|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
3-130 |
3.83e-81 |
|
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and similar proteins; SLMAP, also called sarcolemmal-associated protein (SLAP), is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. It is a cardiac membrane protein that plays an important role in E-C coupling and the adrenergic response of the heart. Overexpression of the SLMAP gene has been associated with diabetes and endothelial dysfunction of macro- and micro-blood vessels. SLMAP contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438731 [Multi-domain] Cd Length: 126 Bit Score: 256.43 E-value: 3.83e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 3 SALAIFTCRPNSHPFQERHVYLDEPIKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINS 82
Cdd:cd22679 1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1799135504 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 |
2.50e-26 |
|
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal membrane-associated protein (SLMAP), also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. SLMAP contains an N-terminal FHA domain followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409287 [Multi-domain] Cd Length: 63 Bit Score: 102.38 E-value: 2.50e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799135504 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQ 225
Cdd:cd21911 1 QELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQLS 63
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
163-812 |
8.11e-23 |
|
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: 105.14 E-value: 8.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSknqteDSLRKELIA 242
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL-----ESLEAELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 243 LQEDKHNYETTAKEsLRRVLQEKIEVVRKLSEVERSLSNT----EDECTHLKEMNERTQEELRELA--------NKYNGA 310
Cdd:TIGR02168 363 LEAELEELESRLEE-LEEQLETLRSKVAQLELQIASLNNEierlEARLERLEDRRERLQQEIEELLkkleeaelKELQAE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 311 VNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQA-DNDFTNERLTALQVRLEHLQEKTL 389
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERlQENLEGFSEGVKALLKNQSGLSGI 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 390 KECSSLGIQVD------------DFLPKINGSTEK------EHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKAVEETKL 451
Cdd:TIGR02168 522 LGVLSELISVDegyeaaieaalgGRLQAVVVENLNaakkaiAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFL 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 452 SKENQTRAKESDFSDTLSP--SKEKSSDDTTDAQMDEQDLNEPLAKVSL-----------LKDDLQGAQSEIEAKQEIQH 518
Cdd:TIGR02168 602 GVAKDLVKFDPKLRKALSYllGGVLVVDDLDNALELAKKLRPGYRIVTLdgdlvrpggviTGGSAKTNSSILERRREIEE 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 519 LRKELIEAQELARTSKQKCFEL---QALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEkdseITSTRDELL 595
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELrkeLEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER----IAQLSKELT 757
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 596 SARDEILLLHQAAAKV---ASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSF---QLRCQQCEDQQREEA 669
Cdd:TIGR02168 758 ELEAEIEELEERLEEAeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATE 837
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 670 TRL----------QGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQV 739
Cdd:TIGR02168 838 RRLedleeqieelSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799135504 740 GSLKEQHlrdsADLKTLLSKAENQAKDVQkeyektQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 812
Cdd:TIGR02168 918 EELREKL----AQLELRLEGLEVRIDNLQ------ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| FHA_DMA-like |
cd22692 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest ... |
27-108 |
1.88e-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: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 27 PIKIGRSVARCRPAQNNAT-FDCKVLSRNHALVWfdHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQF 105
Cdd:cd22692 38 QIHIGRYTERVRQAIYHPVvFKSKVVSRTHGCIK--VDEGNWYIKDVKSSSGTFLNHQRLSPASRTSKPYPLRDGDILQL 115
|
...
gi 1799135504 106 GVD 108
Cdd:cd22692 116 GMD 118
|
|
| FHA_VPS64-like |
cd22695 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ... |
6-126 |
5.92e-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: 5.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 6 AIFTCRPNSHPFQERHV---YLDEPIKIGRSVARCRPAQN---------------NATFDCKVLSRNHALVWFDHKTGKF 67
Cdd:cd22695 2 HILVLKSLNATFETKFLvvpFKPDGLKLGRPVTNSVNKNNsgskrdlfsqqvrpdNGNFDSRVLSRNHACLSCDPTTGKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135504 68 YLQDTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFGVDVTEntrKVTHGCIVSTIK 126
Cdd:cd22695 82 YIRDLKSSNGTFVNGQKIRQND-----VELKVGDEVDLGTDIDS---KIEHRKISAYVE 132
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
13-106 |
5.27e-14 |
|
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.
Pssm-ID: 438714 [Multi-domain] Cd Length: 92 Bit Score: 68.07 E-value: 5.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 13 NSHPFQERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINSQRLsrgseeS 92
Cdd:cd00060 6 DGDGGGREFPLTKGVVTIGRS------PDCDIVLDDPSVSRRHARIEVDG--GGVYLEDLGSTNGTFVNGKRI------T 71
|
90
....*....|....
gi 1799135504 93 PPCEILSGDIIQFG 106
Cdd:cd00060 72 PPVPLQDGDVIRLG 85
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
28-105 |
1.54e-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: 1.54e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135504 28 IKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRLSRgseesPPCEILSGDIIQF 105
Cdd:pfam00498 1 VTIGRS------PDCDIVLDDPSVSRRHAEIRYD-GGGRFYLEDLGSTNGTFVNGQRLGP-----EPVRLKDGDVIRL 66
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
494-791 |
1.88e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 494 AKVSLLKDDLQGAQSEiEAKQEIQHLRKELIEAQELartskqkcfelQALLEEERKAYRNQVEESTKQIQVLQAQLQRLH 573
Cdd:COG1196 227 AELLLLKLRELEAELE-ELEAELEELEAELEELEAE-----------LAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 574 IDTENLREEKDSEitstRDELLSARDEILLLHQAAAKVASErdtdIASLQEELKKVRAELERWRKAASEYEKEITSLQNS 653
Cdd:COG1196 295 AELARLEQDIARL----EERRRELEERLEELEEELAELEEE----LEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 654 FQLRCQQCEDQQREEATRLQGELEKLRKEwNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRK 733
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAA-AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135504 734 ELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQE 791
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
515-812 |
1.98e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 74.72 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 515 EIQHLRKELIEAQELARTSKQKCFELQALLEEERKA----YRNQVEESTKQIQVLQAQLQRLhidtENLREEKDSEITST 590
Cdd:TIGR02169 188 RLDLIIDEKRQQLERLRREREKAERYQALLKEKREYegyeLLKEKEALERQKEAIERQLASL----EEELEKLTEEISEL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 591 RDELLSARDeilLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNsfQLRCQQCE-DQQREEA 669
Cdd:TIGR02169 264 EKRLEEIEQ---LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE--RLAKLEAEiDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 670 TRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRD 749
Cdd:TIGR02169 339 EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL 418
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799135504 750 SADlktlLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 812
Cdd:TIGR02169 419 SEE----LADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
|
| CC1_SLMAP-like |
cd21868 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ... |
167-204 |
1.18e-12 |
|
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar proteins; The family includes Sarcolemmal membrane-associated protein (SLMAP), its paralog TRAF3-interacting JNK-activating modulator (T3JAM), and similar proteins. SLMAP, also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. T3JAM, also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. SLMAP contains an N-terminal FHA domain, followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409286 [Multi-domain] Cd Length: 38 Bit Score: 62.50 E-value: 1.18e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1799135504 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21868 1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
161-782 |
4.03e-12 |
|
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: 70.15 E-value: 4.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 161 YSQELFQLSQYLQEA--LHREQ--MLEQKLATLQRLLAITQEASDtswqALIDedrlLSRLEvmgNQLQACSKNQTEDSL 236
Cdd:pfam15921 83 YSHQVKDLQRRLNESneLHEKQkfYLRQSVIDLQTKLQEMQMERD----AMAD----IRRRE---SQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 237 RKELIA--LQEDKHNYETTAKESLRR-------VLQEKIEVVRKLSEVERSLSNTEDECT--HLKEMNERTQEELRELAN 305
Cdd:pfam15921 152 HELEAAkcLKEDMLEDSNTQIEQLRKmmlshegVLQEIRSILVDFEEASGKKIYEHDSMStmHFRSLGSAISKILRELDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 306 kyngavnEIKDLSDKLKVAEGKQEEIQQKGQAEKKEL-QHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHL 384
Cdd:pfam15921 232 -------EISYLKGRIFPVEDQLEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEII 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 385 QEKTLKECSSLGIQVDDFlpkinGSTEKEHLLSKSGGDCTFIHQFIECQKKLIV-EGHLTKA-VEETKLSKE--NQTRAK 460
Cdd:pfam15921 305 QEQARNQNSMYMRQLSDL-----ESTVSQLRSELREAKRMYEDKIEELEKQLVLaNSELTEArTERDQFSQEsgNLDDQL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 461 ESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLK--DDLQGAQSEIEA-----KQEIQHLRKELIEAQELARTS 533
Cdd:pfam15921 380 QKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRelDDRNMEVQRLEAllkamKSECQGQMERQMAAIQGKNES 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 534 KQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQlQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVAS 613
Cdd:pfam15921 460 LEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS-ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKN 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 614 ERDtdiaslqeELKKVRAELERWRKAASEYEKEITSLQNSFQlRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSL 693
Cdd:pfam15921 539 EGD--------HLRNVQTECEALKLQMAEKDKVIEILRQQIE-NMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEF 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 694 K----------RENVLLSSELQRQEKELHNSQKQSLELTSD--------LSILQMSRKELEN---QVGSLKEQHLRDSAD 752
Cdd:pfam15921 610 KilkdkkdakiRELEARVSDLELEKVKLVNAGSERLRAVKDikqerdqlLNEVKTSRNELNSlseDYEVLKRNFRNKSEE 689
|
650 660 670
....*....|....*....|....*....|
gi 1799135504 753 LKTLLSKAENQAKDVQKEYEKTQTVLSELK 782
Cdd:pfam15921 690 METTTNKLKMQLKSAQSELEQTRNTLKSME 719
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
229-798 |
1.12e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.01 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 229 KNQTEDSLRKELIALQEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELAnkyn 308
Cdd:PTZ00121 1249 RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKA---- 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 309 gavNEIKDLSDKLKvaeGKQEEIQQKGQAEKKELQHKIDEMEEKEQelqaKIEALQADNDFTNERLTALQVRLEHLQ--E 386
Cdd:PTZ00121 1325 ---EEAKKKADAAK---KKAEEAKKAAEAAKAEAEAAADEAEAAEE----KAEAAEKKKEEAKKKADAAKKKAEEKKkaD 1394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 387 KTLKECSSLGIQVDDFLPKINGSTEKEHLLSKSggdctfihqfiECQKKlivEGHLTKAVEETKLSKENQTRAKESDFSD 466
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKA-----------EEKKK---ADEAKKKAEEAKKADEAKKKAEEAKKAE 1460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 467 TLSPSKE--KSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRK--ELIEAQELARTSKQKCFELQA 542
Cdd:PTZ00121 1461 EAKKKAEeaKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKaeEAKKADEAKKAEEAKKADEAK 1540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 543 LLEEERKAYR-NQVEESTKQIQVLQAQLQRlhidtenlREEKDSEITSTRDELLSardeilllhqaaaKVASERDTDIAS 621
Cdd:PTZ00121 1541 KAEEKKKADElKKAEELKKAEEKKKAEEAK--------KAEEDKNMALRKAEEAK-------------KAEEARIEEVMK 1599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 622 LQEELKKVRAE----LERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKREN 697
Cdd:PTZ00121 1600 LYEEEKKMKAEeakkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 698 VLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYE---KT 774
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEekkKI 1759
|
570 580
....*....|....*....|....
gi 1799135504 775 QTVLSELKLKFEMTEQEKQSITDE 798
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
14-106 |
1.21e-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: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 14 SHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716 8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
|
90
....*....|....
gi 1799135504 93 pPCEILSGDIIQFG 106
Cdd:COG1716 75 -PAPLRDGDVIRLG 87
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
298-811 |
1.24e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.53 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 298 EELRELANKYNGAVNEIkdLSDKLKVAEGKQEEIQQKgqaEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTAL 377
Cdd:PRK02224 165 EEYRERASDARLGVERV--LSDQRGSLDQLKAQIEEK---EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 378 QVRLEHlQEKTLKECSSLGIQVDDFLPKINGsTEKEHllsksggdctfihqfiECQKKLIVEghLTKAVEEtkLSKENQT 457
Cdd:PRK02224 240 DEVLEE-HEERREELETLEAEIEDLRETIAE-TERER----------------EELAEEVRD--LRERLEE--LEEERDD 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 458 RAKESDFSDtlspskekSSDDTTDAQMDEQDlneplAKVSLLKDDLQGAQSEI-EAKQEIQHLRKELIEAQELARTSKQK 536
Cdd:PRK02224 298 LLAEAGLDD--------ADAEAVEARREELE-----DRDEELRDRLEECRVAAqAHNEEAESLREDADDLEERAEELREE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 537 CFELQALLEEERKA---YRNQVEESTKQIQVLQAQLQRLHIDTEN-------LREEKD---SEITSTRDELLSARDEI-- 601
Cdd:PRK02224 365 AAELESELEEAREAvedRREEIEELEEEIEELRERFGDAPVDLGNaedfleeLREERDelrEREAELEATLRTARERVee 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 602 ---LLlhqAAAK---------------VASERDTDIASLQEELKKVRAELERWR------KAASEYEKEITSLQNSFQlR 657
Cdd:PRK02224 445 aeaLL---EAGKcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEerleraEDLVEAEDRIERLEERRE-D 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 658 CQQCEDQQREEATRLQGELEKLRKEWNALETECHSlKRE---NVLLSSELQRQEKELHNSQ----KQSLELTSDLSILQM 730
Cdd:PRK02224 521 LEELIAERRETIEEKRERAEELRERAAELEAEAEE-KREaaaEAEEEAEEAREEVAELNSKlaelKERIESLERIRTLLA 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 731 SRKELENQVGSLKEQ-------------HLRDSADLKTLLSKA--ENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSI 795
Cdd:PRK02224 600 AIADAEDEIERLREKrealaelnderreRLAEKRERKRELEAEfdEARIEEAREDKERAEEYLEQVEEKLDELREERDDL 679
|
570
....*....|....*.
