|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
3-130 |
1.95e-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: 256.04 E-value: 1.95e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 3 SALAIFTCRPNSHPFQERHVYLDEPIKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINS 82
Cdd:cd22679 1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1799135557 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 |
6.63e-27 |
|
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal membrane-associated protein (SLMAP), also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. SLMAP contains an N-terminal FHA domain followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409287 [Multi-domain] Cd Length: 63 Bit Score: 103.92 E-value: 6.63e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799135557 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQ 225
Cdd:cd21911 1 QELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQLS 63
|
|
| FHA_DMA-like |
cd22692 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest ... |
27-108 |
1.74e-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: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 27 PIKIGRSVARCRPAQNNAT-FDCKVLSRNHALVWfdHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQF 105
Cdd:cd22692 38 QIHIGRYTERVRQAIYHPVvFKSKVVSRTHGCIK--VDEGNWYIKDVKSSSGTFLNHQRLSPASRTSKPYPLRDGDILQL 115
|
...
gi 1799135557 106 GVD 108
Cdd:cd22692 116 GMD 118
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-754 |
3.38e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 86.65 E-value: 3.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 156 NTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQA--CSKNQTE 233
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvAQLELQI 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 234 DSLRKELIAL------QEDKHNYETTAKESLRRVLQE--KIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELAN 305
Cdd:TIGR02168 396 ASLNNEIERLearlerLEDRRERLQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 306 KYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKidemEEKEQELQAKIEALQADNDFTNERLTALQGIqVDDF 385
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ----SGLSGILGVLSELISVDEGYEAAIEAALGGR-LQAV 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 386 LPKINGSTEK--EHLLSKSGGDCTFI------HQFIECQKKLIVEGH----------------LTKAVE----------- 430
Cdd:TIGR02168 551 VVENLNAAKKaiAFLKQNELGRVTFLpldsikGTEIQGNDREILKNIegflgvakdlvkfdpkLRKALSyllggvlvvdd 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 431 -ETKLSKENQTRAKESDFS---DTLSP--------SKEKSSDDTTDAQMDEqdLNEPLAKVSLLKALLEEERKAYRNQVE 498
Cdd:TIGR02168 631 lDNALELAKKLRPGYRIVTldgDLVRPggvitggsAKTNSSILERRREIEE--LEEKIEELEEKIAELEKALAELRKELE 708
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 499 ESTKQIQVLQAQLQRLHIDTENLREEKD----------SEITSTRDELLSARDEILLLHQAAAKV---ASERDTDIASLQ 565
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLArleaeveqleERIAQLSKELTELEAEIEELEERLEEAeeeLAEAEAEIEELE 788
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 566 EELKKVRAELERWRKAASEYEKEITSLQNSF---QLRCQQCEDQQREEATRL----------QGELEKLRKEWNALETEC 632
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATERRLedleeqieelSEDIESLAAEIEELEELI 868
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 633 HSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHlrdsADLKTLLSKAENQAKDVQke 712
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL----AQLELRLEGLEVRIDNLQ-- 942
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1799135557 713 yektQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 754
Cdd:TIGR02168 943 ----ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| FHA_VPS64-like |
cd22695 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ... |
6-126 |
5.75e-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: 5.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 6 AIFTCRPNSHPFQERHV---YLDEPIKIGRSVARCRPAQN---------------NATFDCKVLSRNHALVWFDHKTGKF 67
Cdd:cd22695 2 HILVLKSLNATFETKFLvvpFKPDGLKLGRPVTNSVNKNNsgskrdlfsqqvrpdNGNFDSRVLSRNHACLSCDPTTGKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135557 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 |
4.89e-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: 4.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 13 NSHPFQERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINSQRLsrgseeS 92
Cdd:cd00060 6 DGDGGGREFPLTKGVVTIGRS------PDCDIVLDDPSVSRRHARIEVDG--GGVYLEDLGSTNGTFVNGKRI------T 71
|
90
....*....|....
gi 1799135557 93 PPCEILSGDIIQFG 106
Cdd:cd00060 72 PPVPLQDGDVIRLG 85
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
28-105 |
1.43e-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: 1.43e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135557 28 IKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRLSRgseesPPCEILSGDIIQF 105
Cdd:pfam00498 1 VTIGRS------PDCDIVLDDPSVSRRHAEIRYD-GGGRFYLEDLGSTNGTFVNGQRLGP-----EPVRLKDGDVIRL 66
|
|
| CC1_SLMAP-like |
cd21868 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ... |
167-204 |
6.31e-13 |
|
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar proteins; The family includes Sarcolemmal membrane-associated protein (SLMAP), its paralog TRAF3-interacting JNK-activating modulator (T3JAM), and similar proteins. SLMAP, also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. T3JAM, also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. SLMAP contains an N-terminal FHA domain, followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409286 [Multi-domain] Cd Length: 38 Bit Score: 63.27 E-value: 6.31e-13
10 20 30
....*....|....*....|....*....|....*...
gi 1799135557 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21868 1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
481-754 |
9.31e-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: 72.02 E-value: 9.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 481 LLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLhidtENLREEKDSEITSTRDELLSARDeilLLHQAAAKVASERDTD 560
Cdd:TIGR02169 216 LLKEKREYEGYELLKEKEALERQKEAIERQLASL----EEELEKLTEEISELEKRLEEIEQ---LLEELNKKIKDLGEEE 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 561 IASLQEELKKVRAELERWRKAASEYEKEITSLQNsfQLRCQQCE-DQQREEATRLQGELEKLRKEWNALETECHSLKREN 639
Cdd:TIGR02169 289 QLRVKEKIGELEAEIASLERSIAEKERELEDAEE--RLAKLEAEiDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 640 VLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADlktlLSKAENQAKDVQKEYEKTQTV 719
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEE----LADLNAAIAGIEAKINELEEE 442
|
250 260 270
....*....|....*....|....*....|....*
gi 1799135557 720 LSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 754
Cdd:TIGR02169 443 KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
239-740 |
1.41e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 71.71 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 239 ELIALQEDKHNYETTAKESLRRV--LQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKD 316
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 317 LSDKLKVAEGKQEEIQQKGQAEKK--ELQHKIDEMEEKEQELQAKIEALQ---ADNDFTNERLTALQGIQVDDFLPKING 391
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKkaaAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 392 STEKEHLLSKSGgdctfihqfiECQKKlivEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKE---KSSDDTTDAQMD 468
Cdd:PTZ00121 1442 EAKKADEAKKKA----------EEAKK---AEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEeakKKADEAKKAAEA 1508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 469 EQDLNEplAKVSLLKALLEEERKA-YRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDEllsARDEILLLH 547
Cdd:PTZ00121 1509 KKKADE--AKKAEEAKKADEAKKAeEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEE---DKNMALRKA 1583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 548 QAAAKVASERDTDIASLQEELKKVRAE----LERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRK 623
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEeakkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA 1663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 624 EWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAE 703
Cdd:PTZ00121 1664 AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK 1743
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1799135557 704 NQAKDVQKEYE---KTQTVLSELKLKFEMTEQEKQSITDE 740
Cdd:PTZ00121 1744 KKAEEAKKDEEekkKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
476-735 |
2.21e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 476 LAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREE------KDSEITSTRDELLSARDEILLLHQA 549
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEleeaqaEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 550 AAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSfqlrcqqcEDQQREEATRLQGELEKLRKEWNALE 629
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE--------LAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 630 TECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDV 709
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260
....*....|....*....|....*.
gi 1799135557 710 QKEYEKTQTVLSELKLKFEMTEQEKQ 735
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAA 491
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
212-753 |
2.37e-12 |
|
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: 70.85 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 212 RLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTAKESLRRVLQEKIEvvrkLSEVERSlSNTEDECTHLKE 291
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE----LDGFERG-PFSERQIKNFHT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 292 MNERTQEELRELANKyngavnEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQadndftn 371
Cdd:TIGR00606 398 LVIERQEDEAKTAAQ------LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ------- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 372 eRLTAlqgiQVDDFLPKINGSTEKEHLLSKSGGDCTfihqfIECQKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTL 451
Cdd:TIGR00606 465 -QLEG----SSDRILELDQELRKAERELSKAEKNSL-----TETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTR 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 452 SPSKEKSSDDTT-DAQMDEQDLNEPLAKVSLL-----KALLEEERKAYRNQVEESTKQIQVLQAQLQRLhidtENLREEK 525
Cdd:TIGR00606 535 TQMEMLTKDKMDkDEQIRKIKSRHSDELTSLLgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASL----EQNKNHI 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 526 DSEITSTRDELLSARDEILllhqaAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQC-- 603
Cdd:TIGR00606 611 NNELESKEEQLSSYEDKLF-----DVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCqr 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 604 ----EDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLL-------SSELQRQEKELHNSQKQSLELTSDLSILQM 672
Cdd:TIGR00606 686 vfqtEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKN 765
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 673 SRKELENQVGSL--KEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVL--SELKLKFEMTEQEKQSITDELKQCKNNL 748
Cdd:TIGR00606 766 DIEEQETLLGTImpEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLqgSDLDRTVQQVNQEKQEKQHELDTVVSKI 845
|
....*
gi 1799135557 749 KLLRE 753
Cdd:TIGR00606 846 ELNRK 850
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
14-106 |
1.12e-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: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 14 SHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716 8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
|
90
....*....|....
gi 1799135557 93 pPCEILSGDIIQFG 106
Cdd:COG1716 75 -PAPLRDGDVIRLG 87
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
163-754 |
1.13e-11 |
|
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: 68.54 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSknqteDSLRKELIA 242
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL-----ESLEAELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 243 LQEDKHNYETTAKEsLRRVLQEKIEVVRKLSEVERSLSNT----EDECTHLKEMNERTQEELRELANKY-NGAVNEIKDL 317
Cdd:TIGR02168 363 LEAELEELESRLEE-LEEQLETLRSKVAQLELQIASLNNEierlEARLERLEDRRERLQQEIEELLKKLeEAELKELQAE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 318 SDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQAdndftneRLTALQGIQvDDFLPKINGSTEKEH 397
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA-------RLDSLERLQ-ENLEGFSEGVKALLK 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 398 LLSKSGGDCTFIHQFIECQKKLiveghlTKAVEET------KLSKENQTRAKesdfsDTLSPSKEKSSDDTTDAQMDEQD 471
Cdd:TIGR02168 514 NQSGLSGILGVLSELISVDEGY------EAAIEAAlggrlqAVVVENLNAAK-----KAIAFLKQNELGRVTFLPLDSIK 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 472 LNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIdTENLREEKDSEITSTRDELL-SARDEILLLHQAA 550
Cdd:TIGR02168 583 GTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLV-VDDLDNALELAKKLRPGYRIvTLDGDLVRPGGVI 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 551 AKVASERDTDIASLQEELKKVRAELErwrkaaseyekeitslqnsfqlrcqqcedQQREEATRLQGELEKLRKEWNALET 630
Cdd:TIGR02168 662 TGGSAKTNSSILERRREIEELEEKIE-----------------------------ELEEKIAELEKALAELRKELEELEE 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 631 ECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQ----------HLRDSADLKTLLS 700
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERleeaeeelaeAEAEIEELEAQIE 792
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1799135557 701 KAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 754
Cdd:TIGR02168 793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
470-743 |
1.16e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 470 QDLNEPLAKVSLLKALLEeeRKAYRNQVEESTKQIQVLQAQLQRLhidtENLREEKDSEITSTRDELLSARDEILLLHQA 549
Cdd:COG1196 216 RELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEEL----EAELAELEAELEELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 550 AAKVASErdtdIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQcEDQQREEATRLQGELEKLRKEWNALE 629
Cdd:COG1196 290 EYELLAE----LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE-LEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 630 TECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDV 709
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
250 260 270
....*....|....*....|....*....|....
gi 1799135557 710 QKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 743
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
484-733 |
1.35e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 484 ALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEitstRDELLSARDEILLLHQAAAKVASErdtdIAS 563
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL----EERRRELEERLEELEEELAELEEE----LEE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 564 LQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEwNALETECHSLKRENVLLS 643
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA-AELAAQLEELEEAEEALL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 644 SELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSEL 723
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
250
....*....|
gi 1799135557 724 KLKFEMTEQE 733
Cdd:COG1196 494 LLLLEAEADY 503
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
52-106 |
1.38e-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: 1.38e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1799135557 52 SRNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQFG 106
Cdd:cd22686 48 SKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPYPLTHGDELKIG 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
161-724 |
5.08e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 161 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKEL 240
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 241 IALQEDkhnyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDK 320
Cdd:COG1196 298 ARLEQD-----------IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 321 LKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDdflpkINGSTEKEHLLS 400
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA-----LAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 401 KsggdctfihQFIECQKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEP----- 475
Cdd:COG1196 442 E---------ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLegvka 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 476 ------LAKVSLLKALLEEERKAYRNQVEEstkqiqVLQAQLQRLHIDTENLREEKDSEITSTRDellsARDEILLLHQA 549
Cdd:COG1196 513 alllagLRGLAGAVAVLIGVEAAYEAALEA------ALAAALQNIVVEDDEVAAAAIEYLKAAKA----GRATFLPLDKI 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 550 AAKVASERDTDIASLQEELKKVrAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQRE----------EATRLQGELE 619
Cdd:COG1196 583 RARAALAAALARGAIGAAVDLV-ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTlagrlrevtlEGEGGSAGGS 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 620 KLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLL 699
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
570 580
....*....|....*....|....*
gi 1799135557 700 SKAENQAKDVQKEYEKTQTVLSELK 724
Cdd:COG1196 742 LEEEELLEEEALEELPEPPDLEELE 766
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
172-743 |
1.30e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 172 LQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRllsrlevmgnqlqacSKNQTEDSLRKELIALQEDKHNYE 251
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS---------------ELEEEIEELQKELYALANEISRLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 252 ttakeslrrvlQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEI 331
Cdd:TIGR02168 302 -----------QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 332 QQKGQAEKKELQH---KIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQvddflpkingsteKEHLLSKSGGDCTF 408
Cdd:TIGR02168 371 ESRLEELEEQLETlrsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI-------------EELLKKLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 409 IHQFIECQKKLIVEGHLTKAVEETKLSK-ENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLE 487
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEElREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 488 ------------EERKAYRNQVEEstkqiqVLQAQLQRLHIDTEN---------------------LREEKDSEITSTRD 534
Cdd:TIGR02168 518 lsgilgvlseliSVDEGYEAAIEA------ALGGRLQAVVVENLNaakkaiaflkqnelgrvtflpLDSIKGTEIQGNDR 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 535 ELLSARDEILLLHQAAAKVASERD-------------TDIASLQEELKKVRA---------ELERWRKAAS--------- 583
Cdd:TIGR02168 592 EILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvDDLDNALELAKKLRPgyrivtldgDLVRPGGVITggsaktnss 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 584 --EYEKEITSLQNSFQLRCQQCEDQQ------REEATRLQGELEKLRKEWNALETECHSLK-------RENVLLSSELQR 648
Cdd:TIGR02168 672 ilERRREIEELEEKIEELEEKIAELEkalaelRKELEELEEELEQLRKELEELSRQISALRkdlarleAEVEQLEERIAQ 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 649 QEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTL---LSKAENQAKDVQKEYEKTQTVLSELKL 725
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALreaLDELRAELTLLNEEAANLRERLESLER 831
|
650
....*....|....*...
