIRLG 85
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
28-105 |
7.94e-15 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 69.91 E-value: 7.94e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581426 28 VKIGRSvarcrpAQNNATFDCKVLSRNHALIWFDhKTGKFYLQDTKSSNGTFINSQRLSRgseesPPCELLSGDIIQF 105
Cdd:pfam00498 1 VTIGRS------PDCDIVLDDPSVSRRHAEIRYD-GGGRFYLEDLGSTNGTFVNGQRLGP-----EPVRLKDGDVIRL 66
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
165-860 |
4.11e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.02 E-value: 4.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 165 QELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGirKELVT 244
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL--EELEA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 245 LQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKY-NGAVNELKEFTEKL 323
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEEL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 324 KQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQAdndftneRLTALQVRLEQLQ-----EKNIKDHNSIG 398
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA-------RLDSLERLQENLEgfsegVKALLKNQSGL 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 399 IQVDDLLpkingstdkehfllksggdcselfQQFIECKNKLKAPVEPTQNNRISNVEDmfeshlENNQTTEED---LKNd 475
Cdd:TIGR02168 519 SGILGVL------------------------SELISVDEGYEAAIEAALGGRLQAVVV------ENLNAAKKAiafLKQ- 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 476 SERFKATLIAEDD--HTKVTEETKLLKENQ---------LEAKESDMSDTLSPSKDRS--SEDTTDYQMDEQELNESLNK 542
Cdd:TIGR02168 568 NELGRVTFLPLDSikGTEIQGNDREILKNIegflgvakdLVKFDPKLRKALSYLLGGVlvVDDLDNALELAKKLRPGYRI 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 543 VSLLKDELQCAHVQTGDSEREKQ---ELQQELKEAQelaisskQKCFEMQALLEEerktAKKQVEESTRQIQALQAHLHK 619
Cdd:TIGR02168 648 VTLDGDLVRPGGVITGGSAKTNSsilERRREIEELE-------EKIEELEEKIAE----LEKALAELRKELEELEEELEQ 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 620 LQKDIEilreDKEIEIIETRDQLASTHKEIvalrQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIfnlq 699
Cdd:TIGR02168 717 LRKELE----ELSRQISALRKDLARLEAEV----EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI---- 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 700 tklqLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVS 779
Cdd:TIGR02168 785 ----EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 780 RKALEVEVGTLKEQR---LQETNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKL 856
Cdd:TIGR02168 861 IEELEELIEELESELealLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
....
gi 1952581426 857 LQQK 860
Cdd:TIGR02168 941 LQER 944
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
205-847 |
1.01e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.48 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 205 SWQALIDE-DRLLSRLEVMGNQLQAYSKNQTE-----DGIRKELVTLQEDKHSYETT---AKESLRRVLQEKIEVVRKLS 275
Cdd:TIGR02168 233 RLEELREElEELQEELKEAEEELEELTAELQEleeklEELRLEVSELEEEIEELQKElyaLANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 276 EVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQH---RIDEME 352
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETlrsKVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 353 EKEQLLQARIEALQAdndftneRLTALQVRLEQLQEKNIKDHNSIGIQVDDLLPKINGSTDKEHFLLKSGGD-----CSE 427
Cdd:TIGR02168 393 LQIASLNNEIERLEA-------RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELErleeaLEE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 428 LFQQFIECKNKLKAPVEPTQ--NNRISNVEDMFESHLENNQTTEEDLKN------------------------------- 474
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAqlQARLDSLERLQENLEGFSEGVKALLKNqsglsgilgvlselisvdegyeaaieaalgg 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 475 ---------------------DSERFKATLIAEDD--HTKVTEETKLLKENQ---------LEAKESDMSDTLSPSKDRS 522
Cdd:TIGR02168 546 rlqavvvenlnaakkaiaflkQNELGRVTFLPLDSikGTEIQGNDREILKNIegflgvakdLVKFDPKLRKALSYLLGGV 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 523 --SEDTTDYQMDEQELNESLNKVSLLKDELQCAHVQTGDSE----------REKQELQQELKEAQELAISSKQKCFEM-- 588
Cdd:TIGR02168 626 lvVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAktnssilerrREIEELEEKIEELEEKIAELEKALAELrk 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 589 -QALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILRE---DKEIEIIETRDQLASTHKEIVALRQTAVEAATGRE 664
Cdd:TIGR02168 706 eLEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEEriaQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 665 SdiaiLQGELHKVQTELEQWRQTASEYESEIFNlqtklqlqtqqqkdkQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQE 744
Cdd:TIGR02168 786 E----LEAQIEQLKEELKALREALDELRAELTL---------------LNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 745 KVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVklahAENETQKFQKQYEADQT 824
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE----LESKRSELRRELEELRE 922
|
730 740
....*....|....*....|...
gi 1952581426 825 MYLELKEKLDKTQKENESITDEL 847
Cdd:TIGR02168 923 KLAQLELRLEGLEVRIDNLQERL 945
|
|
| CC1_SLMAP-like |
cd21868 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ... |
169-206 |
1.81e-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: 65.20 E-value: 1.81e-13
10 20 30
....*....|....*....|....*....|....*...
gi 1952581426 169 QLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSW 206
Cdd:cd21868 1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
14-106 |
6.16e-13 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 65.36 E-value: 6.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 14 SHPFQERHVYLDE-PVKIGRSvarcrpAQNNATFDCKVLSRNHALIWFDHktGKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716 8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
|
90
....*....|....
gi 1952581426 93 pPCELLSGDIIQFG 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 |
1.32e-12 |
|
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: 65.38 E-value: 1.32e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1952581426 52 SRNHALIWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCELLSGDIIQFG 106
Cdd:cd22686 48 SKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPYPLTHGDELKIG 102
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
184-855 |
9.75e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 69.33 E-value: 9.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 184 LEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAysknqTEDGIRKELVTLQEDKHSYETTAKESLrrv 263
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA-----EIEELEREIEEERKRRDKLTEEYAELK--- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 264 lQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKAL---SE 340
Cdd:TIGR02169 364 -EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINeleEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 341 KKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKdhnsIGIQVDDLLPKINGSTDKEHFLLK 420
Cdd:TIGR02169 443 KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE----AEAQARASEERVRGGRAVEEVLKA 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 421 SGGDCSELFQQFIECKNKLKAPVEPTQNNRISN--VED--------------------------MFESHLENNQTTEE-- 470
Cdd:TIGR02169 519 SIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNvvVEDdavakeaiellkrrkagratflplnkMRDERRDLSILSEDgv 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 471 -----DLKNDSERFKA--------TLIAEDDHTK---------VTEETKLLKENQL-------EAKESDMSDTLSPSKDR 521
Cdd:TIGR02169 599 igfavDLVEFDPKYEPafkyvfgdTLVVEDIEAArrlmgkyrmVTLEGELFEKSGAmtggsraPRGGILFSRSEPAELQR 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 522 SSEDTTDYQMDE----QELNESLNKVSLLKDELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKcfemQALLEEERK 597
Cdd:TIGR02169 679 LRERLEGLKRELsslqSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED----LSSLEQEIE 754
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 598 TAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASTHKEIVA---LRQTAVEAATGRES-DIAILQGE 673
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSrieARLREIEQKLNRLTlEKEYLEKE 834
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 674 LHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQqqkdkqkgEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQ 753
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE--------ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 754 WFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETN--GLRVKLAHAENETQKFQ-------KQYEADQT 824
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSleDVQAELQRVEEEIRALEpvnmlaiQEYEEVLK 986
|
730 740 750
....*....|....*....|....*....|.
gi 1952581426 825 MYLELKEKLDKTQKENESITDELENCkENLK 855
Cdd:TIGR02169 987 RLDELKEKRAKLEEERKAILERIEEY-EKKK 1016
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
534-825 |
5.29e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 534 QELNESLN--KVSLLKDELQCAHVQTGDSEREKQELQQELKEAQElaisskqkcfeMQALLEEERKTAKKQVEESTRQIQ 611
Cdd:COG1196 216 RELKEELKelEAELLLLKLRELEAELEELEAELEELEAELEELEA-----------ELAELEAELEELRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 612 ALQAHLHKLQKDIEILREDKE------IEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWR 685
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIArleerrRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 686 QTASEYESEIfNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQ 765
Cdd:COG1196 365 EALLEAEAEL-AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 766 SVKLTKDASGLEVSRKALEVEVgtlkEQRLQETNGLRVKLAHAENETQKFQKQYEADQTM 825
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELL----AELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
159-389 |
1.71e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.09 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 159 SPSMYSQELFQLSQY--LQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEd 236
Cdd:TIGR02169 659 SRAPRGGILFSRSEPaeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE- 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 237 girkelvtLQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQ-EELRELANKYNGAVNE 315
Cdd:TIGR02169 738 --------RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSR 809
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952581426 316 LKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEK 389
Cdd:TIGR02169 810 IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
331-862 |
2.93e-10 |
|
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: 63.97 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 331 EEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQaDNDFTNERLTalqVRLEQLQEKN---IKDHNSIGIQVDDLLPK 407
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQ-ELQFENEKVS---LKLEEEIQENkdlIKENNATRHLCNLLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 408 INGSTDKEHfllKSGGDCSELFQQFIECKNKLKAPVEPTQNNRISNVEDMFESHL------ENNQTTEEDLK---NDSER 478
Cdd:pfam05483 164 CARSAEKTK---KYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFklkedhEKIQHLEEEYKkeiNDKEK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 479 FKATLIAE--DDHTKVTEETKLLKE-----NQLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDELQ 551
Cdd:pfam05483 241 QVSLLLIQitEKENKMKDLTFLLEEsrdkaNQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQ 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 552 CAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIE---ILR 628
Cdd:pfam05483 321 IATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEemtKFK 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 629 EDKEIEIIETRDQLASTHKEIVALRQTA--VEAATGRESDIAIL----QGELHKVQTELEQWRQTASEYESEIfnlqtkl 702
Cdd:pfam05483 401 NNKEVELEELKKILAEDEKLLDEKKQFEkiAEELKGKEQELIFLlqarEKEIHDLEIQLTAIKTSEEHYLKEV------- 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 703 qlqtqqqkDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKA 782
Cdd:pfam05483 474 --------EDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 783 LEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQKGN 862
Cdd:pfam05483 546 LRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGS 625
|
|
| CC1_T3JAM |
cd21912 |
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ... |
166-206 |
1.08e-09 |
|
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: 54.66 E-value: 1.08e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1952581426 166 ELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSW 206
Cdd:cd21912 5 EILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
|
|
| FHA_TCF19 |
cd22685 |
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ... |
28-121 |
1.23e-09 |
|
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: 57.04 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 28 VKIGRSVARCRPAQNNATFDcKVLSRNHALIW---FDHKTGKFYLQDTkSSNGTFINSQRLSRGSEEsppcELLSGDIIQ 104
Cdd:cd22685 30 YRIGRNPEVCDVFLCSSQHP-NLISREHAEIHaerDGNGNWKVLIEDR-STNGTYVNDVRLQDGQRR----ELSDGDTIT 103
|
90
....*....|....*..
gi 1952581426 105 FGVDVTENTRKGKVTHG 121
Cdd:cd22685 104 FGHKNGRRVKQWPYQKS 120
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
592-859 |
1.24e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 592 LEEERKTAKK----QVEESTRQIQALQAHLHKLQKDIEILRED---KEIEIIETRDQLASTHKEIVALRQTAVEAatgrE 664
Cdd:COG1196 205 LERQAEKAERyrelKEELKELEAELLLLKLRELEAELEELEAEleeLEAELEELEAELAELEAELEELRLELEEL----E 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 665 SDIAILQGELHKVQTELEQWRQTASEYESEIfnlqtklqlqtqqqkDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQE 744
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERR---------------RELEERLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 745 KVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYEADQT 824
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270
....*....|....*....|....*....|....*
gi 1952581426 825 MYLELKEKLDKTQKENESITDELENCKENLKLLQQ 859
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
28-85 |
3.91e-09 |
|
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.