gi 1799135504 796 TDELKQCKNNLKLLRE 811
Cdd:PRK02224 680 QAEIGAVENELEELEE 695
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-801 |
1.33e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.56 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 197 QEASDTSWQALIDEDRLLSRLEVMGNQLQacsknqtedSLRKELIALQEDKHNYETTAKESLRRVLQEKI---EVVRKLS 273
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIE---------EERKRRDKLTEEYAELKEELEDLRAELEEVDKefaETRDELK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 274 EVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKvaegkqeeiqqKGQAEKKELQHKIDEMEEKE 353
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKIN-----------ELEEEKEDKALEIKKQEWKL 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 354 QELQAKIEALQADNDFTNERLTALQVRLEHLQektlKECSSLGIQVDDFLPKINGSTEKEHLLSKS-GGDCTFIHQFIEC 432
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQ----RELAEAEAQARASEERVRGGRAVEEVLKASiQGVHGTVAQLGSV 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 433 QKK---------------LIVEGHLTkAVEETKLSKE-----------NQTRAKESDfsdtLSPSKEK------------ 474
Cdd:TIGR02169 534 GERyataievaagnrlnnVVVEDDAV-AKEAIELLKRrkagratflplNKMRDERRD----LSILSEDgvigfavdlvef 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 475 ------------------SSDDTTDAQMD-------EQDLNEP--------LAKVSLLKDDLQGAQSEIEAKQEIQHLRK 521
Cdd:TIGR02169 609 dpkyepafkyvfgdtlvvEDIEAARRLMGkyrmvtlEGELFEKsgamtggsRAPRGGILFSRSEPAELQRLRERLEGLKR 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 522 ELIEAQELARTSKQKCFELQALLEEERKayrnQVEESTKQIQVLQAQLQRLHIDTENLREekdsEITSTRDELLSARDEI 601
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASR----KIGEIEKEIEQLEQEEEKLKERLEELEE----DLSSLEQEIENVKSEL 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 602 lllhQAAAKVASERDTDIASLQEELKKVRAEL--ERWRKAASEYEKEITSLQnsfqlrcqqcedQQREEATRLQGELEKL 679
Cdd:TIGR02169 761 ----KELEARIEELEEDLHKLEEALNDLEARLshSRIPEIQAELSKLEEEVS------------RIEARLREIEQKLNRL 824
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 680 RKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKeqhlRDSADLKTLLSK 759
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK----KERDELEAQLRE 900
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1799135504 760 AENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 801
Cdd:TIGR02169 901 LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE 942
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
52-106 |
1.49e-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: 1.49e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1799135504 52 SRNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQFG 106
Cdd:cd22686 48 SKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPYPLTHGDELKIG 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
163-687 |
1.57e-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: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDtswQALIDEDRLLSRLEVMGNQLQAcsKNQTEDSLRKELIA 242
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRR---ELEERLEELEEELAELEEELEE--LEEELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 243 LQEDkhnyETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLK 322
Cdd:COG1196 349 AEEE----LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 323 VAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLKEcsSLGIQVDDF 402
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL--LLLLEAEAD 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 403 LPKINGSTEKEHLLSKSGGDCTFIHQfiecqkkLIVEGHLTKAVEETKLSK--ENQTRAKESDFSDTLSPSKEKSSDDTT 480
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVAV-------LIGVEAAYEAALEAALAAalQNIVVEDDEVAAAAIEYLKAAKAGRAT 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 481 DAQMDEQDLNEPLAKVSLLKDDLQG----AQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVE 556
Cdd:COG1196 576 FLPLDKIRARAALAAALARGAIGAAvdlvASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEG 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 557 ESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERW 636
Cdd:COG1196 656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1799135504 637 RKAASEYEKEITSLQNSFQlrcqqcEDQQREEATRLQGELEKLRKEWNALE 687
Cdd:COG1196 736 ELLEELLEEEELLEEEALE------ELPEPPDLEELERELERLEREIEALG 780
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
239-777 |
2.52e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.86 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 239 ELIALQEDKHNYETTAKESLRRV--LQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKD 316
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 317 LSDKLKVAEGKQEEIQQKGQAEKK--ELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLKECSS 394
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 395 LGIQVDDFLPKINGSTEKEHLLSKSggdctfihqfiECQKKlivEGHLTKAVEETKLSKENQTRAKESDfsdtlSPSKEK 474
Cdd:PTZ00121 1442 EAKKADEAKKKAEEAKKAEEAKKKA-----------EEAKK---ADEAKKKAEEAKKADEAKKKAEEAK-----KKADEA 1502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 475 SSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFElQALLEEERKAYRNQ 554
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE-EAKKAEEDKNMALR 1581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 555 VEESTKQIQ------VLQAQLQRLHIDTENLREEKDSEITStrDELLSARDEILLLHQAAAKVASERDTdiaslQEELKK 628
Cdd:PTZ00121 1582 KAEEAKKAEearieeVMKLYEEEKKMKAEEAKKAEEAKIKA--EELKKAEEEKKKVEQLKKKEAEEKKK-----AEELKK 1654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 629 vrAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGE----LEKLRKEWNALETECHSLKRENVLLSSEL 704
Cdd:PTZ00121 1655 --AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEeakkAEELKKKEAEEKKKAEELKKAEEENKIKA 1732
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799135504 705 QRQEKELHNSQKQSLELTSDlsilqmsrKELENQVGSLKEQHLRDSADL---KTLLSKAENQAKDVQKEYEKTQTV 777
Cdd:PTZ00121 1733 EEAKKEAEEDKKKAEEAKKD--------EEEKKKIAHLKKEEEKKAEEIrkeKEAVIEEELDEEDEKRRMEVDKKI 1800
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
486-811 |
5.33e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.63 E-value: 5.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 486 EQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCfelqalLEEERKAYRNQVEESTKQIQVL 565
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEA------LERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 566 QAQLQ-----------RLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASER---DTDIASLQEELKKVRA 631
Cdd:TIGR02169 257 TEEISelekrleeieqLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELedaEERLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 632 ELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQRE------EATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQ 705
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEleevdkEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 706 RQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADlktlLSKAENQAKDVQKEYEKTQTVLSELKLKF 785
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD----LSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
330 340
....*....|....*....|....*.
gi 1799135504 786 EMTEQEKQSITDELKQCKNNLKLLRE 811
Cdd:TIGR02169 493 AEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
233-812 |
6.24e-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: 66.23 E-value: 6.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 233 EDSLRKELIALQ-EDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAV 311
Cdd:TIGR02168 222 LRELELALLVLRlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 312 NEIKDLSDKLKVAEGKQEEIQ---QKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEkt 388
Cdd:TIGR02168 302 QQKQILRERLANLERQLEELEaqlEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE-- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 389 lkecsslgiQVDDFLPKINGSTEKEHLLSKsggdctfihqfiecqkklivegHLTKAVEETKLSKENQTRAKEsdfsDTL 468
Cdd:TIGR02168 380 ---------QLETLRSKVAQLELQIASLNN----------------------EIERLEARLERLEDRRERLQQ----EIE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 469 SPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQgaQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEER 548
Cdd:TIGR02168 425 ELLKKLEEAELKELQAELEELEEELEELQEELERLE--EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 549 KAYRNQVEESTKQIQ------------------------VLQAQLQRLHIDTEN---------------------LREEK 583
Cdd:TIGR02168 503 GFSEGVKALLKNQSGlsgilgvlselisvdegyeaaieaALGGRLQAVVVENLNaakkaiaflkqnelgrvtflpLDSIK 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 584 DSEITSTRDELLSARDEILLLHQAAAKVASERD-------------TDIASLQEELKKVRAEL-------ERWRKAASEY 643
Cdd:TIGR02168 583 GTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvDDLDNALELAKKLRPGYrivtldgDLVRPGGVIT 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 644 ---EKEITSLQNSFQ--LRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQS 718
Cdd:TIGR02168 663 ggsAKTNSSILERRReiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 719 LELTSDLSILQMSRKELENQVGSLKEQ----------HLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMT 788
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERleeaeeelaeAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
650 660
....*....|....*....|....
gi 1799135504 789 EQEKQSITDELKQCKNNLKLLREK 812
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQ 846
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
162-634 |
1.57e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 162 SQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgNQLQAcsKNQTEDSLRKELI 241
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE---AELAE--AEEELEELAEELL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 242 ALQEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKL 321
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 322 KVAEGKQEEIQQKGQAE---KKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLKECSSLGIQ 398
Cdd:COG1196 470 EEAALLEAALAELLEELaeaAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 399 VDDFLPKINGSTEKEHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKAVEETKLSKENQTR---AKESDFSDTLSpskeks 475
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLReadARYYVLGDTLL------ 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 476 sDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQV 555
Cdd:COG1196 624 -GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 556 EESTKQIQVLQAQLQRLHIDTENLREEKDSEitstRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKV---RAE 632
Cdd:COG1196 703 EEEERELAEAEEERLEEELEEEALEEQLEAE----REELLEELLEEEELLEEEALEELPEPPDLEELERELERLereIEA 778
|
..
gi 1799135504 633 LE 634
Cdd:COG1196 779 LG 780
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
228-721 |
3.97e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 228 SKNQTEDSLRKELIALQEDKHNYETTA------KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEmNERTQEELR 301
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKELEELKeeieelEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE-KVKELKELK 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 302 ELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHK---IDEMEEKEQELQAKIEALQADNDfTNERLT 375
Cdd:PRK03918 290 EKAEEYiklSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKeerLEELKKKLKELEKRLEELEERHE-LYEEAK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 376 ALQVRLEHLQEKtlKECSSLGIQVDDFLPKINGSTEKEHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKAV--------- 446
Cdd:PRK03918 369 AKKEELERLKKR--LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelt 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 447 EETKLSKENQTRAKESDFSDTLSPSKEKSSDdttdAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEA 526
Cdd:PRK03918 447 EEHRKELLEEYTAELKRIEKELKEIEEKERK----LRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEK 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 527 Q-ELARTSKQKCFELQALLE------EERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARD 599
Cdd:PRK03918 523 KaEEYEKLKEKLIKLKGEIKslkkelEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYN 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 600 EILLLHQAAAKVASERDtDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFqlrcqqcedqQREEATRLQGELEKL 679
Cdd:PRK03918 603 EYLELKDAEKELEREEK-ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY----------SEEEYEELREEYLEL 671
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1799135504 680 RKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLEL 721
Cdd:PRK03918 672 SRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL 713
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
563-811 |
4.61e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 563 QVLQAQLQRLHIdteNLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASE 642
Cdd:COG1196 216 RELKEELKELEA---ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 643 YEKEITSLQNSFQLRCQQCEDQQREEAtRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELT 722
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLE-ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 723 SDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQC 802
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
....*....
gi 1799135504 803 KNNLKLLRE 811
Cdd:COG1196 452 AELEEEEEA 460
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
299-812 |
5.96e-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: 63.12 E-value: 5.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 299 ELRELANKYNGAVNEIKDLSDKLKVAEG---KQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLT 375
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKnlnKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 376 aLQVRLEHLQEKTLKECSSLGIQVDDFLPKINGS-TEKEHLLSKSGGDCTFIHQFIECQKKlivEGHLTKAVEETKLSKE 454
Cdd:TIGR04523 114 -NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEiKKKEKELEKLNNKYNDLKKQKEELEN---ELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 455 NQTRAKESDFSDTLSPSKEKSSDDTTDaqmdEQDLNEPLAKVSLLKDDLQgaqseiEAKQEIQHLRKELIEAQELARTSK 534
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQKNKSL----ESQISELKKQNNQLKDNIE------KKQQEINEKTTEISNTQTQLNQLK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 535 QKCFELQALLEEERKayrnQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILllhQAAAKVASE 614
Cdd:TIGR04523 260 DEQNKIKKQLSEKQK----ELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKL---EEIQNQISQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 615 RDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNsfqlrcqQCEDQQREEATRLQgELEKLRKEWNALETECHSLK 694
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQN-------EIEKLKKENQSYKQ-EIKNLESQINDLESKIQNQE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 695 RENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHlrdsADLKTLLSKAENQAKDVQKEYEKT 774
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELII----KNLDNTRESLETQLKVLSRSINKI 480
|
490 500 510
....*....|....*....|....*....|....*...
gi 1799135504 775 QTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 812
Cdd:TIGR04523 481 KQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK 518
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
271-804 |
6.55e-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: 62.73 E-value: 6.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 271 KLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHK----- 345
Cdd:TIGR04523 125 ELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLellls 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 346 -IDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKtLKECSSLGIQVDDFLPKINGSTEKEHllsksggdct 424
Cdd:TIGR04523 205 nLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTE-ISNTQTQLNQLKDEQNKIKKQLSEKQ---------- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 425 fihQFIECQKKLIVEghLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMD----EQDLNEPLAKVSLLK 500
Cdd:TIGR04523 274 ---KELEQNNKKIKE--LEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQisqnNKIISQLNEQISQLK 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 501 DDLQGAQSEIEAKQEiqHLRKELIEAQELARTSKQKCFELQALlEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLR 580
Cdd:TIGR04523 349 KELTNSESENSEKQR--ELEEKQNEIEKLKKENQSYKQEIKNL-ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 581 EEKD---SEITSTRDELLSARDEILLLHQAAAKVASERD---TDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSF 654
Cdd:TIGR04523 426 KEIErlkETIIKNNSEIKDLTNQDSVKELIIKNLDNTREsleTQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 655 QLRCQQCEDQQREEATRLQGElEKLRKEWNALETECHSLKRENVLLSSELQRQ--EKELHNSQKQSLELTSDLSILQMSR 732
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKI-EKLESEKKEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQ 584
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799135504 733 KELENQVGSLKEQHL---RDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKN 804
Cdd:TIGR04523 585 EEKQELIDQKEKEKKdliKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
255-812 |
6.58e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 6.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 255 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNgAVNEIKDLSDKLKVAEGKQEEIQQK 334
Cdd:PRK03918 178 IERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 335 GQAEKKELQHKIDEMEEKEQELQAKIEALQadndfTNERLTALQVRLEHLQEKTLKECSSLGIQVDDFLPKINGSTEKEH 414
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKELK-----ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 415 LLSKSGGDctfihqfIECQKKLIVEGHLTKAVEETKLSKENQTRAKEsdfsDTLSPSKEKSSDDTTDaqmdeqDLNEPLA 494
Cdd:PRK03918 332 ELEEKEER-------LEELKKKLKELEKRLEELEERHELYEEAKAKK----EELERLKKRLTGLTPE------KLEKELE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 495 KVSLLKDDLQGAQSEIEAKQ-EIQHLRKELIEAQELARTSKQKCFELQALLEEERKAyrNQVEESTKQIQVLQAQLQRLH 573
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIgELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRK--ELLEEYTAELKRIEKELKEIE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 574 IDTENLREEKdseitSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNS 653
Cdd:PRK03918 473 EKERKLRKEL-----RELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 654 FqlrcqqcedqqrEEATRLQGELEKLRKEWNALETECHSLKRENVLLS----SELQRQEKELHNSQKQSLELT---SDLS 726
Cdd:PRK03918 548 L------------EKLEELKKKLAELEKKLDELEEELAELLKELEELGfesvEELEERLKELEPFYNEYLELKdaeKELE 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 727 ILQMSRKELENQVGSLKEQHLRDSADLKTLLSK--------AENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDE 798
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKEleelekkySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKT 695
|
570
....*....|....