gi 1799135557 726 KFEMTEQEKQSITDELKQ 743
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEE 849
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
505-753 |
2.38e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 505 QVLQAQLQRLHIdteNLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASE 584
Cdd:COG1196 216 RELKEELKELEA---ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 585 YEKEITSLQNSFQLRCQQCEDQQREEAtRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELT 664
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLE-ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 665 SDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQC 744
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
....*....
gi 1799135557 745 KNNLKLLRE 753
Cdd:COG1196 452 AELEEEEEA 460
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
267-754 |
3.69e-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: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 267 EVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKI 346
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 347 DEMEEKEQE---LQAKIEALQADNDFTNERLTALQGIQVDdfLPKINGSTEKEHLLSKSGGDcTFIHQFIECQKKlIVEG 423
Cdd:TIGR04523 117 EQKNKLEVElnkLEKQKKENKKNIDKFLTEIKKKEKELEK--LNNKYNDLKKQKEELENELN-LLEKEKLNIQKN-IDKI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 424 HLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSL----LKALLEEERKAYR----- 494
Cdd:TIGR04523 193 KNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNtqtqLNQLKDEQNKIKKqlsek 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 495 -NQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILllhQAAAKVASERDTDIASLQEELKKVRA 573
Cdd:TIGR04523 273 qKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKL---EEIQNQISQNNKIISQLNEQISQLKK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 574 ELERWRKAASEYEKEITSLQNsfqlrcqQCEDQQREEATRLQgELEKLRKEWNALETECHSLKRENVLLSSELQRQEKEL 653
Cdd:TIGR04523 350 ELTNSESENSEKQRELEEKQN-------EIEKLKKENQSYKQ-EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 654 HNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHlrdsADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQE 733
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKELII----KNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
490 500
....*....|....*....|.
gi 1799135557 734 KQSITDELKQCKNNLKLLREK 754
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKK 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
163-679 |
3.91e-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: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDtswQALIDEDRLLSRLEVMGNQLQACSKNQTE-----DSLR 237
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRR---ELEERLEELEEELAELEEELEELEEELEEleeelEEAE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 238 KELIALQEDKHNYETTAKESLRRVL---QEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEI 314
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAeaeEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 315 KDLSDKLKVAEGKQEEIQQK---GQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDDflPKING 391
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEeaeLEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY--EGFLE 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 392 STEKEHLLSKSGGDCTFIHQFIECQKKL--------------IVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEK 457
Cdd:COG1196 509 GVKAALLLAGLRGLAGAVAVLIGVEAAYeaaleaalaaalqnIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAAL 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 458 SSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQV----EESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTR 533
Cdd:COG1196 589 AAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVaarlEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 534 DELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATR 613
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799135557 614 LQGELEKLRKE--WNALETECHSLKRE-------NVLLSSELQRQEKELHnsqkqslELTSDLSILQMSRKELEN 679
Cdd:COG1196 749 EEEALEELPEPpdLEELERELERLEREiealgpvNLLAIEEYEELEERYD-------FLSEQREDLEEARETLEE 816
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
256-749 |
4.62e-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: 63.60 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 256 ESLRRVLQEKIEVVRKLSE--VERSLSNTEDECTHLKEmnerTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQ-EEIQ 332
Cdd:pfam15921 248 EALKSESQNKIELLLQQHQdrIEQLISEHEVEITGLTE----KASSARSQANSIQSQLEIIQEQARNQNSMYMRQlSDLE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 333 QKGQAEKKELQHKIDEMEEKEQELQAKIeaLQADNDFTNERLTALQGIQ----VDDFLPKING---STEKEHLLSKSggd 405
Cdd:pfam15921 324 STVSQLRSELREAKRMYEDKIEELEKQL--VLANSELTEARTERDQFSQesgnLDDQLQKLLAdlhKREKELSLEKE--- 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 406 ctfihqfiecQKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDE-QDLNEPLAKVSLLKA 484
Cdd:pfam15921 399 ----------QNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAiQGKNESLEKVSSLTA 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 485 LLEEERKAYRNQVEESTKQIQVLQAQlQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDtdiasl 564
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESS-ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGD------ 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 565 qeELKKVRAELERWRKAASEYEKEITSLQNSFQlRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLK-------- 636
Cdd:pfam15921 542 --HLRNVQTECEALKLQMAEKDKVIEILRQQIE-NMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKilkdkkda 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 637 --RENVLLSSELQRQEKELHNSQKQSLELTSDlsiLQMSRKELENQVGSLKEqhlrdsaDLKTLLSKAENQAKDVQKEYE 714
Cdd:pfam15921 619 kiRELEARVSDLELEKVKLVNAGSERLRAVKD---IKQERDQLLNEVKTSRN-------ELNSLSEDYEVLKRNFRNKSE 688
|
490 500 510
....*....|....*....|....*....|....*
gi 1799135557 715 KTQTVLSELKLKFemteqekQSITDELKQCKNNLK 749
Cdd:pfam15921 689 EMETTTNKLKMQL-------KSAQSELEQTRNTLK 716
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
135-696 |
9.06e-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: 62.44 E-value: 9.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 135 ARLRSDVIHAPLpSPVDKVAANTPSMYSQELFQL----SQYLQEALHREQMLEQKLATLQRLLAItqeASDTSWQALIDE 210
Cdd:pfam15921 290 ARSQANSIQSQL-EIIQEQARNQNSMYMRQLSDLestvSQLRSELREAKRMYEDKIEELEKQLVL---ANSELTEARTER 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 211 DRLLSRLEVMGNQLQAC----SKNQTEDSLRKELIALQEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNtedec 286
Cdd:pfam15921 366 DQFSQESGNLDDQLQKLladlHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKS----- 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 287 thlkEMNERTQEELRELANKyNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQAd 366
Cdd:pfam15921 441 ----ECQGQMERQMAAIQGK-NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEA- 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 367 ndfTNERLTALQGiQVDDFLPKING-STEKEHLLsksggdctfiHQFIECQKKLIVEGHLTKAVEETKLSKENQTR--AK 443
Cdd:pfam15921 515 ---TNAEITKLRS-RVDLKLQELQHlKNEGDHLR----------NVQTECEALKLQMAEKDKVIEILRQQIENMTQlvGQ 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 444 ESDFSDTLSPSKEKSSDDTTDAQMDEQDLNeplakvsllkaLLEEERKAYRNQVEESTKQIQVLQAQLqrLHIDTENLRE 523
Cdd:pfam15921 581 HGRTAGAMQVEKAQLEKEINDRRLELQEFK-----------ILKDKKDAKIRELEARVSDLELEKVKL--VNAGSERLRA 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 524 EKD---------SEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWR--------------K 580
Cdd:pfam15921 648 VKDikqerdqllNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRntlksmegsdghamK 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 581 AASEYEKEITSLQNsfQLRCQQCEDQQREEATR--------LQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKE 652
Cdd:pfam15921 728 VAMGMQKQITAKRG--QIDALQSKIQFLEEAMTnankekhfLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEK 805
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1799135557 653 LHNSQ----KQSLELTSDLSILQmsRKELENQvgSLKEQHLRDSADLK 696
Cdd:pfam15921 806 VANMEvaldKASLQFAECQDIIQ--RQEQESV--RLKLQHTLDVKELQ 849
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
233-757 |
9.97e-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: 62.38 E-value: 9.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 233 EDSLRKELIALQ-EDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAV 311
Cdd:TIGR02168 222 LRELELALLVLRlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 312 NEIKDLSDKLKVAEGKQEEIQ---QKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDDFlPK 388
Cdd:TIGR02168 302 QQKQILRERLANLERQLEELEaqlEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE-EQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 389 INGSTEKEHLLSKSGGDCTFIHQFIECQKKlivegHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMD 468
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLE-----RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 469 EQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKD------------SEITSTR--- 533
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKnqsglsgilgvlSELISVDegy 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 534 -----------------DELLSARDEILLLHQAAAKVA------SERDTDIASLQEELKK----VRAELERWRKAASEYE 586
Cdd:TIGR02168 536 eaaieaalggrlqavvvENLNAAKKAIAFLKQNELGRVtflpldSIKGTEIQGNDREILKniegFLGVAKDLVKFDPKLR 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 587 KEI----------TSLQNSFQLRCQQCEDQQ--------------------REEATRL--QGELEKLRKEWNALETECHS 634
Cdd:TIGR02168 616 KALsyllggvlvvDDLDNALELAKKLRPGYRivtldgdlvrpggvitggsaKTNSSILerRREIEELEEKIEELEEKIAE 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 635 LKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYE 714
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1799135557 715 KTQTVLSE---LKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNN 757
Cdd:TIGR02168 776 ELAEAEAEieeLEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
234-663 |
1.24e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 234 DSLRKELIALQEDKHNYETTAKEsLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLK------EMNERTQEELRELANKY 307
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEING-IEERIKELEEKEERLEELKKKLKELEKRLEELEerhelyEEAKAKKEELERLKKRL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 308 NGavNEIKDLSDKLKVAEGKQEEIQQkgqaEKKELQHKIDEMEEKEQELQAKIEALQAD-----------NDFTNERLTA 376
Cdd:PRK03918 382 TG--LTPEKLEKELEELEKAKEEIEE----EISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrelTEEHRKELLE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 377 LQGIQVDDFLPKINGSTEKEHLLSKsggdctfihQFIECQKKLIVEGHLTKAVEETKLSKENQTRAKESDfsdtlspsKE 456
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLRK---------ELRELEKVLKKESELIKLKELAEQLKELEEKLKKYN--------LE 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 457 KSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEErKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDEL 536
Cdd:PRK03918 519 ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL-EELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKEL 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 537 LSARDEILLLHQAAAKVASERDtDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFqlrcqqcedqQREEATRLQG 616
Cdd:PRK03918 598 EPFYNEYLELKDAEKELEREEK-ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY----------SEEEYEELRE 666
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1799135557 617 ELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLEL 663
Cdd:PRK03918 667 EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL 713
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
296-659 |
2.06e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 296 TQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQ---KGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNE 372
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEeleQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 373 RLTALQgiqvddflpkingstekehllsksggdctfihqfiecQKKLIVEGHLTKAVEETKLSKENQTRAKESdfSDTLS 452
Cdd:TIGR02168 755 ELTELE-------------------------------------AEIEELEERLEEAEEELAEAEAEIEELEAQ--IEQLK 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 453 PSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDsEITST 532
Cdd:TIGR02168 796 EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE-ELESE 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 533 RDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNsfqlrcqqcedqqreeat 612
Cdd:TIGR02168 875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV------------------ 936
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1799135557 613 RLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQ 659
Cdd:TIGR02168 937 RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-743 |
2.07e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.24 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 197 QEASDTSWQALIDEDRLLSRLEVMGNQLQacsknqtedSLRKELIALQEDKHNYETTAKESLRRVLQEKI---EVVRKLS 273
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIE---------EERKRRDKLTEEYAELKEELEDLRAELEEVDKefaETRDELK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 274 EVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIqqkgQAEKKELQHKIDEMEEKE 353
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK----ALEIKKQEWKLEQLAADL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 354 QELQAKIEALQADNDFTNERLTALQG------IQVDDFLPKINGSTEKEHLLSKS-GGDCTFIHQFIECQKK-------- 418
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELSKLQRelaeaeAQARASEERVRGGRAVEEVLKASiQGVHGTVAQLGSVGERyataieva 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 419 -------LIVEGHLTkAVEETKLSKE-----------NQTRAKESDfsdtLSPSKEKSSDDTTDAQMDEQDLNEPLAK-- 478
Cdd:TIGR02169 545 agnrlnnVVVEDDAV-AKEAIELLKRrkagratflplNKMRDERRD----LSILSEDGVIGFAVDLVEFDPKYEPAFKyv 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 479 ----------------------VSLLKALLE----------EERKAYRNQVEESTKqIQVLQAQLQRLHIDTENLREEKD 526
Cdd:TIGR02169 620 fgdtlvvedieaarrlmgkyrmVTLEGELFEksgamtggsrAPRGGILFSRSEPAE-LQRLRERLEGLKRELSSLQSELR 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 527 sEITSTRDELLSARD-----------EILLLHQAAAKVA----------SERDTDIASLQEELKKVRAELERWRKAASEY 585
Cdd:TIGR02169 699 -RIENRLDELSQELSdasrkigeiekEIEQLEQEEEKLKerleeleedlSSLEQEIENVKSELKELEARIEELEEDLHKL 777
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 586 EKEITSLQNSF----------QLRCQQCEDQQREEATR-LQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELH 654
Cdd:TIGR02169 778 EEALNDLEARLshsripeiqaELSKLEEEVSRIEARLReIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE 857
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 655 NSQKQSLELTSDLSILQMSRKELENQVGSLKeqhlRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEK 734
Cdd:TIGR02169 858 NLNGKKEELEEELEELEAALRDLESRLGDLK----KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
....*....
