|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
3-132 |
1.51e-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: 251.80 E-value: 1.51e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 3 SALAIFTCRPNSHPFQERHVYLDEPIKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINS 82
Cdd:cd22679 1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 530373136 83 QRLSRGSEESPPCEILSGDIIQFGVDVTENTRKgtVTHGCIVSTIKLFLP 132
Cdd:cd22679 79 QRLSKGSEESEPRELHSGDIVQFGVDVVENSRK--VTHGCIVATVTLFLP 126
|
|
| CC1_SLMAP |
cd21911 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal ... |
165-227 |
1.79e-26 |
|
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: 102.76 E-value: 1.79e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530373136 165 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQ 227
Cdd:cd21911 1 QELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQLS 63
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
158-797 |
8.75e-22 |
|
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: 101.67 E-value: 8.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 158 NTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQA--CSKNQTE 235
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvAQLELQI 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 236 DSLRKELIAL------QEDKHNYETTAKESLRRVLQE--KIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELAN 307
Cdd:TIGR02168 396 ASLNNEIERLearlerLEDRRERLQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 308 KYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKidemEEKEQELQAKIEALQADNDFTNERLTALQGIqVDDF 387
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ----SGLSGILGVLSELISVDEGYEAAIEAALGGR-LQAV 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 388 LPKINGSTEK--EHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSP--SKEKSSDD 463
Cdd:TIGR02168 551 VVENLNAAKKaiAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllGGVLVVDD 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 464 TTDAQMDEQDLNEPLAKVSL-----------LKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFEL---QALL 529
Cdd:TIGR02168 631 LDNALELAKKLRPGYRIVTLdgdlvrpggviTGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELrkeLEEL 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 530 EEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEkdseITSTRDELLSARDEILLLHQAAAKV---ASERDTDIAS 606
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER----IAQLSKELTELEAEIEELEERLEEAeeeLAEAEAEIEE 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 607 LQEELKKVRAELERWRKAASEYEKEITSLQNSF---QLRCQQCEDQQREEATRL----------QGELEKLRKEWNALET 673
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATERRLedleeqieelSEDIESLAAEIEELEE 866
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 674 ECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHlrdsADLKTLLSKAENQAKDVQ 753
Cdd:TIGR02168 867 LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL----AQLELRLEGLEVRIDNLQ 942
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 530373136 754 keyektQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 797
Cdd:TIGR02168 943 ------ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| FHA_DMA-like |
cd22692 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest ... |
27-108 |
1.85e-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: 82.62 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 27 PIKIGRSVARCRPAQNNAT-FDCKVLSRNHALVWfdHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQF 105
Cdd:cd22692 38 QIHIGRYTERVRQAIYHPVvFKSKVVSRTHGCIK--VDEGNWYIKDVKSSSGTFLNHQRLSPASRTSKPYPLRDGDILQL 115
|
...
gi 530373136 106 GVD 108
Cdd:cd22692 116 GMD 118
|
|
| FHA_VPS64-like |
cd22695 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ... |
6-109 |
7.87e-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: 74.65 E-value: 7.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 6 AIFTCRPNSHPFQERHV---YLDEPIKIGRSVARCRPAQN---------------NATFDCKVLSRNHALVWFDHKTGKF 67
Cdd:cd22695 2 HILVLKSLNATFETKFLvvpFKPDGLKLGRPVTNSVNKNNsgskrdlfsqqvrpdNGNFDSRVLSRNHACLSCDPTTGKV 81
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 530373136 68 YLQDTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFGVDV 109
Cdd:cd22695 82 YIRDLKSSNGTFVNGQKIRQND-----VELKVGDEVDLGTDI 118
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
13-106 |
5.19e-14 |
|
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: 68.07 E-value: 5.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 13 NSHPFQERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINSQRLsrgseeS 92
Cdd:cd00060 6 DGDGGGREFPLTKGVVTIGRS------PDCDIVLDDPSVSRRHARIEVDG--GGVYLEDLGSTNGTFVNGKRI------T 71
|
90
....*....|....
gi 530373136 93 PPCEILSGDIIQFG 106
Cdd:cd00060 72 PPVPLQDGDVIRLG 85
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
174-797 |
8.14e-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: 75.86 E-value: 8.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 174 LQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRllsrlevmgnqlqacSKNQTEDSLRKELIALQEDKHNYE 253
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS---------------ELEEEIEELQKELYALANEISRLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 254 ttakeslrrvlQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEI 333
Cdd:TIGR02168 302 -----------QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 334 QQKGQAEKKELQH---KIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQvddflpkingsteKEHLLSKSGGDCTF 410
Cdd:TIGR02168 371 ESRLEELEEQLETlrsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI-------------EELLKKLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 411 IHQFIECQKKLIVEGHLTKAVEETKLSK-ENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLK---- 485
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEElREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKnqsg 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 486 -DDLQGAQSEI----------------------------EAKQEIQHLRKE----------------LIEAQELARTSKQ 520
Cdd:TIGR02168 518 lSGILGVLSELisvdegyeaaieaalggrlqavvvenlnAAKKAIAFLKQNelgrvtflpldsikgtEIQGNDREILKNI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 521 KCFELQAL-LEEERKAYRNQVE--------------------------------------------ESTKQIQVLQAQLQ 555
Cdd:TIGR02168 598 EGFLGVAKdLVKFDPKLRKALSyllggvlvvddldnalelakklrpgyrivtldgdlvrpggvitgGSAKTNSSILERRR 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 556 RLHIDTENLR--EEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEIT 633
Cdd:TIGR02168 678 EIEELEEKIEelEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 634 SLQNSFQLRCQQCEdQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSIL 713
Cdd:TIGR02168 758 ELEAEIEELEERLE-EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 714 QMSRKELENQVGSLKEQHLRDSA---DLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNN 790
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAeieELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
....*..
gi 530373136 791 LKLLREK 797
Cdd:TIGR02168 917 LEELREK 923
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
28-105 |
1.52e-13 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 66.06 E-value: 1.52e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530373136 28 IKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRLSRgseesPPCEILSGDIIQF 105
Cdd:pfam00498 1 VTIGRS------PDCDIVLDDPSVSRRHAEIRYD-GGGRFYLEDLGSTNGTFVNGQRLGP-----EPVRLKDGDVIRL 66
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
500-797 |
2.16e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 74.33 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 500 EIQHLRKELIEAQELARTSKQKCFELQALLEEERKA----YRNQVEESTKQIQVLQAQLQRLhidtENLREEKDSEITST 575
Cdd:TIGR02169 188 RLDLIIDEKRQQLERLRREREKAERYQALLKEKREYegyeLLKEKEALERQKEAIERQLASL----EEELEKLTEEISEL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 576 RDELLSARDeilLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNsfQLRCQQCE-DQQREEA 654
Cdd:TIGR02169 264 EKRLEEIEQ---LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE--RLAKLEAEiDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 655 TRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRD 734
Cdd:TIGR02169 339 EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL 418
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530373136 735 SADlktlLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 797
Cdd:TIGR02169 419 SEE----LADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
479-776 |
2.21e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 479 AKVSLLKDDLQGAQSEiEAKQEIQHLRKELIEAQELartskqkcfelQALLEEERKAYRNQVEESTKQIQVLQAQLQRLH 558
Cdd:COG1196 227 AELLLLKLRELEAELE-ELEAELEELEAELEELEAE-----------LAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 559 IDTENLREEKDSEitstRDELLSARDEILLLHQAAAKVASErdtdIASLQEELKKVRAELERWRKAASEYEKEITSLQNS 638
Cdd:COG1196 295 AELARLEQDIARL----EERRRELEERLEELEEELAELEEE----LEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 639 FQLRCQQCEDQQREEATRLQGELEKLRKEwNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRK 718
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAA-AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 530373136 719 ELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQE 776
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
241-783 |
6.74e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.87 E-value: 6.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 241 ELIALQEDKHNYETTAKESLRRV--LQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKD 318
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 319 LSDKLKVAEGKQEEIQQKGQAEKK--ELQHKIDEMEEKEQELQAKIEALQadndftnerltalqgiqvddflpKINGSTE 396
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELK-----------------------KAAAAKK 1418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 397 KEHLLSKSGgdctfihqfiECQKKlivEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKE--KSSDDTTDAQMDEQDL 474
Cdd:PTZ00121 1419 KADEAKKKA----------EEKKK---ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEeaKKADEAKKKAEEAKKA 1485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 475 NEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRK--ELIEAQELARTSKQKCFELQALLEEERKAYR-NQVEESTKQIQVLQ 551
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKaeEAKKADEAKKAEEAKKADEAKKAEEKKKADElKKAEELKKAEEKKK 1565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 552 AQLQRlhidtenlREEKDSEITSTRDELLSardeilllhqaaaKVASERDTDIASLQEELKKVRAE----LERWRKAASE 627
Cdd:PTZ00121 1566 AEEAK--------KAEEDKNMALRKAEEAK-------------KAEEARIEEVMKLYEEEKKMKAEeakkAEEAKIKAEE 1624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 628 YEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELT 707
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA 1704
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530373136 708 SDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYE---KTQTVLSELKLKFEMTEQEKQSITDE 783
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEekkKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| CC1_SLMAP-like |
cd21868 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ... |
169-206 |
1.02e-12 |
|
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: 62.89 E-value: 1.02e-12
10 20 30
....*....|....*....|....*....|....*...
gi 530373136 169 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 206
Cdd:cd21868 1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
14-106 |
1.19e-11 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 61.51 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 14 SHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716 8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
|
90
....*....|....
gi 530373136 93 pPCEILSGDIIQFG 106
Cdd:COG1716 75 -PAPLRDGDVIRLG 87
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
237-789 |
1.39e-11 |
|
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: 68.12 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 237 SLRKELIALQEDKHNYETTAKE--SLRRVLQEKIEVVRKLSEVERSLsntEDECTHLKEMNERTQEELRELANKYNGAVN 314
Cdd:TIGR04523 170 ELENELNLLEKEKLNIQKNIDKikNKLLKLELLLSNLKKKIQKNKSL---ESQISELKKQNNQLKDNIEKKQQEINEKTT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 315 EIKDLSDKLKVAEGKQEEIQQKGQAEKKELQH---KIDEMEEKEQELQAKIEALQadndftnerltalqgiqvddflpki 391
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLN------------------------- 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 392 ngsTEKEHLLSKSggdctfIHQFIECQKKLIVEghltkavEETKLSKENQtraKESDFSDTLSPSKEKSSDDTTDAQMDE 471
Cdd:TIGR04523 302 ---NQKEQDWNKE------LKSELKNQEKKLEE-------IQNQISQNNK---IISQLNEQISQLKKELTNSESENSEKQ 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 472 QDLNEPLAKVSLLKDDLQGAQSEIEA-KQEIQHLRKELIEAQELArtskqkcfelqALLEEERKAYRNQVEESTKQIQVL 550
Cdd:TIGR04523 363 RELEEKQNEIEKLKKENQSYKQEIKNlESQINDLESKIQNQEKLN-----------QQKDEQIKKLQQEKELLEKEIERL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 551 QAQLQRLHIDTENLrEEKDSEITSTRDELLSARDEIlllhqaaakvaserDTDIASLQEELKKVRAELERWRKAASEYEK 630
Cdd:TIGR04523 432 KETIIKNNSEIKDL-TNQDSVKELIIKNLDNTRESL--------------ETQLKVLSRSINKIKQNLEQKQKELKSKEK 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 631 EITSLQNSFQLRCQQCEDQQREEATRLQGElEKLRKEWNALETECHSLKRENVLLSSELQRQ--EKELHNSQKQSLELTS 708
Cdd:TIGR04523 497 ELKKLNEEKKELEEKVKDLTKKISSLKEKI-EKLESEKKEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQ 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 709 DLSILQMSRKELENQVGSLKEQHL---RDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELK 785
Cdd:TIGR04523 576 TQKSLKKKQEEKQELIDQKEKEKKdliKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIK 655
|
....
gi 530373136 786 QCKN 789
Cdd:TIGR04523 656 EIRN 659
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
52-106 |
1.46e-11 |
|
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 (AGGF1) and similar proteins; AGGF1, also called angiogenic factor VG5Q, or G patch domain-containing protein 7 (GPATC7), or vasculogenesis gene on 5q protein, is an angiogenic factor involved in vascular development, angiogenesis, specification of hemangioblasts, and differentiation of veins. It promotes angiogenesis and the proliferation of endothelial cells. It inhibits inflammatory effect and preserve vascular integrity in non-nervous system diseases. Mutated AGGF1 causes susceptibility to Klippel-Trenaunay syndrome, a vascular disorder. Increased AGGF1 expression is associated with tumor angiogenesis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438738 [Multi-domain] Cd Length: 123 Bit Score: 62.30 E-value: 1.46e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 530373136 52 SRNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQFG 106
Cdd:cd22686 48 SKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPYPLTHGDELKIG 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
524-786 |
1.50e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 524 ELQALLEE-ERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREE---KDSEITSTRDELLSARDEILLLHQAAAKVASE 599
Cdd:COG1196 217 ELKEELKElEAELLLLKLRELEAELEELEAELEELEAELEELEAElaeLEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 600 rdtdIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQcEDQQREEATRLQGELEKLRKEWNALETECHSLK 679
Cdd:COG1196 297 ----LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE-LEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 680 RENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKT 759
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260
....*....|....*....|....*..
gi 530373136 760 QTVLSELKLKFEMTEQEKQSITDELKQ 786
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAA 478
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
471-796 |
5.93e-11 |
|
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: 66.63 E-value: 5.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 471 EQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCfelqalLEEERKAYRNQVEESTKQIQVL 550
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEA------LERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 551 QAQLQ-----------RLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASER---DTDIASLQEELKKVRA 616
Cdd:TIGR02169 257 TEEISelekrleeieqLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELedaEERLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 617 ELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQRE------EATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQ 690
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEleevdkEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 691 RQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADlktlLSKAENQAKDVQKEYEKTQTVLSELKLKF 770
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD----LSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
330 340
....*....|....*....|....*.
gi 530373136 771 EMTEQEKQSITDELKQCKNNLKLLRE 796
Cdd:TIGR02169 493 AEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
199-786 |
7.28e-11 |
|
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: 66.24 E-value: 7.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 199 QEASDTSWQALIDEDRLLSRLEVMGNQLQacsknqtedSLRKELIALQEDKHNYETTAKESLRRVLQEKI---EVVRKLS 275
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIE---------EERKRRDKLTEEYAELKEELEDLRAELEEVDKefaETRDELK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 276 EVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIqqkgQAEKKELQHKIDEMEEKE 355
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK----ALEIKKQEWKLEQLAADL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 356 QELQAKIEALQADNDFTNERLTALQG------IQVDDFLPKINGSTEKEHLLSKS-GGDCTFIHQFIECQKK-------- 420
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELSKLQRelaeaeAQARASEERVRGGRAVEEVLKASiQGVHGTVAQLGSVGERyataieva 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 421 -------LIVEGHLTkAVEETKLSKE-----------NQTRAKESDfsdtLSPSKEK----------------------- 459
Cdd:TIGR02169 545 agnrlnnVVVEDDAV-AKEAIELLKRrkagratflplNKMRDERRD----LSILSEDgvigfavdlvefdpkyepafkyv 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 460 -------SSDDTTDAQMD-------EQDLNEP--------LAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELART 517
Cdd:TIGR02169 620 fgdtlvvEDIEAARRLMGkyrmvtlEGELFEKsgamtggsRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRR 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 518 SKQKCFELQALLEEERKayrnQVEESTKQIQVLQAQLQRLHIDTENLREekdsEITSTRDELLSARDEIlllhQAAAKVA 597
Cdd:TIGR02169 700 IENRLDELSQELSDASR----KIGEIEKEIEQLEQEEEKLKERLEELEE----DLSSLEQEIENVKSEL----KELEARI 767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 598 SERDTDIASLQEELKKVRAEL--ERWRKAASEYEKEITSLQnsfqlrcqqcedQQREEATRLQGELEKLRKEWNALETEC 675
Cdd:TIGR02169 768 EELEEDLHKLEEALNDLEARLshSRIPEIQAELSKLEEEVS------------RIEARLREIEQKLNRLTLEKEYLEKEI 835
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 676 HSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKeqhlRDSADLKTLLSKAENQAKDVQKE 755
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK----KERDELEAQLRELERKIEELEAQ 911
|
650 660 670
....*....|....*....|....*....|.