gi 1799135504 799 LKQCKNNLKLLREK 812
Cdd:PRK03918 696 LEKLKEELEEREKA 709
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
501-720 |
8.56e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.63 E-value: 8.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 501 DDLQGAQSEIE-AKQEIQHLRkELIEAQELARTSKQKCFELQALLEeerkayRNQVEESTKQIQVLQAQLQRLhidtENL 579
Cdd:COG4913 235 DDLERAHEALEdAREQIELLE-PIRELAERYAAARERLAELEYLRA------ALRLWFAQRRLELLEAELEEL----RAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 580 REEKDSEITSTRDELLSARDEILLLHQAAAKVASERdtdIASLQEELKKVRAELERWRKAASEYEKEITSLQNSfqlrcq 659
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRGNGGDR---LEQLEREIERLERELEERERRRARLEALLAALGLP------ 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799135504 660 qcEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNsQKQSLE 720
Cdd:COG4913 375 --LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA-EIASLE 432
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
250-812 |
1.09e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 250 YETTAKES--LRRVLQEKIEVVRKL----SEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLsDKLKV 323
Cdd:PRK03918 160 YENAYKNLgeVIKEIKRRIERLEKFikrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-EELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 324 AEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQAdndfTNERLTALQ------VRLEHLQEKTLKECSSLGI 397
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE----KVKELKELKekaeeyIKLSEFYEEYLDELREIEK 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 398 QVDDFLPKINGSTEKEHLLSKSggdctfiHQFIECQKKLIVEGHLTKAVEETKLSKENQTRAKEsdfsDTLSPSKEKSSD 477
Cdd:PRK03918 315 RLSRLEEEINGIEERIKELEEK-------EERLEELKKKLKELEKRLEELEERHELYEEAKAKK----EELERLKKRLTG 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 478 DTTDaqmdeqDLNEPLAKVSLLKDDLQGAQSEIEAKQ-EIQHLRKELIEAQELARTSKQKCFELQALLEEERKAyrNQVE 556
Cdd:PRK03918 384 LTPE------KLEKELEELEKAKEEIEEEISKITARIgELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRK--ELLE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 557 ESTKQIQVLQAQLQRLHIDTENLREEKdseitSTRDELLSARDEILLLHQAAAKvaserdtdIASLQEELKKVraELERW 636
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLRKEL-----RELEKVLKKESELIKLKELAEQ--------LKELEEKLKKY--NLEEL 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 637 RKAASEYEKeitslqnsfqlrcqqcedqQREEATRLQGELEKLRKEWNALEtechSLKRENVLLSSELQRQEKELHNSQK 716
Cdd:PRK03918 521 EKKAEEYEK-------------------LKEKLIKLKGEIKSLKKELEKLE----ELKKKLAELEKKLDELEEELAELLK 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 717 QSLELT-SDLSILQMSRKELE---NQVGSLK------EQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFe 786
Cdd:PRK03918 578 ELEELGfESVEELEERLKELEpfyNEYLELKdaekelEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY- 656
|
570 580
....*....|....*....|....*.
gi 1799135504 787 mTEQEKQSITDELKQCKNNLKLLREK 812
Cdd:PRK03918 657 -SEEEYEELREEYLELSRELAGLRAE 681
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
217-754 |
1.82e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 61.67 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 217 LEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTakeslrrvlqekieVVRKLSEVERSLSNTEDECTHLKEMNERT 296
Cdd:pfam15921 278 VEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSM--------------YMRQLSDLESTVSQLRSELREAKRMYEDK 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 297 QEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAK-------IEALQADNDF 369
Cdd:pfam15921 344 IEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDD 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 370 TNERLTalqvRLEHLQEKTLKECSSlgiQVDDFLPKINGSTEKEHLLSKsggdctfIHQFIECQKKLiveghLTKAVEET 449
Cdd:pfam15921 424 RNMEVQ----RLEALLKAMKSECQG---QMERQMAAIQGKNESLEKVSS-------LTAQLESTKEM-----LRKVVEEL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 450 KlSKENQTRAKESDFSDTLSPSKEKS-SDDTTDAQMDE--QDLNEPLAKVSLLK---DDLQGAQSEIEA----------- 512
Cdd:pfam15921 485 T-AKKMTLESSERTVSDLTASLQEKErAIEATNAEITKlrSRVDLKLQELQHLKnegDHLRNVQTECEAlklqmaekdkv 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 513 ----KQEI--------QHLRKE---LIEAQELARTSKQKCFELQAL--LEEERKAYRNQVEESTKQIQVLQAQLqrLHID 575
Cdd:pfam15921 564 ieilRQQIenmtqlvgQHGRTAgamQVEKAQLEKEINDRRLELQEFkiLKDKKDAKIRELEARVSDLELEKVKL--VNAG 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 576 TENLREEKD---------SEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWR--------- 637
Cdd:pfam15921 642 SERLRAVKDikqerdqllNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRntlksmegs 721
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 638 -----KAASEYEKEITSLQNsfQLRCQQCEDQQREEATR--------LQGELEKLRKEWNALETECHSLKRENVLLSSEL 704
Cdd:pfam15921 722 dghamKVAMGMQKQITAKRG--QIDALQSKIQFLEEAMTnankekhfLKEEKNKLSQELSTVATEKNKMAGELEVLRSQE 799
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1799135504 705 QRQEKELHNSQ----KQSLELTSDLSILQmsRKELENQvgSLKEQHLRDSADLK 754
Cdd:pfam15921 800 RRLKEKVANMEvaldKASLQFAECQDIIQ--RQEQESV--RLKLQHTLDVKELQ 849
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
167-386 |
2.20e-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: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTE-----DSLRKELI 241
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvkselKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 242 ALQEDKHNYETTAKESLRRVLQEKI-EVVRKLSEVERSLSNTEDECTHL-KEMNERTQE------ELRELANKYNGAVNE 313
Cdd:TIGR02169 769 ELEEDLHKLEEALNDLEARLSHSRIpEIQAELSKLEEEVSRIEARLREIeQKLNRLTLEkeylekEIQELQEQRIDLKEQ 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 314 IKDLSDKLKVAEGKQEEIQQKGQ----------AEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEH 383
Cdd:TIGR02169 849 IKSIEKEIENLNGKKEELEEELEeleaalrdleSRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
|
...
gi 1799135504 384 LQE 386
Cdd:TIGR02169 929 LEE 931
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
543-812 |
3.00e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 543 LLEEERKAYRNQVEESTKQIQVLQAQLQRLhidtENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERD---TDI 619
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAEL----EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIArleERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 620 ASLQEELKKVRAELERWRKAASEYEKEItslqnsfqlrcqqceDQQREEATRLQGELEKLRKEWNALETECHSLKREnvl 699
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEEL---------------EELEEELEEAEEELEEAEAELAEAEEALLEAEAE--- 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 700 lSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLS 779
Cdd:COG1196 374 -LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270
....*....|....*....|....*....|...
gi 1799135504 780 ELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 812
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-717 |
4.21e-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: 60.46 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 156 NTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQA--CSKNQTE 233
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvAQLELQI 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 234 DSLRKELIAL------QEDKHNYETTAKESLRRVLQE--KIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELAN 305
Cdd:TIGR02168 396 ASLNNEIERLearlerLEDRRERLQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 306 KYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKidemEEKEQELQAKIEALQADNDFTNERLTALQVRLEHL- 384
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ----SGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVv 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 385 ---QEKTLKECSSLG---------IQVDDFLPKINGSTEKEHLLSKSGGD--------------------------CTFI 426
Cdd:TIGR02168 552 venLNAAKKAIAFLKqnelgrvtfLPLDSIKGTEIQGNDREILKNIEGFLgvakdlvkfdpklrkalsyllggvlvVDDL 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 427 HQFIECQKKL-------IVEGHL-------TKAVEETKLSKENQTR-------------AKESDFSDTLSPSKEKSSDDT 479
Cdd:TIGR02168 632 DNALELAKKLrpgyrivTLDGDLvrpggviTGGSAKTNSSILERRReieeleekieeleEKIAELEKALAELRKELEELE 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 480 TDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIE-AKQEIQHLRKELIEAQ----------ELARTSKQKCFELQALLEEER 548
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVEqLEERIAQLSKELTELEaeieeleerlEEAEEELAEAEAEIEELEAQI 791
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 549 KAYRNQVEESTKQIQVLQAQLQRLHIDTENLRE-----EKDSEITSTRDELLSARDEILLLHQAAAKVA----------- 612
Cdd:TIGR02168 792 EQLKEELKALREALDELRAELTLLNEEAANLRErleslERRIAATERRLEDLEEQIEELSEDIESLAAEieeleelieel 871
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 613 -----------SERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQ---NSFQLRCQQCEdqqreeaTRLQGELEK 678
Cdd:TIGR02168 872 eseleallnerASLEEALALLRSELEELSEELRELESKRSELRRELEELReklAQLELRLEGLE-------VRIDNLQER 944
|
650 660 670
....*....|....*....|....*....|....*....
gi 1799135504 679 LRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQ 717
Cdd:TIGR02168 945 LSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-687 |
8.52e-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: 59.30 E-value: 8.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 263 QEKIEVVRKLSEVERSLSNTEDEcthLKEMNERTQ--EELRELANKYNGAVNEIKDLSDKLKVAEGKQEEiqqkgqAEKK 340
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDI---LNELERQLKslERQAEKAERYKELKAELRELELALLVLRLEELR------EELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 341 ELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLkecsSLGIQVDDflpkingstekehllsksg 420
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY----ALANEISR------------------- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 421 gdctfihqfiecqkkliVEGHLTKAVEETKLSKENQTRAkesdfsdtlspskekssddTTDAQMDEQDLNEPLAKVSLLK 500
Cdd:TIGR02168 300 -----------------LEQQKQILRERLANLERQLEEL-------------------EAQLEELESKLDELAEELAELE 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 501 DDLQGAQSEIEAkqeiqhLRKELIEAQELARTSKQKCFELQALLEEERKAY---RNQVEESTKQIQVLQAQLQRLhidtE 577
Cdd:TIGR02168 344 EKLEELKEELES------LEAELEELEAELEELESRLEELEEQLETLRSKVaqlELQIASLNNEIERLEARLERL----E 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 578 NLREEKDSEITSTRDELLSARdeillLHQAAAKVAsERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSF--- 654
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEEAE-----LKELQAELE-ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELaql 487
|
410 420 430
....*....|....*....|....*....|...
gi 1799135504 655 QLRCQQCEDQQReeatRLQGELEKLRKEWNALE 687
Cdd:TIGR02168 488 QARLDSLERLQE----NLEGFSEGVKALLKNQS 516
|
|
| CC1_T3JAM |
cd21912 |
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ... |
164-204 |
9.60e-09 |
|
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; TRAF3-interacting JNK-activating modulator (T3JAM), also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. The model corresponds to a conserved region that shows high sequence similarity with the first CC (CC1) domain of Sarcolemmal membrane-associated protein (SLMAP), which is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409288 [Multi-domain] Cd Length: 45 Bit Score: 51.58 E-value: 9.60e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1799135504 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21912 5 EILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
233-793 |
1.15e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 233 EDSLRKELIALQEDKhnyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVN 312
Cdd:COG1196 222 LKELEAELLLLKLRE------LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 313 EIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQAdndfTNERLTALQVRLEHLQEKTLKEC 392
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE----AEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 393 SSLGIQVDDFlpkingSTEKEHLLSKsggdctfIHQFIECQKKLIvegHLTKAVEETKLSKENQTRAKESDFSDTLSPSK 472
Cdd:COG1196 372 AELAEAEEEL------EELAEELLEA-------LRAAAELAAQLE---ELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 473 EKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKqkcfELQALLEEERKAYR 552
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL----EAEADYEGFLEGVK 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 553 NQVEES----------------TKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERD 616
Cdd:COG1196 512 AALLLAglrglagavavligveAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAA 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 617 TDIASLQEELKKVrAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRE 696
Cdd:COG1196 592 LARGAIGAAVDLV-ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 697 NVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKT-Q 775
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLeE 750
|
570
....*....|....*...
gi 1799135504 776 TVLSELKLKFEMTEQEKQ 793
Cdd:COG1196 751 EALEELPEPPDLEELERE 768
|
|
| FHA_TCF19 |
cd22685 |
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ... |
29-119 |
1.17e-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: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 29 KIGRSVARCRPAQNNATFDcKVLSRNHALVW---FDHKTGKFYLQDTkSSNGTFINSQRLSRGSEEsppcEILSGDIIQF 105
Cdd:cd22685 31 RIGRNPEVCDVFLCSSQHP-NLISREHAEIHaerDGNGNWKVLIEDR-STNGTYVNDVRLQDGQRR----ELSDGDTITF 104
|
90
....*....|....*.
gi 1799135504 106 G--VDVTENTRKVTHG 119
Cdd:cd22685 105 GhkNGRRVKQWPYQKS 120
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
555-811 |
1.83e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 555 VEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDtdiaSLQEELKKVRAELE 634
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELE----ELTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 635 RWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEAtRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNS 714
Cdd:TIGR02168 271 ELRLEVSELEEEIEELQKELYALANEISRLEQQKQ-ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 715 QKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQK-EYEKTQTVLSELKLKFEMTEQEKQ 793
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERlEARLERLEDRRERLQQEIEELLKK 429
|
250
....*....|....*...
gi 1799135504 794 SITDELKQCKNNLKLLRE 811
Cdd:TIGR02168 430 LEEAELKELQAELEELEE 447
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
256-786 |
2.32e-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: 57.88 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 256 ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQE---ELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQ 332
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETElcaEAEEMRARLAARKQELEEILHELESRLEEEEERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 333 QKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVR---LEHLQEKTLKECSSLGIQVDDFLPKINGS 409
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDillLEDQNSKLSKERKLLEERISEFTSNLAEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 410 TEKEHLLSKsggdctfihqfiecqkkLIVEGHLTKAVEETKLSKENQTRAKesdfsdtLSPSKEKSSDDTTDAQMDEQDL 489
Cdd:pfam01576 172 EEKAKSLSK-----------------LKNKHEAMISDLEERLKKEEKGRQE-------LEKAKRKLEGESTDLQEQIAEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 490 NEPLA--KVSLLK--DDLQGAQSEIEAKQ-----------EIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQ 554
Cdd:pfam01576 228 QAQIAelRAQLAKkeEELQAALARLEEETaqknnalkkirELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 555 VEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSAR-------DEILLLHQAAAKVASERDTDIASLQEELK 627
Cdd:pfam01576 308 LEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRqkhtqalEELTEQLEQAKRNKANLEKAKQALESENA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 628 KVRAELERWRKAASEYE---KEITSLQNSFQLRCQQCEDQQREEA---TRLQGELEKLRKEWNALETECHSLKRENVLLS 701
Cdd:pfam01576 388 ELQAELRTLQQAKQDSEhkrKKLEGQLQELQARLSESERQRAELAeklSKLQSELESVSSLLNEAEGKNIKLSKDVSSLE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 702 SELQRQEKELHNSQKQSLELTSDLsilqmsrKELENQVGSLKEQhlrdsadlktlLSKAENQAKDVQKEYEKTQTVLSEL 781
Cdd:pfam01576 468 SQLQDTQELLQEETRQKLNLSTRL-------RQLEDERNSLQEQ-----------LEEEEEAKRNVERQLSTLQAQLSDM 529
|
....*
gi 1799135504 782 KLKFE 786
Cdd:pfam01576 530 KKKLE 534
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
506-745 |
2.48e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 506 AQSEIEAKQEIQHLRKELIEAQELARTSKQKcfelQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREekds 585
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 586 EITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQnsfqlrcqqcedQQ 665
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR------------AD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 666 REEATRLQGELEKLRKEWNALETEchsLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQ 745
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAE---LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
14-110 |
2.83e-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: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 14 SHPFQERHV---YLDEPIKIGRSvARCRPAQNNATfdckvLSRNHALVW---FDHKTG-KFYLQDTkSSNGTFINSQRLS 86
Cdd:cd22670 7 SSPGSTDIVlpiYKNQVITIGRS-PSCDIVINDPF-----VSRTHCRIYsvqFDESSApLVYVEDL-SSNGTYLNGKLIG 79
|
90 100
....*....|....*....|....*
gi 1799135504 87 RGseespPCEILS-GDIIQFGVDVT 110
Cdd:cd22670 80 RN-----NTVLLSdGDVIEIAHSAT 99
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
28-85 |
4.61e-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: 4.61e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135504 28 IKIGRSvarcrPAQNNATFDCKVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRL 85
Cdd:smart00240 1 VTIGRS-----SEDCDIQLDGPSISRRHAVIVYD-GGGRFYLIDLGSTNGTFVNGKRI 52
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
267-812 |
1.02e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.80 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 267 EVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKI 346
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 347 DEMEEKEQE---LQAKIEALQADNDFTNERLTALQVRLEHLQEK---TLKECSSLGIQVDDFLPKINgstEKEHLLSKSG 420
Cdd:TIGR04523 117 EQKNKLEVElnkLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKyndLKKQKEELENELNLLEKEKL---NIQKNIDKIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 421 GDCTFIHQFIECQKKLIvEGHLTKAVEETKLSKENQTrakesdFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLK 500
Cdd:TIGR04523 194 NKLLKLELLLSNLKKKI-QKNKSLESQISELKKQNNQ------LKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 501 DDLQGAQSEIE-AKQEIQHLRKELIEAQ-ELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTEN 578
Cdd:TIGR04523 267 KQLSEKQKELEqNNKKIKELEKQLNQLKsEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 579 LREE---KDSEITSTRDELLSARDEILLLHqaaaKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQ 655
Cdd:TIGR04523 347 LKKEltnSESENSEKQRELEEKQNEIEKLK----KENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 656 LRCQQCED------QQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQ 729
Cdd:TIGR04523 423 LLEKEIERlketiiKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLN 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 730 MSRKELENQVGSLKEQH---LRDSADLKTLLSKAENQAKDVQKEYEKTQTVLselklKFEMTEQEKQSITDELKQCKNNL 806
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKIsslKEKIEKLESEKKEKESKISDLEDELNKDDFEL-----KKENLEKEIDEKNKEIEELKQTQ 577
|
....*.