gi 1799135557 735 QSITDELKQ 743
Cdd:TIGR02169 934 SEIEDPKGE 942
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
486-753 |
3.60e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 486 LEEERKAYRNQVEESTKQIQVLQAQLQ-----------RLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVA 554
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISelekrleeieqLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 555 SER---DTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQRE------EATRLQGELEKLRKEW 625
Cdd:TIGR02169 315 RELedaEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEleevdkEFAETRDELKDYREKL 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 626 NALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADlktlLSKAENQ 705
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD----LSKYEQE 470
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1799135557 706 AKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLRE 753
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| CC1_T3JAM |
cd21912 |
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ... |
164-204 |
4.92e-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: 52.35 E-value: 4.92e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1799135557 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21912 5 EILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
271-728 |
1.01e-08 |
|
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: 59.03 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 271 KLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAvneIKDLSDKLKvaegKQEEIQQKGQAEKKELQHKIDEME 350
Cdd:pfam01576 149 KLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAM---ISDLEERLK----KEEKGRQELEKAKRKLEGESTDLQ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 351 EKEQELQAKIEALQADNDFTNERLTALQGIQVDDFLPKINGSTEKEHLLSksggdctfihQFIECQKKLIVEGHLTKAVE 430
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEA----------QISELQEDLESERAARNKAE 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 431 ETKLSKENQTRAKESDFSDTLspskekssdDTTDAQMDEQDLNEplAKVSLLKALLEEERKAYRNQVEEstkqiqvlqaq 510
Cdd:pfam01576 292 KQRRDLGEELEALKTELEDTL---------DTTAAQQELRSKRE--QEVTELKKALEEETRSHEAQLQE----------- 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 511 lqrlhidtenLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERdtdiASLQEELKKVRAelerwRKAASEYEKEIT 590
Cdd:pfam01576 350 ----------MRQKHTQALEELTEQLEQAKRNKANLEKAKQALESEN----AELQAELRTLQQ-----AKQDSEHKRKKL 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 591 SLQ-NSFQLRCQQCEDQQREEA---TRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSD 666
Cdd:pfam01576 411 EGQlQELQARLSESERQRAELAeklSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTR 490
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799135557 667 LsilqmsrKELENQVGSLKEQhlrdsadlktlLSKAENQAKDVQKEYEKTQTVLSELKLKFE 728
Cdd:pfam01576 491 L-------RQLEDERNSLQEQ-----------LEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
|
| FHA_TCF19 |
cd22685 |
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ... |
29-119 |
1.08e-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: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 29 KIGRSVARCRPAQNNATFDcKVLSRNHALVW---FDHKTGKFYLQDTkSSNGTFINSQRLSRGSEEsppcEILSGDIIQF 105
Cdd:cd22685 31 RIGRNPEVCDVFLCSSQHP-NLISREHAEIHaerDGNGNWKVLIEDR-STNGTYVNDVRLQDGQRR----ELSDGDTITF 104
|
90
....*....|....*.
gi 1799135557 106 G--VDVTENTRKVTHG 119
Cdd:cd22685 105 GhkNGRRVKQWPYQKS 120
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
298-754 |
1.21e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 298 EELRELANKYNGAVNEIkdLSDKLKVAEGKQEEIQQKgqaEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTAL 377
Cdd:PRK02224 165 EEYRERASDARLGVERV--LSDQRGSLDQLKAQIEEK---EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 378 QGIqvddflpkingstekehllsksggdctfIHQFIECQKKLIVeghLTKAVEETKLSKENQTRAKEsDFSDTLSPSKEK 457
Cdd:PRK02224 240 DEV----------------------------LEEHEERREELET---LEAEIEDLRETIAETERERE-ELAEEVRDLRER 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 458 SSD--DTTDAQMDEQDLNEPLAK-VSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEK--------- 525
Cdd:PRK02224 288 LEEleEERDDLLAEAGLDDADAEaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAeelreeaae 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 526 -DSEITSTRDELLSARDEILLLhQAAAKVASER----DTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSF---- 596
Cdd:PRK02224 368 lESELEEAREAVEDRREEIEEL-EEEIEELRERfgdaPVDLGNAEDFLEELREERDELREREAELEATLRTARERVeeae 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 597 QLR----CQQCE------------DQQREEATRLQGELEKLRKEWNALETECHSLKrenvllssELQRQEKELHNSQKQS 660
Cdd:PRK02224 447 ALLeagkCPECGqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAE--------DLVEAEDRIERLEERR 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 661 LELTSDLSILQMSRKELENQVGSLKEQhlrdSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS---- 736
Cdd:PRK02224 519 EDLEELIAERRETIEEKRERAEELRER----AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESleri 594
|
490 500
....*....|....*....|
gi 1799135557 737 --ITDELKQCKNNLKLLREK 754
Cdd:PRK02224 595 rtLLAAIADAEDEIERLREK 614
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
235-754 |
2.08e-08 |
|
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: 57.72 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 235 SLRKELIALQEDKHNYETTAKE--SLRRVLQEKIEVVRKLSEVERSLsntEDECTHLKEMNERTQEELRELANKYNGAVN 312
Cdd:TIGR04523 170 ELENELNLLEKEKLNIQKNIDKikNKLLKLELLLSNLKKKIQKNKSL---ESQISELKKQNNQLKDNIEKKQQEINEKTT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 313 EIKDLSDKLKVAEGKQEEIQQKGQAEKKELQH---KIDEMEEKEQELQAKIEALQadndftnerltalqgiqvddflpki 389
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLN------------------------- 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 390 ngsTEKEHLLSKSggdctfIHQFIECQKKLIVEghltkavEETKLSKENQtraKESDFSDTLSPSKEKSSDDTTDAQMDE 469
Cdd:TIGR04523 302 ---NQKEQDWNKE------LKSELKNQEKKLEE-------IQNQISQNNK---IISQLNEQISQLKKELTNSESENSEKQ 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 470 QDLNEPLAKVSLLKalleEERKAYRNQVEESTKQIQVLQAQLQrlhiDTENLREEKDSEITSTRDELLSardeilllhqa 549
Cdd:TIGR04523 363 RELEEKQNEIEKLK----KENQSYKQEIKNLESQINDLESKIQ----NQEKLNQQKDEQIKKLQQEKEL----------- 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 550 aakvaserdtdiasLQEELKKVRAELERWRKAASEYEKEITSLQNSFQlrcqqcedqqreeatrlqgELEKLRKEwnaLE 629
Cdd:TIGR04523 424 --------------LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK-------------------NLDNTRES---LE 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 630 TECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQhlrdSADLKTLLSKAENQAKDV 709
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK----IEKLESEKKEKESKISDL 543
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1799135557 710 QKEYEKTQTVLselklKFEMTEQEKQSITDELKQCKNNLKLLREK 754
Cdd:TIGR04523 544 EDELNKDDFEL-----KKENLEKEIDEKNKEIEELKQTQKSLKKK 583
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
14-110 |
2.62e-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: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 14 SHPFQERHV---YLDEPIKIGRSvARCRPAQNNATfdckvLSRNHALVW---FDHKTG-KFYLQDTkSSNGTFINSQRLS 86
Cdd:cd22670 7 SSPGSTDIVlpiYKNQVITIGRS-PSCDIVINDPF-----VSRTHCRIYsvqFDESSApLVYVEDL-SSNGTYLNGKLIG 79
|
90 100
....*....|....*....|....*
gi 1799135557 87 RGseespPCEILS-GDIIQFGVDVT 110
Cdd:cd22670 80 RN-----NTVLLSdGDVIEIAHSAT 99
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
255-754 |
3.77e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 255 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNgAVNEIKDLSDKLKVAEGKQEEIQQK 334
Cdd:PRK03918 178 IERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 335 GQAEKKELQHKIDEMEEKEQELQAKIEALqadndfTNERLTALQGIQVDDFLPKIN-GSTEKEHLLSKsggdctfIHQFI 413
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKEL------KELKEKAEEYIKLSEFYEEYLdELREIEKRLSR-------LEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 414 ECQKKLIVEGhltkaveETKLSKENQTRAKESDFSDTLSPSKEKSSD-DTTDAQMDE-QDLNEPLAKVSLLKalLEEERK 491
Cdd:PRK03918 324 NGIEERIKEL-------EEKEERLEELKKKLKELEKRLEELEERHELyEEAKAKKEElERLKKRLTGLTPEK--LEKELE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 492 AYRNQVEESTKQIQVLQAQLQRLHIDTENLRE-----EKDSEITSTRDELLSARDEILLLHQAAAKVASERDtDIASLQE 566
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKELKKaieelKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEK-ELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 567 ELKKVRAELERWRKAASEYEKEITSLQNSFQLRC--QQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRE---NVL 641
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESELIKLKELAEQLKEleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKElekLEE 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 642 LSSELQRQEKELHNSQKQSLELTSDLSILQM-SRKELENQVGSLKEQH-----LRDSA----DLKTLLSKAENQAKDVQK 711
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLKELEELGFeSVEELEERLKELEPFYneyleLKDAEkeleREEKELKKLEEELDKAFE 633
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1799135557 712 EYEKTQTVLSELK-----LKFEMTEQEKQSITDELKQCKNNLKLLREK 754
Cdd:PRK03918 634 ELAETEKRLEELRkeleeLEKKYSEEEYEELREEYLELSRELAGLRAE 681
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
28-85 |
4.29e-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: 4.29e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135557 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 |
4.91e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTE-----DSLRKELI 241
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvkselKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 242 ALQEDKHNYETTAKESLRRVLQEKI-EVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDK 320
Cdd:TIGR02169 769 ELEEDLHKLEEALNDLEARLSHSRIpEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1799135557 321 LKVAEGKQEEIQ---QKGQAEKKELQHKIDEMEEKEQELQAKIEALQAD 366
Cdd:TIGR02169 849 IKSIEKEIENLNgkkEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
233-743 |
6.42e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 6.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 233 EDSLRKELIALQEDKHNYETTAKESLRRVLQEKIEV-VRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAV 311
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEElEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 312 NEIKDLSDKLKVAEGKQEEIQQ---KGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDDflpk 388
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEelaELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA---- 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 389 inGSTEKEHLLSKSggdcTFIHQFIECQKKLIvegHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMD 468
Cdd:COG1196 378 --EEELEELAEELL----EALRAAAELAAQLE---ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 469 EQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQ 548
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 549 AAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKE-----------------------ITSLQNSFQLRCQQCED 605
Cdd:COG1196 529 LIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAakagratflpldkiraraalaaaLARGAIGAAVDLVASDL 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 606 QQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLK 685
Cdd:COG1196 609 READARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERL 688
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135557 686 EQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 743
Cdd:COG1196 689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
481-659 |
1.17e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 481 LLKALLEEERKAYR----------NQVEESTKQIQVLQAQLQRLHIDTENLrEEKDSEITSTRDELLSARDEILLLHQAA 550
Cdd:COG4717 47 LLERLEKEADELFKpqgrkpelnlKELKELEEELKEAEEKEEEYAELQEEL-EELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 551 AKVA-----SERDTDIASLQEELKKVRAELERWRKAASEY---EKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLR 622
Cdd:COG4717 126 QLLPlyqelEALEAELAELPERLEELEERLEELRELEEELeelEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190
....*....|....*....|....*....|....*..
gi 1799135557 623 KEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQ 659
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
152-630 |
1.37e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 152 KVAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDtswqaliDEDRLLSRLEVMGNQLQACSKNQ 231
Cdd:COG4717 60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA-------ELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 232 TEDSLRKELIALQEdkhnyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKE-MNERTQEELRELANKYNGA 310
Cdd:COG4717 133 ELEALEAELAELPE--------RLEELEERLEELRELEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 311 VNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHkidemEEKEQELQAKIEALQAdndftnerLTALQGIQVDDFLPKIN 390
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEA-----AALEERLKEARLLLLI--------AAALLALLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 391 GSTEKEHLLSKSGGdctFIHQFIECQKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDtLSPSKEKSSDDTTDAQMDEQ 470
Cdd:COG4717 272 ILTIAGVLFLVLGL---LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAA-LGLPPDLSPEELLELLDRIE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 471 DLNEPLAKVSLLKAllEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILllHQAA 550
Cdd:COG4717 348 ELQELLREAEELEE--ELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELE--ELLE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 551 AKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLrcqqceDQQREEATRLQGELEKLRKEWNALET 630
Cdd:COG4717 424 ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL------AELLQELEELKAELRELAEEWAALKL 497
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
228-754 |
2.95e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 228 SKNQTEDSLRKELIALQEDKHNYETTAKEsLRRVLQEKIEVVRKLSEVERSlsntEDECTHLKEMNERTQEELRELANKY 307
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEE-LKKEIEELEEKVKELKELKEK----AEEYIKLSEFYEEYLDELREIEKRL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 308 NGAVNEIKDLSDKLKVAEGKQEEIQqKGQAEKKELQHKIDEMEEKEQELQaKIEALQADNDFTNERLTALQGIQVDDFLP 387
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEKLEKELE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 388 KI-NGSTEKEHLLSKSGGDCTFIHQFIECQKKLIVEghLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQ 466
Cdd:PRK03918 395 ELeKAKEEIEEEISKITARIGELKKEIKELKKAIEE--LKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 467 MDEQDLNEPLAKVsllKALLEEERKAYRNqvEESTKQIQVLQAQLQRlhIDTENLrEEKDSEITSTRDELLSARDEILLL 546
Cdd:PRK03918 473 EKERKLRKELREL---EKVLKKESELIKL--KELAEQLKELEEKLKK--YNLEEL-EKKAEEYEKLKEKLIKLKGEIKSL 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 547 HQAAAKVaserdtdiaslqEELKKVRAELErwrKAASEYEKEITSLQNSFQLRCQQCEDQQREEAtrlqGELEKLRKEWN 626
Cdd:PRK03918 545 KKELEKL------------EELKKKLAELE---KKLDELEEELAELLKELEELGFESVEELEERL----KELEPFYNEYL 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 627 ALETECHSLKREnvllsseLQRQEKELHNSQKQSLELTSDLSILQMSRKELEnqvgslkeqhlrdsaDLKTLLSKAENqa 706
Cdd:PRK03918 606 ELKDAEKELERE-------EKELKKLEEELDKAFEELAETEKRLEELRKELE---------------ELEKKYSEEEY-- 661
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1799135557 707 KDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 754
Cdd:PRK03918 662 EELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
289-526 |
3.02e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.86 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 289 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALqadnd 368
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEEL----- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 369 ftNERLTAL--QGIQVDDFLPKIN----------GSTEKEHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKAVEETKLSK 436
Cdd:PHA02562 240 --TDELLNLvmDIEDPSAALNKLNtaaakikskiEQFQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 437 ENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEEstkqIQVLQAQLQRLHI 516
Cdd:PHA02562 318 LDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEE----LAKLQDELDKIVK 393
|
250
....*....|
gi 1799135557 517 DTENLREEKD 526
Cdd:PHA02562 394 TKSELVKEKY 403
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
27-106 |
3.47e-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: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 27 PIKIGRSVARcRPAQNNATFDC-----KVLSRNHALVWFDHKTGKFYLQdTKSSNGTFINSQRLSRGseeSPPCEILSGD 101
Cdd:cd22701 18 EVVLGRNSKN-SSSTAADSVDIdlgpsKKISRRHARIFYDFTTQCFELS-VLGRNGVKVDGILVKPG---SPPVPLRSGS 92
|
....*
gi 1799135557 102 IIQFG 106
Cdd:cd22701 93 LIQIG 97
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
482-736 |
3.49e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 482 LKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDseITSTRDELLSARDEIlllhqaaakvaSERDTDI 561
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG--LVDLSEEAKLLLQQL-----------SELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 562 ASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRcqqcedQQREEATRLQGELEKLRKEWnaleTECHSLKREnvl 641
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQ------QLRAQLAELEAELAELSARY----TPNHPDVIA--- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 642 LSSELQRQEKELHNSQKQSL-ELTSDLSILQMSRKELENQVGSLKEQHLRdsadlktlLSKAENQAKDVQKEYEKTQTVL 720
Cdd:COG3206 296 LRAQIAALRAQLQQEAQRILaSLEAELEALQAREASLQAQLAQLEARLAE--------LPELEAELRRLEREVEVARELY 367
|
250
....*....|....*.
