|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
3-130 |
2.67e-81 |
|
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and similar proteins; SLMAP, also called sarcolemmal-associated protein (SLAP), is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. It is a cardiac membrane protein that plays an important role in E-C coupling and the adrenergic response of the heart. Overexpression of the SLMAP gene has been associated with diabetes and endothelial dysfunction of macro- and micro-blood vessels. SLMAP contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438731 [Multi-domain] Cd Length: 126 Bit Score: 256.43 E-value: 2.67e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 3 SALAIFTCRPNSHPFQERHVYLDEPIKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINS 82
Cdd:cd22679 1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1799135574 83 QRLSRGSEESPPCEILSGDIIQFGVDVTENTRKVTHGCIVSTIKLFLP 130
Cdd:cd22679 79 QRLSKGSEESEPRELHSGDIVQFGVDVVENSRKVTHGCIVATVTLFLP 126
|
|
| CC1_SLMAP |
cd21911 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal ... |
163-225 |
1.96e-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: 1.96e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799135574 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQ 225
Cdd:cd21911 1 QELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQLS 63
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-795 |
7.21e-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: 7.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 156 NTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQA--CSKNQTE 233
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvAQLELQI 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 234 DSLRKELIAL------QEDKHNYETTAKESLRRVLQE--KIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELAN 305
Cdd:TIGR02168 396 ASLNNEIERLearlerLEDRRERLQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 306 KYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKidemEEKEQELQAKIEALQADNDFTNERLTALQGIqVDDF 385
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ----SGLSGILGVLSELISVDEGYEAAIEAALGGR-LQAV 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 386 LPKINGSTEK--EHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSP--SKEKSSDD 461
Cdd:TIGR02168 551 VVENLNAAKKaiAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllGGVLVVDD 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 462 TTDAQMDEQDLNEPLAKVSL-----------LKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFEL---QALL 527
Cdd:TIGR02168 631 LDNALELAKKLRPGYRIVTLdgdlvrpggviTGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELrkeLEEL 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 528 EEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEkdseITSTRDELLSARDEILLLHQAAAKV---ASERDTDIAS 604
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER----IAQLSKELTELEAEIEELEERLEEAeeeLAEAEAEIEE 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 605 LQEELKKVRAELERWRKAASEYEKEITSLQNSF---QLRCQQCEDQQREEATRL----------QGELEKLRKEWNALET 671
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATERRLedleeqieelSEDIESLAAEIEELEE 866
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 672 ECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHlrdsADLKTLLSKAENQAKDVQ 751
Cdd:TIGR02168 867 LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL----AQLELRLEGLEVRIDNLQ 942
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1799135574 752 keyektQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 795
Cdd:TIGR02168 943 ------ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| FHA_DMA-like |
cd22692 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest ... |
27-108 |
1.84e-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: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 27 PIKIGRSVARCRPAQNNAT-FDCKVLSRNHALVWfdHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQF 105
Cdd:cd22692 38 QIHIGRYTERVRQAIYHPVvFKSKVVSRTHGCIK--VDEGNWYIKDVKSSSGTFLNHQRLSPASRTSKPYPLRDGDILQL 115
|
...
gi 1799135574 106 GVD 108
Cdd:cd22692 116 GMD 118
|
|
| FHA_VPS64-like |
cd22695 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ... |
6-126 |
5.85e-16 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 64 (VPS64) and similar proteins; This subfamily includes VPS64 (also called factor arrest protein 9 or FAR9) and factor arrest protein 10 (FAR10), which participate in the control of the re-entry into the cell cycle following pheromone treatment. VPS64 is also involved in vacuolar protein sorting. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438747 [Multi-domain] Cd Length: 133 Bit Score: 75.03 E-value: 5.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 6 AIFTCRPNSHPFQERHV---YLDEPIKIGRSVARCRPAQN---------------NATFDCKVLSRNHALVWFDHKTGKF 67
Cdd:cd22695 2 HILVLKSLNATFETKFLvvpFKPDGLKLGRPVTNSVNKNNsgskrdlfsqqvrpdNGNFDSRVLSRNHACLSCDPTTGKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135574 68 YLQDTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFGVDVTEntrKVTHGCIVSTIK 126
Cdd:cd22695 82 YIRDLKSSNGTFVNGQKIRQND-----VELKVGDEVDLGTDIDS---KIEHRKISAYVE 132
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
13-106 |
5.16e-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: 5.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 13 NSHPFQERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINSQRLsrgseeS 92
Cdd:cd00060 6 DGDGGGREFPLTKGVVTIGRS------PDCDIVLDDPSVSRRHARIEVDG--GGVYLEDLGSTNGTFVNGKRI------T 71
|
90
....*....|....
gi 1799135574 93 PPCEILSGDIIQFG 106
Cdd:cd00060 72 PPVPLQDGDVIRLG 85
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
172-795 |
6.35e-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: 76.25 E-value: 6.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 172 LQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRllsrlevmgnqlqacSKNQTEDSLRKELIALQEDKHNYE 251
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS---------------ELEEEIEELQKELYALANEISRLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 252 ttakeslrrvlQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEI 331
Cdd:TIGR02168 302 -----------QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 332 QQKGQAEKKELQH---KIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQvddflpkingsteKEHLLSKSGGDCTF 408
Cdd:TIGR02168 371 ESRLEELEEQLETlrsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI-------------EELLKKLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 409 IHQFIECQKKLIVEGHLTKAVEETKLSK-ENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLK---- 483
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEElREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKnqsg 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 484 -DDLQGAQSEI----------------------------EAKQEIQHLRKE----------------LIEAQELARTSKQ 518
Cdd:TIGR02168 518 lSGILGVLSELisvdegyeaaieaalggrlqavvvenlnAAKKAIAFLKQNelgrvtflpldsikgtEIQGNDREILKNI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 519 KCFELQAL-LEEERKAYRNQVE--------------------------------------------ESTKQIQVLQAQLQ 553
Cdd:TIGR02168 598 EGFLGVAKdLVKFDPKLRKALSyllggvlvvddldnalelakklrpgyrivtldgdlvrpggvitgGSAKTNSSILERRR 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 554 RLHIDTENLR--EEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEIT 631
Cdd:TIGR02168 678 EIEELEEKIEelEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 632 SLQNSFQLRCQQCEdQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSIL 711
Cdd:TIGR02168 758 ELEAEIEELEERLE-EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 712 QMSRKELENQVGSLKEQHLRDSA---DLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNN 788
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAeieELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
....*..
gi 1799135574 789 LKLLREK 795
Cdd:TIGR02168 917 LEELREK 923
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
28-105 |
1.51e-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: 1.51e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135574 28 IKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRLSRgseesPPCEILSGDIIQF 105
Cdd:pfam00498 1 VTIGRS------PDCDIVLDDPSVSRRHAEIRYD-GGGRFYLEDLGSTNGTFVNGQRLGP-----EPVRLKDGDVIRL 66
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
477-774 |
1.74e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 477 AKVSLLKDDLQGAQSEiEAKQEIQHLRKELIEAQELartskqkcfelQALLEEERKAYRNQVEESTKQIQVLQAQLQRLH 556
Cdd:COG1196 227 AELLLLKLRELEAELE-ELEAELEELEAELEELEAE-----------LAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 557 IDTENLREEKDSEitstRDELLSARDEILLLHQAAAKVASErdtdIASLQEELKKVRAELERWRKAASEYEKEITSLQNS 636
Cdd:COG1196 295 AELARLEQDIARL----EERRRELEERLEELEEELAELEEE----LEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 637 FQLRCQQCEDQQREEATRLQGELEKLRKEwNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRK 716
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAA-AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135574 717 ELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQE 774
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
498-795 |
1.79e-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: 74.72 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 498 EIQHLRKELIEAQELARTSKQKCFELQALLEEERKA----YRNQVEESTKQIQVLQAQLQRLhidtENLREEKDSEITST 573
Cdd:TIGR02169 188 RLDLIIDEKRQQLERLRREREKAERYQALLKEKREYegyeLLKEKEALERQKEAIERQLASL----EEELEKLTEEISEL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 574 RDELLSARDeilLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNsfQLRCQQCE-DQQREEA 652
Cdd:TIGR02169 264 EKRLEEIEQ---LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE--RLAKLEAEiDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 653 TRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRD 732
Cdd:TIGR02169 339 EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL 418
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799135574 733 SADlktlLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 795
Cdd:TIGR02169 419 SEE----LADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
239-781 |
4.88e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.25 E-value: 4.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 239 ELIALQEDKHNYETTAKESLRRV--LQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKD 316
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 317 LSDKLKVAEGKQEEIQQKGQAEKK--ELQHKIDEMEEKEQELQAKIEALQadndftnerltalqgiqvddflpKINGSTE 394
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELK-----------------------KAAAAKK 1418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 395 KEHLLSKSGgdctfihqfiECQKKlivEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKE--KSSDDTTDAQMDEQDL 472
Cdd:PTZ00121 1419 KADEAKKKA----------EEKKK---ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEeaKKADEAKKKAEEAKKA 1485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 473 NEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRK--ELIEAQELARTSKQKCFELQALLEEERKAYR-NQVEESTKQIQVLQ 549
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKaeEAKKADEAKKAEEAKKADEAKKAEEKKKADElKKAEELKKAEEKKK 1565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 550 AQLQRlhidtenlREEKDSEITSTRDELLSardeilllhqaaaKVASERDTDIASLQEELKKVRAE----LERWRKAASE 625
Cdd:PTZ00121 1566 AEEAK--------KAEEDKNMALRKAEEAK-------------KAEEARIEEVMKLYEEEKKMKAEeakkAEEAKIKAEE 1624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 626 YEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELT 705
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA 1704
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135574 706 SDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYE---KTQTVLSELKLKFEMTEQEKQSITDE 781
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEekkKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| CC1_SLMAP-like |
cd21868 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ... |
167-204 |
1.00e-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: 1.00e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1799135574 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21868 1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
522-784 |
1.16e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 522 ELQALLEE-ERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREE---KDSEITSTRDELLSARDEILLLHQAAAKVASE 597
Cdd:COG1196 217 ELKEELKElEAELLLLKLRELEAELEELEAELEELEAELEELEAElaeLEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 598 rdtdIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQcEDQQREEATRLQGELEKLRKEWNALETECHSLK 677
Cdd:COG1196 297 ----LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE-LEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 678 RENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKT 757
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260
....*....|....*....|....*..
gi 1799135574 758 QTVLSELKLKFEMTEQEKQSITDELKQ 784
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAA 478
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
14-106 |
1.18e-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: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 14 SHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716 8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
|
90
....*....|....
gi 1799135574 93 pPCEILSGDIIQFG 106
Cdd:COG1716 75 -PAPLRDGDVIRLG 87
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
52-106 |
1.45e-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: 1.45e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1799135574 52 SRNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQFG 106
Cdd:cd22686 48 SKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPYPLTHGDELKIG 102
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
235-787 |
2.29e-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: 67.35 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 235 SLRKELIALQEDKHNYETTAKE--SLRRVLQEKIEVVRKLSEVERSLsntEDECTHLKEMNERTQEELRELANKYNGAVN 312
Cdd:TIGR04523 170 ELENELNLLEKEKLNIQKNIDKikNKLLKLELLLSNLKKKIQKNKSL---ESQISELKKQNNQLKDNIEKKQQEINEKTT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 313 EIKDLSDKLKVAEGKQEEIQQKGQAEKKELQH---KIDEMEEKEQELQAKIEALQadndftnerltalqgiqvddflpki 389
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLN------------------------- 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 390 ngsTEKEHLLSKSggdctfIHQFIECQKKLIVEghltkavEETKLSKENQtraKESDFSDTLSPSKEKSSDDTTDAQMDE 469
Cdd:TIGR04523 302 ---NQKEQDWNKE------LKSELKNQEKKLEE-------IQNQISQNNK---IISQLNEQISQLKKELTNSESENSEKQ 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 470 QDLNEPLAKVSLLKDDLQGAQSEIEA-KQEIQHLRKELIEAQELArtskqkcfelqALLEEERKAYRNQVEESTKQIQVL 548
Cdd:TIGR04523 363 RELEEKQNEIEKLKKENQSYKQEIKNlESQINDLESKIQNQEKLN-----------QQKDEQIKKLQQEKELLEKEIERL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 549 QAQLQRLHIDTENLrEEKDSEITSTRDELLSARDEIlllhqaaakvaserDTDIASLQEELKKVRAELERWRKAASEYEK 628
Cdd:TIGR04523 432 KETIIKNNSEIKDL-TNQDSVKELIIKNLDNTRESL--------------ETQLKVLSRSINKIKQNLEQKQKELKSKEK 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 629 EITSLQNSFQLRCQQCEDQQREEATRLQGElEKLRKEWNALETECHSLKRENVLLSSELQRQ--EKELHNSQKQSLELTS 706
Cdd:TIGR04523 497 ELKKLNEEKKELEEKVKDLTKKISSLKEKI-EKLESEKKEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQ 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 707 DLSILQMSRKELENQVGSLKEQHL---RDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELK 783
Cdd:TIGR04523 576 TQKSLKKKQEEKQELIDQKEKEKKdliKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIK 655
|
....
gi 1799135574 784 QCKN 787
Cdd:TIGR04523 656 EIRN 659
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
469-794 |
4.40e-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: 67.02 E-value: 4.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 469 EQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCfelqalLEEERKAYRNQVEESTKQIQVL 548
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEA------LERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 549 QAQLQ-----------RLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASER---DTDIASLQEELKKVRA 614
Cdd:TIGR02169 257 TEEISelekrleeieqLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELedaEERLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 615 ELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQRE------EATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQ 688
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEleevdkEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 689 RQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADlktlLSKAENQAKDVQKEYEKTQTVLSELKLKF 768
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD----LSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
330 340
....*....|....*....|....*.
gi 1799135574 769 EMTEQEKQSITDELKQCKNNLKLLRE 794
Cdd:TIGR02169 493 AEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-784 |
5.31e-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: 5.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 197 QEASDTSWQALIDEDRLLSRLEVMGNQLQacsknqtedSLRKELIALQEDKHNYETTAKESLRRVLQEKI---EVVRKLS 273
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIE---------EERKRRDKLTEEYAELKEELEDLRAELEEVDKefaETRDELK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 274 EVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIqqkgQAEKKELQHKIDEMEEKE 353
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK----ALEIKKQEWKLEQLAADL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 354 QELQAKIEALQADNDFTNERLTALQG------IQVDDFLPKINGSTEKEHLLSKS-GGDCTFIHQFIECQKK-------- 418
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELSKLQRelaeaeAQARASEERVRGGRAVEEVLKASiQGVHGTVAQLGSVGERyataieva 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 419 -------LIVEGHLTkAVEETKLSKE-----------NQTRAKESDfsdtLSPSKEK----------------------- 457
Cdd:TIGR02169 545 agnrlnnVVVEDDAV-AKEAIELLKRrkagratflplNKMRDERRD----LSILSEDgvigfavdlvefdpkyepafkyv 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 458 -------SSDDTTDAQMD-------EQDLNEP--------LAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELART 515
Cdd:TIGR02169 620 fgdtlvvEDIEAARRLMGkyrmvtlEGELFEKsgamtggsRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRR 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 516 SKQKCFELQALLEEERKayrnQVEESTKQIQVLQAQLQRLHIDTENLREekdsEITSTRDELLSARDEIlllhQAAAKVA 595
Cdd:TIGR02169 700 IENRLDELSQELSDASR----KIGEIEKEIEQLEQEEEKLKERLEELEE----DLSSLEQEIENVKSEL----KELEARI 767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 596 SERDTDIASLQEELKKVRAEL--ERWRKAASEYEKEITSLQnsfqlrcqqcedQQREEATRLQGELEKLRKEWNALETEC 673
Cdd:TIGR02169 768 EELEEDLHKLEEALNDLEARLshSRIPEIQAELSKLEEEVS------------RIEARLREIEQKLNRLTLEKEYLEKEI 835
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 674 HSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKeqhlRDSADLKTLLSKAENQAKDVQKE 753
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK----KERDELEAQLRELERKIEELEAQ 911
|
650 660 670
....*....|....*....|....*....|.