gi 1799135504 807 KLLREK 812
Cdd:TIGR04523 578 KSLKKK 583
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
504-689 |
2.84e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 504 QGAQSEIEAK-QEIQHLRKELIEAQELARTSKQKcfelQALLEEERKAYRNQVEESTKQIQVLQAQLQRlhidtENLREE 582
Cdd:COG4913 606 FDNRAKLAALeAELAELEEELAEAEERLEALEAE----LDALQERREALQRLAEYSWDEIDVASAEREI-----AELEAE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 583 KDsEITSTRDELLSARDEILLLHQAAAKVASERD---TDIASLQEELKKVRAELERWRKAASEYEKEITSLQNS-FQLRC 658
Cdd:COG4913 677 LE-RLDASSDDLAALEEQLEELEAELEELEEELDelkGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERF 755
|
170 180 190
....*....|....*....|....*....|...
gi 1799135504 659 QQ--CEDQQREEATRLQGELEKLRKEWNALETE 689
Cdd:COG4913 756 AAalGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
27-106 |
3.75e-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: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 27 PIKIGRSVARcRPAQNNATFDC-----KVLSRNHALVWFDHKTGKFYLQdTKSSNGTFINSQRLSRGseeSPPCEILSGD 101
Cdd:cd22701 18 EVVLGRNSKN-SSSTAADSVDIdlgpsKKISRRHARIFYDFTTQCFELS-VLGRNGVKVDGILVKPG---SPPVPLRSGS 92
|
....*
gi 1799135504 102 IIQFG 106
Cdd:cd22701 93 LIQIG 97
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
289-557 |
5.61e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.09 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 289 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALqadnd 368
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEEL----- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 369 ftNERLTALQVRLEHlQEKTLKECSSLGIQVDDFLPKINgsteKEHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKAVEE 448
Cdd:PHA02562 240 --TDELLNLVMDIED-PSAALNKLNTAAAKIKSKIEQFQ----KVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 449 TKLSKENQTRAKEsdfsdtlspskEKSSDDTTDAQMDEQDLNeplAKVSLLKDDLQGAQSEI-EAKQEIQHLRKE-LIEA 526
Cdd:PHA02562 313 HSLEKLDTAIDEL-----------EEIMDEFNEQSKKLLELK---NKISTNKQSLITLVDKAkKVKAAIEELQAEfVDNA 378
|
250 260 270
....*....|....*....|....*....|.
gi 1799135504 527 QELArtskqkcfELQALLEEERKAYRNQVEE 557
Cdd:PHA02562 379 EELA--------KLQDELDKIVKTKSELVKE 401
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
211-635 |
5.92e-07 |
|
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: 53.52 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 211 DRLLSRLEVMGNQLQACSKNQTEdsLRKELIALQEDkhnyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLK 290
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAE--LRKELEELEEE-----------LEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 291 EMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEgkqeeiqqkgqAEKKELQHKIDEMEEKEQELQAKIEALQADNDFT 370
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAE-----------AEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 371 NERLTALQVRLEHLQEKTlkecsslgiqvddflpkinGSTEKEhllsksggdCTFIHQFIECQKKLIVEghLTKAVEETK 450
Cdd:TIGR02168 816 NEEAANLRERLESLERRI-------------------AATERR---------LEDLEEQIEELSEDIES--LAAEIEELE 865
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 451 LSKENQTRAKESdFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEA-KQEIQHLRKELIEAQEL 529
Cdd:TIGR02168 866 ELIEELESELEA-LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQlELRLEGLEVRIDNLQER 944
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 530 ARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDT-ENLREEKD--SEITSTRDELLSARDEILLLHQ 606
Cdd:TIGR02168 945 LSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAiEEYEELKEryDFLTAQKEDLTEAKETLEEAIE 1024
|
410 420
....*....|....*....|....*....
gi 1799135504 607 AAAKVASERdtdiasLQEELKKVRAELER 635
Cdd:TIGR02168 1025 EIDREARER------FKDTFDQVNENFQR 1047
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
553-717 |
7.45e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 7.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 553 NQVEESTKQIQVLQAQLQRLHIDTENLrEEKDSEITSTRDELLSARDEILLLHQAAAKVA-----SERDTDIASLQEELK 627
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEEL-EELEEELEELEAELEELREELEKLEKLLQLLPlyqelEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 628 KVRAELERWRKAASEY---EKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSEL 704
Cdd:COG4717 150 ELEERLEELRELEEELeelEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170
....*....|...
gi 1799135504 705 QRQEKELHNSQKQ 717
Cdd:COG4717 230 EQLENELEAAALE 242
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
25-114 |
9.30e-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: 9.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 25 DEPIKIGRSVArcrpAQNNATFDC-KVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDII 103
Cdd:cd22663 20 GKEVTVGRGLG----VTYQLVSTCpLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERI----EPLKPYPLNEGDLI 90
|
90
....*....|.
gi 1799135504 104 QFGVDVTENTR 114
Cdd:cd22663 91 QLGVPPENKEP 101
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
26-106 |
1.25e-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: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 26 EPIKIGRSVArcrpaqNNATFDCKVLSRNHALVwfDHKTGKFYLQDTKSSNGTFINSQRLSRGseesppcEILSGDIIQF 105
Cdd:cd22698 21 DEFTIGRSSN------NDIRLNDHSVSRHHARI--VRQGDKCNLTDLGSTNGTFLNGIRVGTH-------ELKHGDRIQL 85
|
.
gi 1799135504 106 G 106
Cdd:cd22698 86 G 86
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
234-688 |
1.26e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 234 DSLRKELIALQEDKHNYETtAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNER--TQEELRELANKYNGAV 311
Cdd:COG4717 74 KELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELeaLEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 312 NEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQ-------HKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHL 384
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEqlslateEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 385 QEKTLKECSSLGIQVDDFLPKINGStekehLLSKSGGDCTFIHQFIECQKKLIVEGHLTkAVEETKLSKENQTRAKESDF 464
Cdd:COG4717 233 ENELEAAALEERLKEARLLLLIAAA-----LLALLGLGGSLLSLILTIAGVLFLVLGLL-ALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 465 SDTLsPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLkddlqgaqseiEAKQEIQHLRKELIEAQELARTSKQKCF--ELQA 542
Cdd:COG4717 307 LQAL-PALEELEEEELEELLAALGLPPDLSPEELL-----------ELLDRIEELQELLREAEELEEELQLEELeqEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 543 LLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSeitstrdellsardeilLLHQAAAKVASERDTDIASL 622
Cdd:COG4717 375 LLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGE-----------------LEELLEALDEEELEEELEEL 437
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799135504 623 QEELKKVRAELERWRKAASEYEKEITSLQNSFQLrcqqceDQQREEATRLQGELEKLRKEWNALET 688
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEEDGEL------AELLQELEELKAELRELAEEWAALKL 497
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
212-811 |
1.28e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 52.36 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 212 RLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTAKESLRRVLQEKIEvvrkLSEVERSlSNTEDECTHLKE 291
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE----LDGFERG-PFSERQIKNFHT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 292 MNERTQEELRELANKyngavnEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQadndftn 371
Cdd:TIGR00606 398 LVIERQEDEAKTAAQ------LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ------- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 372 eRLTALQVRLEHLQEKTLKECSSlgiqvddfLPKINGSTEKEHLLSKSggdctfihQFIECQKKLIVEGHLTKAVEETKL 451
Cdd:TIGR00606 465 -QLEGSSDRILELDQELRKAERE--------LSKAEKNSLTETLKKEV--------KSLQNEKADLDRKLRKLDQEMEQL 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 452 SKENQTRAKesdfsdTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQElar 531
Cdd:TIGR00606 528 NHHTTTRTQ------MEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNK--- 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 532 tskqkcfELQAlLEEERKAYRNQVEESTKQIQVLqaqlqrlhidtenlrEEKDSEITSTRDEllsardeilllhqaaakv 611
Cdd:TIGR00606 599 -------ELAS-LEQNKNHINNELESKEEQLSSY---------------EDKLFDVCGSQDE------------------ 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 612 aserDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQC------EDQQREEATRLQGELEKLRKEWNA 685
Cdd:TIGR00606 638 ----ESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCqrvfqtEAELQEFISDLQSKLRLAPDKLKS 713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 686 LETECHSLKRENVLL-------SSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSL--KEQHLRDSADLKTL 756
Cdd:TIGR00606 714 TESELKKKEKRRDEMlglapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTImpEEESAKVCLTDVTI 793
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135504 757 LSKAENQAKDVQKEYEKTQTVL--SELKLKFEMTEQEKQSITDELKQCKNNLKLLRE 811
Cdd:TIGR00606 794 MERFQMELKDVERKIAQQAAKLqgSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
55-108 |
1.40e-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: 1.40e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1799135504 55 HALVWFDHKTGKFYLQDTKSSNGTFINSQRLSrgseESPPCEILSGDIIQFGVD 108
Cdd:cd22704 39 HAVITYDQIDNEFKIKDLGSLNGTFVNDSRIP----EQTYITLKLGDSIRFGYD 88
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
228-801 |
1.85e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 228 SKNQTEDSLRKELIALQEDKHNYETTAKESLRRVLQE--KIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELR-ELA 304
Cdd:PTZ00121 1096 AFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEarKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKaEDA 1175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 305 NKYNGA--------VNEIKDLSDKLKVAEGKQ-EEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLT 375
Cdd:PTZ00121 1176 KKAEAArkaeevrkAEELRKAEDARKAEAARKaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR 1255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 376 ALQ-VRLEHLQEKTLKECSSLGIQVDDFlpKINGSTEKEHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKAVEETKLSKE 454
Cdd:PTZ00121 1256 KFEeARMAHFARRQAAIKAEEARKADEL--KKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 455 NQTRAKESDFSDTLSPSKEKSSDDTTDA-----QMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQEl 529
Cdd:PTZ00121 1334 AKKKAEEAKKAAEAAKAEAEAAADEAEAaeekaEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK- 1412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 530 ARTSKQKCFELQALLEEERKA--YRNQVEESTKQIQVLQAQLQRLhiDTENLReeKDSEITSTRDELLSARDEILLLHQA 607
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAK--KAEEAK--KKAEEAKKADEAKKKAEEAKKADEA 1488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 608 AAKVA-SERDTDIASLQEELKKVRAELERWRKAASEYE-KEITSLQNSFQLRcqQCEDQQREEATRLQGELEKLRKEWNA 685
Cdd:PTZ00121 1489 KKKAEeAKKKADEAKKAAEAKKKADEAKKAEEAKKADEaKKAEEAKKADEAK--KAEEKKKADELKKAEELKKAEEKKKA 1566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 686 LETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLK----EQHLRDSADLKTLLSKAE 761
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkaEEEKKKVEQLKKKEAEEK 1646
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1799135504 762 NQAKDVQKEYEKTQTVLSELKLKfemtEQEKQSITDELKQ 801
Cdd:PTZ00121 1647 KKAEELKKAEEENKIKAAEEAKK----AEEDKKKAEEAKK 1682
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
542-717 |
2.40e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 542 ALLEEERKAYRNQVEESTKQIQVLQAQLQRLhiDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVaSERDTDIAS 621
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDAL--QERREALQRLAEYSWDEIDVASAEREIAELEAELERL-DASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 622 LQEELKKVRAELERWRKAASEYEKEITSLQNSFqlrcQQCEDQQREEATRLQGELEKLRKEWNA-LETECHSLKRENVL- 699
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKEL----EQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALGDAVEr 765
|
170 180
....*....|....*....|...
gi 1799135504 700 -----LSSELQRQEKELHNSQKQ 717
Cdd:COG4913 766 elrenLEERIDALRARLNRAEEE 788
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
486-651 |
3.32e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 486 EQDLNEPLAKVSLLKDDLQGAQSEI-EAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQ--- 561
Cdd:COG4942 40 EKELAALKKEEKALLKQLAALERRIaALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLgrq 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 562 -------------------------IQVLQAQLQRLHIDTENLREEKDsEITSTRDELLSARDEILLLHQAAAKVASERD 616
Cdd:COG4942 120 pplalllspedfldavrrlqylkylAPARREQAEELRADLAELAALRA-ELEAERAELEALLAELEEERAALEALKAERQ 198
|
170 180 190
....*....|....*....|....*....|....*
gi 1799135504 617 TDIASLQEELKKVRAELERWRKAASEYEKEITSLQ 651
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
622-812 |
3.41e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 622 LQEELKKVRAELERWRKAASEYeKEITSLQNSFQLRCQQCEDQQREEatrlqgELEKLRKEWNALETECHSLKRENVLLS 701
Cdd:COG1196 194 ILGELERQLEPLERQAEKAERY-RELKEELKELEAELLLLKLRELEA------ELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 702 SELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQhlrdSADLKTLLSKAENQAKDVQKEYEKTQTVLSEL 781
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER----RRELEERLEELEEELAELEEELEELEEELEEL 342
|
170 180 190
....*....|....*....|....*....|.
gi 1799135504 782 KLKFEMTEQEKQSITDELKQCKNNLKLLREK 812
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
|
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
496-633 |
4.29e-06 |
|
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.