gi 1799135557 721 SELKLKFEMTEQEKQS 736
Cdd:COG3206 368 ESLLQRLEEARLAEAL 383
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
25-114 |
8.70e-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: 8.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 25 DEPIKIGRSVArcrpAQNNATFDC-KVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDII 103
Cdd:cd22663 20 GKEVTVGRGLG----VTYQLVSTCpLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERI----EPLKPYPLNEGDLI 90
|
90
....*....|.
gi 1799135557 104 QFGVDVTENTR 114
Cdd:cd22663 91 QLGVPPENKEP 101
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
458-687 |
8.83e-07 |
|
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: 52.07 E-value: 8.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 458 SSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREE---KDSEITSTRD 534
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaeLEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 535 ELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQnsfqlrcqqcedQQREEATRL 614
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR------------ADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799135557 615 QGELEKLRKEWNALETEchsLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQ 687
Cdd:COG4942 166 RAELEAERAELEALLAE---LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
470-662 |
9.79e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 9.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 470 QDLNEPLAKVSLLKALLEEERKAYRnqVEESTKQIQVLQAQLQRLhidtENLREEKDSEITSTRDELLSARDEILLLHQA 549
Cdd:COG4913 258 RELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEEL----RAELARLEAELERLEARLDALREELDELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 550 AAKVASERdtdIASLQEELKKVRAELERWRKAASEYEKEITSLQNSfqlrcqqcEDQQREEATRLQGELEKLRKEWNALE 629
Cdd:COG4913 332 IRGNGGDR---LEQLEREIERLERELEERERRRARLEALLAALGLP--------LPASAEEFAALRAEAAALLEALEEEL 400
|
170 180 190
....*....|....*....|....*....|...
gi 1799135557 630 TECHSLKRENVLLSSELQRQEKELHNsQKQSLE 662
Cdd:COG4913 401 EALEEALAEAEAALRDLRRELRELEA-EIASLE 432
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
26-106 |
1.07e-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: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 26 EPIKIGRSVArcrpaqNNATFDCKVLSRNHALVwfDHKTGKFYLQDTKSSNGTFINSQRLSRGseesppcEILSGDIIQF 105
Cdd:cd22698 21 DEFTIGRSSN------NDIRLNDHSVSRHHARI--VRQGDKCNLTDLGSTNGTFLNGIRVGTH-------ELKHGDRIQL 85
|
.
gi 1799135557 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 |
1.27e-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: 1.27e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1799135557 55 HALVWFDHKTGKFYLQDTKSSNGTFINSQRLSrgseESPPCEILSGDIIQFGVD 108
Cdd:cd22704 39 HAVITYDQIDNEFKIKDLGSLNGTFVNDSRIP----EQTYITLKLGDSIRFGYD 88
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
484-659 |
1.39e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 484 ALLEEERKAYRNQVEESTKQIQVLQAQLQRLhiDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVaSERDTDIAS 563
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDAL--QERREALQRLAEYSWDEIDVASAEREIAELEAELERL-DASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 564 LQEELKKVRAELERWRKAASEYEKEITSLQNSFqlrcQQCEDQQREEATRLQGELEKLRKEWNA-LETECHSLKRENVL- 641
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKEL----EQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALGDAVEr 765
|
170 180
....*....|....*....|...
gi 1799135557 642 -----LSSELQRQEKELHNSQKQ 659
Cdd:COG4913 766 elrenLEERIDALRARLNRAEEE 788
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
162-732 |
1.83e-06 |
|
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: 51.36 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 162 SQELFQLSQYLQEALHR----EQMLEQKLATLQRLLAITQEASDTSWQALIDEDRllsRLEVMGNQLQACSKNQTEDSLR 237
Cdd:pfam10174 129 AKELFLLRKTLEEMELRietqKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWER---TRRIAEAEMQLGHLEVLLDQKE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 238 KELIALQEDKH-NYETTAKESLRRVLQEKIEVV-RKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKyngaVNEIK 315
Cdd:pfam10174 206 KENIHLREELHrRNQLQPDPAKTKALQTVIEMKdTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQ----MEVYK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 316 DLSD--KLKVAEGKQEeiQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQgIQVDDFLPKINgst 393
Cdd:pfam10174 282 SHSKfmKNKIDQLKQE--LSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQ-TEVDALRLRLE--- 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 394 EKEHLLSKSGgdcTFIHQFIECQKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSpSKEKSSDDTTDA--QMDEQD 471
Cdd:pfam10174 356 EKESFLNKKT---KQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLR-DKDKQLAGLKERvkSLQTDS 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 472 LNEPLAKVSLLKALLEEERKAYRNQvEESTKQIQVLQAQLQRLHIDTENLREekdsEITSTRDELLSARDEILLLHQAAA 551
Cdd:pfam10174 432 SNTDTALTTLEEALSEKERIIERLK-EQREREDRERLEELESLKKENKDLKE----KVSALQPELTEKESSLIDLKEHAS 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 552 KVAS---ERDTDIASLQEELKKVRAELERW----RKAASEYEKEITSLQNSFQLRCQQCEDQQ-REEATRLQGELEKLRK 623
Cdd:pfam10174 507 SLASsglKKDSKLKSLEIAVEQKKEECSKLenqlKKAHNAEEAVRTNPEINDRIRLLEQEVARyKEESGKAQAEVERLLG 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 624 EWNALETECHSLKRENVLLSSELQRQEKELHNSQKQsleltsdlsiLQMSRKELENQVGSLKEQHLRDSADLKTllSKAE 703
Cdd:pfam10174 587 ILREVENEKNDKDKKIAELESLTLRQMKEQNKKVAN----------IKHGQQEMKKKGAQLLEEARRREDNLAD--NSQQ 654
|
570 580
....*....|....*....|....*....
gi 1799135557 704 NQAKDVQKEYEKTQTVLSELKLKFEMTEQ 732
Cdd:pfam10174 655 LQLEELMGALEKTRQELDATKARLSSTQQ 683
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
564-754 |
1.84e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 564 LQEELKKVRAELERWRKAASEYeKEITSLQNSFQLRCQQCEDQQREEatrlqgELEKLRKEWNALETECHSLKRENVLLS 643
Cdd:COG1196 194 ILGELERQLEPLERQAEKAERY-RELKEELKELEAELLLLKLRELEA------ELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 644 SELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQhlrdSADLKTLLSKAENQAKDVQKEYEKTQTVLSEL 723
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER----RRELEERLEELEEELAELEEELEELEEELEEL 342
|
170 180 190
....*....|....*....|....*....|.
gi 1799135557 724 KLKFEMTEQEKQSITDELKQCKNNLKLLREK 754
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
336-714 |
3.48e-06 |
|
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: 50.46 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 336 QAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDD--------FLPKINGSTEKEHLLSKSGGDCT 407
Cdd:pfam05622 6 QEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGtpggkkylLLQKQLEQLQEENFRLETARDDY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 408 FIHqfIECQKKLIVE-----GHLTKAVEETKLSKENQTRAKESdfSDTLSpsKEKSSDDTTDAQMdeQDLNEPLAKVSLL 482
Cdd:pfam05622 86 RIK--CEELEKEVLElqhrnEELTSLAEEAQALKDEMDILRES--SDKVK--KLEATVETYKKKL--EDLGDLRRQVKLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 483 ----------KALLEEERKAY---RNQVEESTKQIQVLQAQLQRLHIDTENLR------EEKDSEITSTRDELLSARD-- 541
Cdd:pfam05622 158 eernaeymqrTLQLEEELKKAnalRGQLETYKRQVQELHGKLSEESKKADKLEfeykklEEKLEALQKEKERLIIERDtl 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 542 ----EILLLHQAAAKVASERDTDIASLQEELKKVRAELerwrkAASEYEKEITSLQNSFQ-LRCQQcEDQQREEATRLQG 616
Cdd:pfam05622 238 retnEELRCAQLQQAELSQADALLSPSSDPGDNLAAEI-----MPAEIREKLIRLQHENKmLRLGQ-EGSYRERLTELQQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 617 ELEKLRKEWNALETEcHSLKRENVLLSS----ELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQ--HLR 690
Cdd:pfam05622 312 LLEDANRRKNELETQ-NRLANQRILELQqqveELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQieELE 390
|
410 420
....*....|....*....|....
gi 1799135557 691 DSADLKTLLSKAENQAKDVQKEYE 714
Cdd:pfam05622 391 PKQDSNLAQKIDELQEALRKKDED 414
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
27-117 |
5.02e-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: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 27 PIKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLsrgSEESPPCEILSGDIIQFG 106
Cdd:cd22678 24 PLTIGRIQ------RGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESI---SPNGRPVVLSSGDVITLG 94
|
90
....*....|.
gi 1799135557 107 vdvTENTRKVT 117
Cdd:cd22678 95 ---SETKILVR 102
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
229-757 |
6.31e-06 |
|
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: 49.72 E-value: 6.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 229 KNQTEDSLRKELIALQEDKHNYETTAK---------ESLRRVLQEKIEVVRKLSEVERSlsnTEDECTHLKEMNERTQEE 299
Cdd:pfam05483 94 KVSIEAELKQKENKLQENRKIIEAQRKaiqelqfenEKVSLKLEEEIQENKDLIKENNA---TRHLCNLLKETCARSAEK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 300 LRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNdftnERLTALQG 379
Cdd:pfam05483 171 TKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDK----EKQVSLLL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 380 IQvddflpkingSTEKEHLLSksggDCTFIHQfiECQKKLiveghlTKAVEETKLSKENQTRAKESdfSDTLSPSKEKSS 459
Cdd:pfam05483 247 IQ----------ITEKENKMK----DLTFLLE--ESRDKA------NQLEEKTKLQDENLKELIEK--KDHLTKELEDIK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 460 DDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAyrnQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEitstRDELLSA 539
Cdd:pfam05483 303 MSLQRSMSTQKALEEDLQIATKTICQLTEEKEA---QMEELNKAKAAHSFVVTEFEATTCSLEELLRTE----QQRLEKN 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 540 RDEILLLHQAAAKVASERDtDIASLQ-------EELKKVRAELERWRKAASEYEKEITSLQNSFQlrcqqcedqqreeat 612
Cdd:pfam05483 376 EDQLKIITMELQKKSSELE-EMTKFKnnkevelEELKKILAEDEKLLDEKKQFEKIAEELKGKEQ--------------- 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 613 RLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSL-------- 684
Cdd:pfam05483 440 ELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMtlelkkhq 519
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135557 685 ------KEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNN 757
Cdd:pfam05483 520 ediincKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN 598
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
163-366 |
7.54e-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: 48.99 E-value: 7.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQAcSKNQTEDSLRKELIA 242
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA-ELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 243 LQedKHNYETTAKESLR-RVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKL 321
Cdd:COG4942 113 LY--RLGRQPPLALLLSpEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1799135557 322 KVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQAD 366
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
257-542 |
7.70e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 49.54 E-value: 7.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 257 SLRRVLQEKIEVVRKLSEVERslsnteDECTHLKEmNERTqEELRELANKYNGAVNEIKDLSDKLKVAEGKQ-------- 328
Cdd:PRK05771 13 TLKSYKDEVLEALHELGVVHI------EDLKEELS-NERL-RKLRSLLTKLSEALDKLRSYLPKLNPLREEKkkvsvksl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 329 EEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADndftNERLTALQGIQVDDflpkingstekEHLLSKSggdctF 408
Cdd:PRK05771 85 EELIKDVEEELEKIEKEIKELEEEISELENEIKELEQE----IERLEPWGNFDLDL-----------SLLLGFK-----Y 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 409 IHQFIecqkkliveGHLTKAVEETKLSKENQTRAKESDFSDTLSP-----SKEkssddttdaqmDEQDLNEPLAKVSLLK 483
Cdd:PRK05771 145 VSVFV---------GTVPEDKLEELKLESDVENVEYISTDKGYVYvvvvvLKE-----------LSDEVEEELKKLGFER 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135557 484 ALLEEERKAYRnQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDE 542
Cdd:PRK05771 205 LELEEEGTPSE-LIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIELER 262
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
255-588 |
8.51e-06 |
|
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: 49.68 E-value: 8.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 255 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQK 334
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 335 GQAEKKELQHKIDEMEEKEQ---ELQAKIEALQADNDftnerltalqgiqvDDFLPKINGSTEK-EHLLSKSGGDCTFIH 410
Cdd:TIGR02169 753 IENVKSELKELEARIEELEEdlhKLEEALNDLEARLS--------------HSRIPEIQAELSKlEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 411 QfiECQKKLIVEGHLTKAVEEtKLSKENQTRAKESDFSDTLSpskekssddttDAQMDEQDLNEPLAKVSLLKALLEEER 490
Cdd:TIGR02169 819 Q--KLNRLTLEKEYLEKEIQE-LQEQRIDLKEQIKSIEKEIE-----------NLNGKKEELEEELEELEAALRDLESRL 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 491 KAYRNQVEESTKQIQVLQAQLQRLHIDTENLReEKDSEITSTRDELLSARDEILLLhQAAAKVASERDTDIASLQEELKK 570
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKR-KRLSELKAKLEALEEELSEIEDP-KGEDEEIPEEELSLEDVQAELQR 962
|
330 340
....*....|....*....|..