Pssm-ID: 214578 [Multi-domain] Cd Length: 52 Bit Score: 52.95 E-value: 3.91e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581426 28 VKIGRSvarcrPAQNNATFDCKVLSRNHALIWFDhKTGKFYLQDTKSSNGTFINSQRL 85
Cdd:smart00240 1 VTIGRS-----SEDCDIQLDGPSISRRHAVIVYD-GGGRFYLIDLGSTNGTFVNGKRI 52
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
27-106 |
5.42e-09 |
|
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: 54.55 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 27 PVKIGRSVARcRPAQNNATFDC-----KVLSRNHALIWFDHKTGKFYLQdTKSSNGTFINSQRLSRGseeSPPCELLSGD 101
Cdd:cd22701 18 EVVLGRNSKN-SSSTAADSVDIdlgpsKKISRRHARIFYDFTTQCFELS-VLGRNGVKVDGILVKPG---SPPVPLRSGS 92
|
....*
gi 1952581426 102 IIQFG 106
Cdd:cd22701 93 LIQIG 97
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
296-849 |
7.64e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 7.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 296 DRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALsekkELQHRIDEMEEKEQLLQARIEALQADNDFTNER 375
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE----ELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 376 LTALQVRLEQLQEKNIKDHNSIGIQVDDLLpkingstdkehfllksggdcsELFQQFIECKNKLKAPVEpTQNNRISNVE 455
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELE---------------------ELEEELEEAEEELEEAEA-ELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 456 DMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEETKLLKENQLEAKESDMSDTLSPSKDRSSEDTTdyQMDEQE 535
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE--EEALEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 536 LNESLNKVSLLKDELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEES-----TRQI 610
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAglrglAGAV 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 611 QALQAHLHKLQKDIEILREDKEIEIIETRDQLASthKEIVALRQTAVEAAT---------GRESDIAILQGELHKVQTEL 681
Cdd:COG1196 527 AVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA--AAIEYLKAAKAGRATflpldkiraRAALAAALARGAIGAAVDLV 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 682 EQWRQTASEYESEIFNL---QTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEE 758
Cdd:COG1196 605 ASDLREADARYYVLGDTllgRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 759 LRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYEADQTM---YLELKEKLDK 835
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEaleELPEPPDLEE 764
|
570
....*....|....
gi 1952581426 836 TQKENESITDELEN 849
Cdd:COG1196 765 LERELERLEREIEA 778
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
535-848 |
1.12e-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: 59.31 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 535 ELNESLNKVSLLKDELQcAHVQTGDSEREKQELQQELK-EAQELAisskqkcfemQALLEEERKTAKKQVEESTRQIQAL 613
Cdd:TIGR02169 181 EVEENIERLDLIIDEKR-QQLERLRREREKAERYQALLkEKREYE----------GYELLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 614 QAHLHKLQKDIEilreDKEIEIIETRDQLASTHKEIVALRqtaveaatgrESDIAILQGELHKVQTELEQWRQTASEYES 693
Cdd:TIGR02169 250 EEELEKLTEEIS----ELEKRLEEIEQLLEELNKKIKDLG----------EEEQLRVKEKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 694 EIfNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDA 773
Cdd:TIGR02169 316 EL-EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 774 SGLEVSRKALEVEVGTLKEQRLQ------------------------ETNGLRVKLAHAENETQKFQKQYEADQTMYLEL 829
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRlseeladlnaaiagieakineleeEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
330
....*....|....*....
gi 1952581426 830 KEKLDKTQKENESITDELE 848
Cdd:TIGR02169 475 KEEYDRVEKELSKLQRELA 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
565-860 |
2.20e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 565 QELQQELKEAQeLAISSKQKCFemqalLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEilredkeieiiETRDQLAS 644
Cdd:TIGR02168 216 KELKAELRELE-LALLVLRLEE-----LREELEELQEELKEAEEELEELTAELQELEEKLE-----------ELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 645 THKEIVALrQTAVEAATgreSDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQqqkdkqkgEAVQLQGKL 724
Cdd:TIGR02168 279 LEEEIEEL-QKELYALA---NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE--------ELAELEEKL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 725 DELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLK---EQRLQETNGL 801
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEdrrERLQQEIEEL 426
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581426 802 RVKLahAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQK 860
Cdd:TIGR02168 427 LKKL--EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
14-110 |
2.43e-08 |
|
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: 52.62 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 14 SHPFQERHV---YLDEPVKIGRSvARCRPAQNNATfdckvLSRNHALIW---FDHKTG-KFYLQDTkSSNGTFINSQRLS 86
Cdd:cd22670 7 SSPGSTDIVlpiYKNQVITIGRS-PSCDIVINDPF-----VSRTHCRIYsvqFDESSApLVYVEDL-SSNGTYLNGKLIG 79
|
90 100
....*....|....*....|....*
gi 1952581426 87 RGseespPCELLS-GDIIQFGVDVT 110
Cdd:cd22670 80 RN-----NTVLLSdGDVIEIAHSAT 99
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
163-389 |
4.09e-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: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 163 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGIRKEL 242
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 243 VTLQEDKHSyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEK 322
Cdd:COG1196 298 ARLEQDIAR----LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 323 LKQAEGKQEEIQQK---ALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEK 389
Cdd:COG1196 374 LAEAEEELEELAEElleALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
273-859 |
1.11e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.80 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 273 KLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKAlsekKELQHRIDEME 352
Cdd:TIGR04523 97 KINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKY----NDLKKQKEELE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 353 EKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNiKDHNSIGIQVDDLLPKINGSTDKehfLLKSGGDCSELFQQF 432
Cdd:TIGR04523 173 NELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKI-QKNKSLESQISELKKQNNQLKDN---IEKKQQEINEKTTEI 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 433 IECKNKLKAPVEptQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKATlIAEDDHTKVTEETKLLKEnQLEAKESDMS 512
Cdd:TIGR04523 249 SNTQTQLNQLKD--EQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSE-ISDLNNQKEQDWNKELKS-ELKNQEKKLE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 513 DTlspskdrssedttdyqmdEQELNESLNKVSLLKDELQCAHVQTGDSEREKQELQQELKEAQELAISSK----QKCFEM 588
Cdd:TIGR04523 325 EI------------------QNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKkenqSYKQEI 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 589 QAL------LEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREdkeiEIIETRDQLASTHKEIVALRQTAVEAATG 662
Cdd:TIGR04523 387 KNLesqindLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKE----TIIKNNSEIKDLTNQDSVKELIIKNLDNT 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 663 RES---DIAILQGELHKVQTELEQWRQTASEYESEIFNLQTklqlqtqqqkdkqkgEAVQLQGKLDELQKQSNGLKNDCD 739
Cdd:TIGR04523 463 RESletQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE---------------EKKELEEKVKDLTKKISSLKEKIE 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 740 SLRQEKVLLTEKLQWFEEELrcaqqQSVKLTKDASGLEVSRKALEVEVGTLKEQR---LQETNGLRVKLAHAENETQKFQ 816
Cdd:TIGR04523 528 KLESEKKEKESKISDLEDEL-----NKDDFELKKENLEKEIDEKNKEIEELKQTQkslKKKQEEKQELIDQKEKEKKDLI 602
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1952581426 817 KQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQ 859
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQ 645
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
55-108 |
1.26e-07 |
|
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: 50.40 E-value: 1.26e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1952581426 55 HALIWFDHKTGKFYLQDTKSSNGTFINSQRLSrgseESPPCELLSGDIIQFGVD 108
Cdd:cd22704 39 HAVITYDQIDNEFKIKDLGSLNGTFVNDSRIP----EQTYITLKLGDSIRFGYD 88
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
25-114 |
1.49e-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: 50.43 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 25 DEPVKIGRSVArcrpAQNNATFDC-KVLSRNHALIWFDhKTGKFYLQDTKSSNGTFINSQRLsrgsEESPPCELLSGDII 103
Cdd:cd22663 20 GKEVTVGRGLG----VTYQLVSTCpLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERI----EPLKPYPLNEGDLI 90
|
90
....*....|.
gi 1952581426 104 QFGVDVTENTR 114
Cdd:cd22663 91 QLGVPPENKEP 101
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
277-833 |
1.54e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 277 VERSLSNTEDECTHLKEMNDRTQEelRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQK------ALSEKKELQHRIDE 350
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEE--KDLHERLNGLESELAELDEEIERYEEQREQARETrdeadeVLEEHEERREELET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 351 MEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNikdhnsigiqvDDLLPKIN-GSTDKEHFLLKS---GGDCS 426
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEER-----------DDLLAEAGlDDADAEAVEARReelEDRDE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 427 ELFQQFIECKNKLKAPVEPTQNNR--ISNVEDMFESHLENNQTTEEDLKNDSE---RFKATLIAEDDHTKVTEETKLLKE 501
Cdd:PRK02224 325 ELRDRLEECRVAAQAHNEEAESLRedADDLEERAEELREEAAELESELEEAREaveDRREEIEELEEEIEELRERFGDAP 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 502 NQLEAKEsDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDELQC----------AHVQTGDSEREK-QELQQE 570
Cdd:PRK02224 405 VDLGNAE-DFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCpecgqpvegsPHVETIEEDRERvEELEAE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 571 LKEAQElaisskqkcfEMQALleEERKTAKKQVEESTRQIQALQAHLhklqKDIEILREDKEIEIIETRDQLASTHKEIV 650
Cdd:PRK02224 484 LEDLEE----------EVEEV--EERLERAEDLVEAEDRIERLEERR----EDLEELIAERRETIEEKRERAEELRERAA 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 651 ALRQTAVE----AATGRE------SDIAILQGELHKVQTELEQWRqTASEYESEIFNLQTklqlqtqqqkdkqkgEAVQL 720
Cdd:PRK02224 548 ELEAEAEEkreaAAEAEEeaeearEEVAELNSKLAELKERIESLE-RIRTLLAAIADAED---------------EIERL 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 721 QGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFE-EELRCAQQQSVKLTKDASG----LEVSRKALEVEVGTLkEQRL 795
Cdd:PRK02224 612 REKREALAELNDERRERLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEkldeLREERDDLQAEIGAV-ENEL 690
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1952581426 796 QETNGLRVKLAHAENETQKFQKQY---EADQTMYLELKEKL 833
Cdd:PRK02224 691 EELEELRERREALENRVEALEALYdeaEELESMYGDLRAEL 731
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
184-834 |
1.70e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.12 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 184 LEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGIRKELVTLQEDKHSYETTakeslrrv 263
Cdd:pfam15921 243 VEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSM-------- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 264 lqekieVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKE 343
Cdd:pfam15921 315 ------YMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 344 LQHRIDEMEEKEQLLQAR-------IEALQADNDFTNERLTALQVRLEQLQEKnikdhnsIGIQVDDLLPKINGSTDkeh 416
Cdd:pfam15921 389 REKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSE-------CQGQMERQMAAIQGKNE--- 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 417 fllkSGGDCSELFQQFIECKNKLKAPVEPTQNNRISnvedmfeshLENNQTTEEDLKND-SERFKATLIAEDDHTKVTEE 495
Cdd:pfam15921 459 ----SLEKVSSLTAQLESTKEMLRKVVEELTAKKMT---------LESSERTVSDLTASlQEKERAIEATNAEITKLRSR 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 496 TKL-LKENQLEAKESDMSDTLSPSKD----RSSEDTTDYQMDEQELNESLNKVSLLKDELQCAHVQTGDSEREKQELQQE 570
Cdd:pfam15921 526 VDLkLQELQHLKNEGDHLRNVQTECEalklQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLE 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 571 LKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALqahlhklqKDIEILREDKEIEIIETRDQLASTHKEIV 650
Cdd:pfam15921 606 LQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAV--------KDIKQERDQLLNEVKTSRNELNSLSEDYE 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 651 ALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESeifnlqtklqlqtqqqkdkQKGEAVQLQGKldeLQKQ 730
Cdd:pfam15921 678 VLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEG-------------------SDGHAMKVAMG---MQKQ 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 731 SNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGL--EVSRKALEVEVGTLKEQRLQE-TNGLRVKLAH 807
Cdd:pfam15921 736 ITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVatEKNKMAGELEVLRSQERRLKEkVANMEVALDK 815
|
650 660
....*....|....*....|....*....