gi 530373136 756 YEKTQTVLSELKLKFEMTEQEKQSITDELKQ 786
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEELSEIEDPKGE 942
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
524-797 |
1.52e-10 |
|
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: 65.08 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 524 ELQALLEEERKAYRNQVEE-----STKQIQVLQAQLQRLHIDTENLREEKDsEITSTRDELLSARDEILLLHQAAAKVAS 598
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRElelalLVLRLEELREELEELQEELKEAEEELE-ELTAELQELEEKLEELRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 599 ERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQlRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSL 678
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE-ELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 679 KRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKA-ENQAKDVQKEYE 757
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELE 443
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 530373136 758 KTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 797
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
269-797 |
3.21e-10 |
|
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: 63.89 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 269 EVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKI 348
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 349 DEMEEKEQELqAKIEALQADNDftnerltalqgIQVDDFLPKIngsTEKEHLLSKSGGDCTFIHQFIECQKKlivEGHLT 428
Cdd:TIGR04523 117 EQKNKLEVEL-NKLEKQKKENK-----------KNIDKFLTEI---KKKEKELEKLNNKYNDLKKQKEELEN---ELNLL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 429 KAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDaqmdEQDLNEPLAKVSLLKDDLQgaqseiEAKQEIQHLRKEL 508
Cdd:TIGR04523 179 EKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSL----ESQISELKKQNNQLKDNIE------KKQQEINEKTTEI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 509 IEAQELARTSKQKCFELQALLEEERKayrnQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILl 588
Cdd:TIGR04523 249 SNTQTQLNQLKDEQNKIKKQLSEKQK----ELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKL- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 589 lhQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNsfqlrcqQCEDQQREEATRLQgELEKLRKEW 668
Cdd:TIGR04523 324 --EEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQN-------EIEKLKKENQSYKQ-EIKNLESQI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 669 NALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHlrdsADLKTLLSKAENQ 748
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELII----KNLDNTRESLETQ 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 530373136 749 AKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 797
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
548-796 |
5.13e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 548 QVLQAQLQRLHIdteNLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASE 627
Cdd:COG1196 216 RELKEELKELEA---ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 628 YEKEITSLQNSFQLRCQQCEDQQREEAtRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELT 707
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLE-ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 708 SDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQC 787
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
....*....
gi 530373136 788 KNNLKLLRE 796
Cdd:COG1196 452 AELEEEEEA 460
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
486-705 |
9.21e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.63 E-value: 9.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 486 DDLQGAQSEIE-AKQEIQHLRkELIEAQELARTSKQKCFELQALLEeerkayRNQVEESTKQIQVLQAQLQRLhidtENL 564
Cdd:COG4913 235 DDLERAHEALEdAREQIELLE-PIRELAERYAAARERLAELEYLRA------ALRLWFAQRRLELLEAELEEL----RAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 565 REEKDSEITSTRDELLSARDEILLLHQAAAKVASERdtdIASLQEELKKVRAELERWRKAASEYEKEITSLQNSfqlrcq 644
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRGNGGDR---LEQLEREIERLERELEERERRRARLEALLAALGLP------ 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530373136 645 qcEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNsQKQSLE 705
Cdd:COG4913 375 --LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA-EIASLE 432
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
163-767 |
1.90e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 61.67 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 163 YSQELFQLSQYLQEA--LHREQ--MLEQKLATLQRLLAITQEASDtswqALIDedrlLSRLEvmgNQLQACSKNQTEDSL 238
Cdd:pfam15921 83 YSHQVKDLQRRLNESneLHEKQkfYLRQSVIDLQTKLQEMQMERD----AMAD----IRRRE---SQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 239 RKELIA--LQEDKHNYETTAKESLRR-------VLQEKIEVVRKLSEVERSLSNTEDECT--HLKEMNERTQEELRELAN 307
Cdd:pfam15921 152 HELEAAkcLKEDMLEDSNTQIEQLRKmmlshegVLQEIRSILVDFEEASGKKIYEHDSMStmHFRSLGSAISKILRELDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 308 KYNGAVNEIKDLSDKLKVAEGK-QEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDD 386
Cdd:pfam15921 232 EISYLKGRIFPVEDQLEALKSEsQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 387 FLPKINGSTEKEHLLSKSGGDC-----TFIHQFIECQKKLIV-EGHLTKA-VEETKLSKE--NQTRAKESDFSDTLSPSK 457
Cdd:pfam15921 312 NSMYMRQLSDLESTVSQLRSELreakrMYEDKIEELEKQLVLaNSELTEArTERDQFSQEsgNLDDQLQKLLADLHKREK 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 458 EKSSDDTTDAQMDEQDLNEPLAKVSLLK--DDLQGAQSEIEA-----KQEIQHLRKELIEAQELARTSKQKCFELQALLE 530
Cdd:pfam15921 392 ELSLEKEQNKRLWDRDTGNSITIDHLRRelDDRNMEVQRLEAllkamKSECQGQMERQMAAIQGKNESLEKVSSLTAQLE 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 531 EERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLrEEKDSEITSTRDELLSARDEILLLHQAAAKVASERDtdiaslqeE 610
Cdd:pfam15921 472 STKEMLRKVVEELTAKKMTLESSERTVSDLTASL-QEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGD--------H 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 611 LKKVRAELERWRKAASEYEKEITSLQNSFQlRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLK----------R 680
Cdd:pfam15921 543 LRNVQTECEALKLQMAEKDKVIEILRQQIE-NMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKilkdkkdakiR 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 681 ENVLLSSELQRQEKELHNSQKQSLELTSD--------LSILQMSRKELEN---QVGSLKEQHLRDSADLKTLLSKAENQA 749
Cdd:pfam15921 622 ELEARVSDLELEKVKLVNAGSERLRAVKDikqerdqlLNEVKTSRNELNSlseDYEVLKRNFRNKSEEMETTTNKLKMQL 701
|
650
....*....|....*...
gi 530373136 750 KDVQKEYEKTQTVLSELK 767
Cdd:pfam15921 702 KSAQSELEQTRNTLKSME 719
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
230-706 |
1.91e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 230 SKNQTEDSLRKELIALQEDKHNYETTAKEsLRRVLQEKIEVVRKLSEVERSlsntEDECTHLKEMNERTQEELRELANKY 309
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEE-LKKEIEELEEKVKELKELKEK----AEEYIKLSEFYEEYLDELREIEKRL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 310 NGAVNEIKDLSDKLKVAEGKQEEIQqKGQAEKKELQHKIDEMEEKEQELQaKIEALQADNDFTNERLTALQGIQVDDFLP 389
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEKLEKELE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 390 KI-NGSTEKEHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKAV---------EETKLSKENQTRAKESDFSDTLSPSKEK 459
Cdd:PRK03918 395 ELeKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEK 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 460 SSDdttdAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQ-ELARTSKQKCFELQALLE------EE 532
Cdd:PRK03918 475 ERK----LRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKaEEYEKLKEKLIKLKGEIKslkkelEK 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 533 RKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDtDIASLQEELK 612
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEK-ELKKLEEELD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 613 KVRAELERWRKAASEYEKEITSLQNSFqlrcqqcedqQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQ 692
Cdd:PRK03918 630 KAFEELAETEKRLEELRKELEELEKKY----------SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
490
....*....|....
gi 530373136 693 EKELHNSQKQSLEL 706
Cdd:PRK03918 700 KEELEEREKAKKEL 713
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
300-796 |
2.44e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.21 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 300 EELRELANKYNGAVNEIkdLSDKLKVAEGKQEEIQQKgqaEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTAL 379
Cdd:PRK02224 165 EEYRERASDARLGVERV--LSDQRGSLDQLKAQIEEK---EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 380 QGIqvddflpkingstekehllsksggdctfIHQFIECQKKLIVeghLTKAVEETKLSKENQTRAKEsDFSDTLSPSKEK 459
Cdd:PRK02224 240 DEV----------------------------LEEHEERREELET---LEAEIEDLRETIAETERERE-ELAEEVRDLRER 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 460 SSD--DTTDAQMDEQDLNEPLAK-VSLLKDDLQGAQSEIE------------AKQEIQHLRKELIEAQELARTSKQKCFE 524
Cdd:PRK02224 288 LEEleEERDDLLAEAGLDDADAEaVEARREELEDRDEELRdrleecrvaaqaHNEEAESLREDADDLEERAEELREEAAE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 525 LQALLEEERKA---YRNQVEESTKQIQVLQAQLQRLHIDTEN-------LREEKD---SEITSTRDELLSARDEI----- 586
Cdd:PRK02224 368 LESELEEAREAvedRREEIEELEEEIEELRERFGDAPVDLGNaedfleeLREERDelrEREAELEATLRTARERVeeaea 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 587 LLlhqAAAK---------------VASERDTDIASLQEELKKVRAELERWR------KAASEYEKEITSLQNSFQlRCQQ 645
Cdd:PRK02224 448 LL---EAGKcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEerleraEDLVEAEDRIERLEERRE-DLEE 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 646 CEDQQREEATRLQGELEKLRKEWNALETECHSlKRE---NVLLSSELQRQEKELHNSQ----KQSLELTSDLSILQMSRK 718
Cdd:PRK02224 524 LIAERRETIEEKRERAEELRERAAELEAEAEE-KREaaaEAEEEAEEAREEVAELNSKlaelKERIESLERIRTLLAAIA 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 719 ELENQVGSLKEQ-------------HLRDSADLKTLLSKA--ENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDE 783
Cdd:PRK02224 603 DAEDEIERLREKrealaelnderreRLAEKRERKRELEAEfdEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAE 682
|
570
....*....|...
gi 530373136 784 LKQCKNNLKLLRE 796
Cdd:PRK02224 683 IGAVENELEELEE 695
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
257-797 |
2.46e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 257 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNgAVNEIKDLSDKLKVAEGKQEEIQQK 336
Cdd:PRK03918 178 IERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 337 GQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTaLQGIQVDDFLPKINGSTEKEHLLSKSGGdctFIHQFIE 416
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEING---IEERIKE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 417 CQKKLIVEGHLTKAVEETKlSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIE 496
Cdd:PRK03918 333 LEEKEERLEELKKKLKELE-KRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKIT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 497 AKQ-EIQHLRKELIEAQELARTSKQKCFELQALLEEERKAyrNQVEESTKQIQVLQAQLQRLHIDTENLREEKdseitST 575
Cdd:PRK03918 412 ARIgELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRK--ELLEEYTAELKRIEKELKEIEEKERKLRKEL-----RE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 576 RDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFqlrcqqcedqqrEEAT 655
Cdd:PRK03918 485 LEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL------------EKLE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 656 RLQGELEKLRKEWNALETECHSLKRENVLLS----SELQRQEKELHNSQKQSLELT---SDLSILQMSRKELENQVGSLK 728
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAELLKELEELGfesvEELEERLKELEPFYNEYLELKdaeKELEREEKELKKLEEELDKAF 632
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530373136 729 EQHLRDSADLKTLLSK--------AENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 797
Cdd:PRK03918 633 EELAETEKRLEELRKEleelekkySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
252-797 |
4.36e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 252 YETTAKES--LRRVLQEKIEVVRKL----SEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLsDKLKV 325
Cdd:PRK03918 160 YENAYKNLgeVIKEIKRRIERLEKFikrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-EELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 326 AEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQAdndfTNERLTALQG-----IQVDDFLPKIN-GSTEKEH 399
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE----KVKELKELKEkaeeyIKLSEFYEEYLdELREIEK 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 400 LLSKSGGDCTFIHQFI-ECQKKLIVEGHLTKAVEETKlSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPL 478
Cdd:PRK03918 315 RLSRLEEEINGIEERIkELEEKEERLEELKKKLKELE-KRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 479 AKVSLLKDDLQGAQSEIEAKQ-EIQHLRKELIEAQELARTSKQKCFELQALLEEERKAyrNQVEESTKQIQVLQAQLQRL 557
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIgELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRK--ELLEEYTAELKRIEKELKEI 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 558 HIDTENLREEKdseitSTRDELLSARDEILLLHQAAAKvaserdtdIASLQEELKKVraELERWRKAASEYEKeitslqn 637
Cdd:PRK03918 472 EEKERKLRKEL-----RELEKVLKKESELIKLKELAEQ--------LKELEEKLKKY--NLEELEKKAEEYEK------- 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 638 sfqlrcqqcedqQREEATRLQGELEKLRKEWNALEtechSLKRENVLLSSELQRQEKELHNSQKQSLELT-SDLSILQMS 716
Cdd:PRK03918 530 ------------LKEKLIKLKGEIKSLKKELEKLE----ELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEER 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 717 RKELE---NQVGSLK------EQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFemTEQEKQSITDELKQC 787
Cdd:PRK03918 594 LKELEpfyNEYLELKdaekelEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY--SEEEYEELREEYLEL 671
|
570
....*....|
gi 530373136 788 KNNLKLLREK 797
Cdd:PRK03918 672 SRELAGLRAE 681
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
169-620 |
4.63e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 169 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQAC--SKNQTEDSLRKELIALQ 246
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAElaEAEEELEELAEELLEAL 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 247 EDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVA 326
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 327 EGKQEEIQQ-KGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDDF-------------LPKIN 392
Cdd:COG1196 473 ALLEAALAElLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAayeaaleaalaaaLQNIV 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 393 GSTEK------EHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKAVEETKLSKENQTR---AKESDFSDTLspskeksSDD 463
Cdd:COG1196 553 VEDDEvaaaaiEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLReadARYYVLGDTL-------LGR 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 464 TTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEES 543
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE 705
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530373136 544 TKQIQVLQAQLQRLHIDTENLREEKDSEitstRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELER 620
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAE----REELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| CC1_T3JAM |
cd21912 |
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ... |
166-206 |
7.27e-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: 51.96 E-value: 7.27e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 530373136 166 ELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 206
Cdd:cd21912 5 EILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
169-619 |
8.76e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 8.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 169 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQAcsKNQTEDSLRKELIALQED 248
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE--LEEAEEALLERLERLEEE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 249 KhnyeTTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEG 328
Cdd:COG1196 423 L----EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 329 KQEEIQQKGQAEKKelQHKIDEMEEKEQELQAKIEALQADNDFTNERLTA-LQGIQVDDFLpkiNGSTEKEHLLSKSGGD 407
Cdd:COG1196 499 AEADYEGFLEGVKA--ALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAaLQNIVVEDDE---VAAAAIEYLKAAKAGR 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 408 CTFIHQFIECQKKLIVEGHLTKAVEETKLSKENQTR---AKESDFSDTLSpskekssDDTTDAQMDEQDLNEPLAKVSLL 484
Cdd:COG1196 574 ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLReadARYYVLGDTLL-------GRTLVAARLEAALRRAVTLAGRL 646
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 485 KDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENL 564
Cdd:COG1196 647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL 726
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 530373136 565 REEKDSEitstRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKV---RAELE 619
Cdd:COG1196 727 EEQLEAE----REELLEELLEEEELLEEEALEELPEPPDLEELERELERLereIEALG 780
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
98-739 |
1.65e-08 |
|
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: 58.59 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 98 LSGDIIQFGVDVTENTRKGTVTHGCIVSTIKLFLPDGMEARLRSDVIHAPLPSPVDKVAANTPSMYSQELFQLSQYLQEA 177
Cdd:pfam15921 160 LKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGR 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 178 LHR-EQMLEQKLATLQRLLAITQEASDTSWQALIDEdrllSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTa 256
Cdd:pfam15921 240 IFPvEDQLEALKSESQNKIELLLQQHQDRIEQLISE----HEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSM- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 257 keslrrvlqekieVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQK 336
Cdd:pfam15921 315 -------------YMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQK 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 337 GQAEKKELQHKIDEMEEKEQELQAK-------IEALQADNDFTN---ERLTAL--------QGiQVDDFLPKINGSTEKE 398
Cdd:pfam15921 382 LLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNmevQRLEALlkamksecQG-QMERQMAAIQGKNESL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 399 HLLSKsggdctfIHQFIECQKKLiveghLTKAVEETKlSKENQTRAKESDFSDTLSPSKEKS-SDDTTDAQMDE--QDLN 475
Cdd:pfam15921 461 EKVSS-------LTAQLESTKEM-----LRKVVEELT-AKKMTLESSERTVSDLTASLQEKErAIEATNAEITKlrSRVD 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 476 EPLAKVSLLK---DDLQGAQSEIEA---------------KQEI--------QHLRKE---LIEAQELARTSKQKCFELQ 526
Cdd:pfam15921 528 LKLQELQHLKnegDHLRNVQTECEAlklqmaekdkvieilRQQIenmtqlvgQHGRTAgamQVEKAQLEKEINDRRLELQ 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 527 AL--LEEERKAYRNQVEESTKQIQVLQAQLqrLHIDTENLREEKD---------SEITSTRDELLSARDEILLLHQAAAK 595
Cdd:pfam15921 608 EFkiLKDKKDAKIRELEARVSDLELEKVKL--VNAGSERLRAVKDikqerdqllNEVKTSRNELNSLSEDYEVLKRNFRN 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 596 VASERDTDIASLQEELKKVRAELERWR--------------KAASEYEKEITSLQNsfQLRCQQCEDQQREEATR----- 656
Cdd:pfam15921 686 KSEEMETTTNKLKMQLKSAQSELEQTRntlksmegsdghamKVAMGMQKQITAKRG--QIDALQSKIQFLEEAMTnanke 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 657 ---LQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQ----KQSLELTSDLSILQmsRKELENQvgSLKE 729
Cdd:pfam15921 764 khfLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEvaldKASLQFAECQDIIQ--RQEQESV--RLKL 839
|
730
....*....|
gi 530373136 730 QHLRDSADLK 739
Cdd:pfam15921 840 QHTLDVKELQ 849
|
|
| FHA_TCF19 |
cd22685 |
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ... |
29-106 |
2.29e-08 |
|
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar proteins; TCF-19, also called transcription factor SC1, was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It also functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. TCF-19 contains an N-terminal fork head association domain (FHA), a proline rich region, and a C-terminal plant homeodomain (PHD) finger. The FHA domain may serve as a nuclear signaling domain or as a phosphoprotein binding domain. The proline rich region is a common characteristic of trans-activating factors. The PHD finger may allow TCF-19 to interact with chromatin via methylated histone H3.