Pssm-ID: 462015 [Multi-domain] Cd Length: 198 Bit Score: 48.46 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 496 VSLLKDDLQGAQSEIEAK-QEIQHLRKELIEAQELARTSKQKCFELQAlleeerkayrnQVEESTKQIQVLQAQLQRLHI 574
Cdd:pfam06818 12 ISLLKQQLKDSQAEVTQKlNEIVALRAQLRELRAKLEEKEEQIQELED-----------SLRSKTLELEVCENELQRKKN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799135504 575 DTENLRE---EKDSEITSTRDEL--LSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAEL 633
Cdd:pfam06818 81 EAELLREkvgKLEEEVSGLREALsdVSPSGYESVYESDEAKEQRQEEADLGSLRREVERLRAEL 144
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
27-117 |
5.42e-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: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 27 PIKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLsrgSEESPPCEILSGDIIQFG 106
Cdd:cd22678 24 PLTIGRIQ------RGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESI---SPNGRPVVLSSGDVITLG 94
|
90
....*....|.
gi 1799135504 107 vdvTENTRKVT 117
Cdd:cd22678 95 ---SETKILVR 102
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
449-746 |
8.88e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.66 E-value: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 449 TKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQdLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQE 528
Cdd:TIGR00606 758 RDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMER-FQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQH 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 529 LARTSKQKCFELQALLEEERKAYRN----QVEESTKQIQVLQAQLQRLHIDTENlrEEKDSEITSTRDELLSARDEILLL 604
Cdd:TIGR00606 837 ELDTVVSKIELNRKLIQDQQEQIQHlkskTNELKSEKLQIGTNLQRRQQFEEQL--VELSTEVQSLIREIKDAKEQDSPL 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 605 HQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGEL-------E 677
Cdd:TIGR00606 915 ETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLeecekhqE 994
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799135504 678 KLRKEWNALETECHSLKRENVLLSSELQRQE-----KELHNSQKQSLELTSDLSILQMSR--KELENQVGSLKEQH 746
Cdd:TIGR00606 995 KINEDMRLMRQDIDTQKIQERWLQDNLTLRKrenelKEVEEELKQHLKEMGQMQVLQMKQehQKLEENIDLIKRNH 1070
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
51-106 |
1.10e-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: 1.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799135504 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 |
1.29e-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: 1.29e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135504 52 SRNH-ALVWfdHK-TGKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22674 48 SRVHaALVY--HKhLNRVFLIDLGSTHGTFVGGIRL----EPHKPQQLPIDSTLRFG 98
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
182-693 |
1.44e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 182 LEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgnqlqacSKNQTEDSLRKELIALQEDKHNYETTaKESLRRV 261
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHE---------ERREELETLEAEIEDLRETIAETERE-REELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 262 LQEKIEVVRKLSEVERSL-----------SNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEE 330
Cdd:PRK02224 281 VRDLRERLEELEEERDDLlaeaglddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 331 IQQKGQAEKKELQH---KIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLKECSSLGIQVDDFLPKIN 407
Cdd:PRK02224 361 LREEAAELESELEEareAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 408 GSTEKEHLLSKsgGDCTfihqfiECQKKLIVEGHLtKAVEETKLSKENQTRAKEsDFSDTLSpSKEKSSDDTTDAQMDEQ 487
Cdd:PRK02224 441 RVEEAEALLEA--GKCP------ECGQPVEGSPHV-ETIEEDRERVEELEAELE-DLEEEVE-EVEERLERAEDLVEAED 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 488 DLNEPLAKVSLLKDDLQGAQSEIEAKQE-IQHLRKeliEAQELARTSKQKcfelqallEEERKAYRNQVEESTKQIQVLQ 566
Cdd:PRK02224 510 RIERLEERREDLEELIAERRETIEEKRErAEELRE---RAAELEAEAEEK--------REAAAEAEEEAEEAREEVAELN 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 567 AQLQRLHIDTENLR--EEKDSEITSTRDELLSARDEilllHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYE 644
Cdd:PRK02224 579 SKLAELKERIESLEriRTLLAAIADAEDEIERLREK----REALAELNDERRERLAEKRERKRELEAEFDEARIEEARED 654
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135504 645 KEITSlqnSFQLRCQQCEDQQREEATRLQG----------ELEKLRKEWNALETECHSL 693
Cdd:PRK02224 655 KERAE---EYLEQVEEKLDELREERDDLQAeigaveneleELEELRERREALENRVEAL 710
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
28-106 |
1.96e-05 |
|
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438732 [Multi-domain] Cd Length: 96 Bit Score: 43.87 E-value: 1.96e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135504 28 IKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDhkTGKFYLQDTKSSNGTFINSQRlsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22680 23 VSIGRDP------ENVIVIPDPFVSRNHARITVD--SNEIYIEDLGSTNGTFVNDFK-----RIKGPAKLHPNDIIKLG 88
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
258-387 |
2.05e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 258 LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQ----- 332
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkey 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1799135504 333 QKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEK 387
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
544-772 |
2.08e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 48.15 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 544 LEEERKAY---RNQVEESTKQIQVLQAQLQRLHIDTENLR------EEKDSEITSTRDELLSARD------EILLLHQAA 608
Cdd:pfam05622 171 LEEELKKAnalRGQLETYKRQVQELHGKLSEESKKADKLEfeykklEEKLEALQKEKERLIIERDtlretnEELRCAQLQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 609 AKVASERDTDIASLQEELKKVRAELerwrkAASEYEKEITSLQNSFQ-LRCQQcEDQQREEATRLQGELEKLRKEWNALE 687
Cdd:pfam05622 251 QAELSQADALLSPSSDPGDNLAAEI-----MPAEIREKLIRLQHENKmLRLGQ-EGSYRERLTELQQLLEDANRRKNELE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 688 TEcHSLKRENVLLSS----ELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQ--HLRDSADLKTLLSKAE 761
Cdd:pfam05622 325 TQ-NRLANQRILELQqqveELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQieELEPKQDSNLAQKIDE 403
|
250
....*....|.
gi 1799135504 762 NQAKDVQKEYE 772
Cdd:pfam05622 404 LQEALRKKDED 414
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
289-794 |
2.21e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 289 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKgQAEKKELQHKIDEMEEKEQELQAKIEALQADND 368
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 369 F---------TNERLTALQVRLEHLQEKtlkecsslgiqvddflpkingstekehllsksggdctfIHQFIECQKKLive 439
Cdd:COG4717 127 LlplyqeleaLEAELAELPERLEELEER--------------------------------------LEELRELEEEL--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 440 ghltKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHL 519
Cdd:COG4717 166 ----EELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 520 RKELIEAQELARTskqkcFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARD 599
Cdd:COG4717 242 EERLKEARLLLLI-----AAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 600 EILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAAS--------EYEKEITSLQNSFQLrcqQCEDQQREEATR 671
Cdd:COG4717 317 EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEleeelqleELEQEIAALLAEAGV---EDEEELRAALEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 672 LQgELEKLRKEWNALETECHSLKRENVLLSSELQRQ--EKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHlrD 749
Cdd:COG4717 394 AE-EYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREELAELEAELEQLEEDG--E 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1799135504 750 SADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 794
Cdd:COG4717 471 LAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLP 515
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
567-782 |
2.42e-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: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 567 AQLQRLHIDTENLREEKD--SEITSTRDELLSARDEILLLHQAAAKVASERD-TDIASLQEELKKVRAELERWRKAASEY 643
Cdd:COG4913 235 DDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAqRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 644 EKEITSLQNsfqlRCQQCEDQQREEATRlqgELEKLRKEWNALETECHSLKREnvllSSELQRQEKELHnsqkqsLELTS 723
Cdd:COG4913 315 EARLDALRE----ELDELEAQIRGNGGD---RLEQLEREIERLERELEERERR----RARLEALLAALG------LPLPA 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135504 724 DLSILQMSRKELENQVGSLKEQHlrdsADLKTLLSKAENQAKDVQKEYEKTQTVLSELK 782
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEEL----EALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| FHA_RAD53-like_rpt2 |
cd22690 |
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
12-103 |
3.16e-05 |
|
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine/threonine-protein kinase RAD53 and similar proteins; RAD53, also called CHEK2 homolog, or serine-protein kinase 1 (Spk1), is a nuclear protein kinase that phosphorylates proteins on serine, threonine, and tyrosine. It controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints and prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. It may be involved in the phosphorylation of RPH1. RAD53 contains two FHA domains. This model corresponds to the second one. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438742 [Multi-domain] Cd Length: 105 Bit Score: 43.82 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 12 PNSHPfqerHVYL-DEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFD-HKTGK--FYLQDTkSSNGTFINSQRLSR 87
Cdd:cd22690 8 NPSYP----DIELtQNTTFIGRS------KDCDEEITDPRISKHHCIITRKrSGKGLddVYVTDT-STNGTFINNNRLGK 76
|
90
....*....|....*.
gi 1799135504 88 GSEesppCEILSGDII 103
Cdd:cd22690 77 GSQ----SLLQDGDEI 88
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
256-815 |
3.27e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.79 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 256 ESLRRVLQEKIEVVRKLSEVERSlsntedECTHLKEMNERTQEELRELANKYNGAV---NEIKDLSDKLKVAEGKQEEIQ 332
Cdd:pfam05483 98 EAELKQKENKLQENRKIIEAQRK------AIQELQFENEKVSLKLEEEIQENKDLIkenNATRHLCNLLKETCARSAEKT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 333 QKGQAEKKE-------LQHKIDEMEEKEQELQAKIEALQADNDFtneRLTALQVRLEHLQEKTLKECSSLGIQVDDFLPK 405
Cdd:pfam05483 172 KKYEYEREEtrqvymdLNNNIEKMILAFEELRVQAENARLEMHF---KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQ 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 406 IngsTEKEHLLSksggDCTFIhqfiecqkkliveghltkaVEETKlSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMD 485
Cdd:pfam05483 249 I---TEKENKMK----DLTFL-------------------LEESR-DKANQLEEKTKLQDENLKELIEKKDHLTKELEDI 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 486 EQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQAL-LEEERKAYRNQVEESTKQIQV 564
Cdd:pfam05483 302 KMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCsLEELLRTEQQRLEKNEDQLKI 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 565 LQAQLQRlhidtenlreeKDSEItstrdellsardeilllhQAAAKVASERDTDIaslqEELKKVRAELERWRKAASEYE 644
Cdd:pfam05483 382 ITMELQK-----------KSSEL------------------EEMTKFKNNKEVEL----EELKKILAEDEKLLDEKKQFE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 645 KEITSLQNSFQlrcqqcedqqreeatRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSD 724
Cdd:pfam05483 429 KIAEELKGKEQ---------------ELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAH 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 725 LSILQMSRKELENQVGSL--------------KEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQ 790
Cdd:pfam05483 494 CDKLLLENKELTQEASDMtlelkkhqediincKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEE 573
|
570 580
....*....|....*....|....*
gi 1799135504 791 EKQSITDELKQCKNNLKLLREKGNN 815
Cdd:pfam05483 574 NARSIEYEVLKKEKQMKILENKCNN 598
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
512-734 |
3.53e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 512 AKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAY---RNQVEESTKQIQVLQAQLQRLHIDTENLREE------ 582
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYnelQAELEALQAEIDKLQAEIAEAEAEIEERREElgerar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 583 ---KDSEITSTRDELLSARDEILLLHQAAA-KVASERDTDIAslqEELKKVRAELERWRKAASEYEKEITSLQnsfqlrc 658
Cdd:COG3883 94 alyRSGGSVSYLDVLLGSESFSDFLDRLSAlSKIADADADLL---EELKADKAELEAKKAELEAKLAELEALK------- 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799135504 659 qqceDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKE 734
Cdd:COG3883 164 ----AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
478-639 |
4.03e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 478 DTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIE-AKQEIQHLRKELIEAQELARTSKQKcfelQALLEEERKAYRNQVE 556
Cdd:COG4913 662 DVASAEREIAELEAELERLDASSDDLAALEEQLEeLEAELEELEEELDELKGEIGRLEKE----LEQAEEELDELQDRLE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 557 ESTKQIQV-----LQAQLQRLHID--TENLREEKDSEITSTRDELLSARDEILLLHQAAAKV----ASERDTDIASL--- 622
Cdd:COG4913 738 AAEDLARLelralLEERFAAALGDavERELRENLEERIDALRARLNRAEEELERAMRAFNREwpaeTADLDADLESLpey 817
|
170 180
....*....|....*....|..
gi 1799135504 623 QEELKKVRAE-----LERWRKA 639
Cdd:COG4913 818 LALLDRLEEDglpeyEERFKEL 839
|
|
| FHA_CHFR |
cd22672 |
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ... |
49-105 |
4.07e-05 |
|
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains protein (CHFR); CHFR, also called RING finger protein 196 (RNF196), is a checkpoint protein that delays entry into mitosis in response to stress. It functions as an E3 ubiquitin ligase that ubiquitinates and degrades its target proteins, such as Aurora-A, Plk1, Kif22 and PARP-1, which are critical for proper mitotic transitions. It also plays an important role in cell cycle progression and tumor suppression and is negatively regulated by SUMOylation-mediated proteasomal ubiquitylation. Moreover, CHFR is involved in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation. CHFR contains a fork head associated-(FHA) domain and a RING-HC finger. The CHFR FHA domain has been crystallized as a segment-swapped dimer. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438724 [Multi-domain] Cd Length: 108 Bit Score: 43.43 E-value: 4.07e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135504 49 KVLSRNHALVWFDHKtGKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQF 105
Cdd:cd22672 39 KLVSGDHCKIIRDEK-GQVWLEDT-STNGTLVNKVKVVKGQK----VELKHGDVIYL 89
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
25-108 |
4.43e-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: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 25 DEPIKIGRsvarcRPAQNNAT----FDCKVLSRNHALVWFdhKTGKFYLQDTKSSNGTFINSQRLSR-GSEESPPCEILS 99
Cdd:cd22702 31 KQPCIIGS-----DPHQAISGisvvIPSPQVSELHARITC--KNGAFFLTDLGSEHGTWINDNEGRRyRAPPNFPVRLHP 103
|
....*....
gi 1799135504 100 GDIIQFGVD 108
Cdd:cd22702 104 SDVIEFGSD 112
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
14-106 |
4.51e-05 |
|
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.