gi 1952581426 808 AENETQKFQK--QYEADQTMYLELKEKLD 834
Cdd:pfam15921 816 ASLQFAECQDiiQRQEQESVRLKLQHTLD 844
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
30-106 |
3.90e-07 |
|
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: 48.95 E-value: 3.90e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581426 30 IGRSVArcrpaqNNATFDCKVLSRNHALIwfDHKTGKFYLQDTKSSNGTFINSQRLSRGseesppcELLSGDIIQFG 106
Cdd:cd22698 25 IGRSSN------NDIRLNDHSVSRHHARI--VRQGDKCNLTDLGSTNGTFLNGIRVGTH-------ELKHGDRIQLG 86
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
256-843 |
5.07e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 5.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 256 AKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQ 335
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 336 kalsEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKDHNSIGIQVDDLlpkingstdke 415
Cdd:COG1196 317 ----RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL----------- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 416 hfllksggdcSELFQQFIECKNKLKApveptQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKvTEE 495
Cdd:COG1196 382 ----------EELAEELLEALRAAAE-----LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE-ALE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 496 TKLLKENQLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDELQCAHVQTGDSEREKQELQQELKEAQ 575
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 576 ELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKeieiIETRDQLASTHKEIVALRQT 655
Cdd:COG1196 526 VAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDK----IRARAALAAALARGAIGAAV 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 656 AVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEifnlqtklqlQTQQQKDKQKGEAVQLQGKLDELQKQSNGLK 735
Cdd:COG1196 602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV----------TLAGRLREVTLEGEGGSAGGSLTGGSRRELL 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 736 NDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQKF 815
Cdd:COG1196 672 AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
570 580
....*....|....*....|....*...
gi 1952581426 816 QKQYEADQTMYLELKEKLDKTQKENESI 843
Cdd:COG1196 752 ALEELPEPPDLEELERELERLEREIEAL 779
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
27-106 |
2.04e-06 |
|
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: 46.97 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 27 PVKIGRSVarcrpaQNNATFDCKVLSRNHALIWFDHKTGKFYLQDTKSSNGTFINSQRLsrgSEESPPCELLSGDIIQFG 106
Cdd:cd22678 24 PLTIGRIQ------RGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESI---SPNGRPVVLSSGDVITLG 94
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
236-760 |
2.47e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 236 DGIRKELVTLQEDKHSYETTAKEsLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEmNDRTQEELRELANKYNgavnE 315
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKE-LESLEGSKRKLEEKIRELEERIEELKKEIEELEE-KVKELKELKEKAEEYI----K 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 316 LKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQL----------LQARIEALQADNDfTNERLTALQVRLEQ 385
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERleelkkklkeLEKRLEELEERHE-LYEEAKAKKEELER 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 386 LQ--------EKNIKDHNSIGIQVDDLLPKINGSTDKEHFLLKSGGdcsELFQQFIECKN-KLKAPV---EPTQNNRisn 453
Cdd:PRK03918 377 LKkrltgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIK---ELKKAIEELKKaKGKCPVcgrELTEEHR--- 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 454 VEDMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEETKLLKE----NQLEAKESDMSdtlSPSKDRSSEDTTDY 529
Cdd:PRK03918 451 KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLkelaEQLKELEEKLK---KYNLEELEKKAEEY 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 530 QMDEQELNESLNKVSLLKDELQcahvQTGDSEREKQELQQELKEAQElaisskqkcfEMQALLEEERKTAKKQVEESTRQ 609
Cdd:PRK03918 528 EKLKEKLIKLKGEIKSLKKELE----KLEELKKKLAELEKKLDELEE----------ELAELLKELEELGFESVEELEER 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 610 IQALQAHLHKLqkdIEILREDKEIEIIEtrdqlasthKEIVALRQTAVEAatgrESDIAILQGELHKVQTELEQWRQtas 689
Cdd:PRK03918 594 LKELEPFYNEY---LELKDAEKELEREE---------KELKKLEEELDKA----FEELAETEKRLEELRKELEELEK--- 654
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952581426 690 EYESEIFNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQ--EKVLLTEKLQWFEEELR 760
Cdd:PRK03918 655 KYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKakKELEKLEKALERVEELR 727
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
559-782 |
2.55e-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: 50.53 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 559 DSEREKQELQQELKEAQELAISSKQKcfemQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREdkeiEIIET 638
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK----EIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 639 RDQLASTHKEIValRQTAVEAATGRESDIAIL--QGELHKVQTELeQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKGE 716
Cdd:COG4942 96 RAELEAQKEELA--ELLRALYRLGRQPPLALLlsPEDFLDAVRRL-QYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952581426 717 AVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKA 782
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
51-106 |
3.04e-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: 46.78 E-value: 3.04e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952581426 51 LSRNHALIWF----DHKTGKFYLQDTKSSNGTFINSQRLsrgseesPP---CELLSGDIIQFG 106
Cdd:cd22677 41 ISRYHAVLQYrgdaDDHDGGFYLYDLGSTHGTFLNKQRI-------PPkqyYRLRVGHVLKFG 96
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
227-867 |
5.01e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 5.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 227 QAYSKNQTEDGIRKELVTLQEDKHSYETTAK-ESLRRV--LQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELR 303
Cdd:PTZ00121 1195 KAEDARKAEAARKAEEERKAEEARKAEDAKKaEAVKKAeeAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA 1274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 304 ELANKyngaVNELKEFTEKLKQAEGKQ-------EEIQQKALSEKK--ELQHRIDEMEEKEQLLQARIEALQADNDFTNE 374
Cdd:PTZ00121 1275 EEARK----ADELKKAEEKKKADEAKKaeekkkaDEAKKKAEEAKKadEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKA 1350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 375 RLTALQVRLEQLQEKNIKDH--NSIGIQVDDLLPKINGSTDKEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQNNRIS 452
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEkkKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK 1430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 453 NVEDMFESHLENNQTTEEDLKNDSERFKAtliaeDDHTKVTEETKLLKENQLEAKESDMSDTLSPSKDRSSEDTTDYQMD 532
Cdd:PTZ00121 1431 KKADEAKKKAEEAKKADEAKKKAEEAKKA-----EEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 533 EQELNESlnkvsllkDELQCAHVQTGDSEREKQELQQ---ELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQ 609
Cdd:PTZ00121 1506 AEAKKKA--------DEAKKAEEAKKADEAKKAEEAKkadEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKN 1577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 610 IQALQAhlhklqkdiEILREDKEIEIIETRDQLASTHKEIVALRQTAVEAATGREsdiailqgELHKVQTELEQWRQTAS 689
Cdd:PTZ00121 1578 MALRKA---------EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE--------ELKKAEEEKKKVEQLKK 1640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 690 EYESEIFNLQTKLQLQTQQQ--KDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLR---QEKVLLTEKLQWFEEELRCAQQ 764
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKikAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKkeaEEAKKAEELKKKEAEEKKKAEE 1720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 765 QSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESIT 844
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKI 1800
|
650 660
....*....|....*....|...
gi 1952581426 845 DELencKENLKLLQQKGNNGGLF 867
Cdd:PTZ00121 1801 KDI---FDNFANIIEGGKEGNLV 1820
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
471-812 |
5.04e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 471 DLKNDSERFKATLI------AEDDHTKVTEETKLLKE--NQLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNK 542
Cdd:COG1196 217 ELKEELKELEAELLllklreLEAELEELEAELEELEAelEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 543 VSLLKDELQCAHVQTGDSEREKQELQQELKEAQelaisskqkcfEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQK 622
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELE-----------EELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 623 DIEILREdKEIEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIfNLQTKL 702
Cdd:COG1196 366 ALLEAEA-ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE-EEEEEA 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 703 QLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQ--QSVKLTKDASGLEVSR 780
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGflEGVKAALLLAGLRGLA 523
|
330 340 350
....*....|....*....|....*....|..
gi 1952581426 781 KALEVEVGTLKEQRLQETNGLRVKLAHAENET 812
Cdd:COG1196 524 GAVAVLIGVEAAYEAALEAALAAALQNIVVED 555
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
603-863 |
6.61e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 6.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 603 VEESTRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASTHKEIVALRQTAVEAatgrESDIAILQGELHKVQTELE 682
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEA----EEELEELTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 683 QWRQTASEYESEIfnlqtklqlqtqqqkdkqkgeaVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCA 762
Cdd:TIGR02168 271 ELRLEVSELEEEI----------------------EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 763 QQQSVKLTKDAsglevsrKALEVEVGTLKEQRlqetNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENES 842
Cdd:TIGR02168 329 ESKLDELAEEL-------AELEEKLEELKEEL----ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
250 260
....*....|....*....|.
gi 1952581426 843 ITDELENCKENLKLLQQKGNN 863
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRER 418
|
|
| FHA_CHFR |
cd22672 |
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ... |
49-105 |
7.46e-06 |
|
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: 45.75 E-value: 7.46e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581426 49 KVLSRNHALIWFDHKtGKFYLQDTkSSNGTFINSQRLSRGSEesppCELLSGDIIQF 105
Cdd:cd22672 39 KLVSGDHCKIIRDEK-GQVWLEDT-STNGTLVNKVKVVKGQK----VELKHGDVIYL 89
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
52-106 |
7.60e-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: 45.72 E-value: 7.60e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1952581426 52 SRNHALIWFDHKTGKFYLQDTKSSNGTFINSQRLsrgsEESPPCELLSGDIIQFG 106
Cdd:cd22674 48 SRVHAALVYHKHLNRVFLIDLGSTHGTFVGGIRL----EPHKPQQLPIDSTLRFG 98
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
25-108 |
8.38e-06 |
|
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: 45.88 E-value: 8.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 25 DEPVKIGRsvarcRPAQNNAT----FDCKVLSRNHALIWFdhKTGKFYLQDTKSSNGTFINSQRLSR-GSEESPPCELLS 99
Cdd:cd22702 31 KQPCIIGS-----DPHQAISGisvvIPSPQVSELHARITC--KNGAFFLTDLGSEHGTWINDNEGRRyRAPPNFPVRLHP 103
|
....*....
gi 1952581426 100 GDIIQFGVD 108
Cdd:cd22702 104 SDVIEFGSD 112
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
241-632 |
1.41e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.74 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 241 ELVTLQEDKHSYE------------TTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRElanK 308
Cdd:pfam07888 5 ELVTLEEESHGEEggtdmllvvpraELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELES---R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 309 YNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQllqaRIEALQADNDFTNERLTALQVRLEQLQE 388
Cdd:pfam07888 82 VAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEA----RIRELEEDIKTLTQRVLERETELERMKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 389 KNIKDHNSIGIQVDDllpkingSTDKEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQnnrisnvedmfesHLENNQTT 468
Cdd:pfam07888 158 RAKKAGAQRKEEEAE-------RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVL-------------QLQDTITT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 469 EEDLKNDSERFKATLIAEDDHTKVTEETKLLKENQLEAKESDMSDTLSpSKDRSSEDTTDYQMDEQELNESLNKVSLLKD 548
Cdd:pfam07888 218 LTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAA-QRDRTQAELHQARLQAAQLTLQLADASLALR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 549 ELQC-------AHVQTGDSEREK-QELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKL 620
Cdd:pfam07888 297 EGRArwaqereTLQQSAEADKDRiEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVA 376
|
410
....*....|..