gi 1799135574 754 YEKTQTVLSELKLKFEMTEQEKQSITDELKQ 784
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEELSEIEDPKGE 942
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
522-795 |
1.35e-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: 65.46 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 522 ELQALLEEERKAYRNQVEE-----STKQIQVLQAQLQRLHIDTENLREEKDsEITSTRDELLSARDEILLLHQAAAKVAS 596
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRElelalLVLRLEELREELEELQEELKEAEEELE-ELTAELQELEEKLEELRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 597 ERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQlRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSL 676
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE-ELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 677 KRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKA-ENQAKDVQKEYE 755
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELE 443
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1799135574 756 KTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 795
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
546-794 |
4.18e-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: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 546 QVLQAQLQRLHIdteNLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASE 625
Cdd:COG1196 216 RELKEELKELEA---ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 626 YEKEITSLQNSFQLRCQQCEDQQREEAtRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELT 705
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLE-ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 706 SDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQC 785
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
....*....
gi 1799135574 786 KNNLKLLRE 794
Cdd:COG1196 452 AELEEEEEA 460
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
267-795 |
4.29e-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: 63.50 E-value: 4.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 267 EVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKI 346
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 347 DEMEEKEQELqAKIEALQADNDftnerltalqgIQVDDFLPKIngsTEKEHLLSKSGGDCTFIHQFIECQKKlivEGHLT 426
Cdd:TIGR04523 117 EQKNKLEVEL-NKLEKQKKENK-----------KNIDKFLTEI---KKKEKELEKLNNKYNDLKKQKEELEN---ELNLL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 427 KAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDaqmdEQDLNEPLAKVSLLKDDLQgaqseiEAKQEIQHLRKEL 506
Cdd:TIGR04523 179 EKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSL----ESQISELKKQNNQLKDNIE------KKQQEINEKTTEI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 507 IEAQELARTSKQKCFELQALLEEERKayrnQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILl 586
Cdd:TIGR04523 249 SNTQTQLNQLKDEQNKIKKQLSEKQK----ELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKL- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 587 lhQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNsfqlrcqQCEDQQREEATRLQgELEKLRKEW 666
Cdd:TIGR04523 324 --EEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQN-------EIEKLKKENQSYKQ-EIKNLESQI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 667 NALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHlrdsADLKTLLSKAENQ 746
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELII----KNLDNTRESLETQ 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1799135574 747 AKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 795
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK 518
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
161-765 |
5.47e-10 |
|
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: 63.21 E-value: 5.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 161 YSQELFQLSQYLQEA--LHREQ--MLEQKLATLQRLLAITQEASDtswqALIDedrlLSRLEvmgNQLQACSKNQTEDSL 236
Cdd:pfam15921 83 YSHQVKDLQRRLNESneLHEKQkfYLRQSVIDLQTKLQEMQMERD----AMAD----IRRRE---SQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 237 RKELIA--LQEDKHNYETTAKESLRR-------VLQEKIEVVRKLSEVERSLSNTEDECT--HLKEMNERTQEELRELAN 305
Cdd:pfam15921 152 HELEAAkcLKEDMLEDSNTQIEQLRKmmlshegVLQEIRSILVDFEEASGKKIYEHDSMStmHFRSLGSAISKILRELDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 306 KYNGAVNEIKDLSDKLKVAEGK-QEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDD 384
Cdd:pfam15921 232 EISYLKGRIFPVEDQLEALKSEsQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 385 FLPKINGSTEKEHLLSKSGGDC-----TFIHQFIECQKKLIV-EGHLTKA-VEETKLSKE--NQTRAKESDFSDTLSPSK 455
Cdd:pfam15921 312 NSMYMRQLSDLESTVSQLRSELreakrMYEDKIEELEKQLVLaNSELTEArTERDQFSQEsgNLDDQLQKLLADLHKREK 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 456 EKSSDDTTDAQMDEQDLNEPLAKVSLLK--DDLQGAQSEIEA-----KQEIQHLRKELIEAQELARTSKQKCFELQALLE 528
Cdd:pfam15921 392 ELSLEKEQNKRLWDRDTGNSITIDHLRRelDDRNMEVQRLEAllkamKSECQGQMERQMAAIQGKNESLEKVSSLTAQLE 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 529 EERKAYRNQVEESTKQIQVLQAQlQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDtdiaslqeE 608
Cdd:pfam15921 472 STKEMLRKVVEELTAKKMTLESS-ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGD--------H 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 609 LKKVRAELERWRKAASEYEKEITSLQNSFQlRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLK----------R 678
Cdd:pfam15921 543 LRNVQTECEALKLQMAEKDKVIEILRQQIE-NMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKilkdkkdakiR 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 679 ENVLLSSELQRQEKELHNSQKQSLELTSD--------LSILQMSRKELEN---QVGSLKEQHLRDSADLKTLLSKAENQA 747
Cdd:pfam15921 622 ELEARVSDLELEKVKLVNAGSERLRAVKDikqerdqlLNEVKTSRNELNSlseDYEVLKRNFRNKSEEMETTTNKLKMQL 701
|
650
....*....|....*...
gi 1799135574 748 KDVQKEYEKTQTVLSELK 765
Cdd:pfam15921 702 KSAQSELEQTRNTLKSME 719
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
484-703 |
8.24e-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: 8.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 484 DDLQGAQSEIE-AKQEIQHLRkELIEAQELARTSKQKCFELQALLEeerkayRNQVEESTKQIQVLQAQLQRLhidtENL 562
Cdd:COG4913 235 DDLERAHEALEdAREQIELLE-PIRELAERYAAARERLAELEYLRA------ALRLWFAQRRLELLEAELEEL----RAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 563 REEKDSEITSTRDELLSARDEILLLHQAAAKVASERdtdIASLQEELKKVRAELERWRKAASEYEKEITSLQNSfqlrcq 642
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRGNGGDR---LEQLEREIERLERELEERERRRARLEALLAALGLP------ 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799135574 643 qcEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNsQKQSLE 703
Cdd:COG4913 375 --LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA-EIASLE 432
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
298-794 |
1.41e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 298 EELRELANKYNGAVNEIkdLSDKLKVAEGKQEEIQQKgqaEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTAL 377
Cdd:PRK02224 165 EEYRERASDARLGVERV--LSDQRGSLDQLKAQIEEK---EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 378 QGIqvddflpkingstekehllsksggdctfIHQFIECQKKLIVeghLTKAVEETKLSKENQTRAKEsDFSDTLSPSKEK 457
Cdd:PRK02224 240 DEV----------------------------LEEHEERREELET---LEAEIEDLRETIAETERERE-ELAEEVRDLRER 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 458 SSD--DTTDAQMDEQDLNEPLAK-VSLLKDDLQGAQSEIE------------AKQEIQHLRKELIEAQELARTSKQKCFE 522
Cdd:PRK02224 288 LEEleEERDDLLAEAGLDDADAEaVEARREELEDRDEELRdrleecrvaaqaHNEEAESLREDADDLEERAEELREEAAE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 523 LQALLEEERKA---YRNQVEESTKQIQVLQAQLQRLHIDTEN-------LREEKD---SEITSTRDELLSARDEI----- 584
Cdd:PRK02224 368 LESELEEAREAvedRREEIEELEEEIEELRERFGDAPVDLGNaedfleeLREERDelrEREAELEATLRTARERVeeaea 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 585 LLlhqAAAK---------------VASERDTDIASLQEELKKVRAELERWR------KAASEYEKEITSLQNSFQlRCQQ 643
Cdd:PRK02224 448 LL---EAGKcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEerleraEDLVEAEDRIERLEERRE-DLEE 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 644 CEDQQREEATRLQGELEKLRKEWNALETECHSlKRE---NVLLSSELQRQEKELHNSQ----KQSLELTSDLSILQMSRK 716
Cdd:PRK02224 524 LIAERRETIEEKRERAEELRERAAELEAEAEE-KREaaaEAEEEAEEAREEVAELNSKlaelKERIESLERIRTLLAAIA 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 717 ELENQVGSLKEQ-------------HLRDSADLKTLLSKA--ENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDE 781
Cdd:PRK02224 603 DAEDEIERLREKrealaelnderreRLAEKRERKRELEAEfdEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAE 682
|
570
....*....|...
gi 1799135574 782 LKQCKNNLKLLRE 794
Cdd:PRK02224 683 IGAVENELEELEE 695
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
228-704 |
1.70e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 228 SKNQTEDSLRKELIALQEDKHNYETTAKEsLRRVLQEKIEVVRKLSEVERSlsntEDECTHLKEMNERTQEELRELANKY 307
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEE-LKKEIEELEEKVKELKELKEK----AEEYIKLSEFYEEYLDELREIEKRL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 308 NGAVNEIKDLSDKLKVAEGKQEEIQqKGQAEKKELQHKIDEMEEKEQELQaKIEALQADNDFTNERLTALQGIQVDDFLP 387
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEKLEKELE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 388 KI-NGSTEKEHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKAV---------EETKLSKENQTRAKESDFSDTLSPSKEK 457
Cdd:PRK03918 395 ELeKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEK 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 458 SSDdttdAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQ-ELARTSKQKCFELQALLE------EE 530
Cdd:PRK03918 475 ERK----LRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKaEEYEKLKEKLIKLKGEIKslkkelEK 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 531 RKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDtDIASLQEELK 610
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEK-ELKKLEEELD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 611 KVRAELERWRKAASEYEKEITSLQNSFqlrcqqcedqQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQ 690
Cdd:PRK03918 630 KAFEELAETEKRLEELRKELEELEKKY----------SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
490
....*....|....
gi 1799135574 691 EKELHNSQKQSLEL 704
Cdd:PRK03918 700 KEELEEREKAKKEL 713
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
255-795 |
2.40e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 255 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNgAVNEIKDLSDKLKVAEGKQEEIQQK 334
Cdd:PRK03918 178 IERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 335 GQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTaLQGIQVDDFLPKINGSTEKEHLLSKSGGdctFIHQFIE 414
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEING---IEERIKE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 415 CQKKLIVEGHLTKAVEETKlSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIE 494
Cdd:PRK03918 333 LEEKEERLEELKKKLKELE-KRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKIT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 495 AKQ-EIQHLRKELIEAQELARTSKQKCFELQALLEEERKAyrNQVEESTKQIQVLQAQLQRLHIDTENLREEKdseitST 573
Cdd:PRK03918 412 ARIgELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRK--ELLEEYTAELKRIEKELKEIEEKERKLRKEL-----RE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 574 RDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFqlrcqqcedqqrEEAT 653
Cdd:PRK03918 485 LEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL------------EKLE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 654 RLQGELEKLRKEWNALETECHSLKRENVLLS----SELQRQEKELHNSQKQSLELT---SDLSILQMSRKELENQVGSLK 726
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAELLKELEELGfesvEELEERLKELEPFYNEYLELKdaeKELEREEKELKKLEEELDKAF 632
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135574 727 EQHLRDSADLKTLLSK--------AENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 795
Cdd:PRK03918 633 EELAETEKRLEELRKEleelekkySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
167-618 |
3.71e-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: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQAC--SKNQTEDSLRKELIALQ 244
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAElaEAEEELEELAEELLEAL 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 245 EDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVA 324
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 325 EGKQEEIQQ-KGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDDF-------------LPKIN 390
Cdd:COG1196 473 ALLEAALAElLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAayeaaleaalaaaLQNIV 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 391 GSTEK------EHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKAVEETKLSKENQTR---AKESDFSDTLspskeksSDD 461
Cdd:COG1196 553 VEDDEvaaaaiEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLReadARYYVLGDTL-------LGR 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 462 TTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEES 541
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE 705
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135574 542 TKQIQVLQAQLQRLHIDTENLREEKDSEitstRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELER 618
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAE----REELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
250-795 |
3.84e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 250 YETTAKES--LRRVLQEKIEVVRKL----SEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLsDKLKV 323
Cdd:PRK03918 160 YENAYKNLgeVIKEIKRRIERLEKFikrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-EELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 324 AEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQAdndfTNERLTALQG-----IQVDDFLPKIN-GSTEKEH 397
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE----KVKELKELKEkaeeyIKLSEFYEEYLdELREIEK 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 398 LLSKSGGDCTFIHQFI-ECQKKLIVEGHLTKAVEETKlSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPL 476
Cdd:PRK03918 315 RLSRLEEEINGIEERIkELEEKEERLEELKKKLKELE-KRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 477 AKVSLLKDDLQGAQSEIEAKQ-EIQHLRKELIEAQELARTSKQKCFELQALLEEERKAyrNQVEESTKQIQVLQAQLQRL 555
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIgELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRK--ELLEEYTAELKRIEKELKEI 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 556 HIDTENLREEKdseitSTRDELLSARDEILLLHQAAAKvaserdtdIASLQEELKKVraELERWRKAASEYEKeitslqn 635
Cdd:PRK03918 472 EEKERKLRKEL-----RELEKVLKKESELIKLKELAEQ--------LKELEEKLKKY--NLEELEKKAEEYEK------- 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 636 sfqlrcqqcedqQREEATRLQGELEKLRKEWNALEtechSLKRENVLLSSELQRQEKELHNSQKQSLELT-SDLSILQMS 714
Cdd:PRK03918 530 ------------LKEKLIKLKGEIKSLKKELEKLE----ELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEER 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 715 RKELE---NQVGSLK------EQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFemTEQEKQSITDELKQC 785
Cdd:PRK03918 594 LKELEpfyNEYLELKdaekelEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY--SEEEYEELREEYLEL 671
|
570
....*....|
gi 1799135574 786 KNNLKLLREK 795
Cdd:PRK03918 672 SRELAGLRAE 681
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
167-617 |
6.45e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 6.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQAcsKNQTEDSLRKELIALQED 246
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE--LEEAEEALLERLERLEEE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 247 KhnyeTTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEG 326
Cdd:COG1196 423 L----EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 327 KQEEIQQKGQAEKKelQHKIDEMEEKEQELQAKIEALQADNDFTNERLTA-LQGIQVDDFLpkiNGSTEKEHLLSKSGGD 405
Cdd:COG1196 499 AEADYEGFLEGVKA--ALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAaLQNIVVEDDE---VAAAAIEYLKAAKAGR 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 406 CTFIHQFIECQKKLIVEGHLTKAVEETKLSKENQTR---AKESDFSDTLSpskekssDDTTDAQMDEQDLNEPLAKVSLL 482
Cdd:COG1196 574 ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLReadARYYVLGDTLL-------GRTLVAARLEAALRRAVTLAGRL 646
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 483 KDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENL 562
Cdd:COG1196 647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL 726
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135574 563 REEKDSEitstRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKV---RAELE 617
Cdd:COG1196 727 EEQLEAE----REELLEELLEEEELLEEEALEELPEPPDLEELERELERLereIEALG 780
|
|
| CC1_T3JAM |
cd21912 |
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ... |
164-204 |
7.81e-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: 7.81e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1799135574 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21912 5 EILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
|
|
| FHA_TCF19 |
cd22685 |
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ... |
29-119 |
1.15e-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: 54.34 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 29 KIGRSVARCRPAQNNATFDcKVLSRNHALVW---FDHKTGKFYLQDTkSSNGTFINSQRLSRGSEEsppcEILSGDIIQF 105
Cdd:cd22685 31 RIGRNPEVCDVFLCSSQHP-NLISREHAEIHaerDGNGNWKVLIEDR-STNGTYVNDVRLQDGQRR----ELSDGDTITF 104
|
90
....*....|....*.