Pssm-ID: 438737 [Multi-domain] Cd Length: 130 Bit Score: 53.19 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 29 KIGRSVARCRPAQNNATFDcKVLSRNHALVW---FDHKTGKFYLQDTkSSNGTFINSQRLSRGSEEsppcEILSGDIIQF 105
Cdd:cd22685 31 RIGRNPEVCDVFLCSSQHP-NLISREHAEIHaerDGNGNWKVLIEDR-STNGTYVNDVRLQDGQRR----ELSDGDTITF 104
|
.
gi 530373136 106 G 106
Cdd:cd22685 105 G 105
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
214-796 |
2.40e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 58.13 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 214 RLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTAKESLRRVLQEKIEvvrkLSEVERSlSNTEDECTHLKE 293
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE----LDGFERG-PFSERQIKNFHT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 294 MNERTQEELRELANKyngavnEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQadndftn 373
Cdd:TIGR00606 398 LVIERQEDEAKTAAQ------LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ------- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 374 eRLTAlqgiQVDDFLPKINGSTEKEHLLSKSGGDCTfihqfIECQKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTL 453
Cdd:TIGR00606 465 -QLEG----SSDRILELDQELRKAERELSKAEKNSL-----TETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTR 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 454 SpSKEKSSDDTTDAQMDEQDLNeplakvSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEER 533
Cdd:TIGR00606 535 T-QMEMLTKDKMDKDEQIRKIK------SRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNK 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 534 KAYRNQVEESTKQIQVLqaqlqrlhidtenlrEEKDSEITSTRDEllsardeilllhqaaakvaserDTDIASLQEELKK 613
Cdd:TIGR00606 608 NHINNELESKEEQLSSY---------------EDKLFDVCGSQDE----------------------ESDLERLKEEIEK 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 614 VRAELERWRKAASEYEKEITSLQNSFQLRCQQC------EDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLL-- 685
Cdd:TIGR00606 651 SSKQRAMLAGATAVYSQFITQLTDENQSCCPVCqrvfqtEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlg 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 686 -----SSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSL--KEQHLRDSADLKTLLSKAENQAKDVQKEYEK 758
Cdd:TIGR00606 731 lapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTImpEEESAKVCLTDVTIMERFQMELKDVERKIAQ 810
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 530373136 759 TQTVL--SELKLKFEMTEQEKQSITDELKQCKNNLKLLRE 796
Cdd:TIGR00606 811 QAAKLqgSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
14-110 |
2.78e-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: 52.23 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 14 SHPFQERHV---YLDEPIKIGRSvARCRPAQNNATfdckvLSRNHALVW---FDHKTG-KFYLQDTkSSNGTFINSQRLS 86
Cdd:cd22670 7 SSPGSTDIVlpiYKNQVITIGRS-PSCDIVINDPF-----VSRTHCRIYsvqFDESSApLVYVEDL-SSNGTYLNGKLIG 79
|
90 100
....*....|....*....|....*
gi 530373136 87 RGseespPCEILS-GDIIQFGVDVT 110
Cdd:cd22670 80 RN-----NTVLLSdGDVIEIAHSAT 99
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
235-786 |
3.40e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 235 EDSLRKELIALQEDKHNYETTAKESLRRVLQEKIEV-VRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAV 313
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEElEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 314 NEIKDLSDKLKVAEGKQEEIQQkgqaEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDDflpking 393
Cdd:COG1196 302 QDIARLEERRRELEERLEELEE----ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA------- 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 394 STEKEHLLSKSggdctfihqfiecQKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQD 473
Cdd:COG1196 371 EAELAEAEEEL-------------EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 474 LNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRN-QVEESTKQIQVLQA 552
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADyEGFLEGVKAALLLA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 553 QLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDtdiasLQEELKKVRAELERWRKAASEYEKEI 632
Cdd:COG1196 518 GLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYL-----KAAKAGRATFLPLDKIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 633 TSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSI 712
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA 672
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530373136 713 LQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 786
Cdd:COG1196 673 ALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
491-730 |
3.89e-08 |
|
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: 56.31 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 491 AQSEIEAKQEIQHLRKELIEAQELARTSKQKcfelQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREekds 570
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 571 EITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQnsfqlrcqqcedQQ 650
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR------------AD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 651 REEATRLQGELEKLRKEWNALETEchsLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQ 730
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAE---LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
28-85 |
4.55e-08 |
|
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.
Pssm-ID: 214578 [Multi-domain] Cd Length: 52 Bit Score: 49.87 E-value: 4.55e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 530373136 28 IKIGRSvarcrPAQNNATFDCKVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRL 85
Cdd:smart00240 1 VTIGRS-----SEDCDIQLDGPSISRRHAVIVYD-GGGRFYLIDLGSTNGTFVNGKRI 52
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
169-368 |
9.73e-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: 55.84 E-value: 9.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 169 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTE-----DSLRKELI 243
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvkselKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 244 ALQEDKHNYETTAKESLRRVLQEKI-EVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDK 322
Cdd:TIGR02169 769 ELEEDLHKLEEALNDLEARLSHSRIpEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 530373136 323 LKVAEGKQEEIQ---QKGQAEKKELQHKIDEMEEKEQELQAKIEALQAD 368
Cdd:TIGR02169 849 IKSIEKEIENLNgkkEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
291-542 |
1.45e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 55.02 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 291 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALqadnd 370
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEEL----- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 371 ftNERLTAL--QGIQVDDFLPKIN----------GSTEKEHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKAVEETKLSK 438
Cdd:PHA02562 240 --TDELLNLvmDIEDPSAALNKLNtaaakikskiEQFQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 439 ENQTRAKEsdfsdtlspskEKSSDDTTDAQMDEQDLNeplAKVSLLKDDLQGAQSEI-EAKQEIQHLRKE-LIEAQELAr 516
Cdd:PHA02562 318 LDTAIDEL-----------EEIMDEFNEQSKKLLELK---NKISTNKQSLITLVDKAkKVKAAIEELQAEfVDNAEELA- 382
|
250 260
....*....|....*....|....*.
gi 530373136 517 tskqkcfELQALLEEERKAYRNQVEE 542
Cdd:PHA02562 383 -------KLQDELDKIVKTKSELVKE 401
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
489-674 |
3.24e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 489 QGAQSEIEAK-QEIQHLRKELIEAQELARTSKQKcfelQALLEEERKAYRNQVEESTKQIQVLQAQLQRlhidtENLREE 567
Cdd:COG4913 606 FDNRAKLAALeAELAELEEELAEAEERLEALEAE----LDALQERREALQRLAEYSWDEIDVASAEREI-----AELEAE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 568 KDsEITSTRDELLSARDEILLLHQAAAKVASERD---TDIASLQEELKKVRAELERWRKAASEYEKEITSLQNS-FQLRC 643
Cdd:COG4913 677 LE-RLDASSDDLAALEEQLEELEAELEELEEELDelkGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERF 755
|
170 180 190
....*....|....*....|....*....|...
gi 530373136 644 QQ--CEDQQREEATRLQGELEKLRKEWNALETE 674
Cdd:COG4913 756 AAalGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
27-106 |
3.69e-07 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 (FKH1), 2 (FKH2) and similar proteins; This family includes FKH1 and FKH2, as well as pre-rRNA-processing protein FHL1. FKH1 and FKH2 are forkhead transcription factors that regulate the expression of the CLB2 cluster of genes during the G2/M phase of the mitotic cell cycle. The CLB2 cluster of genes includes mitotic regulators such as CLB1, CLB2, CDC5 and CDC20, as well as SWI5 and ACE2. FKH1 and FKH2 are involved in HMRa silencing. They associate with the coding regions of active genes and influence, in opposing ways, transcriptional elongation and termination, and coordinate early transcription elongation and pre-mRNA processing. Both FKH1 and FKH2 play a role as regulators of lifespan in collaboration with the anaphase-promoting complex (APC), likely through combined regulation of stress response, genomic stability, and cell cycle regulation. They also function in controlling yeast cell morphology by preventing pseudohyphal growth and act as rate-limiting replication origin activators via their interaction with the origin recognition complex (ORC). FHL1 is a forkhead protein that controls the pre-rRNA processing machinery in conjunction with IFH1. It might act as a transcriptional regulator of genes specifically involved in that process. IFH1 convert FHL1 from a repressor to an activator. This family also includes AtFHA1 and AtFHA2, which may play a role in the control of plant organ development. AtFHA2 is specifically involved in the regulation of stamen development. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438753 [Multi-domain] Cd Length: 106 Bit Score: 49.16 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 27 PIKIGRSVARcRPAQNNATFDC-----KVLSRNHALVWFDHKTGKFYLQdTKSSNGTFINSQRLSRGseeSPPCEILSGD 101
Cdd:cd22701 18 EVVLGRNSKN-SSSTAADSVDIdlgpsKKISRRHARIFYDFTTQCFELS-VLGRNGVKVDGILVKPG---SPPVPLRSGS 92
|
....*
gi 530373136 102 IIQFG 106
Cdd:cd22701 93 LIQIG 97
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
538-702 |
6.37e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 538 NQVEESTKQIQVLQAQLQRLHIDTENLrEEKDSEITSTRDELLSARDEILLLHQAAAKVA-----SERDTDIASLQEELK 612
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEEL-EELEEELEELEAELEELREELEKLEKLLQLLPlyqelEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 613 KVRAELERWRKAASEY---EKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSEL 689
Cdd:COG4717 150 ELEERLEELRELEEELeelEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170
....*....|...
gi 530373136 690 QRQEKELHNSQKQ 702
Cdd:COG4717 230 EQLENELEAAALE 242
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
25-114 |
7.84e-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: 48.51 E-value: 7.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 25 DEPIKIGRSVArcrpAQNNATFDC-KVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDII 103
Cdd:cd22663 20 GKEVTVGRGLG----VTYQLVSTCpLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERI----EPLKPYPLNEGDLI 90
|
90
....*....|.
gi 530373136 104 QFGVDVTENTR 114
Cdd:cd22663 91 QLGVPPENKEP 101
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
26-106 |
1.04e-06 |
|
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438750 [Multi-domain] Cd Length: 93 Bit Score: 47.41 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 26 EPIKIGRSVArcrpaqNNATFDCKVLSRNHALVwfDHKTGKFYLQDTKSSNGTFINSQRLSRGseesppcEILSGDIIQF 105
Cdd:cd22698 21 DEFTIGRSSN------NDIRLNDHSVSRHHARI--VRQGDKCNLTDLGSTNGTFLNGIRVGTH-------ELKHGDRIQL 85
|
.
gi 530373136 106 G 106
Cdd:cd22698 86 G 86
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
55-108 |
1.18e-06 |
|
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) family; The Cep170 family includes Cep170 and Cep170B. Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438756 [Multi-domain] Cd Length: 102 Bit Score: 47.70 E-value: 1.18e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 530373136 55 HALVWFDHKTGKFYLQDTKSSNGTFINSQRLSrgseESPPCEILSGDIIQFGVD 108
Cdd:cd22704 39 HAVITYDQIDNEFKIKDLGSLNGTFVNDSRIP----EQTYITLKLGDSIRFGYD 88
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
265-771 |
1.26e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 52.48 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 265 QEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGA----------VNEIKDLSDKLKVAEGKQEEIQ 334
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAeemrarlaarKQELEEILHELESRLEEEEERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 335 QKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQG--IQVDDFLPKINGSTEK-EHLLSKSGGDCTFI 411
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEdiLLLEDQNSKLSKERKLlEERISEFTSNLAEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 412 HQFIECQKKLIVEGHLTKAVEETKLSKENQTRAKesdfsdtLSPSKEKSSDDTTDAQMDEQDLNEPLA--KVSLLK--DD 487
Cdd:pfam01576 172 EEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQE-------LEKAKRKLEGESTDLQEQIAELQAQIAelRAQLAKkeEE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 488 LQGAQSEIEAKQ-----------EIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQR 556
Cdd:pfam01576 245 LQAALARLEEETaqknnalkkirELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 557 LHIDTENLREEKDSEITSTRDELLSAR-------DEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYE 629
Cdd:pfam01576 325 REQEVTELKKALEEETRSHEAQLQEMRqkhtqalEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 630 ---KEITSLQNSFQLRCQQCEDQQREEA---TRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQS 703
Cdd:pfam01576 405 hkrKKLEGQLQELQARLSESERQRAELAeklSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQK 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530373136 704 LELTSDLsilqmsrKELENQVGSLKEQhlrdsadlktlLSKAENQAKDVQKEYEKTQTVLSELKLKFE 771
Cdd:pfam01576 485 LNLSTRL-------RQLEDERNSLQEQ-----------LEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
527-702 |
2.60e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 527 ALLEEERKAYRNQVEESTKQIQVLQAQLQRLhiDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVaSERDTDIAS 606
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDAL--QERREALQRLAEYSWDEIDVASAEREIAELEAELERL-DASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 607 LQEELKKVRAELERWRKAASEYEKEITSLQNSFqlrcQQCEDQQREEATRLQGELEKLRKEWNA-LETECHSLKRENVL- 684
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKEL----EQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALGDAVEr 765
|
170 180
....*....|....*....|...
gi 530373136 685 -----LSSELQRQEKELHNSQKQ 702
Cdd:COG4913 766 elrenLEERIDALRARLNRAEEE 788
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
231-731 |
2.70e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.20 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 231 KNQTEDSLRK---ELIALQEDKHNYettakeslRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELAn 307
Cdd:TIGR00606 586 INQTRDRLAKlnkELASLEQNKNHI--------NNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRA- 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 308 KYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALqadndftnERLTALQGIQVDDF 387
Cdd:TIGR00606 657 MLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKST--------ESELKKKEKRRDEM 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 388 LPKINGSTEKEHLLSKSggdctfIHQFIECQKKLiveghltkaveETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDA 467
Cdd:TIGR00606 729 LGLAPGRQSIIDLKEKE------IPELRNKLQKV-----------NRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDV 791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 468 QMDEQdLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRN----QVEES 543
Cdd:TIGR00606 792 TIMER-FQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHlkskTNELK 870
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 544 TKQIQVLQAQLQRLHIDTENlrEEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRK 623
Cdd:TIGR00606 871 SEKLQIGTNLQRRQQFEEQL--VELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKE 948
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 624 AASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGEL-------EKLRKEWNALETECHSLKRENVLLSSELQRQE--- 693
Cdd:TIGR00606 949 KVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLeecekhqEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKren 1028
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 530373136 694 --KELHNSQKQSLELTSDLSILQMSR--KELENQVGSLKEQH 731
Cdd:TIGR00606 1029 elKEVEEELKQHLKEMGQMQVLQMKQehQKLEENIDLIKRNH 1070
|
|
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
481-618 |
3.70e-06 |
|
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.