gi 1952581426 621 QKDIEILREDKE 632
Cdd:pfam07888 377 QKEKEQLQAEKQ 388
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
258-859 |
1.60e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.89 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 258 ESLRRVLQEKIEVVRK--LSEVERSLSNTEDECTHLKEMN--DRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEI 333
Cdd:TIGR01612 1058 DEIEKEIGKNIELLNKeiLEEAEINITNFNEIKEKLKHYNfdDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEI 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 334 QQKALSEKKELQHRIDEMEEkeqllqariealQADNDFTNERLTALQVRLEQLQEKnIKDHNSIGIQVDDLLPKINGSTD 413
Cdd:TIGR01612 1138 KKKSENYIDEIKAQINDLED------------VADKAISNDDPEEIEKKIENIVTK-IDKKKNIYDEIKKLLNEIAEIEK 1204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 414 KEHFL-------LKSGGDCSELFQQFIECKNKLKAPVEPTQNNRISNVEDMFES--HLENNQTTEEDLKNDSERFKATLI 484
Cdd:TIGR01612 1205 DKTSLeevkginLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKspEIENEMGIEMDIKAEMETFNISHD 1284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 485 AEDDHTKVTEE---------TKLLKENQLEAKESDMSDTlspsKDRSSEDTTDYQMDEQELNESLNKVSLLKDELQCAHV 555
Cdd:TIGR01612 1285 DDKDHHIISKKhdenisdirEKSLKIIEDFSEESDINDI----KKELQKNLLDAQKHNSDINLYLNEIANIYNILKLNKI 1360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 556 Q---------TGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHlhklqkdieI 626
Cdd:TIGR01612 1361 KkiidevkeyTKEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKIESTLDDKDIDECIKKIKELKNH---------I 1431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 627 LREDKEieiIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQ-----GELHKVQTELEQWRQTASEYESEI------ 695
Cdd:TIGR01612 1432 LSEESN---IDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKkdnatNDHDFNINELKEHIDKSKGCKDEAdknaka 1508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 696 --FNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKlqwFEEELRCAQQQSVKLTKDA 773
Cdd:TIGR01612 1509 ieKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEK---SEQKIKEIKKEKFRIEDDA 1585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 774 SGLEVSRKA---LEVEVGTLKEQRLQETNgLRVKLAHAENETQKFQKQ-----YEADQTMYLELKEKLDKTQKENESITD 845
Cdd:TIGR01612 1586 AKNDKSNKAaidIQLSLENFENKFLKISD-IKKKINDCLKETESIEKKissfsIDSQDTELKENGDNLNSLQEFLESLKD 1664
|
650
....*....|....
gi 1952581426 846 ELENCKENLKLLQQ 859
Cdd:TIGR01612 1665 QKKNIEDKKKELDE 1678
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
13-110 |
1.75e-05 |
|
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: 44.14 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 13 NSHPFQERHVYLDE-PVKIGRSvarcrpAQNNATFDCKVLSRNHALIWFDHKTgkFYLQDTKSSNGTFINSQRLSrgsee 91
Cdd:cd22665 7 SQAHGPEKDFPLYEgENVIGRD------PSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRL----- 73
|
90 100
....*....|....*....|.
gi 1952581426 92 SPPC--ELLSGDIIQFGvDVT 110
Cdd:cd22665 74 KPNVryELIDGDLLLFG-DVK 93
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
28-106 |
1.78e-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: 44.25 E-value: 1.78e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581426 28 VKIGRSVarcrpaQNNATFDCKVLSRNHALIWFDhkTGKFYLQDTKSSNGTFINSQRlsrgsEESPPCELLSGDIIQFG 106
Cdd:cd22680 23 VSIGRDP------ENVIVIPDPFVSRNHARITVD--SNEIYIEDLGSTNGTFVNDFK-----RIKGPAKLHPNDIIKLG 88
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
52-107 |
1.94e-05 |
|
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: 44.24 E-value: 1.94e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952581426 52 SRNHALIWFDHKTG---------KFYLQDTkSSNGTFINSQRLSRGSEesppCELLSGDIIQFGV 107
Cdd:cd22667 40 SRKHATLTVLHPEAnlsdpdtrpELTLKDL-SKYGTFVNGEKLKGGSE----VTLKDGDVITFGV 99
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
18-86 |
2.24e-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: 43.86 E-value: 2.24e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581426 18 QERHVYLDEPVKIGRSvarcrpAQNNATFDCKVLSRNHALIWFDhkTGKFYLQDTKSSNGTFINSQRLS 86
Cdd:cd22694 8 GELRFDPGSSVRIGRD------PDADVRLDDPRVSRRHALLEFD--GDGWVYTDLGSRNGTYLNGRRVQ 68
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
1-106 |
2.48e-05 |
|
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: 47.45 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 1 MPSALAIFTCRPNSHPFQERHVYLDEPVKIGRSvARC-----RPAQnnatfdckVLSRNHALIWFDHktGKFYLQDTkSS 75
Cdd:COG3456 1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRS-ADCdwvlpDPDR--------SVSRRHAEIRFRD--GAFCLTDL-ST 68
|
90 100 110
....*....|....*....|....*....|...
gi 1952581426 76 NGTFIN--SQRLSRGSEEsppcELLSGDIIQFG 106
Cdd:COG3456 69 NGTFLNgsDHPLGPGRPV----RLRDGDRLRIG 97
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
248-862 |
2.62e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 248 DKHSYETTAKESLRRVLQEKIEvvrklsEVERSLSNTEDectHLKEMNDRTqEELRELANKYNGAVNELKEFTEKLKQAE 327
Cdd:pfam15921 131 DIRRRESQSQEDLRNQLQNTVH------ELEAAKCLKED---MLEDSNTQI-EQLRKMMLSHEGVLQEIRSILVDFEEAS 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 328 GKQ-------------------EEIQQKALSEKKELQHRI----DEMEEKEQLLQARIE-ALQADNDFTNERLTALQVRL 383
Cdd:pfam15921 201 GKKiyehdsmstmhfrslgsaiSKILRELDTEISYLKGRIfpveDQLEALKSESQNKIElLLQQHQDRIEQLISEHEVEI 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 384 EQLQEKNI---KDHNSIGIQVDDLLPKI-NGSTDKEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQNNRISNVEDMFE 459
Cdd:pfam15921 281 TGLTEKASsarSQANSIQSQLEIIQEQArNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 460 SHLENNQTTEEDLKNDSERFKatLIAedDHTKVTEETKLLKENQLEAKESDMSDTLSPSKDRSSEDttDYQMDEQEL--- 536
Cdd:pfam15921 361 ARTERDQFSQESGNLDDQLQK--LLA--DLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELD--DRNMEVQRLeal 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 537 ----------------------NESLNKVSLLKDELQcahvqtgDSEREKQELQQELKEAQELAISSKQKCFEMQALLEE 594
Cdd:pfam15921 435 lkamksecqgqmerqmaaiqgkNESLEKVSSLTAQLE-------STKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 595 ERKTAKKQVEESTR-------QIQALQ------AHLHKLQKDIEILR-----EDKEIEI----IETRDQLASTHKEIVAL 652
Cdd:pfam15921 508 KERAIEATNAEITKlrsrvdlKLQELQhlknegDHLRNVQTECEALKlqmaeKDKVIEIlrqqIENMTQLVGQHGRTAGA 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 653 RQtaVEAATgresdiaiLQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKGEAVQLQGKLDeLQKQSN 732
Cdd:pfam15921 588 MQ--VEKAQ--------LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKD-IKQERD 656
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 733 GLKNDCDSLRQEKVLLTEKLQWFEEELRC-AQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENE 811
Cdd:pfam15921 657 QLLNEVKTSRNELNSLSEDYEVLKRNFRNkSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQI 736
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1952581426 812 TQKfQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQKGN 862
Cdd:pfam15921 737 TAK-RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKN 786
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
339-683 |
2.80e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 339 SEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQekniKDHNSIGIQVDDLLPKINGSTDKehfl 418
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS----RQISALRKDLARLEAEVEQLEER---- 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 419 lksggdcselfQQFIECKNKLKAPVEPTQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKATliaEDDHTKVTEETKL 498
Cdd:TIGR02168 749 -----------IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL---REALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 499 LKENQLEAKEsdmsdtlspskdRSSEDTTDYQMDEQELNESLNKVSLLKDELQCAHVQTGDSEREKQELQQELKEAQELa 578
Cdd:TIGR02168 815 LNEEAANLRE------------RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE- 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 579 issKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDK---EIEIIETRDQLASTHKeivALRQT 655
Cdd:TIGR02168 882 ---RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLeglEVRIDNLQERLSEEYS---LTLEE 955
|
330 340
....*....|....*....|....*...
gi 1952581426 656 AVEAATGRESDIAILQGELHKVQTELEQ 683
Cdd:TIGR02168 956 AEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| FHA_RAD53-like_rpt2 |
cd22690 |
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
12-103 |
2.90e-05 |
|
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: 43.82 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 12 PNSHPfqerHVYL-DEPVKIGRSvarcrpAQNNATFDCKVLSRNHALIWFD-HKTGK--FYLQDTkSSNGTFINSQRLSR 87
Cdd:cd22690 8 NPSYP----DIELtQNTTFIGRS------KDCDEEITDPRISKHHCIITRKrSGKGLddVYVTDT-STNGTFINNNRLGK 76
|
90
....*....|....*.
gi 1952581426 88 GSEesppCELLSGDII 103
Cdd:cd22690 77 GSQ----SLLQDGDEI 88
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
266-694 |
2.96e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 266 EKIEVVR-KLSEVERSLSNTEDECTHLKEMNDRTQEElRELANKYNGAVNELKEFTEKLKQAEgkqeeiQQKALSEKKEL 344
Cdd:TIGR02169 170 RKKEKALeELEEVEENIERLDLIIDEKRQQLERLRRE-REKAERYQALLKEKREYEGYELLKE------KEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 345 QHRIDEMEEKEQLLQARIEALqadndftNERLTALQVRLEQLQEKnikdhnsigiqvddllpkINGSTDKEHFLLKSggD 424
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISEL-------EKRLEEIEQLLEELNKK------------------IKDLGEEEQLRVKE--K 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 425 CSELFQQFIECKNKLKAPVEptQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKAtliaedDHTKVTEETKLLKE--N 502
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKER--ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK------RRDKLTEEYAELKEelE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 503 QLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDELQCAHVQTGDSEREKQELQQELKEaqelaissk 582
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE--------- 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 583 qkcfemqalLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDkeieiietrdqlasthkeivalrqtaveaatg 662
Cdd:TIGR02169 439 ---------LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE-------------------------------- 477
|
410 420 430
....*....|....*....|....*....|..