gi 1799135574 106 G--VDVTENTRKVTHG 119
Cdd:cd22685 105 GhkNGRRVKQWPYQKS 120
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
217-737 |
1.16e-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: 58.98 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 217 LEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTakeslrrvlqekieVVRKLSEVERSLSNTEDECTHLKEMNERT 296
Cdd:pfam15921 278 VEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSM--------------YMRQLSDLESTVSQLRSELREAKRMYEDK 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 297 QEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAK-------IEALQADNDF 369
Cdd:pfam15921 344 IEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDD 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 370 TN---ERLTAL--------QGiQVDDFLPKINGSTEKEHLLSKsggdctfIHQFIECQKKLiveghLTKAVEETKlSKEN 438
Cdd:pfam15921 424 RNmevQRLEALlkamksecQG-QMERQMAAIQGKNESLEKVSS-------LTAQLESTKEM-----LRKVVEELT-AKKM 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 439 QTRAKESDFSDTLSPSKEKS-SDDTTDAQMDE--QDLNEPLAKVSLLK---DDLQGAQSEIEA---------------KQ 497
Cdd:pfam15921 490 TLESSERTVSDLTASLQEKErAIEATNAEITKlrSRVDLKLQELQHLKnegDHLRNVQTECEAlklqmaekdkvieilRQ 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 498 EI--------QHLRKE---LIEAQELARTSKQKCFELQAL--LEEERKAYRNQVEESTKQIQVLQAQLqrLHIDTENLRE 564
Cdd:pfam15921 570 QIenmtqlvgQHGRTAgamQVEKAQLEKEINDRRLELQEFkiLKDKKDAKIRELEARVSDLELEKVKL--VNAGSERLRA 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 565 EKD---------SEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWR--------------K 621
Cdd:pfam15921 648 VKDikqerdqllNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRntlksmegsdghamK 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 622 AASEYEKEITSLQNsfQLRCQQCEDQQREEATR--------LQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKE 693
Cdd:pfam15921 728 VAMGMQKQITAKRG--QIDALQSKIQFLEEAMTnankekhfLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEK 805
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1799135574 694 LHNSQ----KQSLELTSDLSILQmsRKELENQvgSLKEQHLRDSADLK 737
Cdd:pfam15921 806 VANMEvaldKASLQFAECQDIIQ--RQEQESV--RLKLQHTLDVKELQ 849
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
212-794 |
2.08e-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: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 212 RLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTAKESLRRVLQEKIEvvrkLSEVERSlSNTEDECTHLKE 291
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE----LDGFERG-PFSERQIKNFHT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 292 MNERTQEELRELANKyngavnEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQadndftn 371
Cdd:TIGR00606 398 LVIERQEDEAKTAAQ------LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ------- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 372 eRLTAlqgiQVDDFLPKINGSTEKEHLLSKSGGDCTfihqfIECQKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTL 451
Cdd:TIGR00606 465 -QLEG----SSDRILELDQELRKAERELSKAEKNSL-----TETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTR 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 452 SpSKEKSSDDTTDAQMDEQDLNeplakvSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEER 531
Cdd:TIGR00606 535 T-QMEMLTKDKMDKDEQIRKIK------SRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNK 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 532 KAYRNQVEESTKQIQVLqaqlqrlhidtenlrEEKDSEITSTRDEllsardeilllhqaaakvaserDTDIASLQEELKK 611
Cdd:TIGR00606 608 NHINNELESKEEQLSSY---------------EDKLFDVCGSQDE----------------------ESDLERLKEEIEK 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 612 VRAELERWRKAASEYEKEITSLQNSFQLRCQQC------EDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLL-- 683
Cdd:TIGR00606 651 SSKQRAMLAGATAVYSQFITQLTDENQSCCPVCqrvfqtEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlg 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 684 -----SSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSL--KEQHLRDSADLKTLLSKAENQAKDVQKEYEK 756
Cdd:TIGR00606 731 lapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTImpEEESAKVCLTDVTIMERFQMELKDVERKIAQ 810
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1799135574 757 TQTVL--SELKLKFEMTEQEKQSITDELKQCKNNLKLLRE 794
Cdd:TIGR00606 811 QAAKLqgSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
489-728 |
2.46e-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: 57.08 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 489 AQSEIEAKQEIQHLRKELIEAQELARTSKQKcfelQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREekds 568
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 569 EITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQnsfqlrcqqcedQQ 648
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR------------AD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 649 REEATRLQGELEKLRKEWNALETEchsLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQ 728
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAE---LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
14-110 |
2.76e-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: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 14 SHPFQERHV---YLDEPIKIGRSvARCRPAQNNATfdckvLSRNHALVW---FDHKTG-KFYLQDTkSSNGTFINSQRLS 86
Cdd:cd22670 7 SSPGSTDIVlpiYKNQVITIGRS-PSCDIVINDPF-----VSRTHCRIYsvqFDESSApLVYVEDL-SSNGTYLNGKLIG 79
|
90 100
....*....|....*....|....*
gi 1799135574 87 RGseespPCEILS-GDIIQFGVDVT 110
Cdd:cd22670 80 RN-----NTVLLSdGDVIEIAHSAT 99
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
233-784 |
2.89e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 233 EDSLRKELIALQEDKHNYETTAKESLRRVLQEKIEV-VRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAV 311
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEElEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 312 NEIKDLSDKLKVAEGKQEEIQQkgqaEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDDflpking 391
Cdd:COG1196 302 QDIARLEERRRELEERLEELEE----ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA------- 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 392 STEKEHLLSKSggdctfihqfiecQKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQD 471
Cdd:COG1196 371 EAELAEAEEEL-------------EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 472 LNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRN-QVEESTKQIQVLQA 550
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADyEGFLEGVKAALLLA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 551 QLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDtdiasLQEELKKVRAELERWRKAASEYEKEI 630
Cdd:COG1196 518 GLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYL-----KAAKAGRATFLPLDKIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 631 TSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSI 710
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA 672
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799135574 711 LQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 784
Cdd:COG1196 673 ALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
28-85 |
4.52e-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: 4.52e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135574 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 ... |
167-366 |
8.64e-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: 56.23 E-value: 8.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTE-----DSLRKELI 241
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvkselKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 242 ALQEDKHNYETTAKESLRRVLQEKI-EVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDK 320
Cdd:TIGR02169 769 ELEEDLHKLEEALNDLEARLSHSRIpEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1799135574 321 LKVAEGKQEEIQ---QKGQAEKKELQHKIDEMEEKEQELQAKIEALQAD 366
Cdd:TIGR02169 849 IKSIEKEIENLNgkkEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
289-540 |
1.64e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 54.64 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 289 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALqadnd 368
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEEL----- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 369 ftNERLTAL--QGIQVDDFLPKIN----------GSTEKEHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKAVEETKLSK 436
Cdd:PHA02562 240 --TDELLNLvmDIEDPSAALNKLNtaaakikskiEQFQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 437 ENQTRAKEsdfsdtlspskEKSSDDTTDAQMDEQDLNeplAKVSLLKDDLQGAQSEI-EAKQEIQHLRKE-LIEAQELAr 514
Cdd:PHA02562 318 LDTAIDEL-----------EEIMDEFNEQSKKLLELK---NKISTNKQSLITLVDKAkKVKAAIEELQAEfVDNAEELA- 382
|
250 260
....*....|....*....|....*.
gi 1799135574 515 tskqkcfELQALLEEERKAYRNQVEE 540
Cdd:PHA02562 383 -------KLQDELDKIVKTKSELVKE 401
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
487-672 |
2.76e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 487 QGAQSEIEAK-QEIQHLRKELIEAQELARTSKQKcfelQALLEEERKAYRNQVEESTKQIQVLQAQLQRlhidtENLREE 565
Cdd:COG4913 606 FDNRAKLAALeAELAELEEELAEAEERLEALEAE----LDALQERREALQRLAEYSWDEIDVASAEREI-----AELEAE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 566 KDsEITSTRDELLSARDEILLLHQAAAKVASERD---TDIASLQEELKKVRAELERWRKAASEYEKEITSLQNS-FQLRC 641
Cdd:COG4913 677 LE-RLDASSDDLAALEEQLEELEAELEELEEELDelkGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERF 755
|
170 180 190
....*....|....*....|....*....|...
gi 1799135574 642 QQ--CEDQQREEATRLQGELEKLRKEWNALETE 672
Cdd:COG4913 756 AAalGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
27-106 |
3.67e-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: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 27 PIKIGRSVARcRPAQNNATFDC-----KVLSRNHALVWFDHKTGKFYLQdTKSSNGTFINSQRLSRGseeSPPCEILSGD 101
Cdd:cd22701 18 EVVLGRNSKN-SSSTAADSVDIdlgpsKKISRRHARIFYDFTTQCFELS-VLGRNGVKVDGILVKPG---SPPVPLRSGS 92
|
....*
gi 1799135574 102 IIQFG 106
Cdd:cd22701 93 LIQIG 97
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
231-784 |
4.52e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 231 QTEDSLRKELIALQEDKHNYEttakESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELR-ELANKYNg 309
Cdd:PTZ00121 1147 KAEDAKRVEIARKAEDARKAE----EARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKaEEARKAE- 1221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 310 avnEIKDLSDKLKVAEGKQEEIQQKgQAEKKELQHKIDEMEEKEQELQAKIEA-LQADNDFTNERLTALQGIQVDDFLPK 388
Cdd:PTZ00121 1222 ---DAKKAEAVKKAEEAKKDAEEAK-KAEEERNNEEIRKFEEARMAHFARRQAaIKAEEARKADELKKAEEKKKADEAKK 1297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 389 INGSTEKEHLLSKSggdctfihqfiecQKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDA--- 465
Cdd:PTZ00121 1298 AEEKKKADEAKKKA-------------EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAaee 1364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 466 --QMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQElARTSKQKCFELQALLEEERKA--YRNQVEES 541
Cdd:PTZ00121 1365 kaEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK-AAAAKKKADEAKKKAEEKKKAdeAKKKAEEA 1443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 542 TKQIQVLQAQLQRLhiDTENLReeKDSEITSTRDELLSARDEILLLHQAAAKVA-SERDTDIASLQEELKKVRAELERWR 620
Cdd:PTZ00121 1444 KKADEAKKKAEEAK--KAEEAK--KKAEEAKKADEAKKKAEEAKKADEAKKKAEeAKKKADEAKKAAEAKKKADEAKKAE 1519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 621 KAASEYE-KEITSLQNSFQLRcqQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQK 699
Cdd:PTZ00121 1520 EAKKADEaKKAEEAKKADEAK--KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 700 QSLELTSDLSILQMSRKELENQVGSLK----EQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKfemtEQEK 775
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEElkkaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK----AEED 1673
|
....*....
gi 1799135574 776 QSITDELKQ 784
Cdd:PTZ00121 1674 KKKAEEAKK 1682
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
536-700 |
6.32e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 6.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 536 NQVEESTKQIQVLQAQLQRLHIDTENLrEEKDSEITSTRDELLSARDEILLLHQAAAKVA-----SERDTDIASLQEELK 610
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEEL-EELEEELEELEAELEELREELEKLEKLLQLLPlyqelEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 611 KVRAELERWRKAASEY---EKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSEL 687
Cdd:COG4717 150 ELEERLEELRELEEELeelEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170
....*....|...
gi 1799135574 688 QRQEKELHNSQKQ 700
Cdd:COG4717 230 EQLENELEAAALE 242
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
263-769 |
7.31e-07 |
|
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: 53.26 E-value: 7.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 263 QEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGA----------VNEIKDLSDKLKVAEGKQEEIQ 332
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAeemrarlaarKQELEEILHELESRLEEEEERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 333 QKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQG--IQVDDFLPKINGSTEK-EHLLSKSGGDCTFI 409
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEdiLLLEDQNSKLSKERKLlEERISEFTSNLAEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 410 HQFIECQKKLIVEGHLTKAVEETKLSKENQTRAKesdfsdtLSPSKEKSSDDTTDAQMDEQDLNEPLA--KVSLLK--DD 485
Cdd:pfam01576 172 EEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQE-------LEKAKRKLEGESTDLQEQIAELQAQIAelRAQLAKkeEE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 486 LQGAQSEIEAKQ-----------EIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQR 554
Cdd:pfam01576 245 LQAALARLEEETaqknnalkkirELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 555 LHIDTENLREEKDSEITSTRDELLSAR-------DEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYE 627
Cdd:pfam01576 325 REQEVTELKKALEEETRSHEAQLQEMRqkhtqalEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 628 ---KEITSLQNSFQLRCQQCEDQQREEA---TRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQS 701
Cdd:pfam01576 405 hkrKKLEGQLQELQARLSESERQRAELAeklSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQK 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135574 702 LELTSDLsilqmsrKELENQVGSLKEQhlrdsadlktlLSKAENQAKDVQKEYEKTQTVLSELKLKFE 769
Cdd:pfam01576 485 LNLSTRL-------RQLEDERNSLQEQ-----------LEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
25-114 |
8.75e-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: 48.12 E-value: 8.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 25 DEPIKIGRSVArcrpAQNNATFDC-KVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDII 103
Cdd:cd22663 20 GKEVTVGRGLG----VTYQLVSTCpLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERI----EPLKPYPLNEGDLI 90
|
90
....*....|.
gi 1799135574 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 |
1.23e-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: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 26 EPIKIGRSVArcrpaqNNATFDCKVLSRNHALVwfDHKTGKFYLQDTKSSNGTFINSQRLSRGseesppcEILSGDIIQF 105
Cdd:cd22698 21 DEFTIGRSSN------NDIRLNDHSVSRHHARI--VRQGDKCNLTDLGSTNGTFLNGIRVGTH-------ELKHGDRIQL 85
|
.
gi 1799135574 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 |
1.37e-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: 47.31 E-value: 1.37e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1799135574 55 HALVWFDHKTGKFYLQDTKSSNGTFINSQRLSrgseESPPCEILSGDIIQFGVD 108
Cdd:cd22704 39 HAVITYDQIDNEFKIKDLGSLNGTFVNDSRIP----EQTYITLKLGDSIRFGYD 88
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
525-700 |
2.31e-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: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 525 ALLEEERKAYRNQVEESTKQIQVLQAQLQRLhiDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVaSERDTDIAS 604
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDAL--QERREALQRLAEYSWDEIDVASAEREIAELEAELERL-DASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 605 LQEELKKVRAELERWRKAASEYEKEITSLQNSFqlrcQQCEDQQREEATRLQGELEKLRKEWNA-LETECHSLKRENVL- 682
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKEL----EQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALGDAVEr 765
|
170 180
....*....|....*....|...