Pssm-ID: 438734 [Multi-domain] Cd Length: 96 Bit Score: 42.90 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 14 SHPFQERHvyldepIKIGRSVarcrpaQNNATFDCKVLSRNHALvwFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEesp 93
Cdd:cd22682 14 QFPITEST------IVIGRSV------ESQVQIDDDSVSRYHAK--LAVNPSAVSIIDLGSTNGTIVNGKKIPKLAS--- 76
|
90
....*....|...
gi 1799135504 94 pCEILSGDIIQFG 106
Cdd:cd22682 77 -CDLQNGDQIKIG 88
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
559-771 |
4.69e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 559 TKQIQVLQAQLQRLhidtenlrEEKDSEITSTRDELLSARDEILLLHQAAAKVA--SERDTDIASLQEELKKVRAELERW 636
Cdd:COG4913 609 RAKLAALEAELAEL--------EEELAEAEERLEALEAELDALQERREALQRLAeySWDEIDVASAEREIAELEAELERL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 637 RKAASEYEkeitslqnsfqlrcqqcedqqreeatRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQK 716
Cdd:COG4913 681 DASSDDLA--------------------------ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799135504 717 QSLELTSDLSILQmsRKELENQVGSLKEQHLRDS---------ADLKTLLSKAENQAKDVQKEY 771
Cdd:COG4913 735 RLEAAEDLARLEL--RALLEERFAAALGDAVERElrenleeriDALRARLNRAEEELERAMRAF 796
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
502-652 |
4.73e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 502 DLQGAQSEIE-AKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRN----QVEESTKQIQVLQAQLQRLhidt 576
Cdd:COG4913 282 RLWFAQRRLElLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEER---- 357
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799135504 577 ENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQN 652
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
18-86 |
5.32e-05 |
|
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the first FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438746 [Multi-domain] Cd Length: 93 Bit Score: 42.70 E-value: 5.32e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135504 18 QERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhkTGKFYLQDTKSSNGTFINSQRLS 86
Cdd:cd22694 8 GELRFDPGSSVRIGRD------PDADVRLDDPRVSRRHALLEFD--GDGWVYTDLGSRNGTYLNGRRVQ 68
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
13-110 |
7.11e-05 |
|
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also called nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438717 [Multi-domain] Cd Length: 97 Bit Score: 42.22 E-value: 7.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 13 NSHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTgkFYLQDTKSSNGTFINSQRLSrgsee 91
Cdd:cd22665 7 SQAHGPEKDFPLYEgENVIGRD------PSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRL----- 73
|
90 100
....*....|....*....|.
gi 1799135504 92 SPPC--EILSGDIIQFGvDVT 110
Cdd:cd22665 74 KPNVryELIDGDLLLFG-DVK 93
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
310-387 |
7.68e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 7.68e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135504 310 AVNEIKDLSDKLKVAEGKQEEIQqkgqAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEK 387
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQ----AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
153-388 |
8.93e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 8.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 153 VAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQAcSKNQT 232
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA-ELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 233 EDSLRKELIALQEDKHNYETTAKESLRRVLQEKIEVV---RKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKyng 309
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLlspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL--- 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135504 310 aVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKT 388
Cdd:COG4942 166 -RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
327-795 |
1.25e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 327 KQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQA------------DNDFTNERLTALQVRLEHLQEK------- 387
Cdd:TIGR00618 236 QQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAqeavleetqeriNRARKAAPLAAHIKAVTQIEQQaqrihte 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 388 ---TLKECSSLGIQVDDFLPKINGSTEKEHLLSKSGGDCtfIHQFIECQKKLIVEGHLTKAVEETKLSKENQtRAKESDF 464
Cdd:TIGR00618 316 lqsKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQE--IHIRDAHEVATSIREISCQQHTLTQHIHTLQ-QQKTTLT 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 465 SDTLSPSKEKSSDDTTDAQMDEQDLNEplakvSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQelARTSKQKCFELQALL 544
Cdd:TIGR00618 393 QKLQSLCKELDILQREQATIDTRTSAF-----RDLQGQLAHAKKQQELQQRYAELCAAAITCT--AQCEKLEKIHLQESA 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 545 EEERKayRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTdIASLQE 624
Cdd:TIGR00618 466 QSLKE--REQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQT-YAQLET 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 625 ELKKVRAELERWRKAASEYEKEITSLQNSFQlRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSEL 704
Cdd:TIGR00618 543 SEEDVYHQLTSERKQRASLKEQMQEIQQSFS-ILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKL 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 705 Q----RQEKELHNSQKQSLEltsDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSE 780
Cdd:TIGR00618 622 QpeqdLQDVRLHLQQCSQEL---ALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEM 698
|
490
....*....|....*
gi 1799135504 781 LKLKFEMTEQEKQSI 795
Cdd:TIGR00618 699 LAQCQTLLRELETHI 713
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
608-824 |
1.77e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 608 AAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQlRCQQCEDQQREEATRLQGELEKLRKEwnaLE 687
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE-ALQAEIDKLQAEIAEAEAEIEERREE---LG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 688 TECHSLKRE-------NVLLSSE-----LQRQE--KELHNSQKQSLELTSDLsilqmsRKELENQVGSLKEQhlrdSADL 753
Cdd:COG3883 90 ERARALYRSggsvsylDVLLGSEsfsdfLDRLSalSKIADADADLLEELKAD------KAELEAKKAELEAK----LAEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799135504 754 KTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNNPSILQPVPA 824
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
337-689 |
2.01e-04 |
|
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: 45.05 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 337 AEKKELQHKIDEMEEKEQELQAKIEAlqadndfTNERLTALQVRLEHLQEKTLKECSSLgiqvddfLPKINGSTEKEHLL 416
Cdd:pfam13166 89 EESIEIQEKIAKLKKEIKDHEEKLDA-------AEANLQKLDKEKEKLEADFLDECWKK-------IKRKKNSALSEALN 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 417 SKSGgdctfihqfiecqkkliveghltkavEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTT---DAQMDEQDLNEPL 493
Cdd:pfam13166 155 GFKY--------------------------EANFKSRLLREIEKDNFNAGVLLSDEDRKAALATvfsDNKPEIAPLTFNV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 494 A------KVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKC--------FELQALLEE------------- 546
Cdd:pfam13166 209 IdfdaleKAEILIQKVIGKSSAIEELIKNPDLADWVEQGLELHKAHLDTCpfcgqplpAERKAALEAhfddeftefqnrl 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 547 --------------------------ERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREE--KDSEITSTRDELLSAR 598
Cdd:pfam13166 289 qkliekvesaissllaqlpavsdlasLLSAFELDVEDIESEAEVLNSQLDGLRRALEAKRKDpfKSIELDSVDAKIESIN 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 599 DEILLLHQAAAKvASERDTDIASLQEELKKvraelERWRKAASEYEKEITSLQNSFQLRCQQCEDQQrEEATRLQGELEK 678
Cdd:pfam13166 369 DLVASINELIAK-HNEITDNFEEEKNKAKK-----KLRLHLVEEFKSEIDEYKDKYAGLEKAINSLE-KEIKNLEAEIKK 441
|
410
....*....|.
gi 1799135504 679 LRKEWNALETE 689
Cdd:pfam13166 442 LREEIKELEAQ 452
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
513-708 |
2.04e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 513 KQEIQHLRKELIEAQELARTSKQKcfELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRD 592
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQK--NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 593 ELLSARDEILL--LHQAAAKVASERDT------DIASLQEELKKVRAEL-ERWRKAASEYEKEITSLQNSfqlrcqqcED 663
Cdd:COG3206 259 LLQSPVIQQLRaqLAELEAELAELSARytpnhpDVIALRAQIAALRAQLqQEAQRILASLEAELEALQAR--------EA 330
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1799135504 664 QQREEATRLQGELEKLrkewNALETECHSLKRE----NVLLSSELQRQE 708
Cdd:COG3206 331 SLQAQLAQLEARLAEL----PELEAELRRLEREvevaRELYESLLQRLE 375
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
478-651 |
2.13e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 478 DTTDAQMDE--QDLNEPLAKVSLLKDDLQGAQSEI-EAKQEIQHLRKELIE-AQELARTSKQKCFeLQALLEEE------ 547
Cdd:COG3883 40 DALQAELEElnEEYNELQAELEALQAEIDKLQAEIaEAEAEIEERREELGErARALYRSGGSVSY-LDVLLGSEsfsdfl 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 548 -RKAYRNQVEESTKQ-IQVLQAQLQRLhidtenlrEEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEE 625
Cdd:COG3883 119 dRLSALSKIADADADlLEELKADKAEL--------EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
|
170 180
....*....|....*....|....*.
gi 1799135504 626 LKKVRAELERWRKAASEYEKEITSLQ 651
Cdd:COG3883 191 EAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
485-696 |
2.32e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 485 DEQDLNEPLAKVSLLKDDLQGAQSEIEAKQ-EIQHLRKELIEAQELARTSKQKCFELQALlEEERKAYRNQVEESTKQIQ 563
Cdd:COG4913 645 ERREALQRLAEYSWDEIDVASAEREIAELEaELERLDASSDDLAALEEQLEELEAELEEL-EEELDELKGEIGRLEKELE 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 564 VLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERD---TDIASLQEELKKVRAE-LERWRKA 639
Cdd:COG4913 724 QAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDalrARLNRAEEELERAMRAfNREWPAE 803
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135504 640 ASEYEKEITSLqNSFQlrcQQCEDQQREEATRLQGELEKLRKEW--NALETECHSLKRE 696
Cdd:COG4913 804 TADLDADLESL-PEYL---ALLDRLEEDGLPEYEERFKELLNENsiEFVADLLSKLRRA 858
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
212-635 |
2.47e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 212 RLLSRLEVMGNQLQACSKNQTEdsLRKELIALQEDKHNYETTAK-ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLK 290
Cdd:COG4717 92 ELQEELEELEEELEELEAELEE--LREELEKLEKLLQLLPLYQElEALEAELAELPERLEELEERLEELRELEEELEELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 291 EMNERTQEELRELANKYNGAV-NEIKDLSDKLKVAegkqeeiqqkgQAEKKELQHKIDEMEEKEQELQAKIEALQADndf 369
Cdd:COG4717 170 AELAELQEELEELLEQLSLATeEELQDLAEELEEL-----------QQRLAELEEELEEAQEELEELEEELEQLENE--- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 370 tnERLTALQVRLEHLQEKTLKECSSLGIQVDDFLPKINGSTEKEHLLSKSGGdctFIHQFIECQKKLIVEGHLTKAVEET 449
Cdd:COG4717 236 --LEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL---LALLFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 450 KLSKENQTRAKESDFSDtLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHL----RKELIE 525
Cdd:COG4717 311 PALEELEEEELEELLAA-LGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAgvedEEELRA 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 526 AQELARTSKQkcfelqalLEEERKAYRNQVEESTKQIQVLQAQLqrlhiDTENLREekdsEITSTRDELLSARDEILLLH 605
Cdd:COG4717 390 ALEQAEEYQE--------LKEELEELEEQLEELLGELEELLEAL-----DEEELEE----ELEELEEELEELEEELEELR 452
|
410 420 430
....*....|....*....|....*....|....*
gi 1799135504 606 QAAAKVAS-----ERDTDIASLQEELKKVRAELER 635
Cdd:COG4717 453 EELAELEAeleqlEEDGELAELLQELEELKAELRE 487
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
52-107 |
2.49e-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: 2.49e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799135504 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 |
2.91e-04 |
|
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442679 [Multi-domain] Cd Length: 402 Bit Score: 43.98 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 1 MPSALAIFTCRPNSHPFQERHVYLDEPIKIGRSvARC-----RPAQnnatfdckVLSRNHALVWFDHktGKFYLQDTkSS 75
Cdd:COG3456 1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRS-ADCdwvlpDPDR--------SVSRRHAEIRFRD--GAFCLTDL-ST 68
|
90 100 110
....*....|....*....|....*....|...
gi 1799135504 76 NGTFIN--SQRLSRGSEEsppcEILSGDIIQFG 106
Cdd:COG3456 69 NGTFLNgsDHPLGPGRPV----RLRDGDRLRIG 97
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
294-812 |
3.09e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 294 ERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIqqKGQAEKKELQHKIdeMEEKEQELQAKIEALQADNDFTNER 373
Cdd:PRK01156 165 ERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENI--KKQIADDEKSHSI--TLKEIERLSIEYNNAMDDYNNLKSA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 374 LTALQVRLEHLQ--EKTLKECSSLGIQVDDFLPKINGSTE--KEHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKAVeET 449
Cdd:PRK01156 241 LNELSSLEDMKNryESEIKTAESDLSMELEKNNYYKELEErhMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNI-DA 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 450 KLSKENQTRAKESDFsdtlspskEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEA-KQEIQHLRKElieaQE 528
Cdd:PRK01156 320 EINKYHAIIKKLSVL--------QKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESlKKKIEEYSKN----IE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 529 LARTSKQKCFELQALLEEERKAYRNQVEESTKQIqvlQAQLQRLHIDTENLREEKDSeitstrdelLSARDEILLLHQAA 608
Cdd:PRK01156 388 RMSAFISEILKIQEIDPDAIKKELNEINVKLQDI---SSKVSSLNQRIRALRENLDE---------LSRNMEMLNGQSVC 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 609 AKVASERDTDiaslqeelkKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALET 688
Cdd:PRK01156 456 PVCGTTLGEE---------KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIES 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 689 ECHSLKRenvLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELenqvgsLKEQHLRDSADLKTLLSKAENQAKDVQ 768
Cdd:PRK01156 527 ARADLED---IKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSW------LNALAVISLIDIETNRSRSNEIKKQLN 597
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1799135504 769 KEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 812
Cdd:PRK01156 598 DLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQEN 641
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
313-646 |
3.40e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 313 EIKDLSDKLKVAEGKQEEIQQkgqaEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKtLKEC 392
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQS----ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED-LSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 393 SSlgiqvddflPKINGSTEKEHLLSKsggdctfihqfIECQKKLIVEghLTKAVEETKlSKENQTRAKESDfsDTLSPSK 472
Cdd:TIGR02169 750 EQ---------EIENVKSELKELEAR-----------IEELEEDLHK--LEEALNDLE-ARLSHSRIPEIQ--AELSKLE 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 473 EKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEI-EAKQEIQHLRKELIEAQELARTSKQKCFELQAL---LEEER 548
Cdd:TIGR02169 805 EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRiDLKEQIKSIEKEIENLNGKKEELEEELEELEAAlrdLESRL 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 549 KAYRNQVEESTKQIQVLQAQLQRLHIDTENLReEKDSEITSTRDELLSARDEILLLhQAAAKVASERDTDIASLQEELKK 628
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKR-KRLSELKAKLEALEEELSEIEDP-KGEDEEIPEEELSLEDVQAELQR 962
|
330 340
....*....|....*....|..