gi 1952581426 663 resdIAILQGELHKVQTELEQWRQTASEYESE 694
Cdd:TIGR02169 478 ----YDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
235-663 |
3.66e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 47.74 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 235 EDGIRKELVTLQ----EDKHSYETTAK--ESLRRVLQEKIEVVRKLSE------VERSL-SNTEDECTHLKEMNdrtqEE 301
Cdd:TIGR01612 1269 EMDIKAEMETFNishdDDKDHHIISKKhdENISDIREKSLKIIEDFSEesdindIKKELqKNLLDAQKHNSDIN----LY 1344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 302 LRELANKYN-GAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQL--LQARIEALQADNDFTN--ERL 376
Cdd:TIGR01612 1345 LNEIANIYNiLKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLeeCKSKIESTLDDKDIDEciKKI 1424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 377 TALQVRLeqLQE--------KNIKDHNSigiQVDDLLPKINGSTDKEHFLLKSGGD------------CSELFQQFIECK 436
Cdd:TIGR01612 1425 KELKNHI--LSEesnidtyfKNADENNE---NVLLLFKNIEMADNKSQHILKIKKDnatndhdfnineLKEHIDKSKGCK 1499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 437 NKLKAPVEPTQNNRIsnvedMFESHLEN-----NQTTEEDLKNDSERFKA---TLIAE--DDHTKVT--EETKLLKENQL 504
Cdd:TIGR01612 1500 DEADKNAKAIEKNKE-----LFEQYKKDvtellNKYSALAIKNKFAKTKKdseIIIKEikDAHKKFIleAEKSEQKIKEI 1574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 505 EAKESDMSDTLSpSKDRSSEDTTDYQMDEQELNESLNKVSLLKDELQCAHVQTGDSEREKQELQqelKEAQELAISSKQK 584
Cdd:TIGR01612 1575 KKEKFRIEDDAA-KNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSFS---IDSQDTELKENGD 1650
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581426 585 CFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASTHKEIVALRQTAVEAATGR 663
Cdd:TIGR01612 1651 NLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKEEIESIKELIEPTIEN 1729
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
49-112 |
3.81e-05 |
|
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: 43.97 E-value: 3.81e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581426 49 KVLSRNHALIWFDHKTG--KFYLQDTKSSNGTFINsqrlsrgSEESPPC---ELLSGDIIQFGVDVTEN 112
Cdd:cd22681 64 ETCSKQHCVIQFRNVKGilKPYIMDLDSSNGTCLN-------DNVIPSSryvELRSGDVITFSKSNDYE 125
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
269-394 |
3.95e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.55 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 269 EVVRKLSEveRSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLK-QAEGKQEEIQ--QKALSEKKELQ 345
Cdd:COG2433 380 EALEELIE--KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEaELEEKDERIErlERELSEARSEE 457
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1952581426 346 HRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKDH 394
Cdd:COG2433 458 RREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEH 506
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
30-106 |
4.07e-05 |
|
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: 43.29 E-value: 4.07e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581426 30 IGRSVarcrpaQNNATFDCKVLSRNHALiwFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEesppCELLSGDIIQFG 106
Cdd:cd22682 24 IGRSV------ESQVQIDDDSVSRYHAK--LAVNPSAVSIIDLGSTNGTIVNGKKIPKLAS----CDLQNGDQIKIG 88
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
260-860 |
4.27e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 260 LRRVLQ-EKIE-VVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQqKA 337
Cdd:PRK03918 151 VRQILGlDDYEnAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLE-KE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 338 LSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKnIKDhnsigiqvddlLPKINGSTDKEHF 417
Cdd:PRK03918 230 VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK-VKE-----------LKELKEKAEEYIK 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 418 LlksggdcSELFQQFIECKNKLKAPVEpTQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKATLIAEDDHtKVTEETK 497
Cdd:PRK03918 298 L-------SEFYEEYLDELREIEKRLS-RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERH-ELYEEAK 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 498 LLKEN--QLEAKESDMSdtlspskdrssedttdyqmdEQELNESLNKVSLLKDELQCAHVQTGDSEREKQELQQELKEAQ 575
Cdd:PRK03918 369 AKKEEleRLKKRLTGLT--------------------PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 576 ELAISSKQKCFEMQALLEEERKtaKKQVEESTRQIQALQAHLHKLQKDIEILR-EDKEIEIIETRDqlasthKEIVALRQ 654
Cdd:PRK03918 429 EELKKAKGKCPVCGRELTEEHR--KELLEEYTAELKRIEKELKEIEEKERKLRkELRELEKVLKKE------SELIKLKE 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 655 TAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIfnlqtKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGL 734
Cdd:PRK03918 501 LAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEI-----KSLKKELEKLEELKKKLAELEKKLDELEEELAEL 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 735 KNDCDSLRQEKVlltEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQR--LQETNGLRVKLAHAENET 812
Cdd:PRK03918 576 LKELEELGFESV---EELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFeeLAETEKRLEELRKELEEL 652
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581426 813 QKF--QKQYEADQTMYLEL-------KEKLDKTQKENESITDELENCKENLKLLQQK 860
Cdd:PRK03918 653 EKKysEEEYEELREEYLELsrelaglRAELEELEKRREEIKKTLEKLKEELEEREKA 709
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
241-863 |
4.45e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 241 ELVTLQEDKHSYETTAKESLRRV--LQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKE 318
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 319 FTEKLKQAEGKQEEIQQKA--LSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKDHNS 396
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKAdaAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 397 IGIQVDDLLPKINGSTDKEHFLLKSggdcselfqqfiecKNKLKAPVEPTQNNRISNVEDMFESHLENNQTTEEDLKNDS 476
Cdd:PTZ00121 1442 EAKKADEAKKKAEEAKKAEEAKKKA--------------EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE 1507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 477 ERFKATLIAEDDHTKVTEETKllkenqlEAKESDMSDTLSPSKDRSSEDTTDyQMDEQELNESLNKVSLLKDELQCAHVQ 556
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAK-------KAEEAKKADEAKKAEEKKKADELK-KAEELKKAEEKKKAEEAKKAEEDKNMA 1579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 557 TGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAK--KQVEESTRQIQALQAHLHKLQKDIEILREDKEIE 634
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEelKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEN 1659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 635 IIEtRDQLASTHKEIVALRQTA---------VEAATGRESDIAILQGELHKVQTElEQWRQTASEYESEIFNLQTKLQLQ 705
Cdd:PTZ00121 1660 KIK-AAEEAKKAEEDKKKAEEAkkaeedekkAAEALKKEAEEAKKAEELKKKEAE-EKKKAEELKKAEEENKIKAEEAKK 1737
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 706 TQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEK-VLLTEKLQWFEEELRCAQQQSVKLTKDASG-LEVSRKAL 783
Cdd:PTZ00121 1738 EAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKeAVIEEELDEEDEKRRMEVDKKIKDIFDNFAnIIEGGKEG 1817
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 784 EVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENlKLLQQKGNN 863
Cdd:PTZ00121 1818 NLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEA-DEIEKIDKD 1896
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
180-361 |
5.51e-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: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 180 REQML--EQKLATLQRLLANTQEAsDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGIRKELVTLQEDKHSYE---T 254
Cdd:COG4913 241 HEALEdaREQIELLEPIRELAERY-AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEarlD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 255 TAKESLRRV--------------LQEKIE-VVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEF 319
Cdd:COG4913 320 ALREELDELeaqirgnggdrleqLEREIErLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEE 399
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1952581426 320 TEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEK-----EQLLQAR 361
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERRksnipARLLALR 446
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
166-843 |
6.15e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.89 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 166 ELFQLSQYLQEA---------LHREQMLEQKLATLQRLLANTQeaSDSSWQALIDEDRLLSRLEVMGNQLQaysknQTED 236
Cdd:TIGR00618 171 NLFPLDQYTQLAlmefakkksLHGKAELLTLRSQLLTLCTPCM--PDTYHERKQVLEKELKHLREALQQTQ-----QSHA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 237 GIRKELvTLQEDKHSYETTAKESLRRV------------LQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRE 304
Cdd:TIGR00618 244 YLTQKR-EAQEEQLKKQQLLKQLRARIeelraqeavleeTQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRS 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 305 LANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKK-ELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRL 383
Cdd:TIGR00618 323 RAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAhEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKEL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 384 EQLQEknikdhnsigiQVDDLLPKINGSTDKEHFLLKSGGDCsELFQQFIECKNKLKAPVEPTQNNRISNVEDMFESHLE 463
Cdd:TIGR00618 403 DILQR-----------EQATIDTRTSAFRDLQGQLAHAKKQQ-ELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 464 NNQTtEEDLKNDSERFKATliaeddHTKVTEETKLLKENQLEAKESDMS-DTLSPSKDRSSEDTTDYQMDEQELNESLNK 542
Cdd:TIGR00618 471 REQQ-LQTKEQIHLQETRK------KAVVLARLLELQEEPCPLCGSCIHpNPARQDIDNPGPLTRRMQRGEQTYAQLETS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 543 VSLLKDELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQK 622
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQP 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 623 DIEILREDKEIEIIETRDQLASTHKEivalrQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKL 702
Cdd:TIGR00618 624 EQDLQDVRLHLQQCSQELALKLTALH-----ALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEM 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 703 QLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDcdsLRQEKVLLTEKLQWFEEELRCAQQQSVkltkdasgLEVSRKA 782
Cdd:TIGR00618 699 LAQCQTLLRELETHIEEYDREFNEIENASSSLGSD---LAAREDALNQSLKELMHQARTVLKART--------EAHFNNN 767
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952581426 783 LEVevgTLKEQRLQEtnglrvkLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESI 843
Cdd:TIGR00618 768 EEV---TAALQTGAE-------LSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDI 818
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
296-632 |
6.88e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 296 DRTQEELRELankyNGAVNELKEFTEKLK-QAEGKQEEIQQKAlsEKKELQH-----RIDEMEEKEQLLQARIEALQADN 369
Cdd:TIGR02168 182 ERTRENLDRL----EDILNELERQLKSLErQAEKAERYKELKA--ELRELELallvlRLEELREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 370 DFTNERLTALQVRLEQLQEKNIKDHNSIGIQVDDLLpkingstdkehfllksggdcselfqqfiecknklkapvepTQNN 449
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELY----------------------------------------ALAN 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 450 RISNVEDMFESH---LENNQTTEEDLKNDSERFKATLI-AEDDHTKVTEETKLLKEN--QLEAKESDMSDTLSPSKDRSS 523
Cdd:TIGR02168 296 EISRLEQQKQILrerLANLERQLEELEAQLEELESKLDeLAEELAELEEKLEELKEEleSLEAELEELEAELEELESRLE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 524 EDTTDYQMDEQELNESLNKVSLLKDELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQ-------------- 589
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEleeleeeleelqee 455
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1952581426 590 -ALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKE 632
Cdd:TIGR02168 456 lERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
53-106 |
7.41e-05 |
|
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: 42.24 E-value: 7.41e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1952581426 53 RNHALIWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSeesppCELLSGDIIQFG 106
Cdd:cd22700 36 EQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAA-----VRLAPGDVLRFG 84
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
184-389 |
8.42e-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: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 184 LEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEvmgNQLQAYSKNQTEdgIRKELVTLQEDKHSYETtAKESLRRV 263
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALA---RRIRALEQELAA--LEAELAELEKEIAELRA-ELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 264 LQEKIEVVRKLSEVER--------SLSNTEDECTHLKEMNDRTQEELRELANKY---NGAVNELKEFTEKLKQAEGKQEE 332
Cdd:COG4942 106 LAELLRALYRLGRQPPlalllspeDFLDAVRRLQYLKYLAPARREQAEELRADLaelAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581426 333 IQQKALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEK 389
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
594-794 |
1.19e-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: 45.53 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 594 EERKTAKKQVEESTRQIQALQAHLHKLQKDI-EILREDKEIE--IIETRDQLASTHKEIVALRQTAVEAatgrESDIAIL 670
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEkALLKQLAALErrIAALARRIRALEQELAALEAELAEL----EKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 671 QGELHKVQTELEQ-----WRQTASEYESEIFNLQTKLQLQTQQQKDKQKGEAvqLQGKLDELQKQSNGLKNDCDSLRQEK 745
Cdd:COG4942 96 RAELEAQKEELAEllralYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA--RREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1952581426 746 VLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQR 794
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
525-694 |
1.72e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 525 DTTDYQMDEQELNESLNKVSLLKDELQCAHVQTGDSEREKQELQQELKEAQE--LAISSKQKcfemqALLEEERKTAKKQ 602
Cdd:COG4913 279 AALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAqiRGNGGDRL-----EQLEREIERLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 603 VEESTRQIQALQAHLHKLQKDIeilrEDKEIEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELE 682
Cdd:COG4913 354 LEERERRRARLEALLAALGLPL----PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
170
....*....|..