gi 1799135574 683 -----LSSELQRQEKELHNSQKQ 700
Cdd:COG4913 766 elrenLEERIDALRARLNRAEEE 788
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
229-729 |
2.36e-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: 51.59 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 229 KNQTEDSLRK---ELIALQEDKHNYettakeslRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELAn 305
Cdd:TIGR00606 586 INQTRDRLAKlnkELASLEQNKNHI--------NNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRA- 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 306 KYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALqadndftnERLTALQGIQVDDF 385
Cdd:TIGR00606 657 MLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKST--------ESELKKKEKRRDEM 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 386 LPKINGSTEKEHLLSKSggdctfIHQFIECQKKLiveghltkaveETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDA 465
Cdd:TIGR00606 729 LGLAPGRQSIIDLKEKE------IPELRNKLQKV-----------NRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDV 791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 466 QMDEQdLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRN----QVEES 541
Cdd:TIGR00606 792 TIMER-FQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHlkskTNELK 870
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 542 TKQIQVLQAQLQRLHIDTENlrEEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRK 621
Cdd:TIGR00606 871 SEKLQIGTNLQRRQQFEEQL--VELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKE 948
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 622 AASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGEL-------EKLRKEWNALETECHSLKRENVLLSSELQRQE--- 691
Cdd:TIGR00606 949 KVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLeecekhqEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKren 1028
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1799135574 692 --KELHNSQKQSLELTSDLSILQMSR--KELENQVGSLKEQH 729
Cdd:TIGR00606 1029 elKEVEEELKQHLKEMGQMQVLQMKQehQKLEENIDLIKRNH 1070
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
336-662 |
3.10e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 336 QAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDdflpKINGSTEKEHLLSKSGGDCTFIHQFIEC 415
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE----LSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 416 QKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDttdAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEA 495
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE---LKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 496 KQEIQHLRKELIEaqELARTSKQkcfelqalLEEERKAYRNQVEESTKQIQVLQAQLQRLhidtENLREEKDSEITSTRD 575
Cdd:TIGR02168 829 LERRIAATERRLE--DLEEQIEE--------LSEDIESLAAEIEELEELIEELESELEAL----LNERASLEEALALLRS 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 576 ELLSARDEIlllhQAAAKVASERDTDIASLQEELKKVRAELERWR--------KAASEYEKEITSLQNSFQLRCQQcEDQ 647
Cdd:TIGR02168 895 ELEELSEEL----RELESKRSELRRELEELREKLAQLELRLEGLEvridnlqeRLSEEYSLTLEEAEALENKIEDD-EEE 969
|
330
....*....|....*
gi 1799135574 648 QREEATRLQGELEKL 662
Cdd:TIGR02168 970 ARRRLKRLENKIKEL 984
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
469-634 |
3.21e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 469 EQDLNEPLAKVSLLKDDLQGAQSEI-EAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQ--- 544
Cdd:COG4942 40 EKELAALKKEEKALLKQLAALERRIaALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLgrq 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 545 -------------------------IQVLQAQLQRLHIDTENLREEKDsEITSTRDELLSARDEILLLHQAAAKVASERD 599
Cdd:COG4942 120 pplalllspedfldavrrlqylkylAPARREQAEELRADLAELAALRA-ELEAERAELEALLAELEEERAALEALKAERQ 198
|
170 180 190
....*....|....*....|....*....|....*
gi 1799135574 600 TDIASLQEELKKVRAELERWRKAASEYEKEITSLQ 634
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
605-795 |
3.26e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 605 LQEELKKVRAELERWRKAASEYeKEITSLQNSFQLRCQQCEDQQREEatrlqgELEKLRKEWNALETECHSLKRENVLLS 684
Cdd:COG1196 194 ILGELERQLEPLERQAEKAERY-RELKEELKELEAELLLLKLRELEA------ELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 685 SELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQhlrdSADLKTLLSKAENQAKDVQKEYEKTQTVLSEL 764
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER----RRELEERLEELEEELAELEEELEELEEELEEL 342
|
170 180 190
....*....|....*....|....*....|.
gi 1799135574 765 KLKFEMTEQEKQSITDELKQCKNNLKLLREK 795
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
|
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
479-616 |
3.67e-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: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 479 VSLLKDDLQGAQSEIEAK-QEIQHLRKELIEAQELARTSKQKCFELQAlleeerkayrnQVEESTKQIQVLQAQLQRLHI 557
Cdd:pfam06818 12 ISLLKQQLKDSQAEVTQKlNEIVALRAQLRELRAKLEEKEEQIQELED-----------SLRSKTLELEVCENELQRKKN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799135574 558 DTENLRE---EKDSEITSTRDEL--LSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAEL 616
Cdd:pfam06818 81 EAELLREkvgKLEEEVSGLREALsdVSPSGYESVYESDEAKEQRQEEADLGSLRREVERLRAEL 144
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
289-777 |
4.35e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 289 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKgQAEKKELQHKIDEMEEKEQELQAKIEALQadnd 368
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLE---- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 369 ftnerltalqgiQVDDFLPKINGSTEKEHLLSksggdctfihQFIECQKKLIVEGHLTKAVEETKLSKENQTRAKESDFS 448
Cdd:COG4717 123 ------------KLLQLLPLYQELEALEAELA----------ELPERLEELEERLEELRELEEELEELEAELAELQEELE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 449 DTLSPSKEKSSDDTTDAQMDEQDLNEplaKVSLLKDDLQGAQSEIE-AKQEIQHLRKELIEAQELARTSKQKCFELQALL 527
Cdd:COG4717 181 ELLEQLSLATEEELQDLAEELEELQQ---RLAELEEELEEAQEELEeLEEELEQLENELEAAALEERLKEARLLLLIAAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 528 EEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQE 607
Cdd:COG4717 258 LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 608 ELKKVRAELERWRKAASEYEKEITSLQ--------NSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRE 679
Cdd:COG4717 338 ELLELLDRIEELQELLREAEELEEELQleeleqeiAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGE 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 680 NVLLSSELQRQ--EKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQhlRDSADLKTLLSKAENQAKDVQKEYEKT 757
Cdd:COG4717 418 LEELLEALDEEelEEELEELEEELEELEEELEELREELAELEAELEQLEED--GELAELLQELEELKAELRELAEEWAAL 495
|
490 500
....*....|....*....|
gi 1799135574 758 QTVLSELKLKFEMTEQEKQS 777
Cdd:COG4717 496 KLALELLEEAREEYREERLP 515
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
27-117 |
5.30e-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: 45.81 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 27 PIKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLsrgSEESPPCEILSGDIIQFG 106
Cdd:cd22678 24 PLTIGRIQ------RGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESI---SPNGRPVVLSSGDVITLG 94
|
90
....*....|.
gi 1799135574 107 vdvTENTRKVT 117
Cdd:cd22678 95 ---SETKILVR 102
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
212-671 |
9.97e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 9.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 212 RLLSRLEVMGNQLQACSKNQTEdsLRKELIALQEDKHNYETTAK-ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLK 290
Cdd:COG4717 92 ELQEELEELEEELEELEAELEE--LREELEKLEKLLQLLPLYQElEALEAELAELPERLEELEERLEELRELEEELEELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 291 EMNERTQEELRELANKYNGAV-NEIKDLSDKLKVAEGKQEEIQQkgqaEKKELQHKIDEMEEKEQELQAKIEALQAdndf 369
Cdd:COG4717 170 AELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAELEE----ELEEAQEELEELEEELEQLENELEAAAL---- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 370 tNERLTALQGIQVDDFLpkingstekehLLSKSGGDCTFIHQFIECQKKLIVEGHLTkAVEETKLSKENQTRAKESDFSD 449
Cdd:COG4717 242 -EERLKEARLLLLIAAA-----------LLALLGLGGSLLSLILTIAGVLFLVLGLL-ALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 450 TLsPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLkddlqgaqseiEAKQEIQHLRKELIEAQELARTSKQKCF--ELQALL 527
Cdd:COG4717 309 AL-PALEELEEEELEELLAALGLPPDLSPEELL-----------ELLDRIEELQELLREAEELEEELQLEELeqEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 528 EEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSeitstrdellsardeilLLHQAAAKVASERDTDIASLQE 607
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGE-----------------LEELLEALDEEELEEELEELEE 439
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799135574 608 ELKKVRAELERWRKAASEYEKEITSLQNSFQLrcqqceDQQREEATRLQGELEKLRKEWNALET 671
Cdd:COG4717 440 ELEELEEELEELREELAELEAELEQLEEDGEL------AELLQELEELKAELRELAEEWAALKL 497
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
51-106 |
1.08e-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: 1.08e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799135574 51 LSRNHALVWF----DHKTGKFYLQDTKSSNGTFINSQRLsrgseesPP---CEILSGDIIQFG 106
Cdd:cd22677 41 ISRYHAVLQYrgdaDDHDGGFYLYDLGSTHGTFLNKQRI-------PPkqyYRLRVGHVLKFG 96
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
163-366 |
1.19e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQAcSKNQTEDSLRKELIA 242
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA-ELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 243 LQedKHNYETTAKESLR-RVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKL 321
Cdd:COG4942 113 LY--RLGRQPPLALLLSpEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1799135574 322 KVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQAD 366
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
52-106 |
1.26e-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: 1.26e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135574 52 SRNH-ALVWfdHK-TGKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22674 48 SRVHaALVY--HKhLNRVFLIDLGSTHGTFVGGIRL----EPHKPQQLPIDSTLRFG 98
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
275-759 |
1.31e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 275 VERSLSNTEDECTHLKEMNERTQEelRELANKYNGAVNEIKDLSDKLKVAEGKQEE-IQQKGQA-----EKKELQHKIDE 348
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEE--KDLHERLNGLESELAELDEEIERYEEQREQaRETRDEAdevleEHEERREELET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 349 MEEKEQELQAKIEALQADNDFTNERLTALQGiQVDDFlpkingSTEKEHLLSKSG---GDCTFIHQFIE----------- 414
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRE-RLEEL------EEERDDLLAEAGlddADAEAVEARREeledrdeelrd 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 415 --CQKKLIVEGHLTKAVEETKLSKENQTRAKE-----SDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQ 487
Cdd:PRK02224 329 rlEECRVAAQAHNEEAESLREDADDLEERAEElreeaAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLG 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 488 GAQSEIEAKQE-IQHLRKELIEAQELARTSKQKCFELQALLEE----------ERKAYRNQVEESTKQIQVLQAQLQRLH 556
Cdd:PRK02224 409 NAEDFLEELREeRDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 557 IDTENL-----REEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEIT 631
Cdd:PRK02224 489 EEVEEVeerleRAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 632 SLQN---SFQLRCQQCEDQ------------QREEATRLQGELEKLRKEWNALETECH---SLKRENVL-LSSELQRQEK 692
Cdd:PRK02224 569 EAREevaELNSKLAELKERieslerirtllaAIADAEDEIERLREKREALAELNDERRerlAEKRERKReLEAEFDEARI 648
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799135574 693 ELHNSQKQSLE-----LTSDLSILQMSRKELENQVGSLKEQhLRDSADLKTLLSKAENQAKDVQKEYEKTQT 759
Cdd:PRK02224 649 EEAREDKERAEeyleqVEEKLDELREERDDLQAEIGAVENE-LEELEELRERREALENRVEALEALYDEAEE 719
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
527-755 |
1.53e-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: 48.53 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 527 LEEERKAY---RNQVEESTKQIQVLQAQLQRLHIDTENLR------EEKDSEITSTRDELLSARD------EILLLHQAA 591
Cdd:pfam05622 171 LEEELKKAnalRGQLETYKRQVQELHGKLSEESKKADKLEfeykklEEKLEALQKEKERLIIERDtlretnEELRCAQLQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 592 AKVASERDTDIASLQEELKKVRAELerwrkAASEYEKEITSLQNSFQ-LRCQQcEDQQREEATRLQGELEKLRKEWNALE 670
Cdd:pfam05622 251 QAELSQADALLSPSSDPGDNLAAEI-----MPAEIREKLIRLQHENKmLRLGQ-EGSYRERLTELQQLLEDANRRKNELE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 671 TEcHSLKRENVLLSS----ELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQ--HLRDSADLKTLLSKAE 744
Cdd:pfam05622 325 TQ-NRLANQRILELQqqveELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQieELEPKQDSNLAQKIDE 403
|
250
....*....|.
gi 1799135574 745 NQAKDVQKEYE 755
Cdd:pfam05622 404 LQEALRKKDED 414
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
28-106 |
1.92e-05 |
|
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438732 [Multi-domain] Cd Length: 96 Bit Score: 43.87 E-value: 1.92e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135574 28 IKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDhkTGKFYLQDTKSSNGTFINSQRlsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22680 23 VSIGRDP------ENVIVIPDPFVSRNHARITVD--SNEIYIEDLGSTNGTFVNDFK-----RIKGPAKLHPNDIIKLG 88
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
550-765 |
2.36e-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: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 550 AQLQRLHIDTENLREEKD--SEITSTRDELLSARDEILLLHQAAAKVASERD-TDIASLQEELKKVRAELERWRKAASEY 626
Cdd:COG4913 235 DDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAqRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 627 EKEITSLQNsfqlRCQQCEDQQREEATRlqgELEKLRKEWNALETECHSLKREnvllSSELQRQEKELHnsqkqsLELTS 706
Cdd:COG4913 315 EARLDALRE----ELDELEAQIRGNGGD---RLEQLEREIERLERELEERERR----RARLEALLAALG------LPLPA 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135574 707 DLSILQMSRKELENQVGSLKEQHlrdsADLKTLLSKAENQAKDVQKEYEKTQTVLSELK 765
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEEL----EALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
229-798 |
2.39e-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: 48.18 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 229 KNQTEDSLRKELIALQEDKHNYETTAK---------ESLRRVLQEKIEVVRKLSEVERSlsnTEDECTHLKEMNERTQEE 299
Cdd:pfam05483 94 KVSIEAELKQKENKLQENRKIIEAQRKaiqelqfenEKVSLKLEEEIQENKDLIKENNA---TRHLCNLLKETCARSAEK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 300 LRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNdftnERLTALQG 379
Cdd:pfam05483 171 TKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDK----EKQVSLLL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 380 IQvddflpkingSTEKEHLLSksggDCTFIhqfiecqkkliveghltkaVEETKlSKENQTRAKESDFSDTLSPSKEKSS 459
Cdd:pfam05483 247 IQ----------ITEKENKMK----DLTFL-------------------LEESR-DKANQLEEKTKLQDENLKELIEKKD 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 460 DDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQAL-LEEERKAYRNQV 538
Cdd:pfam05483 293 HLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCsLEELLRTEQQRL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 539 EESTKQIQVLQAQLQRlhidtenlreeKDSEItstrdellsardeilllhQAAAKVASERDTDIaslqEELKKVRAELER 618
Cdd:pfam05483 373 EKNEDQLKIITMELQK-----------KSSEL------------------EEMTKFKNNKEVEL----EELKKILAEDEK 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 619 WRKAASEYEKEITSLQNSFQlrcqqcedqqreeatRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQ 698
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKEQ---------------ELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEK 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 699 KQSLELTSDLSILQMSRKELENQVGSL--------------KEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSEL 764
Cdd:pfam05483 485 LKNIELTAHCDKLLLENKELTQEASDMtlelkkhqediincKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEV 564
|
570 580 590
....*....|....*....|....*....|....