Pssm-ID: 462015 [Multi-domain] Cd Length: 198 Bit Score: 48.46 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 481 VSLLKDDLQGAQSEIEAK-QEIQHLRKELIEAQELARTSKQKCFELQAlleeerkayrnQVEESTKQIQVLQAQLQRLHI 559
Cdd:pfam06818 12 ISLLKQQLKDSQAEVTQKlNEIVALRAQLRELRAKLEEKEEQIQELED-----------SLRSKTLELEVCENELQRKKN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530373136 560 DTENLRE---EKDSEITSTRDEL--LSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAEL 618
Cdd:pfam06818 81 EAELLREkvgKLEEEVSGLREALsdVSPSGYESVYESDEAKEQRQEEADLGSLRREVERLRAEL 144
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
607-797 |
3.73e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 607 LQEELKKVRAELERWRKAASEYeKEITSLQNSFQLRCQQCEDQQREEatrlqgELEKLRKEWNALETECHSLKRENVLLS 686
Cdd:COG1196 194 ILGELERQLEPLERQAEKAERY-RELKEELKELEAELLLLKLRELEA------ELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 687 SELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQhlrdSADLKTLLSKAENQAKDVQKEYEKTQTVLSEL 766
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER----RRELEERLEELEEELAELEEELEELEEELEEL 342
|
170 180 190
....*....|....*....|....*....|.
gi 530373136 767 KLKFEMTEQEKQSITDELKQCKNNLKLLREK 797
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
338-664 |
3.74e-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: 50.83 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 338 QAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDdflpKINGSTEKEHLLSKSGGDCTFIHQFIEC 417
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE----LSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 418 QKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDttdAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEA 497
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE---LKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 498 KQEIQHLRKELIEaqELARTSKQkcfelqalLEEERKAYRNQVEESTKQIQVLQAQLQRLhidtENLREEKDSEITSTRD 577
Cdd:TIGR02168 829 LERRIAATERRLE--DLEEQIEE--------LSEDIESLAAEIEELEELIEELESELEAL----LNERASLEEALALLRS 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 578 ELLSARDEIlllhQAAAKVASERDTDIASLQEELKKVRAELERWR--------KAASEYEKEITSLQNSFQLRCQQcEDQ 649
Cdd:TIGR02168 895 ELEELSEEL----RELESKRSELRRELEELREKLAQLELRLEGLEvridnlqeRLSEEYSLTLEEAEALENKIEDD-EEE 969
|
330
....*....|....*
gi 530373136 650 QREEATRLQGELEKL 664
Cdd:TIGR02168 970 ARRRLKRLENKIKEL 984
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
291-779 |
4.38e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 291 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKgQAEKKELQHKIDEMEEKEQELQAKIEALQadnd 370
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLE---- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 371 ftnerltalqgiQVDDFLPKINGSTEKEHLLSksggdctfihQFIECQKKLIVEGHLTKAVEETKLSKENQTRAKESDFS 450
Cdd:COG4717 123 ------------KLLQLLPLYQELEALEAELA----------ELPERLEELEERLEELRELEEELEELEAELAELQEELE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 451 DTLSPSKEKSSDDTTDAQMDEQDLNEplaKVSLLKDDLQGAQSEIE-AKQEIQHLRKELIEAQELARTSKQKCFELQALL 529
Cdd:COG4717 181 ELLEQLSLATEEELQDLAEELEELQQ---RLAELEEELEEAQEELEeLEEELEQLENELEAAALEERLKEARLLLLIAAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 530 EEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQE 609
Cdd:COG4717 258 LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 610 ELKKVRAELERWRKAASEYEKEITSLQ--------NSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRE 681
Cdd:COG4717 338 ELLELLDRIEELQELLREAEELEEELQleeleqeiAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGE 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 682 NVLLSSELQRQ--EKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQhlRDSADLKTLLSKAENQAKDVQKEYEKT 759
Cdd:COG4717 418 LEELLEALDEEelEEELEELEEELEELEEELEELREELAELEAELEQLEED--GELAELLQELEELKAELRELAEEWAAL 495
|
490 500
....*....|....*....|
gi 530373136 760 QTVLSELKLKFEMTEQEKQS 779
Cdd:COG4717 496 KLALELLEEAREEYREERLP 515
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
471-636 |
4.80e-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: 49.76 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 471 EQDLNEPLAKVSLLKDDLQGAQSEI-EAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQ--- 546
Cdd:COG4942 40 EKELAALKKEEKALLKQLAALERRIaALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLgrq 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 547 -------------------------IQVLQAQLQRLHIDTENLREEKDsEITSTRDELLSARDEILLLHQAAAKVASERD 601
Cdd:COG4942 120 pplalllspedfldavrrlqylkylAPARREQAEELRADLAELAALRA-ELEAERAELEALLAELEEERAALEALKAERQ 198
|
170 180 190
....*....|....*....|....*....|....*
gi 530373136 602 TDIASLQEELKKVRAELERWRKAASEYEKEITSLQ 636
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
27-106 |
6.81e-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: 45.43 E-value: 6.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 27 PIKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLsrgSEESPPCEILSGDIIQFG 106
Cdd:cd22678 24 PLTIGRIQ------RGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESI---SPNGRPVVLSSGDVITLG 94
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
214-673 |
1.02e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 214 RLLSRLEVMGNQLQACSKNQTEdsLRKELIALQEDKHNYETTAK-ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLK 292
Cdd:COG4717 92 ELQEELEELEEELEELEAELEE--LREELEKLEKLLQLLPLYQElEALEAELAELPERLEELEERLEELRELEEELEELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 293 EMNERTQEELRELANKYNGAV-NEIKDLSDKLKVAEGKQEEIQQkgqaEKKELQHKIDEMEEKEQELQAKIEALQAdndf 371
Cdd:COG4717 170 AELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAELEE----ELEEAQEELEELEEELEQLENELEAAAL---- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 372 tNERLTALQGIQVDDFLpkingstekehLLSKSGGDCTFIHQFIECQKKLIVEGHLTkAVEETKLSKENQTRAKESDFSD 451
Cdd:COG4717 242 -EERLKEARLLLLIAAA-----------LLALLGLGGSLLSLILTIAGVLFLVLGLL-ALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 452 TLsPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLkddlqgaqseiEAKQEIQHLRKELIEAQELARTSKQKCF--ELQALL 529
Cdd:COG4717 309 AL-PALEELEEEELEELLAALGLPPDLSPEELL-----------ELLDRIEELQELLREAEELEEELQLEELeqEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 530 EEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSeitstrdellsardeilLLHQAAAKVASERDTDIASLQE 609
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGE-----------------LEELLEALDEEELEEELEELEE 439
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530373136 610 ELKKVRAELERWRKAASEYEKEITSLQNSFQLrcqqceDQQREEATRLQGELEKLRKEWNALET 673
Cdd:COG4717 440 ELEELEEELEELREELAELEAELEQLEEDGEL------AELLQELEELKAELRELAEEWAALKL 497
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
51-106 |
1.09e-05 |
|
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: 44.85 E-value: 1.09e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530373136 51 LSRNHALVWF----DHKTGKFYLQDTKSSNGTFINSQRLsrgseesPP---CEILSGDIIQFG 106
Cdd:cd22677 41 ISRYHAVLQYrgdaDDHDGGFYLYDLGSTHGTFLNKQRI-------PPkqyYRLRVGHVLKFG 96
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
52-106 |
1.27e-05 |
|
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: 44.95 E-value: 1.27e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 530373136 52 SRNH-ALVWfdHK-TGKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22674 48 SRVHaALVY--HKhLNRVFLIDLGSTHGTFVGGIRL----EPHKPQQLPIDSTLRFG 98
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
165-368 |
1.66e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 165 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQAcSKNQTEDSLRKELIA 244
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA-ELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 245 LQedKHNYETTAKESLR-RVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKL 323
Cdd:COG4942 113 LY--RLGRQPPLALLLSpEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 530373136 324 KVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQAD 368
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
28-106 |
1.67e-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: 1.67e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530373136 28 IKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDhkTGKFYLQDTKSSNGTFINSQRlsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22680 23 VSIGRDP------ENVIVIPDPFVSRNHARITVD--SNEIYIEDLGSTNGTFVNDFK-----RIKGPAKLHPNDIIKLG 88
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
277-761 |
1.90e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 277 VERSLSNTEDECTHLKEMNERTQEelRELANKYNGAVNEIKDLSDKLKVAEGKQEE-IQQKGQA-----EKKELQHKIDE 350
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEE--KDLHERLNGLESELAELDEEIERYEEQREQaRETRDEAdevleEHEERREELET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 351 MEEKEQELQAKIEALQADNDFTNERLTALQGiQVDDFlpkingSTEKEHLLSKSG---GDCTFIHQFIE----------- 416
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRE-RLEEL------EEERDDLLAEAGlddADAEAVEARREeledrdeelrd 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 417 --CQKKLIVEGHLTKAVEETKLSKENQTRAKE-----SDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQ 489
Cdd:PRK02224 329 rlEECRVAAQAHNEEAESLREDADDLEERAEElreeaAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLG 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 490 GAQSEIEAKQE-IQHLRKELIEAQELARTSKQKCFELQALLEE----------ERKAYRNQVEESTKQIQVLQAQLQRLH 558
Cdd:PRK02224 409 NAEDFLEELREeRDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 559 IDTENL-----REEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEIT 633
Cdd:PRK02224 489 EEVEEVeerleRAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 634 SLQN---SFQLRCQQCEDQ------------QREEATRLQGELEKLRKEWNALETECH---SLKRENVL-LSSELQRQEK 694
Cdd:PRK02224 569 EAREevaELNSKLAELKERieslerirtllaAIADAEDEIERLREKREALAELNDERRerlAEKRERKReLEAEFDEARI 648
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530373136 695 ELHNSQKQSLE-----LTSDLSILQMSRKELENQVGSLKEQhLRDSADLKTLLSKAENQAKDVQKEYEKTQT 761
Cdd:PRK02224 649 EEAREDKERAEeyleqVEEKLDELREERDDLQAEIGAVENE-LEELEELRERREALENRVEALEALYDEAEE 719
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
253-801 |
1.94e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 253 ETTAKESLRRVLQ-EKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELR-ELANKYNGA--VNEIKDLSDKLKVAE- 327
Cdd:PTZ00121 1114 ARKAEEAKKKAEDaRKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKaEEARKAEDAkkAEAARKAEEVRKAEEl 1193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 328 GKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKI------------EALQADNDFTNERLTALQGIQVDDFLPKINGST 395
Cdd:PTZ00121 1194 RKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAvkkaeeakkdaeEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK 1273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 396 EKEHLLSKSGGDCTFIHQFIECQKKliveghltkavEETKLSKENQTRAKESDFSDTLspsKEKSSDDTTDAQMDEQDLN 475
Cdd:PTZ00121 1274 AEEARKADELKKAEEKKKADEAKKA-----------EEKKKADEAKKKAEEAKKADEA---KKKAEEAKKKADAAKKKAE 1339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 476 EPLAKVSLLKDDLQGAQSEIEA---KQEIQHLRKEliEAQELARTSKQKCFELQALLEEERKAYRNQVE-ESTKQIQVLQ 551
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAaeeKAEAAEKKKE--EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKaDELKKAAAAK 1417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 552 AQLQRLHIDTENLRE----EKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAEL----ERWRK 623
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKadeaKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAkkkaEEAKK 1497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 624 AASEYEKEITSLQNSFQLR----CQQCEDQQREEATRLQGELEKLRKEWNALEtechsLKRENVLLSSELQRQEKELHNS 699
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAKkaeeAKKADEAKKAEEAKKADEAKKAEEKKKADE-----LKKAEELKKAEEKKKAEEAKKA 1572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 700 QKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKlkfemTEQEKQS 779
Cdd:PTZ00121 1573 EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK-----KEAEEKK 1647
|
570 580
....*....|....*....|..
gi 530373136 780 ITDELKQCKNNLKLLREKGNNK 801
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAEEAKK 1669
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
529-757 |
2.09e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 48.15 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 529 LEEERKAY---RNQVEESTKQIQVLQAQLQRLHIDTENLR------EEKDSEITSTRDELLSARD------EILLLHQAA 593
Cdd:pfam05622 171 LEEELKKAnalRGQLETYKRQVQELHGKLSEESKKADKLEfeykklEEKLEALQKEKERLIIERDtlretnEELRCAQLQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 594 AKVASERDTDIASLQEELKKVRAELerwrkAASEYEKEITSLQNSFQ-LRCQQcEDQQREEATRLQGELEKLRKEWNALE 672
Cdd:pfam05622 251 QAELSQADALLSPSSDPGDNLAAEI-----MPAEIREKLIRLQHENKmLRLGQ-EGSYRERLTELQQLLEDANRRKNELE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 673 TEcHSLKRENVLLSS----ELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQ--HLRDSADLKTLLSKAE 746
Cdd:pfam05622 325 TQ-NRLANQRILELQqqveELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQieELEPKQDSNLAQKIDE 403
|
250
....*....|.