gi 1799135504 629 VRAELERWR----KAASEYEKE 646
Cdd:TIGR02169 963 VEEEIRALEpvnmLAIQEYEEV 984
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
266-806 |
3.79e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 266 IEVVRKLSEVERSLSNTEDECTHLKEMNERTQE--ELRELANKYNGAVNEIKDLSDKLKVAEGKQEeiQQKGQAEKKELQ 343
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELLEPIRELAERyaAARERLAELEYLRAALRLWFAQRRLELLEAE--LEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 344 HKIDEMEEKEQELQAKIEALQAD-NDFTNERLTALQVRLEHLqEKTLKECSSLGIQVDDFLPKIngstekehllsksggd 422
Cdd:COG4913 309 AELERLEARLDALREELDELEAQiRGNGGDRLEQLEREIERL-ERELEERERRRARLEALLAAL---------------- 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 423 ctfihqfiecqkklivegHLTKAVEETKLsKENQTRAKEsdFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDD 502
Cdd:COG4913 372 ------------------GLPLPASAEEF-AALRAEAAA--LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 503 LQGAQSEIEAKQeiQHLRKELieAQELARTSKQKCF--ELQALLEEER-------KAYRNQ-----VEESTKQiQVLQA- 567
Cdd:COG4913 431 LERRKSNIPARL--LALRDAL--AEALGLDEAELPFvgELIEVRPEEErwrgaieRVLGGFaltllVPPEHYA-AALRWv 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 568 -QLQ-RLHIDTENLREEKDSEITSTRDEllsardeilllHQAAAKVASERDTDIASLQEELKKVRA--------ELERWR 637
Cdd:COG4913 506 nRLHlRGRLVYERVRTGLPDPERPRLDP-----------DSLAGKLDFKPHPFRAWLEAELGRRFDyvcvdspeELRRHP 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 638 KAaseyekeITS---LQNSFQLRcqQCEDQQREEATRLQGE-----LEKLRKEWNALETECHSLKRENVLLSSELQRQEK 709
Cdd:COG4913 575 RA-------ITRagqVKGNGTRH--EKDDRRRIRSRYVLGFdnrakLAALEAELAELEEELAEAEERLEALEAELDALQE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 710 ELHNSQKQSLELTSDLSILQMSRK--ELENQVGSLkeqhLRDSADLKTLlskaENQAKDVQKEYEKTQTVLSELKLKFEM 787
Cdd:COG4913 646 RREALQRLAEYSWDEIDVASAEREiaELEAELERL----DASSDDLAAL----EEQLEELEAELEELEEELDELKGEIGR 717
|
570
....*....|....*....
gi 1799135504 788 TEQEKQSITDELKQCKNNL 806
Cdd:COG4913 718 LEKELEQAEEELDELQDRL 736
|
|
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
53-106 |
3.95e-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: 3.95e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1799135504 53 RNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPceilsGDIIQFG 106
Cdd:cd22700 36 EQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAP-----GDVLRFG 84
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
544-812 |
4.35e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 544 LEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDellsardeillLHQAAAKVASERDtdiaSLQ 623
Cdd:COG1340 6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKE-----------LREEAQELREKRD----ELN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 624 EELKKVRAELERWRKAASEYEKEITSLQNsfqlrcqqcedqQREEATRLQGELEKLRKEWNALE----TECHSLKRENVL 699
Cdd:COG1340 71 EKVKELKEERDELNEKLNELREELDELRK------------ELAELNKAGGSIDKLRKEIERLEwrqqTEVLSPEEEKEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 700 ------LSSELQRQEKElHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAEN---QAKDVQKE 770
Cdd:COG1340 139 vekikeLEKELEKAKKA-LEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADElrkEADELHKE 217
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1799135504 771 YEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 812
Cdd:COG1340 218 IVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKRE 259
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
668-814 |
4.41e-04 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 43.15 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 668 EATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNsQKQSLELTSDLSilqmsrkELENQVGSLKeqhl 747
Cdd:pfam15294 134 EIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGA-KKDVKSNLKEIS-------DLEEKMAALK---- 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135504 748 rdsADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGN 814
Cdd:pfam15294 202 ---SDLEKTLNASTALQKSLEEDLASTKHELLKVQEQLEMAEKELEKKFQQTAAYRNMKEMLTKKNE 265
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
545-776 |
4.45e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 545 EEERKAYRNQVEESTKQIQVLQAQLQRLhidtenlreekDSEITSTRDELLSARDEILLLHQAAAKVASErdtdIASLQE 624
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDAL-----------QAELEELNEEYNELQAELEALQAEIDKLQAE----IAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 625 ELKKVRAELERWrkAASEYE--------------KEITSLQNSFQLRCQQCEDQQR--EEATRLQGELEKLRKEWNALET 688
Cdd:COG3883 80 EIEERREELGER--ARALYRsggsvsyldvllgsESFSDFLDRLSALSKIADADADllEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 689 ECHSLKRENVLLSSELQRQEKELhnsQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQ 768
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQ---EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
....*...
gi 1799135504 769 KEYEKTQT 776
Cdd:COG3883 235 AAAAAAAA 242
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
322-794 |
4.51e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.96 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 322 KVAEGKQEEIQQKGQAEKKELQHKidemeEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKtlkecsslgiqvdd 401
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHK-----RARIELEKKASALKRQLDRESDRNQELQKRIRLLEKR-------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 402 flpkingSTEKEhllsksggdctfihqfiECQKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTD 481
Cdd:pfam05557 64 -------EAEAE-----------------EALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQ 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 482 AQMDEQDLNEPLAKVSLLKDDLQgaqsEIEAK-QEIQHLRKELIEAQELARTSKQKCFELqalleEERKAYRNQVEESTK 560
Cdd:pfam05557 120 IQRAELELQSTNSELEELQERLD----LLKAKaSEAEQLRQNLEKQQSSLAEAEQRIKEL-----EFEIQSQEQDSEIVK 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 561 QIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDeillLHQAAAKVASERDT--DIASLQEELKKVRAELERWRK 638
Cdd:pfam05557 191 NSKSELARIPELEKELERLREHNKHLNENIENKLLLKEE----VEDLKRKLEREEKYreEAATLELEKEKLEQELQSWVK 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 639 AASEYEKEITS--LQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQK 716
Cdd:pfam05557 267 LAQDTGLNLRSpeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQR 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 717 QSLELTSDL----SILQMSRKELENQVGSlkEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEK 792
Cdd:pfam05557 347 RVLLLTKERdgyrAILESYDKELTMSNYS--PQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLEREL 424
|
..
gi 1799135504 793 QS 794
Cdd:pfam05557 425 QA 426
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
251-815 |
5.86e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 251 ETTAKESLRRVLQEKIEVVRKLSEVERSLSNTE----DECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEG 326
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKeqakKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 327 KQEEIQQKGQ---AEKKELQHKIDEMEEKEQELQ--------AKIEALQADNDFTNERLTALQVRLEHLQEKTLKECSSL 395
Cdd:pfam02463 251 EEIESSKQEIekeEEKLAQVLKENKEEEKEKKLQeeelkllaKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 396 GIQvddflpKINGSTEKEHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKS 475
Cdd:pfam02463 331 KKE------KEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 476 SDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEErkayrnqv 555
Cdd:pfam02463 405 KEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKE-------- 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 556 eesTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELER 635
Cdd:pfam02463 477 ---TQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEV 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 636 WRKAASEYEKEitslqnsfqlRCQQCEDQQREEATRLQGELEKLRKEWNALETECH-SLKRENVLLSSELQRQEKELHNS 714
Cdd:pfam02463 554 SATADEVEERQ----------KLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIdPILNLAQLDKATLEADEDDKRAK 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 715 QKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 794
Cdd:pfam02463 624 VVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK 703
|
570 580
....*....|....*....|.
gi 1799135504 795 ITDELKQCKNNLKLLREKGNN 815
Cdd:pfam02463 704 KEQREKEELKKLKLEAEELLA 724
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
16-111 |
7.22e-04 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaB and similar proteins; FhaB, also called FtsZ-interacting protein A (FipA), is a putative virulence factor involved in regulating cell shape. It can interact with polyketide-associated protein PapA5, a putative membrane protein involved in the biosynthesis of virulence enhancing lipids. FhaB regulates growth and cell division. It is probably required for divisomal protein assembly under oxidative stress. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438745 [Multi-domain] Cd Length: 91 Bit Score: 39.21 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 16 PFQERHVYLD-EPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFdhKTGKFYLQDTKSSNGTFINSQRLSRgseespP 94
Cdd:cd22693 7 TLQGQTFPIDkSGITIGRA------DDNDLVLSDDFVSSRHARIYL--QGSSWYLEDLGSTNGTFVNGNRVTQ------P 72
|
90
....*....|....*..
gi 1799135504 95 CEILSGDIIQFGVDVTE 111
Cdd:cd22693 73 VVVQPGDTIRIGATVFE 89
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
541-781 |
7.28e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 541 QALLEEERKAYRNQVEESTKQIQVLQAQLQrlhiDTENLREEkdseITSTRDELLSARDEILLLHQAAAKVASER--DTD 618
Cdd:PRK11281 51 QKLLEAEDKLVQQDLEQTLALLDKIDRQKE----ETEQLKQQ----LAQAPAKLRQAQAELEALKDDNDEETRETlsTLS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 619 IASLQEELKKVRAELERWRKAASEYEKEITSLQN----------SFQLRCQQCEDQ----QREEATRLQGELEKLRKEWN 684
Cdd:PRK11281 123 LRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTqperaqaalyANSQRLQQIRNLlkggKVGGKALRPSQRVLLQAEQA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 685 ALEtechslkrenvlLSSELQRQEKElHNSQKQSL-ELTSDLSILQMSRKELENQvgslkeqhlrdsaDLKTL-----LS 758
Cdd:PRK11281 203 LLN------------AQNDLQRKSLE-GNTQLQDLlQKQRDYLTARIQRLEHQLQ-------------LLQEAinskrLT 256
|
250 260
....*....|....*....|...
gi 1799135504 759 KAENQAKDVQKEYEKTQTVLSEL 781
Cdd:PRK11281 257 LSEKTVQEAQSQDEAARIQANPL 279
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
663-785 |
8.13e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 663 DQQREEATR----LQGELEKLRKEWNALETECHSLKRENVLLSSELQRQekelhNSQKQSLELTSDLSILQMSRKELENQ 738
Cdd:COG3206 167 ELRREEARKalefLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAK-----LLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1799135504 739 VGSLKEQHLRDSADLKTLLSKAENQakDVQKEYEKTQTVLSELKLKF 785
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPVIQ--QLRAQLAELEAELAELSARY 286
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
49-112 |
8.14e-04 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 (PML1) and similar proteins; PML1 is an FHA domain-containing protein required for efficient splicing and pre-mRNA nuclear retention. It is a component of the pre-mRNA retention and splicing (RES) complex composed of at least BUD13, IST3, and PML1. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438733 [Multi-domain] Cd Length: 129 Bit Score: 40.12 E-value: 8.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135504 49 KVLSRNHALVWFDHKTG--KFYLQDTKSSNGTFINsqrlsrgSEESPPC---EILSGDIIQFGVDVTEN 112
Cdd:cd22681 64 ETCSKQHCVIQFRNVKGilKPYIMDLDSSNGTCLN-------DNVIPSSryvELRSGDVITFSKSNDYE 125
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
541-770 |
8.15e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 8.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 541 QALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASErdtdIA 620
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE----IA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 621 SLQEELKKVRAELER-----WRKAASEYEKEITSLQNSFQL-----RCQQCEDQQREEATRLQGELEKLRKewnaletec 690
Cdd:COG4942 94 ELRAELEAQKEELAEllralYRLGRQPPLALLLSPEDFLDAvrrlqYLKYLAPARREQAEELRADLAELAA--------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 691 hslkrenvlLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQH-------LRDSADLKTLLSKAENQ 763
Cdd:COG4942 165 ---------LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELaaelaelQQEAEELEALIARLEAE 235
|
....*..
gi 1799135504 764 AKDVQKE 770
Cdd:COG4942 236 AAAAAER 242
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
511-717 |
1.03e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 511 EAKQEIQHLRKELIEAQELARTSKQKCFELQALLEE----------ERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLR 580
Cdd:COG1340 19 ELREEIEELKEKRDELNEELKELAEKRDELNAQVKElreeaqelreKRDELNEKVKELKEERDELNEKLNELREELDELR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 581 EEKDSEITSTRD-----------------ELLSARDEILLLHQAAAKVAS-ERDTDIASLQEELKKVRAELERWRKAASE 642
Cdd:COG1340 99 KELAELNKAGGSidklrkeierlewrqqtEVLSPEEEKELVEKIKELEKElEKAKKALEKNEKLKELRAELKELRKEAEE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 643 YEKEITSLQNSFQ------LRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQK 716
Cdd:COG1340 179 IHKKIKELAEEAQelheemIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKR 258
|
.
gi 1799135504 717 Q 717
Cdd:COG1340 259 E 259
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
544-703 |
1.69e-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: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 544 LEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDseitstrdELlsaRDEILllhqaaakvasERDTDIASLQ 623
Cdd:COG2433 390 LPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE--------EL---EAELE-----------EKDERIERLE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 624 EELKKVRAElerwRKAASEYEKEITSLQNsfqlrcqqcedqqreEATRLQGELEKLRKEWNALETECHSLKRENVLLSSE 703
Cdd:COG2433 448 RELSEARSE----ERREIRKDREISRLDR---------------EIERLERELEEERERIEELKRKLERLKELWKLEHSG 508
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
614-815 |
1.83e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 614 ERDT--DIASLQEELKkvraELERWRKAASEYEKEITSLQnsfQLRcqqcedQQREEATRLQGELEKLRKEWNALETECH 691
Cdd:COG4913 220 EPDTfeAADALVEHFD----DLERAHEALEDAREQIELLE---PIR------ELAERYAAARERLAELEYLRAALRLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 692 SLKREnvLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQvgsLKEQHLRDSADLKTLLSKAENQAKDVQKEY 771
Cdd:COG4913 287 QRRLE--LLEAELEELRAELARLEAELERLEARLDALREELDELEAQ---IRGNGGDRLEQLEREIERLERELEERERRR 361
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1799135504 772 EKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNN 815
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
237-637 |
1.93e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 237 RKELIALQEDKHNYETTAK--ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERtQEELRELANKYNGAVNEI 314
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQilSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQ-ILELEGYEMDYNSYLKSI 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 315 KDLSDKLKVAEGKQE-------EIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEK 387
Cdd:PRK01156 373 ESLKKKIEEYSKNIErmsafisEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 388 --------TLKECSSLGIqVDDFLPKINGSTEKehlLSKSGGDCTFIHQFIECQKKLivEGHLTKAVEETKLSKENQTRA 459
Cdd:PRK01156 453 svcpvcgtTLGEEKSNHI-INHYNEKKSRLEEK---IREIEIEVKDIDEKIVDLKKR--KEYLESEEINKSINEYNKIES 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 460 KES---DFSDTLSPSKEK-----------SSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEiEAKQEIQHLRKELIE 525
Cdd:PRK01156 527 ARAdleDIKIKINELKDKhdkyeeiknryKSLKLEDLDSKRTSWLNALAVISLIDIETNRSRSN-EIKKQLNDLESRLQE 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 526 AQELARTSKQKCFELQALLEEERKAYRNQVEEstkqIQVLQAQLQRLHIDTENLREEkdseitstrdelLSARDEILLLH 605
Cdd:PRK01156 606 IEIGFPDDKSYIDKSIREIENEANNLNNKYNE----IQENKILIEKLRGKIDNYKKQ------------IAEIDSIIPDL 669
|
410 420 430
....*....|....*....|....*....|..