gi 1799135574 765 KLKFEMTEQEKQSITDELKQCKNNLKLLREKGNN 798
Cdd:pfam05483 565 KCKLDKSEENARSIEYEVLKKEKQMKILENKCNN 598
|
|
| FHA_RAD53-like_rpt2 |
cd22690 |
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
12-103 |
3.09e-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: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 12 PNSHPfqerHVYL-DEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFD-HKTGK--FYLQDTkSSNGTFINSQRLSR 87
Cdd:cd22690 8 NPSYP----DIELtQNTTFIGRS------KDCDEEITDPRISKHHCIITRKrSGKGLddVYVTDT-STNGTFINNNRLGK 76
|
90
....*....|....*.
gi 1799135574 88 GSEesppCEILSGDII 103
Cdd:cd22690 77 GSQ----SLLQDGDEI 88
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
237-669 |
3.74e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.59 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 237 RKELIALQEDKHNYETTAK--ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERtQEELRELANKYNGAVNEI 314
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQilSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQ-ILELEGYEMDYNSYLKSI 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 315 --------------KDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGI 380
Cdd:PRK01156 373 eslkkkieeyskniERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 381 QVDDFLPKINGSTEKEHLLSKSGGDCTFIHQFIEcqkklivegHLtkaveETKLSKENQTRAKESDFSDTLSpSKEKSSD 460
Cdd:PRK01156 453 SVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIR---------EI-----EIEVKDIDEKIVDLKKRKEYLE-SEEINKS 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 461 DTTDAQMD--EQDLNEPLAKVSLLKDDLQGAQseiEAKQEIQHLRKELIEAQelaRTSKQKCFELQALLEEErkAYRNQV 538
Cdd:PRK01156 518 INEYNKIEsaRADLEDIKIKINELKDKHDKYE---EIKNRYKSLKLEDLDSK---RTSWLNALAVISLIDIE--TNRSRS 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 539 EESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQaaakvaserdtdiasLQEELKKVRAELER 618
Cdd:PRK01156 590 NEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQE---------------NKILIEKLRGKIDN 654
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1799135574 619 WRKAASEyEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKlRKEWNAL 669
Cdd:PRK01156 655 YKKQIAE-IDSIIPDLKEITSRINDIEDNLKKSRKALDDAKAN-RARLEST 703
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
182-676 |
3.76e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 182 LEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgnqlqacSKNQTEDSLRKELIALQEDKHNYETTaKESLRRV 261
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHE---------ERREELETLEAEIEDLRETIAETERE-REELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 262 LQEKIEVVRKLSEVERSL-----------SNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEE 330
Cdd:PRK02224 281 VRDLRERLEELEEERDDLlaeaglddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 331 IQQKGQAEKKELQH---KIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQvDDFLPKINGSTEKEHLLSKSggdct 407
Cdd:PRK02224 361 LREEAAELESELEEareAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL-EELREERDELREREAELEAT----- 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 408 fihqfIECQKKLIVEGHltKAVEETKLSKENQTrAKESDFSDTLSPSKEKSSD---DTTDAQMDEQDLNEPLAKVSLLKD 484
Cdd:PRK02224 435 -----LRTARERVEEAE--ALLEAGKCPECGQP-VEGSPHVETIEEDRERVEEleaELEDLEEEVEEVEERLERAEDLVE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 485 DLQGAQSEIEAKQEIQHL---RKELIEAQELARTSKQK-CFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRL-HIDT 559
Cdd:PRK02224 507 AEDRIERLEERREDLEELiaeRRETIEEKRERAEELRErAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLaELKE 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 560 ENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSlqnSFQL 639
Cdd:PRK02224 587 RIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAE---EYLE 663
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1799135574 640 RCQQCEDQQREEATRLQG----------ELEKLRKEWNALETECHSL 676
Cdd:PRK02224 664 QVEEKLDELREERDDLQAeigaveneleELEELRERREALENRVEAL 710
|
|
| FHA_CHFR |
cd22672 |
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ... |
49-105 |
3.86e-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: 3.86e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135574 49 KVLSRNHALVWFDHKtGKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQF 105
Cdd:cd22672 39 KLVSGDHCKIIRDEK-GQVWLEDT-STNGTLVNKVKVVKGQK----VELKHGDVIYL 89
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
461-622 |
3.92e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 461 DTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIE-AKQEIQHLRKELIEAQELARTSKQKcfelQALLEEERKAYRNQVE 539
Cdd:COG4913 662 DVASAEREIAELEAELERLDASSDDLAALEEQLEeLEAELEELEEELDELKGEIGRLEKE----LEQAEEELDELQDRLE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 540 ESTKQIQV-----LQAQLQRLHID--TENLREEKDSEITSTRDELLSARDEILLLHQAAAKV----ASERDTDIASL--- 605
Cdd:COG4913 738 AAEDLARLelralLEERFAAALGDavERELRENLEERIDALRARLNRAEEELERAMRAFNREwpaeTADLDADLESLpey 817
|
170 180
....*....|....*....|..
gi 1799135574 606 QEELKKVRAE-----LERWRKA 622
Cdd:COG4913 818 LALLDRLEEDglpeyEERFKEL 839
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
495-717 |
4.32e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 495 AKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAY---RNQVEESTKQIQVLQAQLQRLHIDTENLREE------ 565
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYnelQAELEALQAEIDKLQAEIAEAEAEIEERREElgerar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 566 ---KDSEITSTRDELLSARDEILLLHQAAA-KVASERDTDIAslqEELKKVRAELERWRKAASEYEKEITSLQnsfqlrc 641
Cdd:COG3883 94 alyRSGGSVSYLDVLLGSESFSDFLDRLSAlSKIADADADLL---EELKADKAELEAKKAELEAKLAELEALK------- 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799135574 642 qqceDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKE 717
Cdd:COG3883 164 ----AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
25-108 |
4.33e-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: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 25 DEPIKIGRsvarcRPAQNNAT----FDCKVLSRNHALVWFdhKTGKFYLQDTKSSNGTFINSQRLSR-GSEESPPCEILS 99
Cdd:cd22702 31 KQPCIIGS-----DPHQAISGisvvIPSPQVSELHARITC--KNGAFFLTDLGSEHGTWINDNEGRRyRAPPNFPVRLHP 103
|
....*....
gi 1799135574 100 GDIIQFGVD 108
Cdd:cd22702 104 SDVIEFGSD 112
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
14-106 |
4.51e-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: 42.90 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 14 SHPFQERHvyldepIKIGRSVarcrpaQNNATFDCKVLSRNHALvwFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEesp 93
Cdd:cd22682 14 QFPITEST------IVIGRSV------ESQVQIDDDSVSRYHAK--LAVNPSAVSIIDLGSTNGTIVNGKKIPKLAS--- 76
|
90
....*....|...
gi 1799135574 94 pCEILSGDIIQFG 106
Cdd:cd22682 77 -CDLQNGDQIKIG 88
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
337-672 |
4.54e-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: 46.98 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 337 AEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALqgiqVDDFLPKINGSTEKEHLlsksggdctfihqfiecq 416
Cdd:pfam13166 89 EESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKL----EADFLDECWKKIKRKKN------------------ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 417 KKLIVEGHLTKAvEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTT---DAQMDEQDLNEPLA------KVSLLKDDLQ 487
Cdd:pfam13166 147 SALSEALNGFKY-EANFKSRLLREIEKDNFNAGVLLSDEDRKAALATvfsDNKPEIAPLTFNVIdfdaleKAEILIQKVI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 488 GAQSEIEAKQEIQHLRKELIEAQELARTSKQKC--------FELQALLEE------------------------------ 529
Cdd:pfam13166 226 GKSSAIEELIKNPDLADWVEQGLELHKAHLDTCpfcgqplpAERKAALEAhfddeftefqnrlqkliekvesaissllaq 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 530 ---------ERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREE--KDSEITSTRDELLSARDEILLLHQAAAKvASER 598
Cdd:pfam13166 306 lpavsdlasLLSAFELDVEDIESEAEVLNSQLDGLRRALEAKRKDpfKSIELDSVDAKIESINDLVASINELIAK-HNEI 384
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799135574 599 DTDIASLQEELKKvraelERWRKAASEYEKEITSLQNSFQLRCQQCEDQQrEEATRLQGELEKLRKEWNALETE 672
Cdd:pfam13166 385 TDNFEEEKNKAKK-----KLRLHLVEEFKSEIDEYKDKYAGLEKAINSLE-KEIKNLEAEIKKLREEIKELEAQ 452
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
542-754 |
4.57e-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: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 542 TKQIQVLQAQLQRLhidtenlrEEKDSEITSTRDELLSARDEILLLHQAAAKVA--SERDTDIASLQEELKKVRAELERW 619
Cdd:COG4913 609 RAKLAALEAELAEL--------EEELAEAEERLEALEAELDALQERREALQRLAeySWDEIDVASAEREIAELEAELERL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 620 RKAASEYEkeitslqnsfqlrcqqcedqqreeatRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQK 699
Cdd:COG4913 681 DASSDDLA--------------------------ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799135574 700 QSLELTSDLSILQmsRKELENQVGSLKEQHLRDS---------ADLKTLLSKAENQAKDVQKEY 754
Cdd:COG4913 735 RLEAAEDLARLEL--RALLEERFAAALGDAVERElrenleeriDALRARLNRAEEELERAMRAF 796
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
485-635 |
4.57e-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: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 485 DLQGAQSEIE-AKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRN----QVEESTKQIQVLQAQLQRLhidt 559
Cdd:COG4913 282 RLWFAQRRLElLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEER---- 357
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799135574 560 ENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQN 635
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
257-543 |
4.80e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.84 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 257 SLRRVLQEKIEVVRKLSEVERslsnteDECTHLKEmNERTqEELRELANKYNGAVNEIKDLSDKLKVAEGKQ-------- 328
Cdd:PRK05771 13 TLKSYKDEVLEALHELGVVHI------EDLKEELS-NERL-RKLRSLLTKLSEALDKLRSYLPKLNPLREEKkkvsvksl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 329 EEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADndftNERLTALQGIQVDDflpkingstekEHLLSKSggdctF 408
Cdd:PRK05771 85 EELIKDVEEELEKIEKEIKELEEEISELENEIKELEQE----IERLEPWGNFDLDL-----------SLLLGFK-----Y 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 409 IHQFIecqkkliveGHLTKAVEETKLSKENQTRAKESDFSDTLSP-----SKEkssddttdaqmDEQDLNEPLAKVSLLK 483
Cdd:PRK05771 145 VSVFV---------GTVPEDKLEELKLESDVENVEYISTDKGYVYvvvvvLKE-----------LSDEVEEELKKLGFER 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799135574 484 DDLQ--GAQSEI--EAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTK 543
Cdd:PRK05771 205 LELEeeGTPSELirEIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAEALSK 268
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
18-86 |
5.21e-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: 5.21e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135574 18 QERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhkTGKFYLQDTKSSNGTFINSQRLS 86
Cdd:cd22694 8 GELRFDPGSSVRIGRD------PDADVRLDDPRVSRRHALLEFD--GDGWVYTDLGSRNGTYLNGRRVQ 68
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
13-110 |
6.96e-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: 6.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 13 NSHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTgkFYLQDTKSSNGTFINSQRLSrgsee 91
Cdd:cd22665 7 SQAHGPEKDFPLYEgENVIGRD------PSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRL----- 73
|
90 100
....*....|....*....|.
gi 1799135574 92 SPPC--EILSGDIIQFGvDVT 110
Cdd:cd22665 74 KPNVryELIDGDLLLFG-DVK 93
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
255-629 |
1.66e-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: 45.44 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 255 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQK 334
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 335 GQAEKKELQHKIDEMEEKEQ---ELQAKIEALQADNDftnerltalqgiqvDDFLPKINGSTEKehllsksggdctfihq 411
Cdd:TIGR02169 753 IENVKSELKELEARIEELEEdlhKLEEALNDLEARLS--------------HSRIPEIQAELSK---------------- 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 412 fiecqkkliveghltkaVEETKLSKENQTRAKESDFSDtLSPSKEKSSDDTTDAQMDeqdlneplakvsllKDDLQGAQS 491
Cdd:TIGR02169 803 -----------------LEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQ--------------RIDLKEQIK 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 492 EIEAKQEIQHLRKELIEAQElartSKQKCFELQalLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLReEKDSEIT 571
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEEEL----EELEAALRD--LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR-KRLSELK 923
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799135574 572 STRDELLSARDEILLLhQAAAKVASERDTDIASLQEELKKVRAELERWR----KAASEYEKE 629
Cdd:TIGR02169 924 AKLEALEEELSEIEDP-KGEDEEIPEEELSLEDVQAELQRVEEEIRALEpvnmLAIQEYEEV 984
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
497-793 |
1.99e-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: 44.89 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 497 QEIQHLRKELIEAQELARTSKQKCFELQallEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLrEEKDSEITSTRDE 576
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKEKERY---KRDREQWERQRRELESRVAELKEELRQSREKHEEL-EEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 577 LLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWR---KAASEYEKEITSLQNSFQLRCQQCEDQQREEAT 653
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKeraKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 654 RLQG----------------------------------ELEKLRKEWNALETECHSLKRENVLLSSELQ-------RQEK 692
Cdd:pfam07888 193 EFQElrnslaqrdtqvlqlqdtittltqklttahrkeaENEALLEELRSLQERLNASERKVEGLGEELSsmaaqrdRTQA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 693 ELHNSQKQSLELTSDLSILQMSRKELENQvGSLKEQHLRDSADLKTllSKAENQAKDVQKEYEKTQTVLSE-LKLKFEMT 771
Cdd:pfam07888 273 ELHQARLQAAQLTLQLADASLALREGRAR-WAQERETLQQSAEADK--DRIEKLSAELQRLEERLQEERMErEKLEVELG 349
|
330 340
....*....|....*....|..