gi 1799135557 571 VRAELERWR----KAASEYEKE 588
Cdd:TIGR02169 963 VEEEIRALEpvnmLAIQEYEEV 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
213-754 |
9.67e-06 |
|
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: 49.30 E-value: 9.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 213 LLSRLEVMGNQLQACSKNQteDSLRKELIALQE--DKHNYETTAKESLRRVLQEKIE---------VVRKLSEVERSLSN 281
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQL--ASLEEELEKLTEeiSELEKRLEEIEQLLEELNKKIKdlgeeeqlrVKEKIGELEAEIAS 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 282 TEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLsdklkvaEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIE 361
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEEL-------EREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 362 ALQADNDFTNERLTALQGIQ--VDDFLPKINGSTEKEHLLSKSGGDctfihqfIECQKKLIVEGHltKAVEETKLSKENQ 439
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKreINELKRELDRLQEELQRLSEELAD-------LNAAIAGIEAKI--NELEEEKEDKALE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 440 TRAKESDFSdTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLH---- 515
Cdd:TIGR02169 450 IKKQEWKLE-QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHgtva 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 516 -------------------------IDTEN--------LREEKDSEIT---------STRDELLSARDEILLL------- 546
Cdd:TIGR02169 529 qlgsvgeryataievaagnrlnnvvVEDDAvakeaielLKRRKAGRATflplnkmrdERRDLSILSEDGVIGFavdlvef 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 547 --HQAAAKVASERDT----DIASLQEELKKVR---------------------------------AELERWRKAASEYEK 587
Cdd:TIGR02169 609 dpKYEPAFKYVFGDTlvveDIEAARRLMGKYRmvtlegelfeksgamtggsraprggilfsrsepAELQRLRERLEGLKR 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 588 EITSLQnSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDL 667
Cdd:TIGR02169 689 ELSSLQ-SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARI 767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 668 SILQMSRKELENQVGSLkEQHLRDS--ADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCK 745
Cdd:TIGR02169 768 EELEEDLHKLEEALNDL-EARLSHSriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
....*....
gi 1799135557 746 NNLKLLREK 754
Cdd:TIGR02169 847 EQIKSIEKE 855
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
51-106 |
1.02e-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: 1.02e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799135557 51 LSRNHALVWF----DHKTGKFYLQDTKSSNGTFINSQRLsrgseesPP---CEILSGDIIQFG 106
Cdd:cd22677 41 ISRYHAVLQYrgdaDDHDGGFYLYDLGSTHGTFLNKQRI-------PPkqyYRLRVGHVLKFG 96
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
52-106 |
1.20e-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: 1.20e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135557 52 SRNH-ALVWfdHK-TGKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22674 48 SRVHaALVY--HKhLNRVFLIDLGSTHGTFVGGIRL----EPHKPQQLPIDSTLRFG 98
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
509-724 |
1.38e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 509 AQLQRLHIDTENLREEKD--SEITSTRDELLSARDEILLLHQAAAKVASERD-TDIASLQEELKKVRAELERWRKAASEY 585
Cdd:COG4913 235 DDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAqRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 586 EKEITSLQNsfqlRCQQCEDQQREEATRlqgELEKLRKEWNALETECHSLKREnvllSSELQRQEKELHnsqkqsLELTS 665
Cdd:COG4913 315 EARLDALRE----ELDELEAQIRGNGGD---RLEQLEREIERLERELEERERR----RARLEALLAALG------LPLPA 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135557 666 DLSILQMSRKELENQVGSLKEQHlrdsADLKTLLSKAENQAKDVQKEYEKTQTVLSELK 724
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEEL----EALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
289-754 |
1.52e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 289 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKgQAEKKELQHKIDEMEEKEQELQAKIEALQadnd 368
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLE---- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 369 ftnerltalqgiQVDDFLPKINGSTEKEHLLSksggdctfihQFIECQKKLIVEGHLTKAVEETKLSKENQTRAKESDFs 448
Cdd:COG4717 123 ------------KLLQLLPLYQELEALEAELA----------ELPERLEELEERLEELRELEEELEELEAELAELQEEL- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 449 dtlspsKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHiDTENLREEKDS- 527
Cdd:COG4717 180 ------EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA-LEERLKEARLLl 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 528 -------EITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRc 600
Cdd:COG4717 253 liaaallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLP- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 601 qqcEDQQREEATRLQGELEKLRKEWNALETECHSLKRE------NVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSR 674
Cdd:COG4717 332 ---PDLSPEELLELLDRIEELQELLREAEELEEELQLEeleqeiAALLAEAGVEDEEELRAALEQAEEYQELKEELEELE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 675 KELENQVGSLKEQHLR-DSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEK--QSITDELKQCKNNLKLL 751
Cdd:COG4717 409 EQLEELLGELEELLEAlDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELREL 488
|
...
gi 1799135557 752 REK 754
Cdd:COG4717 489 AEE 491
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
223-688 |
1.61e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.50 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 223 QLQACSKNQTEDSLRKELIALQEDKHNYE--------TTAKESLRRVLQEKIEVVRK-----------LSEVERSLSNTE 283
Cdd:TIGR00606 597 NKELASLEQNKNHINNELESKEEQLSSYEdklfdvcgSQDEESDLERLKEEIEKSSKqramlagatavYSQFITQLTDEN 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 284 DECTHLKEMNERTQEELRE----LANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAK 359
Cdd:TIGR00606 677 QSCCPVCQRVFQTEAELQEfisdLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKV 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 360 IEALQADNDFTNERLTALQGIQvddflpkingstEKEHLLSKSGGDCTFIHQFIEcqkkliveghLTKAVEETKLSKENQ 439
Cdd:TIGR00606 757 NRDIQRLKNDIEEQETLLGTIM------------PEEESAKVCLTDVTIMERFQM----------ELKDVERKIAQQAAK 814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 440 TRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAK-----VSLLKALLEEeRKAYRNQVEESTKQIQVLQAQLqrl 514
Cdd:TIGR00606 815 LQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQdqqeqIQHLKSKTNE-LKSEKLQIGTNLQRRQQFEEQL--- 890
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 515 hidtenlrEEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQN 594
Cdd:TIGR00606 891 --------VELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIEN 962
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 595 SFQLRCQQCEDQQREEATRLQGEL-------EKLRKEWNALETECHSLKRENVLLSSELQRQE-----KELHNSQKQSLE 662
Cdd:TIGR00606 963 KIQDGKDDYLKQKETELNTVNAQLeecekhqEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKrenelKEVEEELKQHLK 1042
|
490 500
....*....|....*....|....*...
gi 1799135557 663 LTSDLSILQMSR--KELENQVGSLKEQH 688
Cdd:TIGR00606 1043 EMGQMQVLQMKQehQKLEENIDLIKRNH 1070
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
289-527 |
1.64e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 289 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQkgqaEKKELQHKIDEMEEKEQELQAKIEALQADnd 368
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ----ELAALEAELAELEKEIAELRAELEAQKEE-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 369 fTNERLTALQgiqvddflpKINGSTEKEHLLSKSGgdctfihqFIECQKKLIVEGHLTKAVEEtKLSKENQTRAKESDFS 448
Cdd:COG4942 106 -LAELLRALY---------RLGRQPPLALLLSPED--------FLDAVRRLQYLKYLAPARRE-QAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135557 449 DTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDS 527
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
28-106 |
2.00e-05 |
|
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438732 [Multi-domain] Cd Length: 96 Bit Score: 43.87 E-value: 2.00e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135557 28 IKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDhkTGKFYLQDTKSSNGTFINSQRlsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22680 23 VSIGRDP------ENVIVIPDPFVSRNHARITVD--SNEIYIEDLGSTNGTFVNDFK-----RIKGPAKLHPNDIIKLG 88
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
182-624 |
2.17e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 182 LEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgnqlqacSKNQTEDSLRKELIALQEDKHNYETTaKESLRRV 261
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHE---------ERREELETLEAEIEDLRETIAETERE-REELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 262 LQEKIEVVRKLSEVERSL-----------SNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEE 330
Cdd:PRK02224 281 VRDLRERLEELEEERDDLlaeaglddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 331 IQQKGQAEKKELQH---KIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQvDDFLPKINGSTEKEHLLSKSggdct 407
Cdd:PRK02224 361 LREEAAELESELEEareAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL-EELREERDELREREAELEAT----- 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 408 fihqfIECQKKLIVEGHltKAVEETKLSKENQTrAKESDFSDTLSPSKEKSSD---DTTDAQMDEQDLNEPLAKVSLLKA 484
Cdd:PRK02224 435 -----LRTARERVEEAE--ALLEAGKCPECGQP-VEGSPHVETIEEDRERVEEleaELEDLEEEVEEVEERLERAEDLVE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 485 L------LEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLR---EEKDSEITSTRDELLSARDEILLLHQAAAKVAS 555
Cdd:PRK02224 507 AedrierLEERREDLEELIAERRETIEEKRERAEELRERAAELEaeaEEKREAAAEAEEEAEEAREEVAELNSKLAELKE 586
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799135557 556 ERDT--DIASLQEELKKVRAELERWRkaasEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGE-LEKLRKE 624
Cdd:PRK02224 587 RIESleRIRTLLAAIADAEDEIERLR----EKREALAELNDERRERLAEKRERKRELEAEFDEArIEEARED 654
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
501-713 |
2.66e-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: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 501 TKQIQVLQAQLQRLhidtenlrEEKDSEITSTRDELLSARDEILLLHQAAAKVA--SERDTDIASLQEELKKVRAELERW 578
Cdd:COG4913 609 RAKLAALEAELAEL--------EEELAEAEERLEALEAELDALQERREALQRLAeySWDEIDVASAEREIAELEAELERL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 579 RKAASEYEkeitslqnsfqlrcqqcedqqreeatRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQK 658
Cdd:COG4913 681 DASSDDLA--------------------------ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799135557 659 QSLELTSDLSILQmsRKELENQVGSLKEQHLRDS---------ADLKTLLSKAENQAKDVQKEY 713
Cdd:COG4913 735 RLEAAEDLARLEL--RALLEERFAAALGDAVERElrenleeriDALRARLNRAEEELERAMRAF 796
|
|
| FHA_RAD53-like_rpt2 |
cd22690 |
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
12-103 |
2.93e-05 |
|
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine/threonine-protein kinase RAD53 and similar proteins; RAD53, also called CHEK2 homolog, or serine-protein kinase 1 (Spk1), is a nuclear protein kinase that phosphorylates proteins on serine, threonine, and tyrosine. It controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints and prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. It may be involved in the phosphorylation of RPH1. RAD53 contains two FHA domains. This model corresponds to the second one. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438742 [Multi-domain] Cd Length: 105 Bit Score: 43.82 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 12 PNSHPfqerHVYL-DEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFD-HKTGK--FYLQDTkSSNGTFINSQRLSR 87
Cdd:cd22690 8 NPSYP----DIELtQNTTFIGRS------KDCDEEITDPRISKHHCIITRKrSGKGLddVYVTDT-STNGTFINNNRLGK 76
|
90
....*....|....*.
gi 1799135557 88 GSEesppCEILSGDII 103
Cdd:cd22690 77 GSQ----SLLQDGDEI 88
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
237-628 |
3.36e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.59 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 237 RKELIALQEDKHNYETTAK--ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERtQEELRELANKYNGAVNEI 314
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQilSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQ-ILELEGYEMDYNSYLKSI 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 315 --------------KDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGI 380
Cdd:PRK01156 373 eslkkkieeyskniERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 381 QVDDFLPKINGSTEKEHLLSKSGGDCTFIHQFI---ECQKKLIVEG--HLTKAVE----------ETKLSKENQTRAKES 445
Cdd:PRK01156 453 SVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIreiEIEVKDIDEKivDLKKRKEyleseeinksINEYNKIESARADLE 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 446 DFSDTLSPSKEK-----------SSDDTTDAQMDEQDLNEPLAKVSLLkalleeERKAYRNQVEESTKQIQVLQAQLQRL 514
Cdd:PRK01156 533 DIKIKINELKDKhdkyeeiknryKSLKLEDLDSKRTSWLNALAVISLI------DIETNRSRSNEIKKQLNDLESRLQEI 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 515 HIDTENLREEKDSEITSTRDELLSARDEILLLHQaaakvaserdtdiasLQEELKKVRAELERWRKAASEyEKEITSLQN 594
Cdd:PRK01156 607 EIGFPDDKSYIDKSIREIENEANNLNNKYNEIQE---------------NKILIEKLRGKIDNYKKQIAE-IDSIIPDLK 670
|
410 420 430
....*....|....*....|....*....|....
gi 1799135557 595 SFQLRCQQCEDQQREEATRLQGELEKlRKEWNAL 628
Cdd:PRK01156 671 EITSRINDIEDNLKKSRKALDDAKAN-RARLEST 703
|
|
| FHA_CHFR |
cd22672 |
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ... |
49-105 |
3.73e-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: 3.73e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135557 49 KVLSRNHALVWFDHKtGKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQF 105
Cdd:cd22672 39 KLVSGDHCKIIRDEK-GQVWLEDT-STNGTLVNKVKVVKGQK----VELKHGDVIYL 89
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
14-106 |
3.95e-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: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 14 SHPFQERHvyldepIKIGRSVarcrpaQNNATFDCKVLSRNHALvwFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEesp 93
Cdd:cd22682 14 QFPITEST------IVIGRSV------ESQVQIDDDSVSRYHAK--LAVNPSAVSIIDLGSTNGTIVNGKKIPKLAS--- 76
|
90
....*....|...