gi 530373136 747 NQAKDVQKEYE 757
Cdd:pfam05622 404 LQEALRKKDED 414
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
552-767 |
2.56e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 552 AQLQRLHIDTENLREEKD--SEITSTRDELLSARDEILLLHQAAAKVASERD-TDIASLQEELKKVRAELERWRKAASEY 628
Cdd:COG4913 235 DDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAqRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 629 EKEITSLQNsfqlRCQQCEDQQREEATRlqgELEKLRKEWNALETECHSLKREnvllSSELQRQEKELHnsqkqsLELTS 708
Cdd:COG4913 315 EARLDALRE----ELDELEAQIRGNGGD---RLEQLEREIERLERELEERERR----RARLEALLAALG------LPLPA 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 530373136 709 DLSILQMSRKELENQVGSLKEQHlrdsADLKTLLSKAENQAKDVQKEYEKTQTVLSELK 767
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEEL----EALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
231-800 |
2.73e-05 |
|
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: 47.79 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 231 KNQTEDSLRKELIALQEDKHNYETTAK---------ESLRRVLQEKIEVVRKLSEVERSlsnTEDECTHLKEMNERTQEE 301
Cdd:pfam05483 94 KVSIEAELKQKENKLQENRKIIEAQRKaiqelqfenEKVSLKLEEEIQENKDLIKENNA---TRHLCNLLKETCARSAEK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 302 LRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNdftnERLTALQG 381
Cdd:pfam05483 171 TKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDK----EKQVSLLL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 382 IQvddflpkingSTEKEHLLSksggDCTFIhqfiecqkkliveghltkaVEETKlSKENQTRAKESDFSDTLSPSKEKSS 461
Cdd:pfam05483 247 IQ----------ITEKENKMK----DLTFL-------------------LEESR-DKANQLEEKTKLQDENLKELIEKKD 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 462 DDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQAL-LEEERKAYRNQV 540
Cdd:pfam05483 293 HLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCsLEELLRTEQQRL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 541 EESTKQIQVLQAQLQRlhidtenlreeKDSEItstrdellsardeilllhQAAAKVASERDTDIaslqEELKKVRAELER 620
Cdd:pfam05483 373 EKNEDQLKIITMELQK-----------KSSEL------------------EEMTKFKNNKEVEL----EELKKILAEDEK 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 621 WRKAASEYEKEITSLQNSFQlrcqqcedqqreeatRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQ 700
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKEQ---------------ELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEK 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 701 KQSLELTSDLSILQMSRKELENQVGSL--------------KEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSEL 766
Cdd:pfam05483 485 LKNIELTAHCDKLLLENKELTQEASDMtlelkkhqediincKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEV 564
|
570 580 590
....*....|....*....|....*....|....
gi 530373136 767 KLKFEMTEQEKQSITDELKQCKNNLKLLREKGNN 800
Cdd:pfam05483 565 KCKLDKSEENARSIEYEVLKKEKQMKILENKCNN 598
|
|
| FHA_RAD53-like_rpt2 |
cd22690 |
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
12-103 |
3.11e-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: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 12 PNSHPfqerHVYL-DEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFD-HKTGK--FYLQDTkSSNGTFINSQRLSR 87
Cdd:cd22690 8 NPSYP----DIELtQNTTFIGRS------KDCDEEITDPRISKHHCIITRKrSGKGLddVYVTDT-STNGTFINNNRLGK 76
|
90
....*....|....*.
gi 530373136 88 GSEesppCEILSGDII 103
Cdd:cd22690 77 GSQ----SLLQDGDEI 88
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
339-674 |
3.25e-05 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 47.75 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 339 AEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALqgiqVDDFLPKINGSTEKEHLlsksggdctfihqfiecq 418
Cdd:pfam13166 89 EESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKL----EADFLDECWKKIKRKKN------------------ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 419 KKLIVEGHLTKAvEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTT---DAQMDEQDLNEPLA------KVSLLKDDLQ 489
Cdd:pfam13166 147 SALSEALNGFKY-EANFKSRLLREIEKDNFNAGVLLSDEDRKAALATvfsDNKPEIAPLTFNVIdfdaleKAEILIQKVI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 490 GAQSEIEAKQEIQHLRKELIEAQELARTSKQKC--------FELQALLEE------------------------------ 531
Cdd:pfam13166 226 GKSSAIEELIKNPDLADWVEQGLELHKAHLDTCpfcgqplpAERKAALEAhfddeftefqnrlqkliekvesaissllaq 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 532 ---------ERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREE--KDSEITSTRDELLSARDEILLLHQAAAKvASER 600
Cdd:pfam13166 306 lpavsdlasLLSAFELDVEDIESEAEVLNSQLDGLRRALEAKRKDpfKSIELDSVDAKIESINDLVASINELIAK-HNEI 384
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530373136 601 DTDIASLQEELKKvraelERWRKAASEYEKEITSLQNSFQLRCQQCEDQQrEEATRLQGELEKLRKEWNALETE 674
Cdd:pfam13166 385 TDNFEEEKNKAKK-----KLRLHLVEEFKSEIDEYKDKYAGLEKAINSLE-KEIKNLEAEIKKLREEIKELEAQ 452
|
|
| FHA_CHFR |
cd22672 |
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ... |
49-105 |
3.63e-05 |
|
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains protein (CHFR); CHFR, also called RING finger protein 196 (RNF196), is a checkpoint protein that delays entry into mitosis in response to stress. It functions as an E3 ubiquitin ligase that ubiquitinates and degrades its target proteins, such as Aurora-A, Plk1, Kif22 and PARP-1, which are critical for proper mitotic transitions. It also plays an important role in cell cycle progression and tumor suppression and is negatively regulated by SUMOylation-mediated proteasomal ubiquitylation. Moreover, CHFR is involved in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation. CHFR contains a fork head associated-(FHA) domain and a RING-HC finger. The CHFR FHA domain has been crystallized as a segment-swapped dimer. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438724 [Multi-domain] Cd Length: 108 Bit Score: 43.43 E-value: 3.63e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 530373136 49 KVLSRNHALVWFDHKtGKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQF 105
Cdd:cd22672 39 KLVSGDHCKIIRDEK-GQVWLEDT-STNGTLVNKVKVVKGQK----VELKHGDVIYL 89
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
14-106 |
4.03e-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: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 14 SHPFQERHvyldepIKIGRSVarcrpaQNNATFDCKVLSRNHALvwFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEesp 93
Cdd:cd22682 14 QFPITEST------IVIGRSV------ESQVQIDDDSVSRYHAK--LAVNPSAVSIIDLGSTNGTIVNGKKIPKLAS--- 76
|
90
....*....|...
gi 530373136 94 pCEILSGDIIQFG 106
Cdd:cd22682 77 -CDLQNGDQIKIG 88
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
239-658 |
4.32e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 239 RKELIALQEDKHNYETTAK--ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERtQEELRELANKYNGAVNEI 316
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQilSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQ-ILELEGYEMDYNSYLKSI 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 317 --------------KDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGI 382
Cdd:PRK01156 373 eslkkkieeyskniERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 383 QVDDFLPKINGSTEKEHLLSKSGGDCTFIHQFIEcqkklivegHLtkaveETKLSKENQTRAKESDFSDTLSpSKEKSSD 462
Cdd:PRK01156 453 SVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIR---------EI-----EIEVKDIDEKIVDLKKRKEYLE-SEEINKS 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 463 DTTDAQMD--EQDLNEPLAKVSLLKDDLQGAQseiEAKQEIQHLRKELIEAQelaRTSKQKCFELQALLEEErkAYRNQV 540
Cdd:PRK01156 518 INEYNKIEsaRADLEDIKIKINELKDKHDKYE---EIKNRYKSLKLEDLDSK---RTSWLNALAVISLIDIE--TNRSRS 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 541 EESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQaaakvaserdtdiasLQEELKKVRAELER 620
Cdd:PRK01156 590 NEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQE---------------NKILIEKLRGKIDN 654
|
410 420 430
....*....|....*....|....*....|....*...
gi 530373136 621 WRKAASEyEKEITSLQNSFQLRCQQCEDQQREEATRLQ 658
Cdd:PRK01156 655 YKKQIAE-IDSIIPDLKEITSRINDIEDNLKKSRKALD 691
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
25-108 |
4.36e-05 |
|
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar proteins; ZEP, also called protein ABA DEFICIENT 1, ABA1, protein IMPAIRED IN BABA-INDUCED STERILITY 3, protein LOW EXPRESSION OF OSMOTIC STRESS-RESPONSIVE GENES 6, or protein NON-PHOTOCHEMICAL QUENCHING 2, plays an important role in the xanthophyll cycle and abscisic acid (ABA) biosynthesis. It converts zeaxanthin into antheraxanthin and subsequently violaxanthin. ZEP is required for resistance to osmotic and drought stresses, ABA-dependent stomatal closure, seed development and dormancy, modulation of defense gene expression, and disease resistance and non-photochemical quencing (NPQ). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438754 [Multi-domain] Cd Length: 123 Bit Score: 43.57 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 25 DEPIKIGRsvarcRPAQNNAT----FDCKVLSRNHALVWFdhKTGKFYLQDTKSSNGTFINSQRLSR-GSEESPPCEILS 99
Cdd:cd22702 31 KQPCIIGS-----DPHQAISGisvvIPSPQVSELHARITC--KNGAFFLTDLGSEHGTWINDNEGRRyRAPPNFPVRLHP 103
|
....*....
gi 530373136 100 GDIIQFGVD 108
Cdd:cd22702 104 SDVIEFGSD 112
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
463-624 |
4.45e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 463 DTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIE-AKQEIQHLRKELIEAQELARTSKQKcfelQALLEEERKAYRNQVE 541
Cdd:COG4913 662 DVASAEREIAELEAELERLDASSDDLAALEEQLEeLEAELEELEEELDELKGEIGRLEKE----LEQAEEELDELQDRLE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 542 ESTKQIQV-----LQAQLQRLHID--TENLREEKDSEITSTRDELLSARDEILLLHQAAAKV----ASERDTDIASL--- 607
Cdd:COG4913 738 AAEDLARLelralLEERFAAALGDavERELRENLEERIDALRARLNRAEEELERAMRAFNREwpaeTADLDADLESLpey 817
|
170 180
....*....|....*....|..
gi 530373136 608 QEELKKVRAE-----LERWRKA 624
Cdd:COG4913 818 LALLDRLEEDglpeyEERFKEL 839
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
487-637 |
4.65e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 487 DLQGAQSEIE-AKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRN----QVEESTKQIQVLQAQLQRLhidt 561
Cdd:COG4913 282 RLWFAQRRLElLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEER---- 357
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530373136 562 ENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQN 637
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
259-545 |
4.76e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.84 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 259 SLRRVLQEKIEVVRKLSEVERslsnteDECTHLKEmNERTqEELRELANKYNGAVNEIKDLSDKLKVAEGKQ-------- 330
Cdd:PRK05771 13 TLKSYKDEVLEALHELGVVHI------EDLKEELS-NERL-RKLRSLLTKLSEALDKLRSYLPKLNPLREEKkkvsvksl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 331 EEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADndftNERLTALQGIQVDDflpkingstekEHLLSKSggdctF 410
Cdd:PRK05771 85 EELIKDVEEELEKIEKEIKELEEEISELENEIKELEQE----IERLEPWGNFDLDL-----------SLLLGFK-----Y 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 411 IHQFIecqkkliveGHLTKAVEETKLSKENQTRAKESDFSDTLSP-----SKEkssddttdaqmDEQDLNEPLAKVSLLK 485
Cdd:PRK05771 145 VSVFV---------GTVPEDKLEELKLESDVENVEYISTDKGYVYvvvvvLKE-----------LSDEVEEELKKLGFER 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530373136 486 DDLQ--GAQSEI--EAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTK 545
Cdd:PRK05771 205 LELEeeGTPSELirEIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAEALSK 268
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
544-756 |
4.97e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 544 TKQIQVLQAQLQRLhidtenlrEEKDSEITSTRDELLSARDEILLLHQAAAKVA--SERDTDIASLQEELKKVRAELERW 621
Cdd:COG4913 609 RAKLAALEAELAEL--------EEELAEAEERLEALEAELDALQERREALQRLAeySWDEIDVASAEREIAELEAELERL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 622 RKAASEYEkeitslqnsfqlrcqqcedqqreeatRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQK 701
Cdd:COG4913 681 DASSDDLA--------------------------ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530373136 702 QSLELTSDLSILQmsRKELENQVGSLKEQHLRDS---------ADLKTLLSKAENQAKDVQKEY 756
Cdd:COG4913 735 RLEAAEDLARLEL--RALLEERFAAALGDAVERElrenleeriDALRARLNRAEEELERAMRAF 796
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
18-86 |
5.24e-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: 42.70 E-value: 5.24e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530373136 18 QERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhkTGKFYLQDTKSSNGTFINSQRLS 86
Cdd:cd22694 8 GELRFDPGSSVRIGRD------PDADVRLDDPRVSRRHALLEFD--GDGWVYTDLGSRNGTYLNGRRVQ 68
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
184-678 |
5.33e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 184 LEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgnqlqacSKNQTEDSLRKELIALQEDKHNYETTaKESLRRV 263
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHE---------ERREELETLEAEIEDLRETIAETERE-REELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 264 LQEKIEVVRKLSEVERSL-----------SNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEE 332
Cdd:PRK02224 281 VRDLRERLEELEEERDDLlaeaglddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 333 IQQKGQAEKKELQH---KIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQvDDFLPKINGSTEKEHLLSKSggdct 409
Cdd:PRK02224 361 LREEAAELESELEEareAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL-EELREERDELREREAELEAT----- 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 410 fihqfIECQKKLIVEGHltKAVEETKLSKENQTrAKESDFSDTLSPSKEKSSD---DTTDAQMDEQDLNEPLAKVSLLKD 486
Cdd:PRK02224 435 -----LRTARERVEEAE--ALLEAGKCPECGQP-VEGSPHVETIEEDRERVEEleaELEDLEEEVEEVEERLERAEDLVE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 487 DLQGAQSEIEAKQEIQHL---RKELIEAQELARTSKQK-CFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRL-HIDT 561
Cdd:PRK02224 507 AEDRIERLEERREDLEELiaeRRETIEEKRERAEELRErAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLaELKE 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 562 ENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSlqnSFQL 641
Cdd:PRK02224 587 RIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAE---EYLE 663
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 530373136 642 RCQQCEDQQREEATRLQG----------ELEKLRKEWNALETECHSL 678
Cdd:PRK02224 664 QVEEKLDELREERDDLQAeigaveneleELEELRERREALENRVEAL 710
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
586-805 |
6.09e-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: 46.30 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 586 ILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQcEDQQREEATRLQGELEKLR 665
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-IRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 666 KEWNALETECHSLKRE-----------------NVLLSSE--------LQRQEKELHNSQKQSLELTSDLSILQMSRKEL 720
Cdd:COG4942 90 KEIAELRAELEAQKEElaellralyrlgrqpplALLLSPEdfldavrrLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 721 ENQVGSLKE---QHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 797
Cdd:COG4942 170 EAERAELEAllaELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
....*...
gi 530373136 798 GNNKPWPW 805
Cdd:COG4942 250 ALKGKLPW 257
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
13-110 |
7.00e-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: 42.22 E-value: 7.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 13 NSHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTgkFYLQDTKSSNGTFINSQRLSrgsee 91
Cdd:cd22665 7 SQAHGPEKDFPLYEgENVIGRD------PSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRL----- 73
|
90 100
....*....|....*....|.