gi 1799135574 772 eQEKQSITDELKQCKNNLKLLR 793
Cdd:pfam07888 350 -REKDCNRVQLSESRRELQELK 370
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
496-691 |
2.00e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 496 KQEIQHLRKELIEAQELARTSKQKcfELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRD 575
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQK--NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 576 ELLSARDEILL--LHQAAAKVASERDT------DIASLQEELKKVRAEL-ERWRKAASEYEKEITSLQNSfqlrcqqcED 646
Cdd:COG3206 259 LLQSPVIQQLRaqLAELEAELAELSARytpnhpDVIALRAQIAALRAQLqQEAQRILASLEAELEALQAR--------EA 330
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1799135574 647 QQREEATRLQGELEKLrkewNALETECHSLKRE----NVLLSSELQRQE 691
Cdd:COG3206 331 SLQAQLAQLEARLAEL----PELEAELRRLEREvevaRELYESLLQRLE 375
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
591-807 |
2.05e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 591 AAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQlRCQQCEDQQREEATRLQGELEKLRKEwnaLE 670
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE-ALQAEIDKLQAEIAEAEAEIEERREE---LG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 671 TECHSLKRE-------NVLLSSE-----LQRQE--KELHNSQKQSLELTSDLsilqmsRKELENQVGSLKEQhlrdSADL 736
Cdd:COG3883 90 ERARALYRSggsvsylDVLLGSEsfsdfLDRLSalSKIADADADLLEELKAD------KAELEAKKAELEAK----LAEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799135574 737 KTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNNPSILQPVPA 807
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
322-777 |
2.09e-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: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 322 KVAEGKQEEIQQKGQAEKKELQHKidemeEKEQELQAKIEALQADNDFTNERLTALQGiqvddflpKINGSTEKEHLLSK 401
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHK-----RARIELEKKASALKRQLDRESDRNQELQK--------RIRLLEKREAEAEE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 402 SggdctfihqfiecQKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSL 481
Cdd:pfam05557 70 A-------------LREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 482 LKDDLQgaqsEIEAK-QEIQHLRKELIEAQELARTSKQKCFELqalleEERKAYRNQVEESTKQIQVLQAQLQRLHIDTE 560
Cdd:pfam05557 137 LQERLD----LLKAKaSEAEQLRQNLEKQQSSLAEAEQRIKEL-----EFEIQSQEQDSEIVKNSKSELARIPELEKELE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 561 NLREEKDSEITSTRDELLSARDeillLHQAAAKVASERDT--DIASLQEELKKVRAELERWRKAASEYEKEITS--LQNS 636
Cdd:pfam05557 208 RLREHNKHLNENIENKLLLKEE----VEDLKRKLEREEKYreEAATLELEKEKLEQELQSWVKLAQDTGLNLRSpeDLSR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 637 FQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDL----SILQ 712
Cdd:pfam05557 284 RIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgyrAILE 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799135574 713 MSRKELENQVGSlkEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 777
Cdd:pfam05557 364 SYDKELTMSNYS--PQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQA 426
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
468-679 |
2.28e-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: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 468 DEQDLNEPLAKVSLLKDDLQGAQSEIEAKQ-EIQHLRKELIEAQELARTSKQKCFELQALlEEERKAYRNQVEESTKQIQ 546
Cdd:COG4913 645 ERREALQRLAEYSWDEIDVASAEREIAELEaELERLDASSDDLAALEEQLEELEAELEEL-EEELDELKGEIGRLEKELE 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 547 VLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERD---TDIASLQEELKKVRAE-LERWRKA 622
Cdd:COG4913 724 QAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDalrARLNRAEEELERAMRAfNREWPAE 803
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135574 623 ASEYEKEITSLqNSFQlrcQQCEDQQREEATRLQGELEKLRKEW--NALETECHSLKRE 679
Cdd:COG4913 804 TADLDADLESL-PEYL---ALLDRLEEDGLPEYEERFKELLNENsiEFVADLLSKLRRA 858
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
52-107 |
2.43e-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: 2.43e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799135574 52 SRNHALVWFDHKTG---------KFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQFGV 107
Cdd:cd22667 40 SRKHATLTVLHPEAnlsdpdtrpELTLKDL-SKYGTFVNGEKLKGGSE----VTLKDGDVITFGV 99
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
289-568 |
2.61e-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: 43.98 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 289 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQkgqaEKKELQHKIDEMEEKEQELQAKIEALQADnd 368
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ----ELAALEAELAELEKEIAELRAELEAQKEE-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 369 fTNERLTALQgiqvddflpKINGSTEKEHLLSKSGgdctfihqFIECQKKLIVEGHLTKAVEEtklskenqtrakesdfs 448
Cdd:COG4942 106 -LAELLRALY---------RLGRQPPLALLLSPED--------FLDAVRRLQYLKYLAPARRE----------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 449 dtlspskekssddttdaQMDEqdLNEPLAKVSLLKDDLQgaqseiEAKQEIQHLRKELIEAQELARTSKQKCFELQALLE 528
Cdd:COG4942 151 -----------------QAEE--LRADLAELAALRAELE------AERAELEALLAELEEERAALEALKAERQKLLARLE 205
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1799135574 529 EERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDS 568
Cdd:COG4942 206 KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
461-634 |
2.74e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 461 DTTDAQMDE--QDLNEPLAKVSLLKDDLQGAQSEI-EAKQEIQHLRKELIE-AQELARTSKQKCFeLQALLEEE------ 530
Cdd:COG3883 40 DALQAELEElnEEYNELQAELEALQAEIDKLQAEIaEAEAEIEERREELGErARALYRSGGSVSY-LDVLLGSEsfsdfl 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 531 -RKAYRNQVEESTKQ-IQVLQAQLQRLhidtenlrEEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEE 608
Cdd:COG3883 119 dRLSALSKIADADADlLEELKADKAEL--------EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
|
170 180
....*....|....*....|....*.
gi 1799135574 609 LKKVRAELERWRKAASEYEKEITSLQ 634
Cdd:COG3883 191 EAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
1-106 |
3.12e-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: 43.98 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 1 MPSALAIFTCRPNSHPFQERHVYLDEPIKIGRSvARC-----RPAQnnatfdckVLSRNHALVWFDHktGKFYLQDTkSS 75
Cdd:COG3456 1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRS-ADCdwvlpDPDR--------SVSRRHAEIRFRD--GAFCLTDL-ST 68
|
90 100 110
....*....|....*....|....*....|...
gi 1799135574 76 NGTFIN--SQRLSRGSEEsppcEILSGDIIQFG 106
Cdd:COG3456 69 NGTFLNgsDHPLGPGRPV----RLRDGDRLRIG 97
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
527-795 |
3.28e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 527 LEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDellsardeillLHQAAAKVASERDtdiaSLQ 606
Cdd:COG1340 6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKE-----------LREEAQELREKRD----ELN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 607 EELKKVRAELERWRKAASEYEKEITSLQNsfqlrcqqcedqQREEATRLQGELEKLRKEWNALE----TECHSLKRENVL 682
Cdd:COG1340 71 EKVKELKEERDELNEKLNELREELDELRK------------ELAELNKAGGSIDKLRKEIERLEwrqqTEVLSPEEEKEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 683 ------LSSELQRQEKElHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAEN---QAKDVQKE 753
Cdd:COG1340 139 vekikeLEKELEKAKKA-LEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADElrkEADELHKE 217
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1799135574 754 YEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 795
Cdd:COG1340 218 IVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKRE 259
|
|
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
53-106 |
3.87e-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: 3.87e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1799135574 53 RNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPceilsGDIIQFG 106
Cdd:cd22700 36 EQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAP-----GDVLRFG 84
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
651-797 |
3.94e-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: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 651 EATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNsQKQSLELTSDLSilqmsrkELENQVGSLKeqhl 730
Cdd:pfam15294 134 EIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGA-KKDVKSNLKEIS-------DLEEKMAALK---- 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135574 731 rdsADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGN 797
Cdd:pfam15294 202 ---SDLEKTLNASTALQKSLEEDLASTKHELLKVQEQLEMAEKELEKKFQQTAAYRNMKEMLTKKNE 265
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
528-759 |
5.39e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 528 EEERKAYRNQVEESTKQIQVLQAQLQRLhidtenlreekDSEITSTRDELLSARDEILLLHQAAAKVASErdtdIASLQE 607
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDAL-----------QAELEELNEEYNELQAELEALQAEIDKLQAE----IAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 608 ELKKVRAELERWrkAASEYE--------------KEITSLQNSFQLRCQQCEDQQR--EEATRLQGELEKLRKEWNALET 671
Cdd:COG3883 80 EIEERREELGER--ARALYRsggsvsyldvllgsESFSDFLDRLSALSKIADADADllEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 672 ECHSLKRENVLLSSELQRQEKELhnsQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQ 751
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQ---EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
....*...
gi 1799135574 752 KEYEKTQT 759
Cdd:COG3883 235 AAAAAAAA 242
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
162-773 |
6.66e-04 |
|
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: 43.27 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 162 SQELFQLSQYLQEALHR----EQMLEQKLATLQRLLAITQEASDTSWQALIDEDRllsRLEVMGNQLQACSKNQTEDSLR 237
Cdd:pfam10174 129 AKELFLLRKTLEEMELRietqKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWER---TRRIAEAEMQLGHLEVLLDQKE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 238 KELIALQEDKH-NYETTAKESLRRVLQEKIEVV-RKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKyngaVNEIK 315
Cdd:pfam10174 206 KENIHLREELHrRNQLQPDPAKTKALQTVIEMKdTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQ----MEVYK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 316 DLSD--KLKVAEGKQEeiQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQgIQVDDFLPKINgst 393
Cdd:pfam10174 282 SHSKfmKNKIDQLKQE--LSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQ-TEVDALRLRLE--- 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 394 EKEHLLSKSggdctfihqfiecQKKLiveghltkaveeTKLSKENQTRAKE-SDFSDTLSPSKEKSSDDTTDAQMDEQDL 472
Cdd:pfam10174 356 EKESFLNKK-------------TKQL------------QDLTEEKSTLAGEiRDLKDMLDVKERKINVLQKKIENLQEQL 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 473 NEPLAKVSLLKDDLQGAQSEIEAKQEIqhlrkelIEAQELARTSKQKCFE-LQALLEEERKAYRNQVEESTKQIQVLQAQ 551
Cdd:pfam10174 411 RDKDKQLAGLKERVKSLQTDSSNTDTA-------LTTLEEALSEKERIIErLKEQREREDRERLEELESLKKENKDLKEK 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 552 LQRLHIDtenlREEKDSEITSTRDELLSARDEILllhqaaakvasERDTDIASLQEELKKVRAELERW----RKAASEYE 627
Cdd:pfam10174 484 VSALQPE----LTEKESSLIDLKEHASSLASSGL-----------KKDSKLKSLEIAVEQKKEECSKLenqlKKAHNAEE 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 628 KEITSLQNSFQLRCQQCEDQQ-REEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQslelts 706
Cdd:pfam10174 549 AVRTNPEINDRIRLLEQEVARyKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVAN------ 622
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135574 707 dlsiLQMSRKELENQVGSLKEQHLRDSADLKTllSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQ 773
Cdd:pfam10174 623 ----IKHGQQEMKKKGAQLLEEARRREDNLAD--NSQQLQLEELMGALEKTRQELDATKARLSSTQQ 683
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
327-778 |
6.95e-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: 43.42 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 327 KQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQAdndftnerltalQGIQVDDFLPKINGSTEKEHLLSKSGG-- 404
Cdd:TIGR00618 236 QQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRA------------QEAVLEETQERINRARKAAPLAAHIKAvt 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 405 ----DCTFIHQFIECQK-KLIVEGHLTKAVEETKLSKENQTRAKESDFSD----TLSPSKEKSSDDTTDAQM-DEQDLNE 474
Cdd:TIGR00618 304 qieqQAQRIHTELQSKMrSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQeihiRDAHEVATSIREISCQQHtLTQHIHT 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 475 PLAKVSLLKDDLQGAQSEIEAKQEIQH-----LRKELIEAQELARTSKQKCFElQALLEEERKAYRNQVEESTKQIQVLQ 549
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELDILQREQAtidtrTSAFRDLQGQLAHAKKQQELQ-QRYAELCAAAITCTAQCEKLEKIHLQ 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 550 AQLQRLHIDTENL--------REEKDSEITSTRDELLSARDEIL---LLHQAAAKVASER-----------DTDIASLQE 607
Cdd:TIGR00618 463 ESAQSLKEREQQLqtkeqihlQETRKKAVVLARLLELQEEPCPLcgsCIHPNPARQDIDNpgpltrrmqrgEQTYAQLET 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 608 ELKKVRAELERWRKAASEYEKEITSLQNSFQlRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSEL 687
Cdd:TIGR00618 543 SEEDVYHQLTSERKQRASLKEQMQEIQQSFS-ILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKL 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 688 Q----RQEKELHNSQKQSLEltsDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSE 763
Cdd:TIGR00618 622 QpeqdLQDVRLHLQQCSQEL---ALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEM 698
|
490
....*....|....*
gi 1799135574 764 LKLKFEMTEQEKQSI 778
Cdd:TIGR00618 699 LAQCQTLLRELETHI 713
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
16-111 |
7.06e-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: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 16 PFQERHVYLD-EPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFdhKTGKFYLQDTKSSNGTFINSQRLSRgseespP 94
Cdd:cd22693 7 TLQGQTFPIDkSGITIGRA------DDNDLVLSDDFVSSRHARIYL--QGSSWYLEDLGSTNGTFVNGNRVTQ------P 72
|
90
....*....|....*..
gi 1799135574 95 CEILSGDIIQFGVDVTE 111
Cdd:cd22693 73 VVVQPGDTIRIGATVFE 89
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
524-764 |
7.16e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 524 QALLEEERKAYRNQVEESTKQIQVLQAQLQrlhiDTENLREEkdseITSTRDELLSARDEILLLHQAAAKVASER--DTD 601
Cdd:PRK11281 51 QKLLEAEDKLVQQDLEQTLALLDKIDRQKE----ETEQLKQQ----LAQAPAKLRQAQAELEALKDDNDEETRETlsTLS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 602 IASLQEELKKVRAELERWRKAASEYEKEITSLQN----------SFQLRCQQCEDQ----QREEATRLQGELEKLRKEWN 667
Cdd:PRK11281 123 LRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTqperaqaalyANSQRLQQIRNLlkggKVGGKALRPSQRVLLQAEQA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 668 ALEtechslkrenvlLSSELQRQEKElHNSQKQSL-ELTSDLSILQMSRKELENQvgslkeqhlrdsaDLKTL-----LS 741
Cdd:PRK11281 203 LLN------------AQNDLQRKSLE-GNTQLQDLlQKQRDYLTARIQRLEHQLQ-------------LLQEAinskrLT 256
|
250 260
....*....|....*....|...
gi 1799135574 742 KAENQAKDVQKEYEKTQTVLSEL 764
Cdd:PRK11281 257 LSEKTVQEAQSQDEAARIQANPL 279
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
49-112 |
7.89e-04 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 (PML1) and similar proteins; PML1 is an FHA domain-containing protein required for efficient splicing and pre-mRNA nuclear retention. It is a component of the pre-mRNA retention and splicing (RES) complex composed of at least BUD13, IST3, and PML1. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438733 [Multi-domain] Cd Length: 129 Bit Score: 40.12 E-value: 7.89e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135574 49 KVLSRNHALVWFDHKTG--KFYLQDTKSSNGTFINsqrlsrgSEESPPC---EILSGDIIQFGVDVTEN 112
Cdd:cd22681 64 ETCSKQHCVIQFRNVKGilKPYIMDLDSSNGTCLN-------DNVIPSSryvELRSGDVITFSKSNDYE 125
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
524-753 |
8.02e-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: 42.44 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 524 QALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASErdtdIA 603
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE----IA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 604 SLQEELKKVRAELER-----WRKAASEYEKEITSLQNSFQL-----RCQQCEDQQREEATRLQGELEKLRKewnaletec 673
Cdd:COG4942 94 ELRAELEAQKEELAEllralYRLGRQPPLALLLSPEDFLDAvrrlqYLKYLAPARREQAEELRADLAELAA--------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 674 hslkrenvlLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQH-------LRDSADLKTLLSKAENQ 746
Cdd:COG4942 165 ---------LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELaaelaelQQEAEELEALIARLEAE 235
|
....*..