gi 1799135557 94 pCEILSGDIIQFG 106
Cdd:cd22682 77 -CDLQNGDQIKIG 88
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
25-108 |
4.10e-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: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 25 DEPIKIGRsvarcRPAQNNAT----FDCKVLSRNHALVWFdhKTGKFYLQDTKSSNGTFINSQRLSR-GSEESPPCEILS 99
Cdd:cd22702 31 KQPCIIGS-----DPHQAISGisvvIPSPQVSELHARITC--KNGAFFLTDLGSEHGTWINDNEGRRyRAPPNFPVRLHP 103
|
....*....
gi 1799135557 100 GDIIQFGVD 108
Cdd:cd22702 104 SDVIEFGSD 112
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
18-86 |
4.94e-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: 4.94e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135557 18 QERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhkTGKFYLQDTKSSNGTFINSQRLS 86
Cdd:cd22694 8 GELRFDPGSSVRIGRD------PDADVRLDDPRVSRRHALLEFD--GDGWVYTDLGSRNGTYLNGRRVQ 68
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
481-631 |
6.57e-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: 46.59 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 481 LLKALLEEERK--AYRNQVEESTKQIQVLQAQLQRLHIDTENLREE--KDSEITSTRDELLSARDEILLLHQAAAKvASE 556
Cdd:pfam13166 305 QLPAVSDLASLlsAFELDVEDIESEAEVLNSQLDGLRRALEAKRKDpfKSIELDSVDAKIESINDLVASINELIAK-HNE 383
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799135557 557 RDTDIASLQEELKKvraelERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREeATRLQGELEKLRKEWNALETE 631
Cdd:pfam13166 384 ITDNFEEEKNKAKK-----KLRLHLVEEFKSEIDEYKDKYAGLEKAINSLEKE-IKNLEAEIKKLREEIKELEAQ 452
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
13-110 |
6.59e-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: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 13 NSHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTgkFYLQDTKSSNGTFINSQRLSrgsee 91
Cdd:cd22665 7 SQAHGPEKDFPLYEgENVIGRD------PSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRL----- 73
|
90 100
....*....|....*....|.
gi 1799135557 92 SPPC--EILSGDIIQFGvDVT 110
Cdd:cd22665 74 KPNVryELIDGDLLLFG-DVK 93
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
470-631 |
8.52e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 8.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 470 QDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRlhidtENLREEKDsEITSTRDELLSARDEILLLHQA 549
Cdd:COG4913 627 AEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREI-----AELEAELE-RLDASSDDLAALEEQLEELEAE 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 550 AAKVASERD---TDIASLQEELKKVRAELERWRKAASEYEKEITSLQNS-FQLRCQQ--CEDQQREEATRLQGELEKLRK 623
Cdd:COG4913 701 LEELEEELDelkGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAalGDAVERELRENLEERIDALRA 780
|
....*...
gi 1799135557 624 EWNALETE 631
Cdd:COG4913 781 RLNRAEEE 788
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
266-748 |
1.94e-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: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 266 IEVVRKLSEVERSLSNTEDECTHLkemnertqEELRELANKYNGAVNEIKDLSDKLKVAEgkqeeiQQKGQAEKKELQHK 345
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELL--------EPIRELAERYAAARERLAELEYLRAALR------LWFAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 346 IDEMEEKEQELQAKIEALQADNDFTNERLTALQGiQVDDflpkiNGSTEKEHLlsksggdctfihqfiecqKKLIveghl 425
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEA-QIRG-----NGGDRLEQL------------------EREI----- 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 426 tkaveETKLSKENQTRAKESDFSDTLSPSKEKSSDDttdaqmdEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQ 505
Cdd:COG4913 348 -----ERLERELEERERRRARLEALLAALGLPLPAS-------AEEFAALRAEAAALLEALEEELEALEEALAEAEAALR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 506 VLQAQLQRLHIDTENLREeKDSEITStrdELLSARDEIlllhqAAAKVASERDTDIASlqeELKKVRAELERWRKAA--- 582
Cdd:COG4913 416 DLRRELRELEAEIASLER-RKSNIPA---RLLALRDAL-----AEALGLDEAELPFVG---ELIEVRPEEERWRGAIerv 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 583 -----------SEYEKEIT----SLQNSFQLRCQQCEDQQREEATR---------------------LQGEL-------- 618
Cdd:COG4913 484 lggfaltllvpPEHYAAALrwvnRLHLRGRLVYERVRTGLPDPERPrldpdslagkldfkphpfrawLEAELgrrfdyvc 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 619 ----EKLRKEWNALETEC--------------HSLKRENVL----------LSSELQRQEKELHNSQKQSLELTSDLSIL 670
Cdd:COG4913 564 vdspEELRRHPRAITRAGqvkgngtrhekddrRRIRSRYVLgfdnraklaaLEAELAELEEELAEAEERLEALEAELDAL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 671 QMSR----------------KELENQVGSLKEQH---LRDSADLKTLlskaENQAKDVQKEYEKTQTVLSELKLKFEMTE 731
Cdd:COG4913 644 QERRealqrlaeyswdeidvASAEREIAELEAELerlDASSDDLAAL----EEQLEELEAELEELEEELDELKGEIGRLE 719
|
570
....*....|....*..
gi 1799135557 732 QEKQSITDELKQCKNNL 748
Cdd:COG4913 720 KELEQAEEELDELQDRL 736
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
52-107 |
2.30e-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: 2.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799135557 52 SRNHALVWFDHKTG---------KFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQFGV 107
Cdd:cd22667 40 SRKHATLTVLHPEAnlsdpdtrpELTLKDL-SKYGTFVNGEKLKGGSE----VTLKDGDVITFGV 99
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
1-106 |
2.34e-04 |
|
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442679 [Multi-domain] Cd Length: 402 Bit Score: 44.37 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 1 MPSALAIFTCRPNSHPFQERHVYLDEPIKIGRSvARC-----RPAQnnatfdckVLSRNHALVWFDHktGKFYLQDTkSS 75
Cdd:COG3456 1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRS-ADCdwvlpDPDR--------SVSRRHAEIRFRD--GAFCLTDL-ST 68
|
90 100 110
....*....|....*....|....*....|...
gi 1799135557 76 NGTFIN--SQRLSRGSEEsppcEILSGDIIQFG 106
Cdd:COG3456 69 NGTFLNgsDHPLGPGRPV----RLRDGDRLRIG 97
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
555-754 |
2.62e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 555 SERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQ--LRCQQCEDQQRE-EATRLQGELEKLRKEWNALETE 631
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREkaERYQALLKEKREyEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 632 CHSLKRENVLLSSELQRQEKELHNS----------------------QKQSLELTSDLSILQMSRKELENQVGSLKEQHL 689
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIeqlleelnkkikdlgeeeqlrvKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135557 690 RDSADLKTLLSKAENQAKDV---QKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 754
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIeeeRKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
216-748 |
2.71e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 216 RLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTaKESLRRVLQEKIEVVRKLSEVERSLSNTEDECthlkemnER 295
Cdd:PRK01156 151 RKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYL-EEKLKSSNLELENIKKQIADDEKSHSITLKEI-------ER 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 296 TQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIqQKGQAEKKELQHKIDEMEEKEQELQAKI-EALQADNDFTNERL 374
Cdd:PRK01156 223 LSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI-KTAESDLSMELEKNNYYKELEERHMKIInDPVYKNRNYINDYF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 375 TALQGI-QVDDFLPKINGSTEKEHLLSKSGGDC-TFIHQFIECQKK--------LIVEGH------LTKAVEETKLSKEN 438
Cdd:PRK01156 302 KYKNDIeNKKQILSNIDAEINKYHAIIKKLSVLqKDYNDYIKKKSRyddlnnqiLELEGYemdynsYLKSIESLKKKIEE 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 439 QtRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQlQRLHIDT 518
Cdd:PRK01156 382 Y-SKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQ-SVCPVCG 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 519 ENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEEL--KKVRAELERWRKAASEyEKEITSLQNSF 596
Cdd:PRK01156 460 TTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLesEEINKSINEYNKIESA-RADLEDIKIKI 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 597 QlRCQQCEDQQREEATRLQ----GELEKLRKEWNALETECHSLKRENvlLSSELQRQEKELHNSQKQSLELTSDL----S 668
Cdd:PRK01156 539 N-ELKDKHDKYEEIKNRYKslklEDLDSKRTSWLNALAVISLIDIET--NRSRSNEIKKQLNDLESRLQEIEIGFpddkS 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 669 ILQMSRKELENQVGSLKEQHlRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKlkfEMTEQEKQsITDELKQCKNNL 748
Cdd:PRK01156 616 YIDKSIREIENEANNLNNKY-NEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLK---EITSRIND-IEDNLKKSRKAL 690
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
610-756 |
2.81e-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: 43.54 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 610 EATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNsQKQSLELTSDLSilqmsrkELENQVGSLKeqhl 689
Cdd:pfam15294 134 EIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGA-KKDVKSNLKEIS-------DLEEKMAALK---- 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135557 690 rdsADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGN 756
Cdd:pfam15294 202 ---SDLEKTLNASTALQKSLEEDLASTKHELLKVQEQLEMAEKELEKKFQQTAAYRNMKEMLTKKNE 265
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
251-754 |
3.05e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 251 ETTAKESLRRVLQ-EKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELR-ELANKYNGA--VNEIKDLSDKLKVAE- 325
Cdd:PTZ00121 1114 ARKAEEAKKKAEDaRKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKaEEARKAEDAkkAEAARKAEEVRKAEEl 1193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 326 GKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKI------------EALQADNDFTNERLTALQGIQVDDFLPKINGST 393
Cdd:PTZ00121 1194 RKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAvkkaeeakkdaeEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK 1273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 394 EKEHLLSKSGGDCTFIHQFIECQK----------------KLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEK 457
Cdd:PTZ00121 1274 AEEARKADELKKAEEKKKADEAKKaeekkkadeakkkaeeAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE 1353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 458 SSDDTTD-----AQMDEQDLNEPLAKVSLLKALLEEERKA--YRNQVEESTKQIQVL------QAQLQRLHIDTENLRE- 523
Cdd:PTZ00121 1354 AAADEAEaaeekAEAAEKKKEEAKKKADAAKKKAEEKKKAdeAKKKAEEDKKKADELkkaaaaKKKADEAKKKAEEKKKa 1433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 524 ---EKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAEL----ERWRKAASEYEKEITSLQNSF 596
Cdd:PTZ00121 1434 deaKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAkkkaEEAKKKADEAKKAAEAKKKAD 1513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 597 QLR----CQQCEDQQREEATRLQGELEKLRKEWNALEtechsLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQM 672
Cdd:PTZ00121 1514 EAKkaeeAKKADEAKKAEEAKKADEAKKAEEKKKADE-----LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK 1588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 673 SRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKlkfemTEQEKQSITDELKQCKNNLKLLR 752
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK-----KEAEEKKKAEELKKAEEENKIKA 1663
|
..
gi 1799135557 753 EK 754
Cdd:PTZ00121 1664 AE 1665
|
|
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
53-106 |
3.53e-04 |
|
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 (FHAD1) and similar proteins; FHAD1, also called FHA domain-containing protein 1, is an uncharacterized FHA domain-containing protein. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438752 [Multi-domain] Cd Length: 96 Bit Score: 40.32 E-value: 3.53e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1799135557 53 RNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPceilsGDIIQFG 106
Cdd:cd22700 36 EQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAP-----GDVLRFG 84
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
567-753 |
4.66e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 567 ELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCeDQQREEATRLQGELEKLRK---EWNALETECHSLKRENVLLS 643
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREI-NEISSELPELREELEKLEKevkELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 644 SELQRQEKELHNSQKQSLELTSDLSILQMSRKELEN---------QVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYE 714
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190
....*....|....*....|....*....|....*....
gi 1799135557 715 KtqtvLSELKLKFEMTEQEKQSITDELKQCKNNLKLLRE 753
Cdd:PRK03918 332 E----LEEKEERLEELKKKLKELEKRLEELEERHELYEE 366
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
465-754 |
4.77e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 465 AQMDE------QDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHidTENLREEKD--SEITSTRDEL 536
Cdd:PHA02562 166 SEMDKlnkdkiRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKY--DELVEEAKTikAEIEELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 537 LSARDEIlllhqaaakvaSERDTDIASLQEELKKVRAELERWRKAASEYEKEITslqnsfqlrCQQCEDQQREEATRLQG 616
Cdd:PHA02562 244 LNLVMDI-----------EDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGV---------CPTCTQQISEGPDRITK 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 617 ELEKLrkewnaletechslkrenvllsSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQhlrdsadlk 696
Cdd:PHA02562 304 IKDKL----------------------KELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQS--------- 352
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135557 697 tlLSKAENQAKDVQKEYEKTQTvlselklkfemteqEKQSITDELKQCKNNLKLLREK 754
Cdd:PHA02562 353 --LITLVDKAKKVKAAIEELQA--------------EFVDNAEELAKLQDELDKIVKT 394
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
166-754 |
5.30e-04 |
|
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: 43.56 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 166 FQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDslRKELIalqe 245
Cdd:pfam05483 215 FKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDEN--LKELI---- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 246 DKHNYETTAKESLRRVLQEKIEVVRKLsevERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIK----DLSDKL 321
Cdd:pfam05483 289 EKKDHLTKELEDIKMSLQRSMSTQKAL---EEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEattcSLEELL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 322 KVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTAL-QGIQVDDFLPKINGsTEKEHLLS 400
Cdd:pfam05483 366 RTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLdEKKQFEKIAEELKG-KEQELIFL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 401 KSGGDCTFIHQFIECQKKLIVEGHLTKAVEE--TKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMdeqdlneplak 478
Cdd:pfam05483 445 LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDlkTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTL----------- 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 479 vsllkalleeERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEkdseITSTRDELLSARDEILLLHQAAAKVASERD 558
Cdd:pfam05483 514 ----------ELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDE----LESVREEFIQKGDEVKCKLDKSEENARSIE 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 559 TDIASLQEELKKVRAELERWRKAASEYEKEITSLqnsfqlrcqqcedQQREEATRLQGELEKlrKEWNALETECHSLKRE 638
Cdd:pfam05483 580 YEVLKKEKQMKILENKCNNLKKQIENKNKNIEEL-------------HQENKALKKKGSAEN--KQLNAYEIKVNKLELE 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 639 nvlLSSELQRQEKELHNSQKQ----SLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYE 714
Cdd:pfam05483 645 ---LASAKQKFEEIIDNYQKEiedkKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIE 721
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1799135557 715 KTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 754
Cdd:pfam05483 722 ERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQ 761
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
457-723 |
5.43e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 457 KSSDDTTDAQMDEQDLNEPLAKVSLLKALlEEERKAYRNQVEESTKQIQVLQAQLQRLhidtenlreeKDSEITSTRDEL 536
Cdd:PRK11281 50 KQKLLEAEDKLVQQDLEQTLALLDKIDRQ-KEETEQLKQQLAQAPAKLRQAQAELEAL----------KDDNDEETRETL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 537 lsardeilllhqaaakvaseRDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQN----------SFQLRCQQCEDQ 606
Cdd:PRK11281 119 --------------------STLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTqperaqaalyANSQRLQQIRNL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 607 ----QREEATRLQGELEKLRKEWNALEtechslkrenvlLSSELQRQEKElHNSQKQSL-ELTSDLSILQMSRKELENQv 681
Cdd:PRK11281 179 lkggKVGGKALRPSQRVLLQAEQALLN------------AQNDLQRKSLE-GNTQLQDLlQKQRDYLTARIQRLEHQLQ- 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1799135557 682 gslkeqhlrdsaDLKTL-----LSKAENQAKDVQKEYEKTQTVLSEL 723
Cdd:PRK11281 245 ------------LLQEAinskrLTLSEKTVQEAQSQDEAARIQANPL 279
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
258-378 |
5.57e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 258 LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQ----- 332
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkey 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1799135557 333 QKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQ 378
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE 137
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
16-111 |
6.70e-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: 6.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 16 PFQERHVYLD-EPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFdhKTGKFYLQDTKSSNGTFINSQRLSRgseespP 94
Cdd:cd22693 7 TLQGQTFPIDkSGITIGRA------DDNDLVLSDDFVSSRHARIYL--QGSSWYLEDLGSTNGTFVNGNRVTQ------P 72
|
90
....*....|....*..