gi 530373136 92 SPPC--EILSGDIIQFGvDVT 110
Cdd:cd22665 74 KPNVryELIDGDLLLFG-DVK 93
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
497-719 |
1.14e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 497 AKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAY---RNQVEESTKQIQVLQAQLQRLHIDTENLREE------ 567
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYnelQAELEALQAEIDKLQAEIAEAEAEIEERREElgerar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 568 ---KDSEITSTRDELLSARDEILLLHQAAA-KVASERDTDIAslqEELKKVRAELERWRKAASEYEKEITSLQnsfqlrc 643
Cdd:COG3883 94 alyRSGGSVSYLDVLLGSESFSDFLDRLSAlSKIADADADLL---EELKADKAELEAKKAELEAKLAELEALK------- 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530373136 644 qqceDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKE 719
Cdd:COG3883 164 ----AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
257-631 |
1.95e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 257 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQK 336
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 337 GQAEKKELQHKIDEMEEKEQ---ELQAKIEALQADNDftnerltalqgiqvDDFLPKINGSTEKehllsksggdctfihq 413
Cdd:TIGR02169 753 IENVKSELKELEARIEELEEdlhKLEEALNDLEARLS--------------HSRIPEIQAELSK---------------- 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 414 fiecqkkliveghltkaVEETKLSKENQTRAKESDFSDtLSPSKEKSSDDTTDAQMDeqdlneplakvsllKDDLQGAQS 493
Cdd:TIGR02169 803 -----------------LEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQ--------------RIDLKEQIK 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 494 EIEAKQEIQHLRKELIEAQElartSKQKCFELQalLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLReEKDSEIT 573
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEEEL----EELEAALRD--LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR-KRLSELK 923
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530373136 574 STRDELLSARDEILLLhQAAAKVASERDTDIASLQEELKKVRAELERWR----KAASEYEKE 631
Cdd:TIGR02169 924 AKLEALEEELSEIEDP-KGEDEEIPEEELSLEDVQAELQRVEEEIRALEpvnmLAIQEYEEV 984
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
52-107 |
2.45e-04 |
|
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also called cell cycle regulatory protein p95, or Nijmegen breakage syndrome protein 1 (NBS1), is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. Nibrin modulates the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-dependent protein kinase catalytic subunit (DNA-PKcs) to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. Nibrin also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. Nibrin is a major player in the control of intra-S-phase checkpoint. This subfamily also includes Schizosaccharomyces pombe DNA repair and telomere maintenance protein Nbs1 and Arabidopsis thaliana AtNbs1. SpNbs1 is an FHA domain-containing protein required for DNA damage repair and S-phase DNA damage checkpoint. It is involved in telomere length maintenance and maintenance of chromatin structure. AtNbs1 is a component of MRN complex. It also functions in the very early stages of meiosis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438719 [Multi-domain] Cd Length: 108 Bit Score: 41.16 E-value: 2.45e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530373136 52 SRNHALVWFDHKTG---------KFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQFGV 107
Cdd:cd22667 40 SRKHATLTVLHPEAnlsdpdtrpELTLKDL-SKYGTFVNGEKLKGGSE----VTLKDGDVITFGV 99
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
470-681 |
2.46e-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: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 470 DEQDLNEPLAKVSLLKDDLQGAQSEIEAKQ-EIQHLRKELIEAQELARTSKQKCFELQALlEEERKAYRNQVEESTKQIQ 548
Cdd:COG4913 645 ERREALQRLAEYSWDEIDVASAEREIAELEaELERLDASSDDLAALEEQLEELEAELEEL-EEELDELKGEIGRLEKELE 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 549 VLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERD---TDIASLQEELKKVRAE-LERWRKA 624
Cdd:COG4913 724 QAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDalrARLNRAEEELERAMRAfNREWPAE 803
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 530373136 625 ASEYEKEITSLqNSFQlrcQQCEDQQREEATRLQGELEKLRKEW--NALETECHSLKRE 681
Cdd:COG4913 804 TADLDADLESL-PEYL---ALLDRLEEDGLPEYEERFKELLNENsiEFVADLLSKLRRA 858
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
324-779 |
2.50e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.73 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 324 KVAEGKQEEIQQKGQAEKKELQHKidemeEKEQELQAKIEALQADNDFTNERLTALQGiqvddflpKINGSTEKEHLLSK 403
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHK-----RARIELEKKASALKRQLDRESDRNQELQK--------RIRLLEKREAEAEE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 404 SggdctfihqfiecQKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSL 483
Cdd:pfam05557 70 A-------------LREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 484 LKDDLQgaqsEIEAK-QEIQHLRKELIEAQELARTSKQKCFELqalleEERKAYRNQVEESTKQIQVLQAQLQRLHIDTE 562
Cdd:pfam05557 137 LQERLD----LLKAKaSEAEQLRQNLEKQQSSLAEAEQRIKEL-----EFEIQSQEQDSEIVKNSKSELARIPELEKELE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 563 NLREEKDSEITSTRDELLSARDeillLHQAAAKVASERDT--DIASLQEELKKVRAELERWRKAASEYEKEITS--LQNS 638
Cdd:pfam05557 208 RLREHNKHLNENIENKLLLKEE----VEDLKRKLEREEKYreEAATLELEKEKLEQELQSWVKLAQDTGLNLRSpeDLSR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 639 FQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDL----SILQ 714
Cdd:pfam05557 284 RIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgyrAILE 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530373136 715 MSRKELENQVGSlkEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 779
Cdd:pfam05557 364 SYDKELTMSNYS--PQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQA 426
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
499-795 |
3.01e-04 |
|
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: 44.12 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 499 QEIQHLRKELIEAQELARTSKQKCFELQallEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLrEEKDSEITSTRDE 578
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKEKERY---KRDREQWERQRRELESRVAELKEELRQSREKHEEL-EEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 579 LLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWR---KAASEYEKEITSLQNSFQLRCQQCEDQQREEAT 655
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKeraKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 656 RLQG----------------------------------ELEKLRKEWNALETECHSLKRENVLLSSELQ-------RQEK 694
Cdd:pfam07888 193 EFQElrnslaqrdtqvlqlqdtittltqklttahrkeaENEALLEELRSLQERLNASERKVEGLGEELSsmaaqrdRTQA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 695 ELHNSQKQSLELTSDLSILQMSRKELENQvGSLKEQHLRDSADLKTllSKAENQAKDVQKEYEKTQTVLSE-LKLKFEMT 773
Cdd:pfam07888 273 ELHQARLQAAQLTLQLADASLALREGRAR-WAQERETLQQSAEADK--DRIEKLSAELQRLEERLQEERMErEKLEVELG 349
|
330 340
....*....|....*....|..
gi 530373136 774 eQEKQSITDELKQCKNNLKLLR 795
Cdd:pfam07888 350 -REKDCNRVQLSESRRELQELK 370
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
498-681 |
3.10e-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: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 498 KQEIQHLRKELIEAQELARTSKQKcfELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRD 577
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQK--NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 578 ELLSARDEILL--LHQAAAKVASERDT------DIASLQEELKKVRAEL-ERWRKAASEYEKEITSLQNSfqlrcqqcED 648
Cdd:COG3206 259 LLQSPVIQQLRaqLAELEAELAELSARytpnhpDVIALRAQIAALRAQLqQEAQRILASLEAELEALQAR--------EA 330
|
170 180 190
....*....|....*....|....*....|...
gi 530373136 649 QQREEATRLQGELEKLrkewNALETECHSLKRE 681
Cdd:COG3206 331 SLQAQLAQLEARLAEL----PELEAELRRLERE 359
|
|
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
53-106 |
3.53e-04 |
|
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 (FHAD1) and similar proteins; FHAD1, also called FHA domain-containing protein 1, is an uncharacterized FHA domain-containing protein. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438752 [Multi-domain] Cd Length: 96 Bit Score: 40.32 E-value: 3.53e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 530373136 53 RNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPceilsGDIIQFG 106
Cdd:cd22700 36 EQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAP-----GDVLRFG 84
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
1-106 |
3.81e-04 |
|
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442679 [Multi-domain] Cd Length: 402 Bit Score: 43.60 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 1 MPSALAIFTCRPNSHPFQERHVYLDEPIKIGRSvARC-----RPAQnnatfdckVLSRNHALVWFDHktGKFYLQDTkSS 75
Cdd:COG3456 1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRS-ADCdwvlpDPDR--------SVSRRHAEIRFRD--GAFCLTDL-ST 68
|
90 100 110
....*....|....*....|....*....|...
gi 530373136 76 NGTFIN--SQRLSRGSEEsppcEILSGDIIQFG 106
Cdd:COG3456 69 NGTFLNgsDHPLGPGRPV----RLRDGDRLRIG 97
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
593-818 |
3.87e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 593 AAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQlRCQQCEDQQREEATRLQGELEKLRKEwnaLE 672
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE-ALQAEIDKLQAEIAEAEAEIEERREE---LG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 673 TECHSLKRE-------NVLLSSE-----LQRQE--KELHNSQKQSLELTSDLsilqmsRKELENQVGSLKEQhlrdSADL 738
Cdd:COG3883 90 ERARALYRSggsvsylDVLLGSEsfsdfLDRLSalSKIADADADLLEELKAD------KAELEAKKAELEAK----LAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 739 KTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNNKPWPWMPMLAALVAVTAI 818
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
653-799 |
4.15e-04 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 43.15 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 653 EATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNsQKQSLELTSDLSilqmsrkELENQVGSLKeqhl 732
Cdd:pfam15294 134 EIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGA-KKDVKSNLKEIS-------DLEEKMAALK---- 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530373136 733 rdsADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGN 799
Cdd:pfam15294 202 ---SDLEKTLNASTALQKSLEEDLASTKHELLKVQEQLEMAEKELEKKFQQTAAYRNMKEMLTKKNE 265
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
529-797 |
4.31e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 529 LEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDellsardeillLHQAAAKVASERDtdiaSLQ 608
Cdd:COG1340 6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKE-----------LREEAQELREKRD----ELN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 609 EELKKVRAELERWRKAASEYEKEITSLQNsfqlrcqqcedqQREEATRLQGELEKLRKEWNALE----TECHSLKRENVL 684
Cdd:COG1340 71 EKVKELKEERDELNEKLNELREELDELRK------------ELAELNKAGGSIDKLRKEIERLEwrqqTEVLSPEEEKEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 685 ------LSSELQRQEKElHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAEN---QAKDVQKE 755
Cdd:COG1340 139 vekikeLEKELEKAKKA-LEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADElrkEADELHKE 217
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 530373136 756 YEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 797
Cdd:COG1340 218 IVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKRE 259
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
291-570 |
4.47e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 291 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQkgqaEKKELQHKIDEMEEKEQELQAKIEALQADnd 370
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ----ELAALEAELAELEKEIAELRAELEAQKEE-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 371 fTNERLTALQgiqvddflpKINGSTEKEHLLSKSGgdctfihqFIECQKKLIVEGHLTKAVEEtklskenqtrakesdfs 450
Cdd:COG4942 106 -LAELLRALY---------RLGRQPPLALLLSPED--------FLDAVRRLQYLKYLAPARRE----------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 451 dtlspskekssddttdaQMDEqdLNEPLAKVSLLKDDLQgaqseiEAKQEIQHLRKELIEAQELARTSKQKCFELQALLE 530
Cdd:COG4942 151 -----------------QAEE--LRADLAELAALRAELE------AERAELEALLAELEEERAALEALKAERQKLLARLE 205
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 530373136 531 EERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDS 570
Cdd:COG4942 206 KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
49-112 |
6.61e-04 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 (PML1) and similar proteins; PML1 is an FHA domain-containing protein required for efficient splicing and pre-mRNA nuclear retention. It is a component of the pre-mRNA retention and splicing (RES) complex composed of at least BUD13, IST3, and PML1. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438733 [Multi-domain] Cd Length: 129 Bit Score: 40.50 E-value: 6.61e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530373136 49 KVLSRNHALVWFDHKTG--KFYLQDTKSSNGTFINsqrlsrgSEESPPC---EILSGDIIQFGVDVTEN 112
Cdd:cd22681 64 ETCSKQHCVIQFRNVKGilKPYIMDLDSSNGTCLN-------DNVIPSSryvELRSGDVITFSKSNDYE 125
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
526-766 |
6.68e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 526 QALLEEERKAYRNQVEESTKQIQVLQAQLQrlhiDTENLREEkdseITSTRDELLSARDEILLLHQAAAKVASER--DTD 603
Cdd:PRK11281 51 QKLLEAEDKLVQQDLEQTLALLDKIDRQKE----ETEQLKQQ----LAQAPAKLRQAQAELEALKDDNDEETRETlsTLS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 604 IASLQEELKKVRAELERWRKAASEYEKEITSLQNsfqlrcqQCEDQQREEATRLQgELEKLRKEWNALETECHSLKREN- 682
Cdd:PRK11281 123 LRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQT-------QPERAQAALYANSQ-RLQQIRNLLKGGKVGGKALRPSQr 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 683 VLLSSELQRQekELHNS-QKQSLELTSDLSILQMSRKELENQVGSLKEQHLrdsADLKTL-----LSKAENQAKDVQKEY 756
Cdd:PRK11281 195 VLLQAEQALL--NAQNDlQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQL---QLLQEAinskrLTLSEKTVQEAQSQD 269
|
250
....*....|
gi 530373136 757 EKTQTVLSEL 766
Cdd:PRK11281 270 EAARIQANPL 279
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
16-111 |
7.11e-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: 39.21 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 16 PFQERHVYLD-EPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFdhKTGKFYLQDTKSSNGTFINSQRLSRgseespP 94
Cdd:cd22693 7 TLQGQTFPIDkSGITIGRA------DDNDLVLSDDFVSSRHARIYL--QGSSWYLEDLGSTNGTFVNGNRVTQ------P 72
|
90
....*....|....*..
gi 530373136 95 CEILSGDIIQFGVDVTE 111
Cdd:cd22693 73 VVVQPGDTIRIGATVFE 89
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
463-638 |
7.63e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 463 DTTDAQMDE--QDLNEPLAKVSLLKDDLQGAQSEI-EAKQEIQHLRKELIE-AQELARTSKQKCFeLQALLEEE------ 532
Cdd:COG3883 40 DALQAELEElnEEYNELQAELEALQAEIDKLQAEIaEAEAEIEERREELGErARALYRSGGSVSY-LDVLLGSEsfsdfl 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 533 -RKAYRNQVEESTKQ-IQVLQAQLQRLhidtenlrEEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEE 610
Cdd:COG3883 119 dRLSALSKIADADADlLEELKADKAEL--------EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
|
170 180
....*....|....*....|....*...
gi 530373136 611 LKKVRAELERWRKAASEYEKEITSLQNS 638
Cdd:COG3883 191 EAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
329-780 |
8.66e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 8.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 329 KQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQAdndftnerltalQGIQVDDFLPKINGSTEKEHLLSKSGG-- 406
Cdd:TIGR00618 236 QQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRA------------QEAVLEETQERINRARKAAPLAAHIKAvt 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 407 ----DCTFIHQFIECQK-KLIVEGHLTKAVEETKLSKENQTRAKESDFSD----TLSPSKEKSSDDTTDAQM-DEQDLNE 476
Cdd:TIGR00618 304 qieqQAQRIHTELQSKMrSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQeihiRDAHEVATSIREISCQQHtLTQHIHT 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 477 PLAKVSLLKDDLQGAQSEIEAKQEIQH-----LRKELIEAQELARTSKQKCFElQALLEEERKAYRNQVEESTKQIQVLQ 551
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELDILQREQAtidtrTSAFRDLQGQLAHAKKQQELQ-QRYAELCAAAITCTAQCEKLEKIHLQ 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 552 AQLQRLHIDTENL--------REEKDSEITSTRDELLSARDEIL---LLHQAAAKVASER-----------DTDIASLQE 609
Cdd:TIGR00618 463 ESAQSLKEREQQLqtkeqihlQETRKKAVVLARLLELQEEPCPLcgsCIHPNPARQDIDNpgpltrrmqrgEQTYAQLET 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 610 ELKKVRAELERWRKAASEYEKEITSLQNSFQlRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSEL 689
Cdd:TIGR00618 543 SEEDVYHQLTSERKQRASLKEQMQEIQQSFS-ILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKL 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 690 Q----RQEKELHNSQKQSLEltsDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSE 765
Cdd:TIGR00618 622 QpeqdLQDVRLHLQQCSQEL---ALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEM 698
|
490
....*....|....*
gi 530373136 766 LKLKFEMTEQEKQSI 780
Cdd:TIGR00618 699 LAQCQTLLRELETHI 713
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
257-801 |
9.11e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.04 E-value: 9.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 257 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQE-----------ELRELANKYNGAVNEIKDLSDKLKV 325
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEyyqlkekleleEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 326 AEG----KQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDDFLPKINGSTEKEHLL 401
Cdd:pfam02463 248 DEQeeieSSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 402 SKSGGDCTFIHQFIECQKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKV 481
Cdd:pfam02463 328 KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 482 SLLKDDLQGAQSEIEAKQEIQ-HLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHID 560
Cdd:pfam02463 408 QLLLELARQLEDLLKEEKKEElEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLE 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 561 TENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQ 640
Cdd:pfam02463 488 LLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLV 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 641 LRcqqcEDQQREEATRLQGELEKLRKEWNALETECH-SLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKE 719
Cdd:pfam02463 568 RA----LTELPLGARKLRLLIPKLKLPLKSIAVLEIdPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKA 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 720 LENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGN 799
Cdd:pfam02463 644 KESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELL 723
|
..