gi 1799135574 747 AKDVQKE 753
Cdd:COG4942 236 AAAAAER 242
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
646-768 |
8.14e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 646 DQQREEATR----LQGELEKLRKEWNALETECHSLKRENVLLSSELQRQekelhNSQKQSLELTSDLSILQMSRKELENQ 721
Cdd:COG3206 167 ELRREEARKalefLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAK-----LLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1799135574 722 VGSLKEQHLRDSADLKTLLSKAENQakDVQKEYEKTQTVLSELKLKF 768
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPVIQ--QLRAQLAELEAELAELSARY 286
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
266-789 |
8.36e-04 |
|
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: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 266 IEVVRKLSEVERSLSNTEDECTHLkemnertqEELRELANKYNGA---VNEIKDLSDKLKVAEGKQEeiQQKGQAEKKEL 342
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELL--------EPIRELAERYAAArerLAELEYLRAALRLWFAQRR--LELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 343 QHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDDFLPKINGSTEKEHLLSKSGGDctfihqfiecQKKLIVE 422
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR----------LEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 423 GHLTKAVEETKLsKENQTRAKEsdFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQeiQHL 502
Cdd:COG4913 371 LGLPLPASAEEF-AALRAEAAA--LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL--LAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 503 RKELieAQELARTSKQKCF--ELQALLEEER-------KAYRNQ-----VEESTKQiQVLQA--QLQ-RLHIDTENLREE 565
Cdd:COG4913 446 RDAL--AEALGLDEAELPFvgELIEVRPEEErwrgaieRVLGGFaltllVPPEHYA-AALRWvnRLHlRGRLVYERVRTG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 566 KDSEITSTRDEllsardeilllHQAAAKVASERDTDIASLQEELKKVRA--------ELERWRKAaseyekeITS---LQ 634
Cdd:COG4913 523 LPDPERPRLDP-----------DSLAGKLDFKPHPFRAWLEAELGRRFDyvcvdspeELRRHPRA-------ITRagqVK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 635 NSFQLRcqQCEDQQREEATRLQGE-----LEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLS 709
Cdd:COG4913 585 GNGTRH--EKDDRRRIRSRYVLGFdnrakLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 710 ILQMSRK--ELENQVGSLkeqhLRDSADLKTLlskaENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKN 787
Cdd:COG4913 663 VASAEREiaELEAELERL----DASSDDLAAL----EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
..
gi 1799135574 788 NL 789
Cdd:COG4913 735 RL 736
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
494-700 |
8.61e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 8.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 494 EAKQEIQHLRKELIEAQELARTSKQKCFELQALLEE----------ERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLR 563
Cdd:COG1340 19 ELREEIEELKEKRDELNEELKELAEKRDELNAQVKElreeaqelreKRDELNEKVKELKEERDELNEKLNELREELDELR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 564 EEKDSEITSTRD-----------------ELLSARDEILLLHQAAAKVAS-ERDTDIASLQEELKKVRAELERWRKAASE 625
Cdd:COG1340 99 KELAELNKAGGSidklrkeierlewrqqtEVLSPEEEKELVEKIKELEKElEKAKKALEKNEKLKELRAELKELRKEAEE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 626 YEKEITSLQNSFQ------LRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQK 699
Cdd:COG1340 179 IHKKIKELAEEAQelheemIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKR 258
|
.
gi 1799135574 700 Q 700
Cdd:COG1340 259 E 259
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
258-378 |
9.64e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 9.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 258 LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQ----- 332
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkey 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1799135574 333 QKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQ 378
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE 137
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
255-798 |
1.16e-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: 42.65 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 255 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQE-----------ELRELANKYNGAVNEIKDLSDKLKV 323
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEyyqlkekleleEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 324 AEG----KQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDDFLPKINGSTEKEHLL 399
Cdd:pfam02463 248 DEQeeieSSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 400 SKSGGDCTFIHQFIECQKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKV 479
Cdd:pfam02463 328 KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 480 SLLKDDLQGAQSEIEAKQEIQ-HLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHID 558
Cdd:pfam02463 408 QLLLELARQLEDLLKEEKKEElEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLE 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 559 TENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQ 638
Cdd:pfam02463 488 LLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLV 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 639 LRcqqcEDQQREEATRLQGELEKLRKEWNALETECH-SLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKE 717
Cdd:pfam02463 568 RA----LTELPLGARKLRLLIPKLKLPLKSIAVLEIdPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKA 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 718 LENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGN 797
Cdd:pfam02463 644 KESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELL 723
|
.
gi 1799135574 798 N 798
Cdd:pfam02463 724 A 724
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
163-708 |
1.38e-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: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 163 QELFQLSQYLQEALHREQMLEQKLATLQRL----LAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRK 238
Cdd:TIGR00618 379 QHIHTLQQQKTTLTQKLQSLCKELDILQREqatiDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEK 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 239 elIALQEdkhnyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLS 318
Cdd:TIGR00618 459 --IHLQE------------SAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPG 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 319 DKLKVAEGKQEEIQQKGQAEKKeLQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIqvddflpkINGSTEKEHL 398
Cdd:TIGR00618 525 PLTRRMQRGEQTYAQLETSEED-VYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKED--------IPNLQNITVR 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 399 LSKsggdctFIHQFIECQKKLIVEGHLTKAVEETKLSKEnQTRAKESDFSDTLSpsKEKSSDDTTDAQMDEQDLNEPLAK 478
Cdd:TIGR00618 596 LQD------LTEKLSEAEDMLACEQHALLRKLQPEQDLQ-DVRLHLQQCSQELA--LKLTALHALQLTLTQERVREHALS 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 479 VSLLKddLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHID 558
Cdd:TIGR00618 667 IRVLP--KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQS 744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 559 TENLREEkdseitstRDELLSARDEILLLHQAAAKVASERDTdiaslqeELKKVRAELERWRKAASEYEKEITSLQNSFQ 638
Cdd:TIGR00618 745 LKELMHQ--------ARTVLKARTEAHFNNNEEVTAALQTGA-------ELSHLAAEIQFFNRLREEDTHLLKTLEAEIG 809
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 639 LRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEkELHNSQKQSLELTSDL 708
Cdd:TIGR00618 810 QEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA-QLTQEQAKIIQLSDKL 878
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
527-686 |
1.56e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 527 LEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDseitstrdELlsaRDEILllhqaaakvasERDTDIASLQ 606
Cdd:COG2433 390 LPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE--------EL---EAELE-----------EKDERIERLE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 607 EELKKVRAElerwRKAASEYEKEITSLQNsfqlrcqqcedqqreEATRLQGELEKLRKEWNALETECHSLKRENVLLSSE 686
Cdd:COG2433 448 RELSEARSE----ERREIRKDREISRLDR---------------EIERLERELEEERERIEELKRKLERLKELWKLEHSG 508
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
233-721 |
1.74e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 233 EDSLRKELIAL---QEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELREL--ANKY 307
Cdd:COG4717 48 LERLEKEADELfkpQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 308 NGAVNEIKDLSDKLKVAEGKQEEIQQKgQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERltalqgiQVDDFLP 387
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEER-LEELRELEEELEELEAELAELQEELEELLEQLSLATEE-------ELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 388 KINGSTEKEHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKAVEEtKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQM 467
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE-RLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 468 deQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQveestKQIQV 547
Cdd:COG4717 279 --LFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRI-----EELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 548 LQAQLQRLH--IDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAasE 625
Cdd:COG4717 352 LLREAEELEeeLQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE--E 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 626 YEKEITSLQnsfqlrcqqcedqqrEEATRLQGELEKLRKEWNALETECHSLKRENVL--LSSELQRQEKELHNSQKQSLE 703
Cdd:COG4717 430 LEEELEELE---------------EELEELEEELEELREELAELEAELEQLEEDGELaeLLQELEELKAELRELAEEWAA 494
|
490
....*....|....*...
gi 1799135574 704 LTSDLSILQMSRKELENQ 721
Cdd:COG4717 495 LKLALELLEEAREEYREE 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
597-798 |
1.77e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 597 ERDT--DIASLQEELKkvraELERWRKAASEYEKEITSLQnsfQLRcqqcedQQREEATRLQGELEKLRKEWNALETECH 674
Cdd:COG4913 220 EPDTfeAADALVEHFD----DLERAHEALEDAREQIELLE---PIR------ELAERYAAARERLAELEYLRAALRLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 675 SLKREnvLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQvgsLKEQHLRDSADLKTLLSKAENQAKDVQKEY 754
Cdd:COG4913 287 QRRLE--LLEAELEELRAELARLEAELERLEARLDALREELDELEAQ---IRGNGGDRLEQLEREIERLERELEERERRR 361
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1799135574 755 EKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNN 798
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
216-795 |
1.88e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 216 RLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTaKESLRRVLQEKIEVVRKLSEVERSLSNTEDECthlkemnER 295
Cdd:PRK01156 151 RKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYL-EEKLKSSNLELENIKKQIADDEKSHSITLKEI-------ER 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 296 TQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIqQKGQAEKKELQHKIDEMEEKEQELqakiealqadNDFTNERLT 375
Cdd:PRK01156 223 LSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI-KTAESDLSMELEKNNYYKELEERH----------MKIINDPVY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 376 ALQGiQVDDFLPKINGSTEKEHLLSKSGGDctfIHQFIECQKKLIVeghltkaveetklskenqtraKESDFSDTLSPSK 455
Cdd:PRK01156 292 KNRN-YINDYFKYKNDIENKKQILSNIDAE---INKYHAIIKKLSV---------------------LQKDYNDYIKKKS 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 456 EKssddttdaqmdeQDLNEPLAKVSLLKDDLQGAQSEIEA-KQEIQHLRKElieaQELARTSKQKCFELQALLEEERKAY 534
Cdd:PRK01156 347 RY------------DDLNNQILELEGYEMDYNSYLKSIESlKKKIEEYSKN----IERMSAFISEILKIQEIDPDAIKKE 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 535 RNQVEESTKQIqvlQAQLQRLHIDTENLREEKDSeitstrdelLSARDEILLLHQAAAKVASERDTDiaslqeelkKVRA 614
Cdd:PRK01156 411 LNEINVKLQDI---SSKVSSLNQRIRALRENLDE---------LSRNMEMLNGQSVCPVCGTTLGEE---------KSNH 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 615 ELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRenvLLSSELQRQEKEL 694
Cdd:PRK01156 470 IINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLED---IKIKINELKDKHD 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 695 HNSQKQSLELTSDLSILQMSRKELenqvgsLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQE 774
Cdd:PRK01156 547 KYEEIKNRYKSLKLEDLDSKRTSW------LNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKS 620
|
570 580
....*....|....*....|.
gi 1799135574 775 KQSITDELKQCKNNLKLLREK 795
Cdd:PRK01156 621 IREIENEANNLNNKYNEIQEN 641
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
27-106 |
1.90e-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: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 27 PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTGkfYLQDTKSSNGTFINSQRLsrgseeSPPCEILSGDIIQFG 106
Cdd:cd22668 19 SNIIGRG------SDADFRLPDTGVSRRHAEIRWDGQVA--HLTDLGSTNGTTVNNAPV------TPEWRLADGDVITLG 84
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
207-583 |
2.03e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 41.96 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 207 LIDEDRLLSRLE--------VMGNQLQAcsKNQTEDSLRKELIALQEDKHNYETTAKESLRRVlQEKIEVVRKLSEVERS 278
Cdd:PTZ00108 1001 LGKLERELARLSnkvrfikhVINGELVI--TNAKKKDLVKELKKLGYVRFKDIIKKKSEKITA-EEEEGAEEDDEADDED 1077
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 279 LSNTEDECT---HLKEMN--ERTQEELRELANKYNGAVNEIKDLSDKlkvaegkqeEIQQKGQAEKKELQHKIDEMEEKE 353
Cdd:PTZ00108 1078 DEEELGAAVsydYLLSMPiwSLTKEKVEKLNAELEKKEKELEKLKNT---------TPKDMWLEDLDKFEEALEEQEEVE 1148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 354 QELQAKIEALQADNDFTNERltaLQGIQVDDFLPKINGSTEKEHLLSKSGGDCTFIHQFIecqKKLIVEGHLTKAVEETK 433
Cdd:PTZ00108 1149 EKEIAKEQRLKSKTKGKASK---LRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDE---KRKLDDKPDNKKSNSSG 1222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 434 LSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELA 513
Cdd:PTZ00108 1223 SDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKP 1302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 514 RTS----KQKCFELQALL----EEERKAYRNQVEESTKQIQVLQAQLQRL------HIDTENLREEKDSEITSTRDELLS 579
Cdd:PTZ00108 1303 SSPtkkkVKKRLEGSLAAlkkkKKSEKKTARKKKSKTRVKQASASQSSRLlrrprkKKSDSSSEDDDDSEVDDSEDEDDE 1382
|
....
gi 1799135574 580 ARDE 583
Cdd:PTZ00108 1383 DDED 1386
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
504-797 |
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 1799135574 504 KELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDsEITSTRDELLSARDE 583
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 584 ILLLHQAAAKVaserDTDIASLQEELKKVRAELERWRkaasEYEKEITSLQnsfqlrcqqcedQQREEATRLQGELEKLR 663
Cdd:PRK03918 247 LESLEGSKRKL----EEKIRELEERIEELKKEIEELE----EKVKELKELK------------EKAEEYIKLSEFYEEYL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 664 KEWNALETECHSLKREnvllSSELQRQEKELHNSQKQSLELTSDLsilqmsrKELENQVGSLKEQHlRDSADLKTLLSKA 743
Cdd:PRK03918 307 DELREIEKRLSRLEEE----INGIEERIKELEEKEERLEELKKKL-------KELEKRLEELEERH-ELYEEAKAKKEEL 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1799135574 744 ENQAKdvqkeyEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGN 797
Cdd:PRK03918 375 ERLKK------RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIK 422
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
172-361 |
2.41e-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: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 172 LQEALHREQMLEQKLATLQRLLaitqeasdtswQALIDEDRLLSRLEVmgNQLQACSKNQTEDSLRKELIAlqedKHNYE 251
Cdd:pfam15619 6 LSARLHKIKELQNELAELQSKL-----------EELRKENRLLKRLQK--RQEKALGKYEGTESELPQLIA----RHNEE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 252 T-TAKESLRRvLQEKIEVV-RKLSEVERSLSNTEDECTHL------KEMNERT--QEELRELANKYNGAVNEIKDLSDKL 321
Cdd:pfam15619 69 VrVLRERLRR-LQEKERDLeRKLKEKEAELLRLRDQLKRLeklsedKNLAEREelQKKLEQLEAKLEDKDEKIQDLERKL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1799135574 322 KVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIE 361
Cdd:pfam15619 148 ELENKSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLK 187
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
648-795 |
2.64e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 648 QREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKE 727
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 728 QHLRDSADLKTLLSKAE-------------------------------NQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQ 776
Cdd:COG4942 98 ELEAQKEELAELLRALYrlgrqpplalllspedfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAELE 177
|
170
....*....|....*....