gi 1799135557 95 CEILSGDIIQFGVDVTE 111
Cdd:cd22693 73 VVVQPGDTIRIGATVFE 89
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
49-112 |
7.04e-04 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 (PML1) and similar proteins; PML1 is an FHA domain-containing protein required for efficient splicing and pre-mRNA nuclear retention. It is a component of the pre-mRNA retention and splicing (RES) complex composed of at least BUD13, IST3, and PML1. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438733 [Multi-domain] Cd Length: 129 Bit Score: 40.50 E-value: 7.04e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135557 49 KVLSRNHALVWFDHKTG--KFYLQDTKSSNGTFINsqrlsrgSEESPPC---EILSGDIIQFGVDVTEN 112
Cdd:cd22681 64 ETCSKQHCVIQFRNVKGilKPYIMDLDSSNGTCLN-------DNVIPSSryvELRSGDVITFSKSNDYE 125
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
487-718 |
7.37e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 487 EEERKAYRNQVEESTKQIQVLQAQLQRLhidtenlreekDSEITSTRDELLSARDEILLLHQAAAKVASErdtdIASLQE 566
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDAL-----------QAELEELNEEYNELQAELEALQAEIDKLQAE----IAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 567 ELKKVRAELERWRKAASEYEKEITSLQ-----NSFQ------LRCQQCEDQQREE---ATRLQGELEKLRKEWNALETEC 632
Cdd:COG3883 80 EIEERREELGERARALYRSGGSVSYLDvllgsESFSdfldrlSALSKIADADADLleeLKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 633 HSLKRENVLLSSELQRQEKELhnsQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKE 712
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQ---EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
....*.
gi 1799135557 713 YEKTQT 718
Cdd:COG3883 237 AAAAAA 242
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
172-361 |
9.43e-04 |
|
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: 41.04 E-value: 9.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 172 LQEALHREQMLEQKLATLQRLLaitqeasdtswQALIDEDRLLSRLEVmgNQLQACSKNQTEDSLRKELIAlqedKHNYE 251
Cdd:pfam15619 6 LSARLHKIKELQNELAELQSKL-----------EELRKENRLLKRLQK--RQEKALGKYEGTESELPQLIA----RHNEE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 252 T-TAKESLRRvLQEKIEVV-RKLSEVERSLSNTEDECTHL------KEMNERT--QEELRELANKYNGAVNEIKDLSDKL 321
Cdd:pfam15619 69 VrVLRERLRR-LQEKERDLeRKLKEKEAELLRLRDQLKRLeklsedKNLAEREelQKKLEQLEAKLEDKDEKIQDLERKL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1799135557 322 KVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIE 361
Cdd:pfam15619 148 ELENKSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLK 187
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
476-712 |
1.04e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 476 LAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVAS 555
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 556 ErdtdIASLQEELKKVRAELER-----WRKAASEYEKEITSLQNSFQL-----RCQQCEDQQREEATRLQGELEKLRKew 625
Cdd:COG4942 91 E----IAELRAELEAQKEELAEllralYRLGRQPPLALLLSPEDFLDAvrrlqYLKYLAPARREQAEELRADLAELAA-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 626 naletechslkrenvlLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQH-------LRDSADLKTL 698
Cdd:COG4942 165 ----------------LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELaaelaelQQEAEELEAL 228
|
250
....*....|....
gi 1799135557 699 LSKAENQAKDVQKE 712
Cdd:COG4942 229 IARLEAEAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
556-757 |
1.07e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 556 ERDT--DIASLQEELKkvraELERWRKAASEYEKEITSLQnsfQLRcqqcedQQREEATRLQGELEKLRKEWNALETECH 633
Cdd:COG4913 220 EPDTfeAADALVEHFD----DLERAHEALEDAREQIELLE---PIR------ELAERYAAARERLAELEYLRAALRLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 634 SLKREnvLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQvgsLKEQHLRDSADLKTLLSKAENQAKDVQKEY 713
Cdd:COG4913 287 QRRLE--LLEAELEELRAELARLEAELERLEARLDALREELDELEAQ---IRGNGGDRLEQLEREIERLERELEERERRR 361
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1799135557 714 EKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNN 757
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
486-645 |
1.21e-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: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 486 LEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDseitstrdELlsaRDEILllhqaaakvasERDTDIASLQ 565
Cdd:COG2433 390 LPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE--------EL---EAELE-----------EKDERIERLE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 566 EELKKVRAElerwRKAASEYEKEITSLQNsfqlrcqqcedqqreEATRLQGELEKLRKEWNALETECHSLKRENVLLSSE 645
Cdd:COG2433 448 RELSEARSE----ERREIRKDREISRLDR---------------EIERLERELEEERERIEELKRKLERLKELWKLEHSG 508
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
294-513 |
1.27e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 294 ERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALqadndftNER 373
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL-------GER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 374 LTALQ-GIQVDDFLPKINGSTEKEHLLSKSggdcTFIHQFIECQKKLIveghltKAVEETKLSKENQTRAKESdfsdtls 452
Cdd:COG3883 92 ARALYrSGGSVSYLDVLLGSESFSDFLDRL----SALSKIADADADLL------EELKADKAELEAKKAELEA------- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799135557 453 pSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQR 513
Cdd:COG3883 155 -KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
328-686 |
1.54e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 42.05 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 328 QEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDDFLPKINGSTEKEHLLSKSGGDCT 407
Cdd:pfam09731 43 GEEVVLYALGEDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 408 F--IHQFIECQKKLIVE--GHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLK 483
Cdd:pfam09731 123 EqeKEKALEEVLKEAISkaESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 484 ALLEEERKAYRN---------------QVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDEL----------LS 538
Cdd:pfam09731 203 KQSEEEAAPPLLdaapetppklpehldNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIipvlkednllSN 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 539 ARDEILLLH------QAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQnsfqlrcqqcEDQQREEat 612
Cdd:pfam09731 283 DDLNSLIAHahreidQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAAD----------EAQLRLE-- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 613 rLQGELEKLRKEW-NALETEchsLKRENVL----LSSELQRQEKELHNSQKQSLE---------LTSDLSILQMSRKELE 678
Cdd:pfam09731 351 -FEREREEIRESYeEKLRTE---LERQAEAheehLKDVLVEQEIELQREFLQDIKekveeeragRLLKLNELLANLKGLE 426
|
....*...
gi 1799135557 679 NQVGSLKE 686
Cdd:pfam09731 427 KATSSHSE 434
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
607-754 |
1.71e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 607 QREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKE 686
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 687 QHLRDSADLKTLLSKAE-------------------------------NQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQ 735
Cdd:COG4942 98 ELEAQKEELAELLRALYrlgrqpplalllspedfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAELE 177
|
170
....*....|....*....
gi 1799135557 736 SITDELKQCKNNLKLLREK 754
Cdd:COG4942 178 ALLAELEEERAALEALKAE 196
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
27-106 |
1.80e-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: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 27 PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTGkfYLQDTKSSNGTFINSQRLsrgseeSPPCEILSGDIIQFG 106
Cdd:cd22668 19 SNIIGRG------SDADFRLPDTGVSRRHAEIRWDGQVA--HLTDLGSTNGTTVNNAPV------TPEWRLADGDVITLG 84
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
486-756 |
1.93e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 486 LEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDsEITSTRDELLSARDEILLLHQAAAKVaserDTDIASLQ 565
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRKL----EEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 566 EELKKVRAELERWRkaasEYEKEITSLQnsfqlrcqqcedQQREEATRLQGELEKLRKEWNALETECHSLKREnvllSSE 645
Cdd:PRK03918 266 ERIEELKKEIEELE----EKVKELKELK------------EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE----ING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 646 LQRQEKELHNSQKQSLELTSDLsilqmsrKELENQVGSLKEQHlRDSADLKTLLSKAENQAKdvqkeyEKTQTVLSELKL 725
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKL-------KELEKRLEELEERH-ELYEEAKAKKEELERLKK------RLTGLTPEKLEK 391
|
250 260 270
....*....|....*....|....*....|.
gi 1799135557 726 KFEMTEQEKQSITDELKQCKNNLKLLREKGN 756
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKKEIK 422
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
527-765 |
2.27e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 527 SEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEdQ 606
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE-E 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 607 QREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKE 686
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135557 687 QHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNNPSILQPVP 765
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
256-365 |
2.74e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 256 ESLRRVLQEKI-EVVRKLSEVERSLSNTEDEcthLKEMNERTQEELRELANKYNGAVNE--------IKDLSD--KLKVA 324
Cdd:PRK00409 526 EELERELEQKAeEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLEEAEKEAQQAIKEakkeadeiIKELRQlqKGGYA 602
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1799135557 325 EGKQEEIQQKgqaeKKELQHKIDEMEEKEQELQAKIEALQA 365
Cdd:PRK00409 603 SVKAHELIEA----RKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
208-366 |
3.35e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 208 IDEDRLLSRLEVMGNQLQACSKNQTE---DSLRKELIALQED-KHNYETTAKEslrrvLQEKIEVVRKLSEVERSLsnte 283
Cdd:PRK04778 249 LDHLDIEKEIQDLKEQIDENLALLEEldlDEAEEKNEEIQERiDQLYDILERE-----VKARKYVEKNSDTLPDFL---- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 284 decTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKK---ELQHKIDEMEEKEQELQ 357
Cdd:PRK04778 320 ---EHAKEQNKELKEEIDRVKQSYtlnESELESVRQLEKQLESLEKQYDEITERIAEQEIaysELQEELEEILKQLEEIE 396
|
....*....
gi 1799135557 358 AKIEALQAD 366
Cdd:PRK04778 397 KEQEKLSEM 405
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
173-366 |
3.52e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 173 QEALHREQMLEQKLATLQRLLAitqeasdtswqalidedRLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYET 252
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLK-----------------ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 253 TAKESLRRVLQEKIEVVRKlsevERSLSNTEDECTHLKEMNERTQEELRELankyngaVNEIKDLSDKLKVAEGKQEEIQ 332
Cdd:COG1579 69 EEVEARIKKYEEQLGNVRN----NKEYEALQKEIESLKRRISDLEDEILEL-------MERIEELEEELAELEAELAELE 137
|
170 180 190
....*....|....*....|....*....|....
gi 1799135557 333 QKGQAEKKELQHKIDEMEEKEQELQAKIEALQAD 366
Cdd:COG1579 138 AELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
163-342 |
3.53e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWqALIDEDRLLSRLEVMGNQLQACSKNQTE-DSLRKELI 241
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-DEIDVASAEREIAELEAELERLDASSDDlAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 242 ALQEDkhnyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLK----EMNERTQEELRELANKYNGAVNEIKDL 317
Cdd:COG4913 696 ELEAE-----------LEELEEELDELKGEIGRLEKELEQAEEELDELQdrleAAEDLARLELRALLEERFAAALGDAVE 764
|
170 180
....*....|....*....|....*
gi 1799135557 318 SDKLKVAEGKQEEIQQKGQAEKKEL 342
Cdd:COG4913 765 RELRENLEERIDALRARLNRAEEEL 789
|
|
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
486-575 |
3.57e-03 |
|
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: 39.60 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 486 LEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLRE---EKDSEITSTRDEL--LSARDEILLLHQAAAKVASERDTD 560
Cdd:pfam06818 50 KEEQIQELEDSLRSKTLELEVCENELQRKKNEAELLREkvgKLEEEVSGLREALsdVSPSGYESVYESDEAKEQRQEEAD 129
|
90
....*....|....*
gi 1799135557 561 IASLQEELKKVRAEL 575
Cdd:pfam06818 130 LGSLRREVERLRAEL 144
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
465-676 |
3.84e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 465 AQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREE---KDSEITSTRDEL----- 536
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeAEAEIEERREELgerar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 537 --------LSARDEIL-------LLHQAAA-KVASERDTDIAslqEELKKVRAELERWRKAASEYEKEITSLQnsfqlrc 600
Cdd:COG3883 94 alyrsggsVSYLDVLLgsesfsdFLDRLSAlSKIADADADLL---EELKADKAELEAKKAELEAKLAELEALK------- 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799135557 601 qqceDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKE 676
Cdd:COG3883 164 ----AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
163-365 |
4.00e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.44 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEasdtsWQALIDEDRLLSR----LEVMGNQLQACSKNQT--EDSL 236
Cdd:COG0497 172 KELEELRADEAERARELDLLRFQLEELEAAALQPGE-----EEELEEERRRLSNaeklREALQEALEALSGGEGgaLDLL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 237 RKELIALQEDKHnYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERtQEELRELANKYNGAVNEIKD 316
Cdd:COG0497 247 GQALRALERLAE-YDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEER-LALLRRLARKYGVTVEELLA 324
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1799135557 317 LSDKLkvaegkqeeiqqkgQAEKKELQHKIDEMEEKEQELQAKIEALQA 365
Cdd:COG0497 325 YAEEL--------------RAELAELENSDERLEELEAELAEAEAELLE 359
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
528-754 |
4.04e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 528 EITSTRDELLSARDEILLLHQAAAKVASERDtdiaSLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCED-- 605
Cdd:COG1340 16 KIEELREEIEELKEKRDELNEELKELAEKRD----ELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNElr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 606 -------QQREEATRLQGELEKLRKEWNALE----TECHSLKRENVL------LSSELQRQEKElHNSQKQSLELTSDLS 668
Cdd:COG1340 92 eeldelrKELAELNKAGGSIDKLRKEIERLEwrqqTEVLSPEEEKELvekikeLEKELEKAKKA-LEKNEKLKELRAELK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 669 ILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAEN---QAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCK 745
Cdd:COG1340 171 ELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADElrkEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLR 250
|
....*....