gi 1952581426 683 QWRQTASEYESE 694
Cdd:COG4913 430 SLERRKSNIPAR 441
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
260-389 |
1.81e-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: 44.15 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 260 LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEI----QQ 335
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkEY 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1952581426 336 KALS-EKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEK 389
Cdd:COG1579 92 EALQkEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
255-621 |
2.04e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 255 TAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELR--ELANKYNGAVNEL-----------KEFTE 321
Cdd:PRK04863 297 TSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRqqEKIERYQADLEELeerleeqnevvEEADE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 322 KLKQAEGKQEEIQQKALSEKKEL---QHRIDEMEEK----EQLLQA--RIEALQADNDFT----NERLTALQVRLEQLQE 388
Cdd:PRK04863 377 QQEENEARAEAAEEEVDELKSQLadyQQALDVQQTRaiqyQQAVQAleRAKQLCGLPDLTadnaEDWLEEFQAKEQEATE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 389 KNI---------KDHNSIGIQVDDLLPKINGSTDKEhfllksggDCSELFQQFIECKNKLKAPVEPTQNNRISNVEdmFE 459
Cdd:PRK04863 457 ELLsleqklsvaQAAHSQFEQAYQLVRKIAGEVSRS--------EAWDVARELLRRLREQRHLAEQLQQLRMRLSE--LE 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 460 SHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEEtkllKENQLEakesdmsdTLSPSKDRSSEDTTDYQMDEQELNES 539
Cdd:PRK04863 527 QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEE----LEARLE--------SLSESVSEARERRMALRQQLEQLQAR 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 540 LNKVSLLKDELQCAhvqtgdserekQELQQELKEAQELAISSKQKCFE-MQALLEEERKtAKKQVEESTRQIQALQAHLH 618
Cdd:PRK04863 595 IQRLAARAPAWLAA-----------QDALARLREQSGEEFEDSQDVTEyMQQLLERERE-LTVERDELAARKQALDEEIE 662
|
...
gi 1952581426 619 KLQ 621
Cdd:PRK04863 663 RLS 665
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
154-367 |
2.07e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 154 KVAANSPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDsswqaliDEDRLLSRLEVMGNQLQAYSKNQ 233
Cdd:COG4717 60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA-------ELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 234 TEDGIRKELVTLQEdkhsyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMND-RTQEELRELANKYNGA 312
Cdd:COG4717 133 ELEALEAELAELPE--------RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEEL 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1952581426 313 VNELKEFTEKLKQAEGKQEEIQQkalsEKKELQHRIDEMEEKEQLLQARIEALQA 367
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEE----ELEQLENELEAAALEERLKEARLLLLIA 255
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
200-389 |
2.32e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 200 EASDSSWQALIdEDRLLSRLEvmgNQLQAYSKNQTEDGIR--KELVTLQEDKHSYETTAKEsLRRVLQEKIEVVRKLSEV 277
Cdd:COG4717 33 EAGKSTLLAFI-RAMLLERLE---KEADELFKPQGRKPELnlKELKELEEELKEAEEKEEE-YAELQEELEELEEELEEL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 278 ERSLSNTEDECTHLKEMND---------RTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQHRI 348
Cdd:COG4717 108 EAELEELREELEKLEKLLQllplyqeleALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS 187
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1952581426 349 DEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEK 389
Cdd:COG4717 188 LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
567-765 |
2.70e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 567 LQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREdkeiEIIETRDQLASTH 646
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA----ELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 647 KEIVALRQTAVEAATGREsdIAILQGELHKVQTELEQWRQTASEYES---EIFNLQTKLQLQTQQQKDKQKGEAVQLQGK 723
Cdd:COG4717 123 KLLQLLPLYQELEALEAE--LAELPERLEELEERLEELRELEEELEEleaELAELQEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1952581426 724 LDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQ 765
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
561-744 |
2.86e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 561 EREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAkkQVEESTRQIQALQAHLHKLQKDIEILREDKeIEIIETRD 640
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLA--EYSWDEIDVASAEREIAELEAELERLDASS-DDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 641 QLASTHKEIVALRQ---TAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKgea 717
Cdd:COG4913 693 QLEELEAELEELEEeldELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE--- 769
|
170 180
....*....|....*....|....*..
gi 1952581426 718 vQLQGKLDELQKQSNGLKNDCDSLRQE 744
Cdd:COG4913 770 -NLEERIDALRARLNRAEEELERAMRA 795
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
556-691 |
3.72e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 556 QTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEEStrQIQALQAHLHKLQKDIEILRE---DKE 632
Cdd:COG3206 213 EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP--VIQQLRAQLAELEAELAELSArytPNH 290
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581426 633 IEIIETRDQLASTHKEIVALRQTAVEAAtgrESDIAILQGELHKVQTELEQWRQTASEY 691
Cdd:COG3206 291 PDVIALRAQIAALRAQLQQEAQRILASL---EAELEALQAREASLQAQLAQLEARLAEL 346
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
16-111 |
4.15e-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: 39.98 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 16 PFQERHVYLD-EPVKIGRSvarcrpAQNNATFDCKVLSRNHALIWFdhKTGKFYLQDTKSSNGTFINSQRLSRgseespP 94
Cdd:cd22693 7 TLQGQTFPIDkSGITIGRA------DDNDLVLSDDFVSSRHARIYL--QGSSWYLEDLGSTNGTFVNGNRVTQ------P 72
|
90
....*....|....*..
gi 1952581426 95 CELLSGDIIQFGVDVTE 111
Cdd:cd22693 73 VVVQPGDTIRIGATVFE 89
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
165-364 |
5.26e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.53 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 165 QELFQLSQYLQEALHREQML----------------EQKLATLQRLLANTQ---EASDSSWQALIDEDR-LLSRLEVMGN 224
Cdd:COG0497 172 KELEELRADEAERARELDLLrfqleeleaaalqpgeEEELEEERRRLSNAEklrEALQEALEALSGGEGgALDLLGQALR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 225 QLQAYSKNQTEdgirkelvtLQEdkhsyettAKESLRRVLQEKIEVVRklsEVERSLSNTEDECTHLKEMNDRtQEELRE 304
Cdd:COG0497 252 ALERLAEYDPS---------LAE--------LAERLESALIELEEAAS---ELRRYLDSLEFDPERLEEVEER-LALLRR 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952581426 305 LANKYNGAVNELKEFTEKLKQaegKQEEIQQKAlSEKKELQHRIDEMEEK-----EQLLQARIEA 364
Cdd:COG0497 311 LARKYGVTVEELLAYAEELRA---ELAELENSD-ERLEELEAELAEAEAElleaaEKLSAARKKA 371
|
|
| FHA_SNIP1_DDL-like |
cd22676 |
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ... |
52-106 |
6.64e-04 |
|
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA domain-containing protein DDL, and similar proteins; SNIP1 is an FHA domain-containing protein required for pre-mRNA splicing as a component of the spliceosome. It inhibits NF-kappaB signaling by competing for its binding to the C/H1 domain of CBP/p300 transcriptional co-activators. It is involved in microRNA (miRNA) biogenesis. SNIP1 is a regulator of the cell cycle and cyclin D1 expression and may be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. This family also includes Arabidopsis thaliana FHA domain-containing protein DDL and similar proteins. DDL, also called protein DAWDLE, is involved in the microRNA (miRNA) and short interfering RNA (siRNA) biogenesis. It may facilitate DCL1 to access or recognize primary miRNAs. DDL binds RNA non-specifically. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438728 [Multi-domain] Cd Length: 111 Bit Score: 39.97 E-value: 6.64e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952581426 52 SRNHALIWF----------DHKTGKFYLQDTKSSNGTFINSQRLsrgsEESPPCELLSGDIIQFG 106
Cdd:cd22676 42 SKQHAVIQFrevekrnegdVIENIRPYIIDLGSTNGTFLNGEKI----EPRRYYELREKDVLKFG 102
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
291-548 |
7.01e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 291 LKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALqadnd 370
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEEL----- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 371 ftNERLTALQVRLEQlQEKNIKDHNSIGIQVDDLLPKINgstdKEHFLLKSGGDCSELFQQFIECKNKLKA----PVEPT 446
Cdd:PHA02562 240 --TDELLNLVMDIED-PSAALNKLNTAAAKIKSKIEQFQ----KVIKMYEKGGVCPTCTQQISEGPDRITKikdkLKELQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 447 Q-----NNRISNVEDMFESHLEnNQTTEEDLKNDSERFKATLIAEDDHTKVTEetKLLKenQLEAKESDMSDTLSPSKDR 521
Cdd:PHA02562 313 HsleklDTAIDELEEIMDEFNE-QSKKLLELKNKISTNKQSLITLVDKAKKVK--AAIE--ELQAEFVDNAEELAKLQDE 387
|
250 260
....*....|....*....|....*..
gi 1952581426 522 SSEDTTDYQMDEQELNESLNKVSLLKD 548
Cdd:PHA02562 388 LDKIVKTKSELVKEKYHRGIVTDLLKD 414
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
312-389 |
8.48e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 8.48e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581426 312 AVNELKEFTEKLKQAEGKQEEIQQkalsEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEK 389
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQA----ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
213-653 |
9.57e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 213 DRLLSRLEVMGNQLQAYSKNQTE-DGIRKELVTLQEDKHsyETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHL 291
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEElEELEEELEELEAELE--ELREELEKLEKLLQLLPLYQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 292 KEmndrTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKElqhRIDEMEEKEQLLQARIEALQADNDF 371
Cdd:COG4717 152 EE----RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE---ELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 372 TNERLTALQVRLEQLQEKNIKDHNSIGIQVDDLLPKINGSTDKEHFLLKSGGD-----CSELFQQFIECKNKLKAPVEPT 446
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 447 QNNRISNVEDMFESHLENNQTTEEDLKND---SERFKATLIAEDDHTKVTEETKLLKENQLEAKESDMSDTLSPSKDRSS 523
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDlspEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 524 EDTTDYQMDEQELNESLNKVSLLKDELQcahvqtGDSEREKQELQQELKEAQELAISSkqkcfemqalLEEERKTAKKQV 603
Cdd:COG4717 385 EELRAALEQAEEYQELKEELEELEEQLE------ELLGELEELLEALDEEELEEELEE----------LEEELEELEEEL 448
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1952581426 604 EESTRQIQALQAHLHKLQKDIEIlrEDKEIEIIETRDQLASTHKEIVALR 653
Cdd:COG4717 449 EELREELAELEAELEQLEEDGEL--AELLQELEELKAELRELAEEWAALK 496
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
588-837 |
1.12e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 588 MQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIeiIETRDQLASTHKEIVALRQTAVEAatgrESDI 667
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGL--VDLSEEAKLLLQQLSELESQLAEA----RAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 668 AILQGELHKVQTELEQWRQTASEyeseifnlqtklqLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVL 747
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPE-------------LLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 748 LTEKLQwfeeelRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKeQRLQETNGLRVKLAhaenetqKFQKQYEADQTMYL 827
Cdd:COG3206 303 LRAQLQ------QEAQRILASLEAELEALQAREASLQAQLAQLE-ARLAELPELEAELR-------RLEREVEVARELYE 368
|
250
....*....|
gi 1952581426 828 ELKEKLDKTQ 837
Cdd:COG3206 369 SLLQRLEEAR 378
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
50-106 |
1.13e-03 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaA and similar proteins; FhaA regulates cell growth and peptidoglycan synthesis by binding to MviN. It may inhibit the late stages of peptidoglycan synthesis. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438720 [Multi-domain] Cd Length: 91 Bit Score: 38.99 E-value: 1.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581426 50 VLSRNHALIWFDHKTGkfYLQDTKSSNGTFINSQRLsrgseeSPPCELLSGDIIQFG 106
Cdd:cd22668 36 GVSRRHAEIRWDGQVA--HLTDLGSTNGTTVNNAPV------TPEWRLADGDVITLG 84
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
502-695 |
1.21e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 502 NQLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDELQCAHVQTGDSEREKQELQQELKEAQELAISS 581
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 582 KQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEI------EIIETRDQLASTHKEIVALRQT 655
Cdd:COG4942 110 LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAElaalraELEAERAELEALLAELEEERAA 189
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1952581426 656 AVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEI 695
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
165-368 |
1.22e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 165 QELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALID--------EDRLLSRLEVMGNQLQAYSKNQTED 236
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekeiaelRAELEAQKEELAELLRALYRLGRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 237 GIrkELVTLQEDKHSYETTAK--ESLRRVLQEKIEVVRK-LSEVERSLSNTEDECTHLKEMNDRTQEELRELAnkyngav 313
Cdd:COG4942 121 PL--ALLLSPEDFLDAVRRLQylKYLAPARREQAEELRAdLAELAALRAELEAERAELEALLAELEEERAALE------- 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1952581426 314 nelkefteklkQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQAD 368
Cdd:COG4942 192 -----------ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
299-389 |
1.78e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 299 QEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQkalsEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTA 378
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK----QLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90
....*....|.