gi 1799135574 777 SITDELKQCKNNLKLLREK 795
Cdd:COG4942 178 ALLAELEEERAALEALKAE 196
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
174-694 |
2.87e-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: 41.49 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 174 EALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDR-------LLSRLEVMGNQLQACSKNQTEDSLRKELIALQED 246
Cdd:TIGR00618 369 EISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQReqatidtRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAIT 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 247 KHNYETTAKE----SLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLK 322
Cdd:TIGR00618 449 CTAQCEKLEKihlqESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTR 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 323 VAEGKQEEIQQKGQAEKKeLQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIqvddflpkINGSTEKEHLLSKs 402
Cdd:TIGR00618 529 RMQRGEQTYAQLETSEED-VYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKED--------IPNLQNITVRLQD- 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 403 ggdctFIHQFIECQKKLIVEGHLTKAVEETKLSKEnQTRAKESDFSDTLspSKEKSSDDTTDAQMDEQDLNEPLAKVSLL 482
Cdd:TIGR00618 599 -----LTEKLSEAEDMLACEQHALLRKLQPEQDLQ-DVRLHLQQCSQEL--ALKLTALHALQLTLTQERVREHALSIRVL 670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 483 KddLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENL 562
Cdd:TIGR00618 671 P--KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKEL 748
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 563 REEKDSEITSTRDELLSARDEILLLHQAAAKVA------SERDTDIASLQEELKKVRAELERWRKaasEYEKEITSLQNS 636
Cdd:TIGR00618 749 MHQARTVLKARTEAHFNNNEEVTAALQTGAELShlaaeiQFFNRLREEDTHLLKTLEAEIGQEIP---SDEDILNLQCET 825
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135574 637 FQLRCQQCeDQQREEATRLQGELEKLRKEWNaletECHSLKRENVLLSSELQRQEKEL 694
Cdd:TIGR00618 826 LVQEEEQF-LSRLEEKSATLGEITHQLLKYE----ECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
216-566 |
2.95e-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: 41.03 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 216 RLEVMGNQLQACSKNQTEdsLRKELIALQEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNER 295
Cdd:pfam07888 28 RAELLQNRLEECLQERAE--LLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 296 TQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEE---KEQELQAKIEALQADNDFTNE 372
Cdd:pfam07888 106 LSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKagaQRKEEEAERKQLQAKLQQTEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 373 RLTALQgiqvDDFLPKINGSTEKEHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKA----VEETKLSKENQTRAKESDFS 448
Cdd:pfam07888 186 ELRSLS----KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEelrsLQERLNASERKVEGLGEELS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 449 DTLSpSKEKSSDDTTDAQMDEQDLNEPLAKVSL--------LKDDLQGAQSEIEAKQE-IQHLRKELIEAQELARTSKQK 519
Cdd:pfam07888 262 SMAA-QRDRTQAELHQARLQAAQLTLQLADASLalregrarWAQERETLQQSAEADKDrIEKLSAELQRLEERLQEERME 340
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1799135574 520 CFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEK 566
Cdd:pfam07888 341 REKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEK 387
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
310-597 |
3.34e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 310 AVNEIKDLSDKLKVAEGKQEEIQqkgqAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGiqvddflpKI 389
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQ----AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA--------EI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 390 NgstEKEHLLSKsggdctfihqfiecqkkliveghltkaveetklskenqtRAKESdfsdtlspSKEKSSDDTTDAQMDE 469
Cdd:COG3883 82 E---ERREELGE---------------------------------------RARAL--------YRSGGSVSYLDVLLGS 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 470 QDLNEPLAKVSLLKDDLQGAQSEIEakqEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQ 549
Cdd:COG3883 112 ESFSDFLDRLSALSKIADADADLLE---ELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLS 188
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1799135574 550 AQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASE 597
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
256-365 |
3.50e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 256 ESLRRVLQEKI-EVVRKLSEVERSLSNTEDEcthLKEMNERTQEELRELANKYNGAVNE--------IKDLSD--KLKVA 324
Cdd:PRK00409 526 EELERELEQKAeEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLEEAEKEAQQAIKEakkeadeiIKELRQlqKGGYA 602
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1799135574 325 EGKQEEIQQKgqaeKKELQHKIDEMEEKEQELQAKIEALQA 365
Cdd:PRK00409 603 SVKAHELIEA----RKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
589-781 |
3.59e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 589 QAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRcqqcedQQREEATRLQGELEKLRKEWNa 668
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL------PLYQELEALEAELAELPERLE- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 669 letechslkrenvllssELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDsadLKTLLSKAENQAK 748
Cdd:COG4717 150 -----------------ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD---LAEELEELQQRLA 209
|
170 180 190
....*....|....*....|....*....|...
gi 1799135574 749 DVQKEYEKTQTVLSELKLKFEMTEQEKQSITDE 781
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
511-721 |
3.91e-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: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 511 ELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQA 590
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 591 AAKVASERDTDIASLQEELKKVRaELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEatrlQGELEKLRKEWNALE 670
Cdd:pfam07888 110 SEELSEEKDALLAQRAAHEARIR-ELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEE----EAERKQLQAKLQQTE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1799135574 671 TECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQmsRKELENQ 721
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH--RKEAENE 233
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
163-342 |
5.28e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWqALIDEDRLLSRLEVMGNQLQACSKNQTE-DSLRKELI 241
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-DEIDVASAEREIAELEAELERLDASSDDlAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 242 ALQEDkhnyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLK----EMNERTQEELRELANKYNGAVNEIKDL 317
Cdd:COG4913 696 ELEAE-----------LEELEEELDELKGEIGRLEKELEQAEEELDELQdrleAAEDLARLELRALLEERFAAALGDAVE 764
|
170 180
....*....|....*....|....*
gi 1799135574 318 SDKLKVAEGKQEEIQQKGQAEKKEL 342
Cdd:COG4913 765 RELRENLEERIDALRARLNRAEEEL 789
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
208-366 |
5.51e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 208 IDEDRLLSRLEVMGNQLQACSKNQTE---DSLRKELIALQED-KHNYETTAKEslrrvLQEKIEVVRKLSEVERSLsnte 283
Cdd:PRK04778 249 LDHLDIEKEIQDLKEQIDENLALLEEldlDEAEEKNEEIQERiDQLYDILERE-----VKARKYVEKNSDTLPDFL---- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 284 decTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKK---ELQHKIDEMEEKEQELQ 357
Cdd:PRK04778 320 ---EHAKEQNKELKEEIDRVKQSYtlnESELESVRQLEKQLESLEKQYDEITERIAEQEIaysELQEELEEILKQLEEIE 396
|
....*....
gi 1799135574 358 AKIEALQAD 366
Cdd:PRK04778 397 KEQEKLSEM 405
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
328-568 |
5.76e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 5.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 328 QEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGiQVDDFLPKINGSTEKEHLLSKsggdct 407
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR-RIRALEQELAALEAELAELEK------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 408 fihqfiecqkkliveghltkavEETKLSKENQTRAKEsdFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQ 487
Cdd:COG4942 91 ----------------------EIAELRAELEAQKEE--LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 488 GAQSEIEakqEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKD 567
Cdd:COG4942 147 ARREQAE---ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
.
gi 1799135574 568 S 568
Cdd:COG4942 224 E 224
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
163-365 |
5.79e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.06 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEasdtsWQALIDEDRLLSR----LEVMGNQLQACSKNQT--EDSL 236
Cdd:COG0497 172 KELEELRADEAERARELDLLRFQLEELEAAALQPGE-----EEELEEERRRLSNaeklREALQEALEALSGGEGgaLDLL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 237 RKELIALQEDKHnYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERtQEELRELANKYNGAVNEIKD 316
Cdd:COG0497 247 GQALRALERLAE-YDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEER-LALLRRLARKYGVTVEELLA 324
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1799135574 317 LSDKLkvaegkqeeiqqkgQAEKKELQHKIDEMEEKEQELQAKIEALQA 365
Cdd:COG0497 325 YAEEL--------------RAELAELENSDERLEELEAELAEAEAELLE 359
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
494-732 |
6.01e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 494 EAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITST 573
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 574 RDellsardeillLHQAAAKVASErdtdIASLQEELKKVR--AELERWRKAASEYEKEITSLQNS---FQLRCQQCEDQQ 648
Cdd:PHA02562 258 NK-----------LNTAAAKIKSK----IEQFQKVIKMYEkgGVCPTCTQQISEGPDRITKIKDKlkeLQHSLEKLDTAI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 649 REEATRLQgELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSL-KE 727
Cdd:PHA02562 323 DELEEIMD-EFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELvKE 401
|
....*
gi 1799135574 728 QHLRD 732
Cdd:PHA02562 402 KYHRG 406
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
52-106 |
6.30e-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: 6.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799135574 52 SRNHALVWFDHKTGKFYLQ-----------DTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFG 106
Cdd:cd22683 28 SRSCDLVLSDPSISRFHAElrleqnginviDNNSANGTFINGKRIKGKT-----YILKNGDIIVFG 88
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
274-374 |
6.68e-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: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 274 EVERSLSNTEDECTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEK----------K 340
Cdd:pfam06160 288 YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEvayselqeelE 367
|
90 100 110
....*....|....*....|....*....|....
gi 1799135574 341 ELQHKIDEMEEKEQELQAKIEALQADNDFTNERL 374
Cdd:pfam06160 368 EILEQLEEIEEEQEEFKESLQSLRKDELEAREKL 401
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
294-551 |
6.87e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 294 ERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALqadndftNER 373
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL-------GER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 374 LTALQ-GIQVDDFLPKINGSTEKEHLLSKSggdcTFIHQFIECQKKLIveghltKAVEETKLSKENQtrakesdfsdtls 452
Cdd:COG3883 92 ARALYrSGGSVSYLDVLLGSESFSDFLDRL----SALSKIADADADLL------EELKADKAELEAK------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 453 pskekssddttdaqmdEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERK 532
Cdd:COG3883 149 ----------------KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
250
....*....|....*....
gi 1799135574 533 AYRNQVEESTKQIQVLQAQ 551
Cdd:COG3883 213 AAAAAAAAAAAAAAAAAAA 231
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
173-366 |
7.61e-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: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 173 QEALHREQMLEQKLATLQRLLAitqeasdtswqalidedRLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYET 252
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLK-----------------ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 253 TAKESLRRVLQEKIEVVRKlsevERSLSNTEDECTHLKEMNERTQEELRELankyngaVNEIKDLSDKLKVAEGKQEEIQ 332
Cdd:COG1579 69 EEVEARIKKYEEQLGNVRN----NKEYEALQKEIESLKRRISDLEDEILEL-------MERIEELEEELAELEAELAELE 137
|
170 180 190
....*....|....*....|....*....|....
gi 1799135574 333 QKGQAEKKELQHKIDEMEEKEQELQAKIEALQAD 366
Cdd:COG1579 138 AELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
190-803 |
7.61e-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: 39.95 E-value: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 190 QRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYET----TAKESLRRVLQEK 265
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNeeriDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 266 IEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVA-EGKQEEIQQKGQAEKKELQH 344
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDdEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 345 KIDEMEEKEQEL---QAKIEALQADNDFTNERLTALQGIQVDDFLPKingSTEKEHLLSKSGGDCTFIHQFIECQKKLIV 421
Cdd:pfam02463 333 EKEEIEELEKELkelEIKREAEEEEEEELEKLQEKLEQLEEELLAKK---KLESERLSSAAKLKEEELELKSEEEKEAQL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 422 EGHLTKAVEETKLSKENQTRAKES---DFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQE 498
Cdd:pfam02463 410 LLELARQLEDLLKEEKKEELEILEeeeESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELL 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 499 IQHLRKELIEAQELARTSKQKCFELQ---------------------ALLEEERKAYRNQVEESTKQIQVLQAQLQRLHI 557
Cdd:pfam02463 490 LSRQKLEERSQKESKARSGLKVLLALikdgvggriisahgrlgdlgvAVENYKVAISTAVIVEVSATADEVEERQKLVRA 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 558 DTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSF 637
Cdd:pfam02463 570 LTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLR 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 638 QLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKE 717
Cdd:pfam02463 650 KGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQE 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 718 LENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLkfEMTEQEKQSITDELKQCKNNLKLLREKGN 797
Cdd:pfam02463 730 AQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAE--EREKTEKLKVEEEKEEKLKAQEEELRALE 807
|
....*.
gi 1799135574 798 NPSILQ 803
Cdd:pfam02463 808 EELKEE 813
|
|
| VI_FHA |
TIGR03354 |
type VI secretion system FHA domain protein; Members of this protein family are FHA ... |
49-106 |
8.10e-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: 8.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799135574 49 KVLSRNHALV-WFDhktGKFYLQDTkSSNGTFINS--QRLSRGSEesppcEILS-GDIIQFG 106
Cdd:TIGR03354 43 RHVSGRHARIrYRD---GAYLLTDL-STNGVFLNGsgSPLGRGNP-----VRLEqGDRLRLG 95
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
472-784 |
8.43e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 39.72 E-value: 8.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 472 LNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIE-AQELAR--------TSKQKCFELQAL---------LEEERKA 533
Cdd:pfam17380 271 LNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEkAREVERrrkleeaeKARQAEMDRQAAiyaeqermaMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 534 YRNQVEESTKQIQVLQAQLQRLHI----DTENLREEKDSEITSTRDELLSARDEILL--------------LHQAAAKVA 595
Cdd:pfam17380 351 ERIRQEERKRELERIRQEEIAMEIsrmrELERLQMERQQKNERVRQELEAARKVKILeeerqrkiqqqkveMEQIRAEQE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 596 SERDTDIASLQEELKKvraELERWRKAASEYEKEITSLQnsfqlrcqqcedQQREEATRLQGELEKLRKEWNALETEchs 675
Cdd:pfam17380 431 EARQREVRRLEEERAR---EMERVRLEEQERQQQVERLR------------QQEEERKRKKLELEKEKRDRKRAEEQ--- 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 676 lkRENVLlsselqrqEKELHNSQKQSLELTSDLSILQmsrKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYE 755
Cdd:pfam17380 493 --RRKIL--------EKELEERKQAMIEEERKRKLLE---KEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMR 559
|
330 340
....*....|....*....|....*....
gi 1799135574 756 KTQTVLSELKLKFEMTEQEKQSITDELKQ 784
Cdd:pfam17380 560 KATEERSRLEAMEREREMMRQIVESEKAR 588
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
470-700 |
8.91e-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: 39.94 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 470 QDLNEPLAKVSLLKDDlqgaqseiEAKQEIQHLRKELIEAQELARTSKQKCFELqALLEEERKAYRN---QVEESTKQIQ 546
Cdd:COG3096 874 QLLNKLLPQANLLADE--------TLADRLEELREELDAAQEAQAFIQQHGKAL-AQLEPLVAVLQSdpeQFEQLQADYL 944
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 547 VLQAQLQRLHIDTENLREekdseiTSTRDELLSARDEILLLHQAAAKVASERdTDIASLQEELKKVRAELERWRKAASEY 626
Cdd:COG3096 945 QAKEQQRRLKQQIFALSE------VVQRRPHFSYEDAVGLLGENSDLNEKLR-ARLEQAEEARREAREQLRQAQAQYSQY 1017
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 627 EKEITSLQNSFQLRCQQ------------------CEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQ 688
Cdd:COG3096 1018 NQVLASLKSSRDAKQQTlqeleqeleelgvqadaeAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLR 1097
|
250
....*....|..
gi 1799135574 689 RQEKELHNSQKQ 700
Cdd:COG3096 1098 KAERDYKQEREQ 1109
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
485-634 |
9.03e-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: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135574 485 DLQGAQSEI-EAKQEIQHLRKELIEAQELARTSKQKCFELQALLEE---ERKAYRNQVEESTKQIQVLQAQLQRLHidte 560
Cdd:COG1579 11 DLQELDSELdRLEHRLKELPAELAELEDELAALEARLEAAKTELEDlekEIKRLELEIEEVEARIKKYEEQLGNVR---- 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135574 561 NLREEKD--SEITSTRDELLSARDEILLL---HQAAAKVASERDTDIASLQEELKKVRAELErwrKAASEYEKEITSLQ 634
Cdd:COG1579 87 NNKEYEAlqKEIESLKRRISDLEDEILELmerIEELEEELAELEAELAELEAELEEKKAELD---EELAELEAELEELE 162
|
|
| |