gi 530373136 800 NK 801
Cdd:pfam02463 724 AD 725
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
496-702 |
1.02e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 496 EAKQEIQHLRKELIEAQELARTSKQKCFELQALLEE----------ERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLR 565
Cdd:COG1340 19 ELREEIEELKEKRDELNEELKELAEKRDELNAQVKElreeaqelreKRDELNEKVKELKEERDELNEKLNELREELDELR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 566 EEKDSEITSTRD-----------------ELLSARDEILLLHQAAAKVAS-ERDTDIASLQEELKKVRAELERWRKAASE 627
Cdd:COG1340 99 KELAELNKAGGSidklrkeierlewrqqtEVLSPEEEKELVEKIKELEKElEKAKKALEKNEKLKELRAELKELRKEAEE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 628 YEKEITSLQNSFQ------LRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQK 701
Cdd:COG1340 179 IHKKIKELAEEAQelheemIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKR 258
|
.
gi 530373136 702 Q 702
Cdd:COG1340 259 E 259
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
268-791 |
1.02e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 268 IEVVRKLSEVERSLSNTEDECTHLkemnertqEELRELANKYNGA---VNEIKDLSDKLKVAEGKQEeiQQKGQAEKKEL 344
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELL--------EPIRELAERYAAArerLAELEYLRAALRLWFAQRR--LELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 345 QHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDDFLPKINGSTEKEHLLSKSGGDctfihqfiecQKKLIVE 424
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR----------LEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 425 GHLTKAVEETKLsKENQTRAKEsdFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQeiQHL 504
Cdd:COG4913 371 LGLPLPASAEEF-AALRAEAAA--LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL--LAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 505 RKELieAQELARTSKQKCF--ELQALLEEER-------KAYRNQ-----VEESTKQiQVLQA--QLQ-RLHIDTENLREE 567
Cdd:COG4913 446 RDAL--AEALGLDEAELPFvgELIEVRPEEErwrgaieRVLGGFaltllVPPEHYA-AALRWvnRLHlRGRLVYERVRTG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 568 KDSEITSTRDEllsardeilllHQAAAKVASERDTDIASLQEELKKVRA--------ELERWRKAaseyekeITS---LQ 636
Cdd:COG4913 523 LPDPERPRLDP-----------DSLAGKLDFKPHPFRAWLEAELGRRFDyvcvdspeELRRHPRA-------ITRagqVK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 637 NSFQLRcqQCEDQQREEATRLQGE-----LEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLS 711
Cdd:COG4913 585 GNGTRH--EKDDRRRIRSRYVLGFdnrakLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 712 ILQMSRK--ELENQVGSLkeqhLRDSADLKTLlskaENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKN 789
Cdd:COG4913 663 VASAEREiaELEAELERL----DASSDDLAAL----EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
..
gi 530373136 790 NL 791
Cdd:COG4913 735 RL 736
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
164-775 |
1.14e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 164 SQELFQLSQYLQEALHR----EQMLEQKLATLQRLLAITQEASDTSWQALIDEDRllsRLEVMGNQLQACSKNQTEDSLR 239
Cdd:pfam10174 129 AKELFLLRKTLEEMELRietqKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWER---TRRIAEAEMQLGHLEVLLDQKE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 240 KELIALQEDKH-NYETTAKESLRRVLQEKIEVV-RKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKyngaVNEIK 317
Cdd:pfam10174 206 KENIHLREELHrRNQLQPDPAKTKALQTVIEMKdTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQ----MEVYK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 318 DLSD--KLKVAEGKQEeiQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQgIQVDDFLPKINgst 395
Cdd:pfam10174 282 SHSKfmKNKIDQLKQE--LSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQ-TEVDALRLRLE--- 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 396 EKEHLLSKSggdctfihqfiecQKKLiveghltkaveeTKLSKENQTRAKE-SDFSDTLSPSKEKSSDDTTDAQMDEQDL 474
Cdd:pfam10174 356 EKESFLNKK-------------TKQL------------QDLTEEKSTLAGEiRDLKDMLDVKERKINVLQKKIENLQEQL 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 475 NEPLAKVSLLKDDLQGAQSEIEAKQEIqhlrkelIEAQELARTSKQKCFE-LQALLEEERKAYRNQVEESTKQIQVLQAQ 553
Cdd:pfam10174 411 RDKDKQLAGLKERVKSLQTDSSNTDTA-------LTTLEEALSEKERIIErLKEQREREDRERLEELESLKKENKDLKEK 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 554 LQRLHIDtenlREEKDSEITSTRDELLSARDEILllhqaaakvasERDTDIASLQEELKKVRAELERW----RKAASEYE 629
Cdd:pfam10174 484 VSALQPE----LTEKESSLIDLKEHASSLASSGL-----------KKDSKLKSLEIAVEQKKEECSKLenqlKKAHNAEE 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 630 KEITSLQNSFQLRCQQCEDQQ-REEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQslelts 708
Cdd:pfam10174 549 AVRTNPEINDRIRLLEQEVARyKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVAN------ 622
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530373136 709 dlsiLQMSRKELENQVGSLKEQHLRDSADLKTllSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQ 775
Cdd:pfam10174 623 ----IKHGQQEMKKKGAQLLEEARRREDNLAD--NSQQLQLEELMGALEKTRQELDATKARLSSTQQ 683
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
260-380 |
1.14e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 260 LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQ----- 334
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkey 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 530373136 335 QKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQ 380
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE 137
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
648-770 |
1.14e-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: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 648 DQQREEATR----LQGELEKLRKEWNALETECHSLKRENVLLSSELQRQekelhNSQKQSLELTSDLSILQMSRKELENQ 723
Cdd:COG3206 167 ELRREEARKalefLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAK-----LLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 530373136 724 VGSLKEQHLRDSADLKTLLSKAENQakDVQKEYEKTQTVLSELKLKF 770
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPVIQ--QLRAQLAELEAELAELSARY 286
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
530-761 |
1.49e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 530 EEERKAYRNQVEESTKQIQVLQAQLQRLhidtenlreekDSEITSTRDELLSARDEILLLHQAAAKVASErdtdIASLQE 609
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDAL-----------QAELEELNEEYNELQAELEALQAEIDKLQAE----IAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 610 ELKKVRAELERWrkAASEYE--------------KEITSLQNSFQLRCQQCEDQQR--EEATRLQGELEKLRKEWNALET 673
Cdd:COG3883 80 EIEERREELGER--ARALYRsggsvsyldvllgsESFSDFLDRLSALSKIADADADllEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 674 ECHSLKRENVLLSSELQRQEKELhnsQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQ 753
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQ---EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
....*...
gi 530373136 754 KEYEKTQT 761
Cdd:COG3883 235 AAAAAAAA 242
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
165-710 |
1.49e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 165 QELFQLSQYLQEALHREQMLEQKLATLQRL----LAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRK 240
Cdd:TIGR00618 379 QHIHTLQQQKTTLTQKLQSLCKELDILQREqatiDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEK 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 241 elIALQEdkhnyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLS 320
Cdd:TIGR00618 459 --IHLQE------------SAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPG 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 321 DKLKVAEGKQEEIQQKGQAEKKeLQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIqvddflpkINGSTEKEHL 400
Cdd:TIGR00618 525 PLTRRMQRGEQTYAQLETSEED-VYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKED--------IPNLQNITVR 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 401 LSKsggdctFIHQFIECQKKLIVEGHLTKAVEETKLSKEnQTRAKESDFSDTLSpsKEKSSDDTTDAQMDEQDLNEPLAK 480
Cdd:TIGR00618 596 LQD------LTEKLSEAEDMLACEQHALLRKLQPEQDLQ-DVRLHLQQCSQELA--LKLTALHALQLTLTQERVREHALS 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 481 VSLLKddLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHID 560
Cdd:TIGR00618 667 IRVLP--KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQS 744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 561 TENLREEkdseitstRDELLSARDEILLLHQAAAKVASERDTdiaslqeELKKVRAELERWRKAASEYEKEITSLQNSFQ 640
Cdd:TIGR00618 745 LKELMHQ--------ARTVLKARTEAHFNNNEEVTAALQTGA-------ELSHLAAEIQFFNRLREEDTHLLKTLEAEIG 809
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 641 LRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEkELHNSQKQSLELTSDL 710
Cdd:TIGR00618 810 QEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA-QLTQEQAKIIQLSDKL 878
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
235-723 |
1.79e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 235 EDSLRKELIAL---QEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELREL--ANKY 309
Cdd:COG4717 48 LERLEKEADELfkpQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 310 NGAVNEIKDLSDKLKVAEGKQEEIQQKgQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERltalqgiQVDDFLP 389
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEER-LEELRELEEELEELEAELAELQEELEELLEQLSLATEE-------ELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 390 KINGSTEKEHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKAVEEtKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQM 469
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE-RLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 470 deQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQveestKQIQV 549
Cdd:COG4717 279 --LFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRI-----EELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 550 LQAQLQRLH--IDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAasE 627
Cdd:COG4717 352 LLREAEELEeeLQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE--E 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 628 YEKEITSLQnsfqlrcqqcedqqrEEATRLQGELEKLRKEWNALETECHSLKRENVL--LSSELQRQEKELHNSQKQSLE 705
Cdd:COG4717 430 LEEELEELE---------------EELEELEEELEELREELAELEAELEQLEEDGELaeLLQELEELKAELRELAEEWAA 494
|
490
....*....|....*...
gi 530373136 706 LTSDLSILQMSRKELENQ 723
Cdd:COG4717 495 LKLALELLEEAREEYREE 512
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
209-585 |
1.91e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 41.96 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 209 LIDEDRLLSRLE--------VMGNQLQAcsKNQTEDSLRKELIALQEDKHNYETTAKESLRRVlQEKIEVVRKLSEVERS 280
Cdd:PTZ00108 1001 LGKLERELARLSnkvrfikhVINGELVI--TNAKKKDLVKELKKLGYVRFKDIIKKKSEKITA-EEEEGAEEDDEADDED 1077
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 281 LSNTEDECT---HLKEMN--ERTQEELRELANKYNGAVNEIKDLSDKlkvaegkqeEIQQKGQAEKKELQHKIDEMEEKE 355
Cdd:PTZ00108 1078 DEEELGAAVsydYLLSMPiwSLTKEKVEKLNAELEKKEKELEKLKNT---------TPKDMWLEDLDKFEEALEEQEEVE 1148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 356 QELQAKIEALQADNDFTNERltaLQGIQVDDFLPKINGSTEKEHLLSKSGGDCTFIHQFIecqKKLIVEGHLTKAVEETK 435
Cdd:PTZ00108 1149 EKEIAKEQRLKSKTKGKASK---LRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDE---KRKLDDKPDNKKSNSSG 1222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 436 LSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELA 515
Cdd:PTZ00108 1223 SDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKP 1302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 516 RTS----KQKCFELQALL----EEERKAYRNQVEESTKQIQVLQAQLQRL------HIDTENLREEKDSEITSTRDELLS 581
Cdd:PTZ00108 1303 SSPtkkkVKKRLEGSLAAlkkkKKSEKKTARKKKSKTRVKQASASQSSRLlrrprkKKSDSSSEDDDDSEVDDSEDEDDE 1382
|
....
gi 530373136 582 ARDE 585
Cdd:PTZ00108 1383 DDED 1386
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
27-106 |
1.91e-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: 38.22 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 27 PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTGkfYLQDTKSSNGTFINSQRLsrgseeSPPCEILSGDIIQFG 106
Cdd:cd22668 19 SNIIGRG------SDADFRLPDTGVSRRHAEIRWDGQVA--HLTDLGSTNGTTVNNAPV------TPEWRLADGDVITLG 84
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
599-800 |
1.95e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 599 ERDT--DIASLQEELKkvraELERWRKAASEYEKEITSLQnsfQLRcqqcedQQREEATRLQGELEKLRKEWNALETECH 676
Cdd:COG4913 220 EPDTfeAADALVEHFD----DLERAHEALEDAREQIELLE---PIR------ELAERYAAARERLAELEYLRAALRLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 677 SLKREnvLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQvgsLKEQHLRDSADLKTLLSKAENQAKDVQKEY 756
Cdd:COG4913 287 QRRLE--LLEAELEELRAELARLEAELERLEARLDALREELDELEAQ---IRGNGGDRLEQLEREIERLERELEERERRR 361
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 530373136 757 EKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNN 800
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
529-688 |
2.02e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 529 LEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDseitstrdELlsaRDEILllhqaaakvasERDTDIASLQ 608
Cdd:COG2433 390 LPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE--------EL---EAELE-----------EKDERIERLE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 609 EELKKVRAElerwRKAASEYEKEITSLQNsfqlrcqqcedqqreEATRLQGELEKLRKEWNALETECHSLKRENVLLSSE 688
Cdd:COG2433 448 RELSEARSE----ERREIRKDREISRLDR---------------EIERLERELEEERERIEELKRKLERLKELWKLEHSG 508
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
218-797 |
2.15e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 218 RLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTaKESLRRVLQEKIEVVRKLSEVERSLSNTEDECthlkemnER 297
Cdd:PRK01156 151 RKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYL-EEKLKSSNLELENIKKQIADDEKSHSITLKEI-------ER 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 298 TQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIqQKGQAEKKELQHKIDEMEEKEQELqakiealqadNDFTNERLT 377
Cdd:PRK01156 223 LSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI-KTAESDLSMELEKNNYYKELEERH----------MKIINDPVY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 378 ALQGiQVDDFLPKINGSTEKEHLLSKSGGDctfIHQFIECQKKLIVeghltkaveetklskenqtraKESDFSDTLSPSK 457
Cdd:PRK01156 292 KNRN-YINDYFKYKNDIENKKQILSNIDAE---INKYHAIIKKLSV---------------------LQKDYNDYIKKKS 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 458 EKssddttdaqmdeQDLNEPLAKVSLLKDDLQGAQSEIEA-KQEIQHLRKElieaQELARTSKQKCFELQALLEEERKAY 536
Cdd:PRK01156 347 RY------------DDLNNQILELEGYEMDYNSYLKSIESlKKKIEEYSKN----IERMSAFISEILKIQEIDPDAIKKE 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 537 RNQVEESTKQIqvlQAQLQRLHIDTENLREEKDSeitstrdelLSARDEILLLHQAAAKVASERDTDiaslqeelkKVRA 616
Cdd:PRK01156 411 LNEINVKLQDI---SSKVSSLNQRIRALRENLDE---------LSRNMEMLNGQSVCPVCGTTLGEE---------KSNH 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 617 ELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRenvLLSSELQRQEKEL 696
Cdd:PRK01156 470 IINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLED---IKIKINELKDKHD 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 697 HNSQKQSLELTSDLSILQMSRKELenqvgsLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQE 776
Cdd:PRK01156 547 KYEEIKNRYKSLKLEDLDSKRTSW------LNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKS 620
|
570 580
....*....|....*....|.