gi 1952581426 379 LQVRLEQLQEK 389
Cdd:COG4942 95 LRAELEAQKEE 105
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
592-860 |
1.86e-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: 41.93 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 592 LEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILR----------EDKEIE-------IIETRDQLASTHKEIVALRQ 654
Cdd:TIGR04523 223 LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKdeqnkikkqlSEKQKEleqnnkkIKELEKQLNQLKSEISDLNN 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 655 TAVEAATGR-ESDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKgeavQLQGKLDELQKqsng 733
Cdd:TIGR04523 303 QKEQDWNKElKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQR----ELEEKQNEIEK---- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 734 LKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQ----------ETNGLRV 803
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKnnseikdltnQDSVKEL 454
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581426 804 KLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQK 860
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK 511
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
161-327 |
2.11e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 161 SMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIdEDRLLSRLEVMGNQLQAYSKNQTEDGIRk 240
Cdd:COG3206 215 KLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPV-IQQLRAQLAELEAELAELSARYTPNHPD- 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 241 eLVTLQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFT 320
Cdd:COG3206 293 -VIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLL 371
|
....*..
gi 1952581426 321 EKLKQAE 327
Cdd:COG3206 372 QRLEEAR 378
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
534-683 |
2.52e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 534 QELNESLNKVSLLKDELQCAHVQTGDSEREKQELQQELKEAQELAisskqkcfemqalleeERKTAKKQVEESTRQIQAL 613
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI----------------KKYEEQLGNVRNNKEYEAL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952581426 614 QAHLHKLQKDIEILrEDKEIEIIETRD----QLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQ 683
Cdd:COG1579 95 QKEIESLKRRISDL-EDEILELMERIEeleeELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
174-389 |
2.60e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 174 LQEALHREQMLEQKLATLQRLLAnTQEASdsswqalIDEDRL-LSRLEVMGNQLQAYSKNQTEDGIRKELvtlQEDKHSY 252
Cdd:PRK02224 504 LVEAEDRIERLEERREDLEELIA-ERRET-------IEEKRErAEELRERAAELEAEAEEKREAAAEAEE---EAEEARE 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 253 ETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDEC-------THLKEMNDRTQEEL-------RELANKYNGAvnELKE 318
Cdd:PRK02224 573 EVAELNSKLAELKERIESLERIRTLLAAIADAEDEIerlrekrEALAELNDERRERLaekrerkRELEAEFDEA--RIEE 650
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952581426 319 FTEKLKQAEGKQEEIQQKalsekkelqhrIDEMEEKEQLLQARIEALQADndftNERLTALQVRLEQLQEK 389
Cdd:PRK02224 651 AREDKERAEEYLEQVEEK-----------LDELREERDDLQAEIGAVENE----LEELEELRERREALENR 706
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
215-671 |
2.77e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.35 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 215 LLSRLEVMGNQlQAYSKNQTEdgIRKELVTLQEDKHSYETTAKESLRRVLQEKIEVVRK----LSEVERSLSNTEDECTH 290
Cdd:pfam10174 308 LQTKLETLTNQ-NSDCKQHIE--VLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKktkqLQDLTEEKSTLAGEIRD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 291 LKEMNDRTQEELRELANKYNGAVNELKEfteKLKQAEGKQEEIQ----------------QKALSEKKELQHRIDEMEEK 354
Cdd:pfam10174 385 LKDMLDVKERKINVLQKKIENLQEQLRD---KDKQLAGLKERVKslqtdssntdtalttlEEALSEKERIIERLKEQRER 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 355 E-QLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKDHNSIGIQVDDLLPKINGSTDKEHFLLKSGGDCSELFQQFI 433
Cdd:pfam10174 462 EdRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLK 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 434 ECKN-KLKAPVEPTQNNRISNVEDMFESHLENNQTTEEDLkndsERFKATLiaeddhtKVTEETKLLKENQLEAKESdms 512
Cdd:pfam10174 542 KAHNaEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEV----ERLLGIL-------REVENEKNDKDKKIAELES--- 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 513 dtlspskdrssedTTDYQMDEQElneslnkvsllKDELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKcfEMQALL 592
Cdd:pfam10174 608 -------------LTLRQMKEQN-----------KKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQL--QLEELM 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 593 EEERKTaKKQVEESTRQIQALQAHLHKLQKDIEILRedkeieiIETRDQLasthKEIVALRQTAVEAA-TGRESDIAILQ 671
Cdd:pfam10174 662 GALEKT-RQELDATKARLSSTQQSLAEKDGHLTNLR-------AERRKQL----EEILEMKQEALLAAiSEKDANIALLE 729
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
265-863 |
3.15e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 265 QEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGA----------VNELKEFTEKLKQAEGKQEEIQ 334
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAeemrarlaarKQELEEILHELESRLEEEEERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 335 QKALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKDHnsigiqvddllpkingstdK 414
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLS-------------------K 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 415 EHFLLKSggDCSELFQQFIECKNKLKAPveptqnNRISNVEDMFESHLENNQTTEEDLKNDSERFKATLIAE--DDHTKV 492
Cdd:pfam01576 153 ERKLLEE--RISEFTSNLAEEEEKAKSL------SKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGEstDLQEQI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 493 TEETKLLKE--NQLEAKESDMSDTLspskDRSSEDTTDYQMDEQELNESLNKVSLLKDELQCAHVQTGDSEREKQELQQE 570
Cdd:pfam01576 225 AELQAQIAElrAQLAKKEEELQAAL----ARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 571 LKE--------------AQELAISSKQKCFEMQALLEEERKTAKKQVEE-STRQIQALQahlhKLQKDIEILREDKeIEI 635
Cdd:pfam01576 301 LEAlkteledtldttaaQQELRSKREQEVTELKKALEEETRSHEAQLQEmRQKHTQALE----ELTEQLEQAKRNK-ANL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 636 IETRDQLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYEsEIFNLQTKLQLQTQQQKDKQKG 715
Cdd:pfam01576 376 EKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELA-EKLSKLQSELESVSSLLNEAEG 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 716 EAVQLQGKLDELQKQSnglkNDCDSLRQE----KVLLTEKLQWFEEELRCAQQQsvkltkdASGLEVSRKALEVEVGTLK 791
Cdd:pfam01576 455 KNIKLSKDVSSLESQL----QDTQELLQEetrqKLNLSTRLRQLEDERNSLQEQ-------LEEEEEAKRNVERQLSTLQ 523
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581426 792 EQ------RLQETNGlrvKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQKGNN 863
Cdd:pfam01576 524 AQlsdmkkKLEEDAG---TLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSN 598
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
561-860 |
3.27e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 561 EREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEiEIIETRD 640
Cdd:COG4913 351 ERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR-ELEAEIA 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 641 QLASTHK----EIVALRQTAVEAATGRESDIAILqGELHKVQTELEQWRQTA--------------SEYE---SEIFNLQ 699
Cdd:COG4913 430 SLERRKSnipaRLLALRDALAEALGLDEAELPFV-GELIEVRPEEERWRGAIervlggfaltllvpPEHYaaaLRWVNRL 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 700 TKLQ-------LQTQQQKDKQKGEAVQLQGKL---------------------------DELQ------------KQSNG 733
Cdd:COG4913 509 HLRGrlvyervRTGLPDPERPRLDPDSLAGKLdfkphpfrawleaelgrrfdyvcvdspEELRrhpraitragqvKGNGT 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 734 L--KNDCDSLRQEKVL---LTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLkeQRLQETNGLRVKLAHA 808
Cdd:COG4913 589 RheKDDRRRIRSRYVLgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL--QRLAEYSWDEIDVASA 666
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1952581426 809 ENETQKFQKQY---EADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQK 860
Cdd:COG4913 667 EREIAELEAELerlDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE 721
|
|
| VI_FHA |
TIGR03354 |
type VI secretion system FHA domain protein; Members of this protein family are FHA ... |
49-106 |
3.32e-03 |
|
type VI secretion system FHA domain protein; Members of this protein family are FHA (forkhead-associated) domain-containing proteins that are part of type VI secretion loci in a considerable number of bacteria, most of which are known pathogens. Species include Pseudomonas aeruginosa PAO1, Aeromonas hydrophila, Yersinia pestis, Burkholderia mallei, etc. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274537 [Multi-domain] Cd Length: 396 Bit Score: 40.82 E-value: 3.32e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952581426 49 KVLSRNHA-LIWFDhktGKFYLQDTkSSNGTFINS--QRLSRGSEESppceLLSGDIIQFG 106
Cdd:TIGR03354 43 RHVSGRHArIRYRD---GAYLLTDL-STNGVFLNGsgSPLGRGNPVR----LEQGDRLRLG 95
|
|
| prfA |
PRK00591 |
peptide chain release factor 1; Validated |
562-613 |
3.58e-03 |
|
peptide chain release factor 1; Validated
Pssm-ID: 234801 [Multi-domain] Cd Length: 359 Bit Score: 40.45 E-value: 3.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1952581426 562 REKQELQQELKEAQELAISSKQKcfEMQALLEEERKTAKKQVEESTRQIQAL 613
Cdd:PRK00591 52 REYKQAQEDLEEAKEMLEEESDP--EMREMAKEELKELEERLEELEEELKIL 101
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
170-354 |
3.64e-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: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 170 LSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSwQALIDEDRLlsRLEVMGNQLQAYSKNQTEdgIRKELVTLQED- 248
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI-EKEIENLNG--KKEELEEELEELEAALRD--LESRLGDLKKEr 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 249 -KHSYETTAKESLRRVLQEKIEVVRK-LSEVERSLSNTEDECTH--------------------LKEMNDRTQEELRELA 306
Cdd:TIGR02169 892 dELEAQLRELERKIEELEAQIEKKRKrLSELKAKLEALEEELSEiedpkgedeeipeeelsledVQAELQRVEEEIRALE 971
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1952581426 307 NKYNGAVNELKEFTEKLKQAEGKQEEIQQkalsEKKELQHRIDEMEEK 354
Cdd:TIGR02169 972 PVNMLAIQEYEEVLKRLDELKEKRAKLEE----ERKAILERIEEYEKK 1015
|
|
| FHA_Rv1747-like_rpt2 |
cd22737 |
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
28-106 |
4.20e-03 |
|
second 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 second FHA domain, which has a circularly permuted FHA domain fold with a conserved pThr-binding interface.