gi 1799135557 746 NNLKLLREK 754
Cdd:COG1340 251 KKQRALKRE 259
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
274-374 |
4.09e-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: 40.61 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 274 EVERSLSNTEDECTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEK----------K 340
Cdd:pfam06160 288 YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEvayselqeelE 367
|
90 100 110
....*....|....*....|....*....|....
gi 1799135557 341 ELQHKIDEMEEKEQELQAKIEALQADNDFTNERL 374
Cdd:pfam06160 368 EILEQLEEIEEEQEEFKESLQSLRKDELEAREKL 401
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
487-752 |
4.40e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.26 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 487 EEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLrEEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQE 566
Cdd:pfam07888 65 KRDREQWERQRRELESRVAELKEELRQSREKHEEL-EEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQ 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 567 ELKKVRAELERWR---KAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQG--------------------------- 616
Cdd:pfam07888 144 RVLERETELERMKeraKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQElrnslaqrdtqvlqlqdtittltqklt 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 617 -------ELEKLRKEWNALETECHSLKRENVLLSSELQ-------RQEKELHNSQKQSLELTSDLSILQMSRKELENQvG 682
Cdd:pfam07888 224 tahrkeaENEALLEELRSLQERLNASERKVEGLGEELSsmaaqrdRTQAELHQARLQAAQLTLQLADASLALREGRAR-W 302
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799135557 683 SLKEQHLRDSADLKTllSKAENQAKDVQKEYEKTQTVLSE-LKLKFEMTeQEKQSITDELKQCKNNLKLLR 752
Cdd:pfam07888 303 AQERETLQQSAEADK--DRIEKLSAELQRLEERLQEERMErEKLEVELG-REKDCNRVQLSESRRELQELK 370
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
310-595 |
5.38e-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: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 310 AVNEIKDLSDKLKVAEGKQEEIQqkgqAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGiqvddflpKI 389
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQ----AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA--------EI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 390 NgstEKEHLLSKsggdctfihqfiecqkkliveghltkaveetklskenqtRAKESdfsdtlspSKEKSSDDTTDAQMDE 469
Cdd:COG3883 82 E---ERREELGE---------------------------------------RARAL--------YRSGGSVSYLDVLLGS 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 470 QDLNEPLAKVSLLKALLEEERKAyrnqveesTKQIQVLQAQLqrlhidtenlrEEKDSEITSTRDELLSARDEILLLHQA 549
Cdd:COG3883 112 ESFSDFLDRLSALSKIADADADL--------LEELKADKAEL-----------EAKKAELEAKLAELEALKAELEAAKAE 172
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1799135557 550 AAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNS 595
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
52-106 |
5.97e-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: 5.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799135557 52 SRNHALVWFDHKTGKFYLQ-----------DTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFG 106
Cdd:cd22683 28 SRSCDLVLSDPSISRFHAElrleqnginviDNNSANGTFINGKRIKGKT-----YILKNGDIIVFG 88
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
322-736 |
6.10e-03 |
|
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: 40.11 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 322 KVAEGKQEEIQQKGQAEKKELQHKidemeEKEQELQAKIEALQADNDFTNERLTALQGiqvddflpKINGSTEKEHLLSK 401
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHK-----RARIELEKKASALKRQLDRESDRNQELQK--------RIRLLEKREAEAEE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 402 SggdctfihqfiecQKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSL 481
Cdd:pfam05557 70 A-------------LREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 482 LKALLEEERKAYRN---QVEESTKQIQVLQAQLQRLH-IDTENLREEKDSEITST-RDELLS------------------ 538
Cdd:pfam05557 137 LQERLDLLKAKASEaeqLRQNLEKQQSSLAEAEQRIKeLEFEIQSQEQDSEIVKNsKSELARipelekelerlrehnkhl 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 539 ---ARDEILL---LHQAAAKVASERDT--DIASLQEELKKVRAELERWRKAASEYEKEITS--LQNSFQLRCQQCEDQQR 608
Cdd:pfam05557 217 nenIENKLLLkeeVEDLKRKLEREEKYreEAATLELEKEKLEQELQSWVKLAQDTGLNLRSpeDLSRRIEQLQQREIVLK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 609 EEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDL----SILQMSRKELENQVGSl 684
Cdd:pfam05557 297 EENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgyrAILESYDKELTMSNYS- 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1799135557 685 kEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 736
Cdd:pfam05557 376 -PQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQA 426
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
429-743 |
6.35e-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: 40.11 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 429 VEETKLSKENQTRAKESDFSDTLSPSkEKSSDDTTDAQMDEQDLNEPLAkvsllkalLEEERKAYRNQVEESTKQIQvlQ 508
Cdd:pfam17380 296 MEQERLRQEKEEKAREVERRRKLEEA-EKARQAEMDRQAAIYAEQERMA--------MERERELERIRQEERKRELE--R 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 509 AQLQRLHIDTENLRE------EKDSEITSTRDELLSARDEILLLHQAAAKVASERDT--DIASLQEE--------LKKVR 572
Cdd:pfam17380 365 IRQEEIAMEISRMRElerlqmERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEmeQIRAEQEEarqrevrrLEEER 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 573 A-ELERWRKAASEYEKEITSLQnsfqlrcqqcedQQREEATRLQGELEKLRKEWNALETEchslkRENVLlsselqrqEK 651
Cdd:pfam17380 445 ArEMERVRLEEQERQQQVERLR------------QQEEERKRKKLELEKEKRDRKRAEEQ-----RRKIL--------EK 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 652 ELHNSQKQSLELTSDLSILQmsrKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTE 731
Cdd:pfam17380 500 ELEERKQAMIEEERKRKLLE---KEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERERE 576
|
330
....*....|..
gi 1799135557 732 QEKQSITDELKQ 743
Cdd:pfam17380 577 MMRQIVESEKAR 588
|
|
| VI_FHA |
TIGR03354 |
type VI secretion system FHA domain protein; Members of this protein family are FHA ... |
49-106 |
6.51e-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: 39.66 E-value: 6.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799135557 49 KVLSRNHALV-WFDhktGKFYLQDTkSSNGTFINS--QRLSRGSEesppcEILS-GDIIQFG 106
Cdd:TIGR03354 43 RHVSGRHARIrYRD---GAYLLTDL-STNGVFLNGsgSPLGRGNP-----VRLEqGDRLRLG 95
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
519-667 |
8.07e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 39.60 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 519 ENLREEKDSEITSTRDEL-LSARD--EILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNS 595
Cdd:pfam05262 184 EALREDNEKGVNFRRDMTdLKEREsqEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKP 263
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135557 596 FQLRC----QQCEDQQREEATRLQGELEKLRKE-WNALETECHSLKREnvlLSSELQRQEKELHNSQKQSLELTSDL 667
Cdd:pfam05262 264 ADTSSpkedKQVAENQKREIEKAQIEIKKNDEEaLKAKDHKAFDLKQE---SKASEKEAEDKELEAQKKREPVAEDL 337
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
271-631 |
8.67e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.62 E-value: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 271 KLSEVERSLSNTEDECTHLKEMNERTQEELRElankyngAVNEIKDLsdkLKVAEGKQEEIQQKGQaEKKELQHKIDEME 350
Cdd:TIGR04523 336 IISQLNEQISQLKKELTNSESENSEKQRELEE-------KQNEIEKL---KKENQSYKQEIKNLES-QINDLESKIQNQE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 351 EKEQELQAKIEALQADNDftnerltalqgiqvddflpkingSTEKEHLLSKsggdctfihQFIECQKKLIVEGHLTKAVE 430
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKE-----------------------LLEKEIERLK---------ETIIKNNSEIKDLTNQDSVK 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 431 ETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLqaq 510
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL--- 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 511 lqrlhidtENLREEKDSEITSTRDELLSARDEilLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEIT 590
Cdd:TIGR04523 530 --------ESEKKEKESKISDLEDELNKDDFE--LKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKK 599
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1799135557 591 SLQNSFQLRCQQcedqqreeATRLQGELEKLRKEWNALETE 631
Cdd:TIGR04523 600 DLIKEIEEKEKK--------ISSLEKELEKAKKENEKLSSI 632
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
247-749 |
8.98e-03 |
|
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: 39.64 E-value: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 247 KHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNT---EDECTHLKEMNERTQEELRELANK----YNGAVNEIKDLSD 319
Cdd:TIGR00606 229 KEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKImklDNEIKALKSRKKQMEKDNSELELKmekvFQGTDEQLNDLYH 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 320 ----KLKVAEGKQEEIQQ---KGQAEKKELQHKIDEMEEKEQELQAKIEALQADN-DFTNERLTALQGIQVDDFL--PKI 389
Cdd:TIGR00606 309 nhqrTVREKERELVDCQReleKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIrARDSLIQSLATRLELDGFErgPFS 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 390 NGSTEKEHLLSKSG--GDCTFIHQFI-ECQKKLIVEghlTKAVEETKLSKENQTRAKESDfSDTLSPSKEKSSDDTTDAQ 466
Cdd:TIGR00606 389 ERQIKNFHTLVIERqeDEAKTAAQLCaDLQSKERLK---QEQADEIRDEKKGLGRTIELK-KEILEKKQEELKFVIKELQ 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 467 MDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQ----IQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDE 542
Cdd:TIGR00606 465 QLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKevksLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDK 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 543 iLLLHQAAAKVASERDTDIASLQEELKKvRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLR 622
Cdd:TIGR00606 545 -MDKDEQIRKIKSRHSDELTSLLGYFPN-KKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLS 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 623 KEWNALETECHSLKREnvllsSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRD----------S 692
Cdd:TIGR00606 623 SYEDKLFDVCGSQDEE-----SDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVfqteaelqefI 697
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135557 693 ADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLK 749
Cdd:TIGR00606 698 SDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQ 754
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
433-750 |
9.29e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 39.65 E-value: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 433 KLSKENQTRAKESDFSDTLSPS-KEKSSDDT----TDAQMDEQDLNEPLAKVSLLKA-LLEEERK--AYRNQVEESTKQI 504
Cdd:TIGR01612 1373 EIEENNKNIKDELDKSEKLIKKiKDDINLEEckskIESTLDDKDIDECIKKIKELKNhILSEESNidTYFKNADENNENV 1452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 505 QVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEilllHQAAAKvaserdtdiaSLQEELKKVRAELERWRKAASE 584
Cdd:TIGR01612 1453 LLLFKNIEMADNKSQHILKIKKDNATNDHDFNINELKE----HIDKSK----------GCKDEADKNAKAIEKNKELFEQ 1518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 585 YEKEITSLQNSF-QLRCQQCEDQQREEATRLQGELEKLRK----EWNALETECHSLKRENVLLSSELQRQEK-------- 651
Cdd:TIGR01612 1519 YKKDVTELLNKYsALAIKNKFAKTKKDSEIIIKEIKDAHKkfilEAEKSEQKIKEIKKEKFRIEDDAAKNDKsnkaaidi 1598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 652 --ELHNSQKQSLELTSDLSILQMSRKE---LENQVGSL----KEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSE 722
Cdd:TIGR01612 1599 qlSLENFENKFLKISDIKKKINDCLKEtesIEKKISSFsidsQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDE 1678
|
330 340
....*....|....*....|....*...
gi 1799135557 723 LKLKFEmteqekqSITDELKQCKNNLKL 750
Cdd:TIGR01612 1679 LDSEIE-------KIEIDVDQHKKNYEI 1699
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| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
303-658 |
9.47e-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: 39.11 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 303 LANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQadndftnERLTALQGIQV 382
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSR-------EKHEELEEKYK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 383 DDFLPKINGSTEKEHLLSKSGGDCTFIHQfIECQKKLIVEGHLTKAVEETKLsKENQTRAkesdfSDTLSPSKEKSSDDT 462
Cdd:pfam07888 105 ELSASSEELSEEKDALLAQRAAHEARIRE-LEEDIKTLTQRVLERETELERM-KERAKKA-----GAQRKEEEAERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 463 TDAQMDEQDLNEPLAKVSLLKALLeEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREekdsEITSTRDELLSARDE 542
Cdd:pfam07888 178 AKLQQTEEELRSLSKEFQELRNSL-AQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE----ELRSLQERLNASERK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135557 543 ILLLHQAAAKVASERDTDIASL-QEELKKVRAELE------RWRKAASEYEKEITSLQNSFQLRCQQCEdQQREEATRLQ 615
Cdd:pfam07888 253 VEGLGEELSSMAAQRDRTQAELhQARLQAAQLTLQladaslALREGRARWAQERETLQQSAEADKDRIE-KLSAELQRLE 331
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1799135557 616 GELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQK 658
Cdd:pfam07888 332 ERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLR 374
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