gi 530373136 777 KQSITDELKQCKNNLKLLREK 797
Cdd:PRK01156 621 IREIENEANNLNNKYNEIQEN 641
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
506-801 |
2.36e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 506 KELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDsEITSTRDELLSARDE 585
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 586 ILLLHQAAAKVaserDTDIASLQEELKKVRAELERWRkaasEYEKEITSLQnsfqlrcqqcedQQREEATRLQGELEKLR 665
Cdd:PRK03918 247 LESLEGSKRKL----EEKIRELEERIEELKKEIEELE----EKVKELKELK------------EKAEEYIKLSEFYEEYL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 666 KEWNALETECHSLKREnvllSSELQRQEKELHNSQKQSLELTSDLsilqmsrKELENQVGSLKEQHlRDSADLKTLLSKA 745
Cdd:PRK03918 307 DELREIEKRLSRLEEE----INGIEERIKELEEKEERLEELKKKL-------KELEKRLEELEERH-ELYEEAKAKKEEL 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 530373136 746 ENQAKdvqkeyEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNNK 801
Cdd:PRK03918 375 ERLKK------RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
602-801 |
2.79e-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: 41.16 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 602 TDIASLQEELKKVRAELERWRKAASEYEKEItSLQNSFQLRCQQCEDQQ---REEATRLQGELEKLRKEWNALETECHSL 678
Cdd:TIGR04523 180 KEKLNIQKNIDKIKNKLLKLELLLSNLKKKI-QKNKSLESQISELKKQNnqlKDNIEKKQQEINEKTTEISNTQTQLNQL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 679 KRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQvgslKEQHLrdSADLKTLLSKAENQAKDVQKEYEK 758
Cdd:TIGR04523 259 KDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ----KEQDW--NKELKSELKNQEKKLEEIQNQISQ 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 530373136 759 TQTVLSELKLKFEMTEQEK-------QSITDELKQCKNNLKLLREKGNNK 801
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELtnsesenSEKQRELEEKQNEIEKLKKENQSY 382
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
174-363 |
2.84e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 39.89 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 174 LQEALHREQMLEQKLATLQRLLaitqeasdtswQALIDEDRLLSRLEVmgNQLQACSKNQTEDSLRKELIAlqedKHNYE 253
Cdd:pfam15619 6 LSARLHKIKELQNELAELQSKL-----------EELRKENRLLKRLQK--RQEKALGKYEGTESELPQLIA----RHNEE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 254 T-TAKESLRRvLQEKIEVV-RKLSEVERSLSNTEDECTHL------KEMNERT--QEELRELANKYNGAVNEIKDLSDKL 323
Cdd:pfam15619 69 VrVLRERLRR-LQEKERDLeRKLKEKEAELLRLRDQLKRLeklsedKNLAEREelQKKLEQLEAKLEDKDEKIQDLERKL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 530373136 324 KVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIE 363
Cdd:pfam15619 148 ELENKSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLK 187
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
176-696 |
3.26e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 176 EALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDR-------LLSRLEVMGNQLQACSKNQTEDSLRKELIALQED 248
Cdd:TIGR00618 369 EISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQReqatidtRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAIT 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 249 KHNYETTAKE----SLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLK 324
Cdd:TIGR00618 449 CTAQCEKLEKihlqESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTR 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 325 VAEGKQEEIQQKGQAEKKeLQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIqvddflpkINGSTEKEHLLSKs 404
Cdd:TIGR00618 529 RMQRGEQTYAQLETSEED-VYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKED--------IPNLQNITVRLQD- 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 405 ggdctFIHQFIECQKKLIVEGHLTKAVEETKLSKEnQTRAKESDFSDTLspSKEKSSDDTTDAQMDEQDLNEPLAKVSLL 484
Cdd:TIGR00618 599 -----LTEKLSEAEDMLACEQHALLRKLQPEQDLQ-DVRLHLQQCSQEL--ALKLTALHALQLTLTQERVREHALSIRVL 670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 485 KddLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENL 564
Cdd:TIGR00618 671 P--KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKEL 748
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 565 REEKDSEITSTRDELLSARDEILLLHQAAAKVA------SERDTDIASLQEELKKVRAELERWRKaasEYEKEITSLQNS 638
Cdd:TIGR00618 749 MHQARTVLKARTEAHFNNNEEVTAALQTGAELShlaaeiQFFNRLREEDTHLLKTLEAEIGQEIP---SDEDILNLQCET 825
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 530373136 639 FQLRCQQCeDQQREEATRLQGELEKLRKEWNaletECHSLKRENVLLSSELQRQEKEL 696
Cdd:TIGR00618 826 LVQEEEQF-LSRLEEKSATLGEITHQLLKYE----ECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
258-367 |
3.52e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 258 ESLRRVLQEKI-EVVRKLSEVERSLSNTEDEcthLKEMNERTQEELRELANKYNGAVNE--------IKDLSD--KLKVA 326
Cdd:PRK00409 526 EELERELEQKAeEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLEEAEKEAQQAIKEakkeadeiIKELRQlqKGGYA 602
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 530373136 327 EGKQEEIQQKgqaeKKELQHKIDEMEEKEQELQAKIEALQA 367
Cdd:PRK00409 603 SVKAHELIEA----RKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
591-783 |
3.74e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 591 QAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRcqqcedQQREEATRLQGELEKLRKEWNa 670
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL------PLYQELEALEAELAELPERLE- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 671 letechslkrenvllssELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDsadLKTLLSKAENQAK 750
Cdd:COG4717 150 -----------------ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD---LAEELEELQQRLA 209
|
170 180 190
....*....|....*....|....*....|...
gi 530373136 751 DVQKEYEKTQTVLSELKLKFEMTEQEKQSITDE 783
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
218-568 |
4.04e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.65 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 218 RLEVMGNQLQACSKNQTEdsLRKELIALQEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNER 297
Cdd:pfam07888 28 RAELLQNRLEECLQERAE--LLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 298 TQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEE---KEQELQAKIEALQADNDFTNE 374
Cdd:pfam07888 106 LSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKagaQRKEEEAERKQLQAKLQQTEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 375 RLTALQgiqvDDFLPKINGSTEKEHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKA----VEETKLSKENQTRAKESDFS 450
Cdd:pfam07888 186 ELRSLS----KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEelrsLQERLNASERKVEGLGEELS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 451 DTLSpSKEKSSDDTTDAQMDEQDLNEPLAKVSL--------LKDDLQGAQSEIEAKQE-IQHLRKELIEAQELARTSKQK 521
Cdd:pfam07888 262 SMAA-QRDRTQAELHQARLQAAQLTLQLADASLalregrarWAQERETLQQSAEADKDrIEKLSAELQRLEERLQEERME 340
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 530373136 522 CFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEK 568
Cdd:pfam07888 341 REKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEK 387
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
513-723 |
4.80e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.26 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 513 ELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQA 592
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 593 AAKVASERDTDIASLQEELKKVRaELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEatrlQGELEKLRKEWNALE 672
Cdd:pfam07888 110 SEELSEEKDALLAQRAAHEARIR-ELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEE----EAERKQLQAKLQQTE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 530373136 673 TECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQmsRKELENQ 723
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH--RKEAENE 233
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
496-734 |
5.28e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 496 EAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITST 575
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 576 RDellsardeillLHQAAAKVASErdtdIASLQEELKKVR--AELERWRKAASEYEKEITSLQNS---FQLRCQQCEDQQ 650
Cdd:PHA02562 258 NK-----------LNTAAAKIKSK----IEQFQKVIKMYEkgGVCPTCTQQISEGPDRITKIKDKlkeLQHSLEKLDTAI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 651 REEATRLQgELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSL-KE 729
Cdd:PHA02562 323 DELEEIMD-EFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELvKE 401
|
....*
gi 530373136 730 QHLRD 734
Cdd:PHA02562 402 KYHRG 406
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
210-368 |
5.55e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 210 IDEDRLLSRLEVMGNQLQACSKNQTE---DSLRKELIALQED-KHNYETTAKEslrrvLQEKIEVVRKLSEVERSLsnte 285
Cdd:PRK04778 249 LDHLDIEKEIQDLKEQIDENLALLEEldlDEAEEKNEEIQERiDQLYDILERE-----VKARKYVEKNSDTLPDFL---- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 286 decTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKK---ELQHKIDEMEEKEQELQ 359
Cdd:PRK04778 320 ---EHAKEQNKELKEEIDRVKQSYtlnESELESVRQLEKQLESLEKQYDEITERIAEQEIaysELQEELEEILKQLEEIE 396
|
....*....
gi 530373136 360 AKIEALQAD 368
Cdd:PRK04778 397 KEQEKLSEM 405
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
165-344 |
5.60e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 165 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWqALIDEDRLLSRLEVMGNQLQACSKNQTE-DSLRKELI 243
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-DEIDVASAEREIAELEAELERLDASSDDlAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 244 ALQEDkhnyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLK----EMNERTQEELRELANKYNGAVNEIKDL 319
Cdd:COG4913 696 ELEAE-----------LEELEEELDELKGEIGRLEKELEQAEEELDELQdrleAAEDLARLELRALLEERFAAALGDAVE 764
|
170 180
....*....|....*....|....*
gi 530373136 320 SDKLKVAEGKQEEIQQKGQAEKKEL 344
Cdd:COG4913 765 RELRENLEERIDALRARLNRAEEEL 789
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
52-106 |
6.34e-03 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein kinase DUN1 and similar proteins; DUN1 is a protein kinase that controls the DNA damage response in yeast. It phosphorylates SML1 on serine residues and cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438735 [Multi-domain] Cd Length: 96 Bit Score: 36.70 E-value: 6.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530373136 52 SRNHALVWFDHKTGKFYLQ-----------DTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFG 106
Cdd:cd22683 28 SRSCDLVLSDPSISRFHAElrleqnginviDNNSANGTFINGKRIKGKT-----YILKNGDIIVFG 88
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
165-367 |
6.36e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.06 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 165 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEasdtsWQALIDEDRLLSR----LEVMGNQLQACSKNQT--EDSL 238
Cdd:COG0497 172 KELEELRADEAERARELDLLRFQLEELEAAALQPGE-----EEELEEERRRLSNaeklREALQEALEALSGGEGgaLDLL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 239 RKELIALQEDKHnYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERtQEELRELANKYNGAVNEIKD 318
Cdd:COG0497 247 GQALRALERLAE-YDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEER-LALLRRLARKYGVTVEELLA 324
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 530373136 319 LSDKLkvaegkqeeiqqkgQAEKKELQHKIDEMEEKEQELQAKIEALQA 367
Cdd:COG0497 325 YAEEL--------------RAELAELENSDERLEELEAELAEAEAELLE 359
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
276-376 |
6.51e-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: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 276 EVERSLSNTEDECTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEK----------K 342
Cdd:pfam06160 288 YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEvayselqeelE 367
|
90 100 110
....*....|....*....|....*....|....
gi 530373136 343 ELQHKIDEMEEKEQELQAKIEALQADNDFTNERL 376
Cdd:pfam06160 368 EILEQLEEIEEEQEEFKESLQSLRKDELEAREKL 401
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
192-801 |
6.87e-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: 40.34 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 192 QRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYET----TAKESLRRVLQEK 267
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNeeriDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 268 IEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVA-EGKQEEIQQKGQAEKKELQH 346
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDdEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 347 KIDEMEEKEQEL---QAKIEALQADNDFTNERLTALQGIQVDDFLPKingSTEKEHLLSKSGGDCTFIHQFIECQKKLIV 423
Cdd:pfam02463 333 EKEEIEELEKELkelEIKREAEEEEEEELEKLQEKLEQLEEELLAKK---KLESERLSSAAKLKEEELELKSEEEKEAQL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 424 EGHLTKAVEETKLSKENQTRAKES---DFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQE 500
Cdd:pfam02463 410 LLELARQLEDLLKEEKKEELEILEeeeESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELL 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 501 IQHLRKELIEAQELARTSKQKCFELQ---------------------ALLEEERKAYRNQVEESTKQIQVLQAQLQRLHI 559
Cdd:pfam02463 490 LSRQKLEERSQKESKARSGLKVLLALikdgvggriisahgrlgdlgvAVENYKVAISTAVIVEVSATADEVEERQKLVRA 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 560 DTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSF 639
Cdd:pfam02463 570 LTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLR 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 640 QLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKE 719
Cdd:pfam02463 650 KGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQE 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 720 LENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLkfEMTEQEKQSITDELKQCKNNLKLLREKGN 799
Cdd:pfam02463 730 AQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAE--EREKTEKLKVEEEKEEKLKAQEEELRALE 807
|
..
gi 530373136 800 NK 801
Cdd:pfam02463 808 EE 809
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
330-570 |
8.06e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.36 E-value: 8.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 330 QEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGiQVDDFLPKINGSTEKEHLLSKsggdct 409
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR-RIRALEQELAALEAELAELEK------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 410 fihqfiecqkkliveghltkavEETKLSKENQTRAKEsdFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQ 489
Cdd:COG4942 91 ----------------------EIAELRAELEAQKEE--LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 490 GAQSEIEakqEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKD 569
Cdd:COG4942 147 ARREQAE---ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
.
gi 530373136 570 S 570
Cdd:COG4942 224 E 224
|
|
| VI_FHA |
TIGR03354 |
type VI secretion system FHA domain protein; Members of this protein family are FHA ... |
49-106 |
8.97e-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: 39.28 E-value: 8.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530373136 49 KVLSRNHALV-WFDhktGKFYLQDTkSSNGTFINS--QRLSRGSEesppcEILS-GDIIQFG 106
Cdd:TIGR03354 43 RHVSGRHARIrYRD---GAYLLTDL-STNGVFLNGsgSPLGRGNP-----VRLEqGDRLRLG 95
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
472-702 |
9.61e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.55 E-value: 9.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 472 QDLNEPLAKVSLLKDDlqgaqseiEAKQEIQHLRKELIEAQELARTSKQKCFELqALLEEERKAYRN---QVEESTKQIQ 548
Cdd:COG3096 874 QLLNKLLPQANLLADE--------TLADRLEELREELDAAQEAQAFIQQHGKAL-AQLEPLVAVLQSdpeQFEQLQADYL 944
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 549 VLQAQLQRLHIDTENLREekdseiTSTRDELLSARDEILLLHQAAAKVASERdTDIASLQEELKKVRAELERWRKAASEY 628
Cdd:COG3096 945 QAKEQQRRLKQQIFALSE------VVQRRPHFSYEDAVGLLGENSDLNEKLR-ARLEQAEEARREAREQLRQAQAQYSQY 1017
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 629 EKEITSLQNSFQLRCQQ------------------CEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQ 690
Cdd:COG3096 1018 NQVLASLKSSRDAKQQTlqeleqeleelgvqadaeAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLR 1097
|
250
....*....|..
gi 530373136 691 RQEKELHNSQKQ 702
Cdd:COG3096 1098 KAERDYKQEREQ 1109
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
175-368 |
9.68e-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: 38.75 E-value: 9.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 175 QEALHREQMLEQKLATLQRLLAitqeasdtswqalidedRLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYET 254
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLK-----------------ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373136 255 TAKESLRRVLQEKIEVVRKlsevERSLSNTEDECTHLKEMNERTQEELRELankyngaVNEIKDLSDKLKVAEGKQEEIQ 334
Cdd:COG1579 69 EEVEARIKKYEEQLGNVRN----NKEYEALQKEIESLKRRISDLEDEILEL-------MERIEELEEELAELEAELAELE 137
|
170 180 190
....*....|....*....|....*....|....
gi 530373136 335 QKGQAEKKELQHKIDEMEEKEQELQAKIEALQAD 368
Cdd:COG1579 138 AELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| |