Pssm-ID: 439356 [Multi-domain] Cd Length: 93 Bit Score: 37.47 E-value: 4.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581426 28 VKIGRSvarcrpAQNNATFDCKVLSRNHALIwfDHKTGKFYLQDTKSSNGTFINSQRLSRgseesppCELLSGDIIQFG 106
Cdd:cd22737 23 VRIGRA------SDNDIVIPEGSVSRHHATL--VPTPGGTQIRDLRSTNGTFVNGLRVDA-------ALLHDGDVVTIG 86
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
291-695 |
4.57e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 291 LKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQkalsekkeLQHRIDEMEEKEQLLQARIEALQADND 370
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAE--------LQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 371 FTnERLTALQVRLEQLQEKNIKDhNSIGIQVDDLLPKINGSTDKEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQNNR 450
Cdd:COG4717 120 KL-EKLLQLLPLYQELEALEAEL-AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 451 ISNVEDMF------ESHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEE----------------------------- 495
Cdd:COG4717 198 AEELEELQqrlaelEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllliaaallallglggsllsliltiag 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 496 -------------TKLLKENQLEAKESDMSDTLSPSKDRSSEDTTDYqMDEQELNESLNKVSLLKDELQCAHVQTGDSER 562
Cdd:COG4717 278 vlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEEL-LAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 563 EK-------QELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEilREDKEIEI 635
Cdd:COG4717 357 EEleeelqlEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALD--EEELEEEL 434
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952581426 636 IETRDQLASTHKEIVALRQtaveaatgresDIAILQGELHKVQT--ELEQWRQTASEYESEI 695
Cdd:COG4717 435 EELEEELEELEEELEELRE-----------ELAELEAELEQLEEdgELAELLQELEELKAEL 485
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
272-389 |
4.62e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 272 RKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNgAVNELKEFTEKLKQAEGKQEEIQQ---------KALSEKK 342
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAEYSWDEIDVASAEREIAEleaelerldASSDDLA 688
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1952581426 343 ELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEK 389
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
599-793 |
4.79e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 599 AKKQVEESTRQIQALQAHLHKLQKDIEILREDKEI---EIIETRDQLASTHKEIVALRQTAVEAatgrESDIAILQGELH 675
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKAllkQLAALERRIAALARRIRALEQELAAL----EAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 676 KVQTELEQWRQTASEY-----------------ESEIFNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDC 738
Cdd:COG4942 94 ELRAELEAQKEELAELlralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1952581426 739 DSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQ 793
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| FHA_Ki67 |
cd22673 |
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ... |
52-106 |
4.84e-03 |
|
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438725 [Multi-domain] Cd Length: 95 Bit Score: 37.19 E-value: 4.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1952581426 52 SRNHALIWFDhKTGKFYLQDTKSSNGTFINsqrlsrGSEESPPCELLSGDIIQFG 106
Cdd:cd22673 41 SREHCRIEVD-ENGKAYLENLSTTNPTLVN------GKAIEKSAELKDGDVITIG 88
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
238-860 |
5.21e-03 |
|
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: 40.73 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 238 IRKELVTLQEDKHSYETTAKesLRRVLQEKIEVVRKLSEVERSLSNTE----DECTHLKEMNDRTQEELRELANKYNGAV 313
Cdd:pfam02463 158 IEEEAAGSRLKRKKKEALKK--LIEETENLAELIIDLEELKLQELKLKeqakKALEYYQLKEKLELEEEYLLYLDYLKLN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 314 NELKEFTEKLKQAEGKQEEIQ---QKALSEKKELQHRIDEMEEKEQ--------LLQARIEALQADNDFTNERLTALQVR 382
Cdd:pfam02463 236 EERIDLLQELLRDEQEEIESSkqeIEKEEEKLAQVLKENKEEEKEKklqeeelkLLAKEEEELKSELLKLERRKVDDEEK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 383 LEQLQEKNIKDHNSI------------------------GIQVDDLLPKINGSTDKEHFLLKSGGDCSELFQQFIECKNK 438
Cdd:pfam02463 316 LKESEKEKKKAEKELkkekeeieelekelkeleikreaeEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 439 LKAPVEPTQNNRISN--VEDMFESHLENNQTTEEDLKNDSERFKATL---IAEDDHTKVTEETKLLKENQLEAKESDMSD 513
Cdd:pfam02463 396 ELELKSEEEKEAQLLleLARQLEDLLKEEKKEELEILEEEEESIELKqgkLTEEKEELEKQELKLLKDELELKKSEDLLK 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 514 TLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDELQCAHVQT----GDSEREKQELQQELKEAQELAISSKQKCFEMQ 589
Cdd:pfam02463 476 ETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGvggrIISAHGRLGDLGVAVENYKVAISTAVIVEVSA 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 590 ALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAI 669
Cdd:pfam02463 556 TADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELT 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 670 LQGELHKVQTELEQWRQTASEYESEI--FNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVL 747
Cdd:pfam02463 636 KLKESAKAKESGLRKGVSLEEGLAEKseVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKL 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 748 LTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAE-----NETQKFQKQYEAD 822
Cdd:pfam02463 716 KLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAeerekTEKLKVEEEKEEK 795
|
650 660 670
....*....|....*....|....*....|....*...
gi 1952581426 823 QTMYLELKEKLDKTQKENESITDELENCKENLKLLQQK 860
Cdd:pfam02463 796 LKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEE 833
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
258-367 |
6.26e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 258 ESLRRVLQEKI-EVVRKLSEVERSLSNTEDEcthLKEMNDRTQEELRELANKYNGAVNELKE----------FTEKLKQA 326
Cdd:PRK00409 526 EELERELEQKAeEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLEEAEKEAQQAIKEAKKeadeiikelrQLQKGGYA 602
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1952581426 327 EGKQEEIQQKalseKKELQHRIDEMEEKEQLLQARIEALQA 367
Cdd:PRK00409 603 SVKAHELIEA----RKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
257-391 |
6.36e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 39.71 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 257 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEgkqeEIQQK 336
Cdd:COG4026 113 KNAIIRAGLKSLQNIPEYNELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILE----EEFDN 188
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581426 337 ALSEKKELQHRIDEMEEKEQLLQARIEALQAD---NDFTNERLTALQVrlEQLQEKNI 391
Cdd:COG4026 189 IKSEYSDLKSRFEELLKKRLLEVFSLEELWKElfpEELPEEDFIYFAT--ENLKPGKI 244
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
183-671 |
7.29e-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: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 183 MLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQT--EDGIRKELVTLQEDKHSYETTAKESL 260
Cdd:pfam05483 262 LLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKalEEDLQIATKTICQLTEEKEAQMEELN 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 261 RRVLQEKIEVvrklSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQ------ 334
Cdd:pfam05483 342 KAKAAHSFVV----TEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKkilaed 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 335 QKALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRlEQLQEKNIKDHNSIgiQVDDLLPKINGSTDK 414
Cdd:pfam05483 418 EKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTS-EEHYLKEVEDLKTE--LEKEKLKNIELTAHC 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 415 EHFLLKSggdcSELFQQFIECKNKLKAPVEPTQNNRisNVEDMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKV-- 492
Cdd:pfam05483 495 DKLLLEN----KELTQEASDMTLELKKHQEDIINCK--KQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCkl 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 493 --TEETKLLKENQLEAKESDMSDTLSPSKD--RSSEDTTDYQMDEQELNESLNK-------------VSLLKDELQCAHV 555
Cdd:pfam05483 569 dkSEENARSIEYEVLKKEKQMKILENKCNNlkKQIENKNKNIEELHQENKALKKkgsaenkqlnayeIKVNKLELELASA 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 556 QT------------------------GDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQ 611
Cdd:pfam05483 649 KQkfeeiidnyqkeiedkkiseekllEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELG 728
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 612 ALQAHlhklQKDIEILREDKEIEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQ 671
Cdd:pfam05483 729 LYKNK----EQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILK 784
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
553-697 |
7.81e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.89 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 553 AHVQTGDSEREKQELQQELKEAQElaisskqkcfemQALLEEERKTAKKQVEESTRQIQALQahlhKLQKDIEILRedKE 632
Cdd:PRK11281 27 ARAASNGDLPTEADVQAQLDALNK------------QKLLEAEDKLVQQDLEQTLALLDKID----RQKEETEQLK--QQ 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581426 633 IEiiETRDQLASTHKEIVALRQTAVEAATGRESDIAI--LQGELHKVQTELEQWRQTASEYESEIFN 697
Cdd:PRK11281 89 LA--QAPAKLRQAQAELEALKDDNDEETRETLSTLSLrqLESRLAQTLDQLQNAQNDLAEYNSQLVS 153
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
276-383 |
8.01e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.84 E-value: 8.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 276 EVERSLSNTEDECTHLKEMNDRTQEELRELANKY---NGAVNELKEFTEKLKQAEGKQEEIQQKALSEK----------K 342
Cdd:pfam06160 288 YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEvayselqeelE 367
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1952581426 343 ELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRL 383
Cdd:pfam06160 368 EILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLEL 408
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
548-760 |
8.23e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 548 DELQCAHvQTGDSEREKQELQQELKEAQELAISSKQKcfemQALLEEERKTAkkQVEESTRQIQALQAHLHKLQKDIEIL 627
Cdd:COG4913 235 DDLERAH-EALEDAREQIELLEPIRELAERYAAARER----LAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 628 REDKEieiiETRDQLASTHKEIVALRQtAVEAATGREsdIAILQGELHKVQTELEQWRQTASEYES-------------E 694
Cdd:COG4913 308 EAELE----RLEARLDALREELDELEA-QIRGNGGDR--LEQLEREIERLERELEERERRRARLEAllaalglplpasaE 380
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 695 IFNLQTKLQLQTQQQKDKQKGEAVQ----LQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELR 760
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEalaeAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
240-535 |
8.34e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 240 KELVTLQEDKHSYETTAKESLRRVLQE----KIEVVRKLSEVER---SLSNTEDECTHLKEMNDRTQEELRELANKYNGA 312
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEEnkikAAEEAKKAEEDKKkaeEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 313 VNELKEfTEKLKQAE----GKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQvrlEQLQE 388
Cdd:PTZ00121 1712 AEEKKK-AEELKKAEeenkIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE---EELDE 1787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 389 KNIKDHNSIGIQVDDLLpkingstDKEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQNNRIsNVEDMFESHLEN-NQT 467
Cdd:PTZ00121 1788 EDEKRRMEVDKKIKDIF-------DNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQL-EEADAFEKHKFNkNNE 1859
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581426 468 TEEDLKNDSERFKATLIAEDDHTKVtEETKLLKENQLEAKESDMSDTLSPSKDrssEDTTDYQMDEQE 535
Cdd:PTZ00121 1860 NGEDGNKEADFNKEKDLKEDDEEEI-EEADEIEKIDKDDIEREIPNNNMAGKN---NDIIDDKLDKDE 1923
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
534-860 |
8.75e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 534 QELNESLNKVSLLKDELQCAHVQTGDSEREKQELQQELKEAQElaiSSKQKCFEMQALLEEERKTAKKQVEESTRQIQAL 613
Cdd:COG4717 135 EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQE---ELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 614 QAHLHKLQKDIEILREdkEIEIIETRDQLASTHKEIVALRQTAVEAATgresdIAILQGELHKVQTELEQWRQTASEYES 693
Cdd:COG4717 212 EEELEEAQEELEELEE--ELEQLENELEAAALEERLKEARLLLLIAAA-----LLALLGLGGSLLSLILTIAGVLFLVLG 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 694 EIFNLQTKLQLQTQQQKDKQkgEAVQLQGKLDELQKQSngLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDA 773
Cdd:COG4717 285 LLALLFLLLAREKASLGKEA--EELQALPALEELEEEE--LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 774 SGLEVSRKALEVE-------VGTLKE-----QRLQETNGLRVKLAHAENETQKFQKQYEA--DQTMYLELKEKLDKTQKE 839
Cdd:COG4717 361 EELQLEELEQEIAallaeagVEDEEElraalEQAEEYQELKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEE 440
|
330 340
....*....|....*....|.
gi 1952581426 840 NESITDELENCKENLKLLQQK 860
Cdd:COG4717 441 LEELEEELEELREELAELEAE 461
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
165-393 |
8.89e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 8.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 165 QELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWqALIDEDRLLSRLEVMGNQLQAYSKNQTE-DGIRKELV 243
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-DEIDVASAEREIAELEAELERLDASSDDlAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 244 TLQEDkhsyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLK----EMNDRTQEELRELANKYNGAVNE---- 315
Cdd:COG4913 696 ELEAE-----------LEELEEELDELKGEIGRLEKELEQAEEELDELQdrleAAEDLARLELRALLEERFAAALGdave 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581426 316 ---LKEFTEKLKQAEGKQEEIQQKAL-----------SEKKELQHRIDEMEEKEQLLQaRIEA----------LQADNDF 371
Cdd:COG4913 765 relRENLEERIDALRARLNRAEEELEramrafnrewpAETADLDADLESLPEYLALLD-RLEEdglpeyeerfKELLNEN 843
|
250 260
....*....|....*....|..
gi 1952581426 372 TNERLTALQVRLEQlQEKNIKD 393
Cdd:COG4913 844 SIEFVADLLSKLRR-AIREIKE 864
|
|
| |