gi 1799135504 606 QAAAKVASERDTDIASLQEELKKVRAELERWR 637
Cdd:PRK01156 670 KEITSRINDIEDNLKKSRKALDDAKANRARLE 701
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
27-106 |
1.94e-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: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 27 PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTGkfYLQDTKSSNGTFINSQRLsrgseeSPPCEILSGDIIQFG 106
Cdd:cd22668 19 SNIIGRG------SDADFRLPDTGVSRRHAEIRWDGQVA--HLTDLGSTNGTTVNNAPV------TPEWRLADGDVITLG 84
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
665-812 |
2.75e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 665 QREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKE 744
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 745 QHLRDSADLKTLLSKAE-------------------------------NQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQ 793
Cdd:COG4942 98 ELEAQKEELAELLRALYrlgrqpplalllspedfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAELE 177
|
170
....*....|....*....
gi 1799135504 794 SITDELKQCKNNLKLLREK 812
Cdd:COG4942 178 ALLAELEEERAALEALKAE 196
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
162-790 |
2.76e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.35 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 162 SQELFQLSQYLQEALHR----EQMLEQKLATLQRLLAITQEASDTSWQALIDEDRllsRLEVMGNQLQACSKNQTEDSLR 237
Cdd:pfam10174 129 AKELFLLRKTLEEMELRietqKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWER---TRRIAEAEMQLGHLEVLLDQKE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 238 KELIALQEDKH-NYETTAKESLRRVLQEKIEVV-RKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKyngaVNEIK 315
Cdd:pfam10174 206 KENIHLREELHrRNQLQPDPAKTKALQTVIEMKdTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQ----MEVYK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 316 DLSD--KLKVAEGKQEeiQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQadndftnERLTALQVRLEHLQektlKECS 393
Cdd:pfam10174 282 SHSKfmKNKIDQLKQE--LSKKESELLALQTKLETLTNQNSDCKQHIEVLK-------ESLTAKEQRAAILQ----TEVD 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 394 SLGIQVDdflpkingstEKEHLLSKSggdctfihqfiecQKKLiveghltkaveeTKLSKENQTRAKE-SDFSDTLSPSK 472
Cdd:pfam10174 349 ALRLRLE----------EKESFLNKK-------------TKQL------------QDLTEEKSTLAGEiRDLKDMLDVKE 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 473 EKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIqhlrkelIEAQELARTSKQKCFE-LQALLEEERKAY 551
Cdd:pfam10174 394 RKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTA-------LTTLEEALSEKERIIErLKEQREREDRER 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 552 RNQVEESTKQIQVLQAQLQRLHIDtenlREEKDSEITSTRDELLSARDEILllhqaaakvasERDTDIASLQEELKKVRA 631
Cdd:pfam10174 467 LEELESLKKENKDLKEKVSALQPE----LTEKESSLIDLKEHASSLASSGL-----------KKDSKLKSLEIAVEQKKE 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 632 ELERW----RKAASEYEKEITSLQNSFQLRCQQCEDQQ-REEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQR 706
Cdd:pfam10174 532 ECSKLenqlKKAHNAEEAVRTNPEINDRIRLLEQEVARyKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLR 611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 707 QEKELHNSQKQsleltsdlsiLQMSRKELENQVGSLKEQHLRDSADLKTllSKAENQAKDVQKEYEKTQTVLSELKLKFE 786
Cdd:pfam10174 612 QMKEQNKKVAN----------IKHGQQEMKKKGAQLLEEARRREDNLAD--NSQQLQLEELMGALEKTRQELDATKARLS 679
|
....
gi 1799135504 787 MTEQ 790
Cdd:pfam10174 680 STQQ 683
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
172-387 |
3.02e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 172 LQEALHREQMLEQKLATLQRLLAITQEAsdtswqalIDEDRL-LSRLEVMGNQLQACSKNQTEDSLRKELIAlqeDKHNY 250
Cdd:PRK02224 504 LVEAEDRIERLEERREDLEELIAERRET--------IEEKRErAEELRERAAELEAEAEEKREAAAEAEEEA---EEARE 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 251 ETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDEC-------THLKEMNERTQEELRELANKyngavneIKDLSDKLKv 323
Cdd:PRK02224 573 EVAELNSKLAELKERIESLERIRTLLAAIADAEDEIerlrekrEALAELNDERRERLAEKRER-------KRELEAEFD- 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135504 324 aEGKQEEIQQ-KGQAEK--KELQHKIDEMEEKEQELQAKIEALQADndftNERLTALQVRLEHLQEK 387
Cdd:PRK02224 645 -EARIEEAREdKERAEEylEQVEEKLDELREERDDLQAEIGAVENE----LEELEELRERREALENR 706
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
172-361 |
3.25e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 39.50 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 172 LQEALHREQMLEQKLATLQRLLaitqeasdtswQALIDEDRLLSRLEVmgNQLQACSKNQTEDSLRKELIAlqedKHNYE 251
Cdd:pfam15619 6 LSARLHKIKELQNELAELQSKL-----------EELRKENRLLKRLQK--RQEKALGKYEGTESELPQLIA----RHNEE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 252 T-TAKESLRRvLQEKIEVV-RKLSEVERSLSNTEDECTHL------KEMNERT--QEELRELANKYNGAVNEIKDLSDKL 321
Cdd:pfam15619 69 VrVLRERLRR-LQEKERDLeRKLKEKEAELLRLRDQLKRLeklsedKNLAEREelQKKLEQLEAKLEDKDEKIQDLERKL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1799135504 322 KVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIE 361
Cdd:pfam15619 148 ELENKSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLK 187
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
163-386 |
3.37e-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: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWqALIDEDRLLSRLEVMGNQLQACSKNQTE-DSLRKELI 241
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-DEIDVASAEREIAELEAELERLDASSDDlAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 242 ALQEDkhnyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLK----EMNERTQEELRELANKYNGAVNEIkdl 317
Cdd:COG4913 696 ELEAE-----------LEELEEELDELKGEIGRLEKELEQAEEELDELQdrleAAEDLARLELRALLEERFAAALGD--- 761
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135504 318 sdklKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQE 386
Cdd:COG4913 762 ----AVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEE 826
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
521-814 |
3.40e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 521 KELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDsEITSTRDELLSARDE 600
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 601 ILLLHQAAAKVaserDTDIASLQEELKKVRAELERWRkaasEYEKEITSLQnsfqlrcqqcedQQREEATRLQGELEKLR 680
Cdd:PRK03918 247 LESLEGSKRKL----EEKIRELEERIEELKKEIEELE----EKVKELKELK------------EKAEEYIKLSEFYEEYL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 681 KEWNALETECHSLKREnvllSSELQRQEKELHNSQKQSLELTSDLsilqmsrKELENQVGSLKEQHlRDSADLKTLLSKA 760
Cdd:PRK03918 307 DELREIEKRLSRLEEE----INGIEERIKELEEKEERLEELKKKL-------KELEKRLEELEERH-ELYEEAKAKKEEL 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1799135504 761 ENQAKdvqkeyEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGN 814
Cdd:PRK03918 375 ERLKK------RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIK 422
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
239-812 |
3.53e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.86 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 239 ELIALQEDKHNYETTAKES-LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDL 317
Cdd:pfam05483 222 EKIQHLEEEYKKEINDKEKqVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDI 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 318 SDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKiealQADNDFTNERLTALQVRLEHL----QEKTLKECS 393
Cdd:pfam05483 302 KMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKA----KAAHSFVVTEFEATTCSLEELlrteQQRLEKNED 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 394 SLGIQVDDFLPKINGSTEKEHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKAVEEtklskenQTRAKESDFSDTLSPSKE 473
Cdd:pfam05483 378 QLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAE-------ELKGKEQELIFLLQAREK 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 474 KSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQgaQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELqalleeerKAYRN 553
Cdd:pfam05483 451 EIHDLEIQLTAIKTSEEHYLKEVEDLKTELE--KEKLKNIELTAHCDKLLLENKELTQEASDMTLEL--------KKHQE 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 554 QVEESTKQIQVLQAQLQRLHIDTENLREEkdseITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAEL 633
Cdd:pfam05483 521 DIINCKKQEERMLKQIENLEEKEMNLRDE----LESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKC 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 634 ERWRKAASEYEKEITSLqnsfqlrcqqcedQQREEATRLQGELEKlrKEWNALETECHSLKREnvlLSSELQRQEKELHN 713
Cdd:pfam05483 597 NNLKKQIENKNKNIEEL-------------HQENKALKKKGSAEN--KQLNAYEIKVNKLELE---LASAKQKFEEIIDN 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 714 SQKQ----SLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTE 789
Cdd:pfam05483 659 YQKEiedkKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQS 738
|
570 580
....*....|....*....|...
gi 1799135504 790 QEKQSITDELKQCKNNLKLLREK 812
Cdd:pfam05483 739 SAKAALEIELSNIKAELLSLKKQ 761
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
256-365 |
3.74e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 256 ESLRRVLQEKI-EVVRKLSEVERSLSNTEDEcthLKEMNERTQEELRELANKYNGAVNE--------IKDLSD--KLKVA 324
Cdd:PRK00409 526 EELERELEQKAeEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLEEAEKEAQQAIKEakkeadeiIKELRQlqKGGYA 602
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1799135504 325 EGKQEEIQQKgqaeKKELQHKIDEMEEKEQELQAKIEALQA 365
Cdd:PRK00409 603 SVKAHELIEA----RKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
257-560 |
3.99e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.68 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 257 SLRRVLQEKIEVVRKLSEVERslsnteDECTHLKEmNERTqEELRELANKYNGAVNEIKDLSDKLKVAEGKQ-------- 328
Cdd:PRK05771 13 TLKSYKDEVLEALHELGVVHI------EDLKEELS-NERL-RKLRSLLTKLSEALDKLRSYLPKLNPLREEKkkvsvksl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 329 EEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQAdndftnerltalqvrlehlQEKTLKECSSLGIQVDDFLpking 408
Cdd:PRK05771 85 EELIKDVEEELEKIEKEIKELEEEISELENEIKELEQ-------------------EIERLEPWGNFDLDLSLLL----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 409 stekehllsksggDCTFIHQFIecqkkliveGHLTKAVEETKLSKENQTRAKESDFSDTLSP-----SKEkssddttdaq 483
Cdd:PRK05771 141 -------------GFKYVSVFV---------GTVPEDKLEELKLESDVENVEYISTDKGYVYvvvvvLKE---------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 484 mDEQDLNEPLAKVSLLKDDLQ--GAQSEI--EAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEEST 559
Cdd:PRK05771 189 -LSDEVEEELKKLGFERLELEeeGTPSELirEIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAEALS 267
|
.
gi 1799135504 560 K 560
Cdd:PRK05771 268 K 268
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
606-798 |
4.33e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 606 QAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRcqqcedQQREEATRLQGELEKLRKEWNa 685
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL------PLYQELEALEAELAELPERLE- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 686 letechslkrenvllssELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDsadLKTLLSKAENQAK 765
Cdd:COG4717 150 -----------------ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD---LAEELEELQQRLA 209
|
170 180 190
....*....|....*....|....*....|...
gi 1799135504 766 DVQKEYEKTQTVLSELKLKFEMTEQEKQSITDE 798
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
528-738 |
4.60e-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: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 528 ELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQA 607
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 608 AAKVASERDTDIASLQEELKKVRaELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEatrlQGELEKLRKEWNALE 687
Cdd:pfam07888 110 SEELSEEKDALLAQRAAHEARIR-ELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEE----EAERKQLQAKLQQTE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1799135504 688 TECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQmsRKELENQ 738
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH--RKEAENE 233
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
236-386 |
5.06e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 236 LRKELIALQEDKHNYETTAK--ESLRRVLQEKIEVVRKLSEVERSLSNTEDecthlkemnerTQEELRELANKYNgavnE 313
Cdd:COG4913 615 LEAELAELEEELAEAEERLEalEAELDALQERREALQRLAEYSWDEIDVAS-----------AEREIAELEAELE----R 679
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799135504 314 IKDLSDKLKVAEGKQEEIQqkgqAEKKELQHKIDEMEEKEQELQAKIEALQadndftnERLTALQVRLEHLQE 386
Cdd:COG4913 680 LDASSDDLAALEEQLEELE----AELEELEEELDELKGEIGRLEKELEQAE-------EELDELQDRLEAAED 741
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
207-600 |
5.20e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 40.41 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 207 LIDEDRLLSRLE--------VMGNQLQAcsKNQTEDSLRKELIALQEDKHNYETTAKESLRRVlQEKIEVVRKLSEVERS 278
Cdd:PTZ00108 1001 LGKLERELARLSnkvrfikhVINGELVI--TNAKKKDLVKELKKLGYVRFKDIIKKKSEKITA-EEEEGAEEDDEADDED 1077
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 279 LSNTEDECT---HLKEMN--ERTQEELRELANKYNGAVNEIKDLSDKlkvaegkqeEIQQKGQAEKKELQHKIDEMEEKE 353
Cdd:PTZ00108 1078 DEEELGAAVsydYLLSMPiwSLTKEKVEKLNAELEKKEKELEKLKNT---------TPKDMWLEDLDKFEEALEEQEEVE 1148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 354 QELQAKIEALQADNDFTNERLtalqvrlehLQEKTLKECSSLGIQVDDFLPKINGSTEKEHLLSKSggdctfihqfiecq 433
Cdd:PTZ00108 1149 EKEIAKEQRLKSKTKGKASKL---------RKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDE-------------- 1205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 434 KKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAK 513
Cdd:PTZ00108 1206 KRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSP 1285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 514 QEIQHLRKELIEAQELARTS----KQKCFELQALL----EEERKAYRNQVEESTKQIQVLQAQLQRL------HIDTENL 579
Cdd:PTZ00108 1286 PPPSKRPDGESNGGSKPSSPtkkkVKKRLEGSLAAlkkkKKSEKKTARKKKSKTRVKQASASQSSRLlrrprkKKSDSSS 1365
|
410 420
....*....|....*....|.
gi 1799135504 580 REEKDSEITSTRDELLSARDE 600
Cdd:PTZ00108 1366 EDDDDSEVDDSEDEDDEDDED 1386
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
300-387 |
5.33e-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: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 300 LRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQV 379
Cdd:COG3883 124 LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
....*...
gi 1799135504 380 RLEHLQEK 387
Cdd:COG3883 204 ELAAAEAA 211
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
274-381 |
5.62e-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: 40.22 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 274 EVERSLSNTEDECTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEK----------K 340
Cdd:pfam06160 288 YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEvayselqeelE 367
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1799135504 341 ELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRL 381
Cdd:pfam06160 368 EILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLEL 408
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
511-749 |
6.16e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 511 EAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITST 590
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 591 RDellsardeillLHQAAAKVASErdtdIASLQEELKKVR--AELERWRKAASEYEKEITSLQNS---FQLRCQQCEDQQ 665
Cdd:PHA02562 258 NK-----------LNTAAAKIKSK----IEQFQKVIKMYEkgGVCPTCTQQISEGPDRITKIKDKlkeLQHSLEKLDTAI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 666 REEATRLQgELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSL-KE 744
Cdd:PHA02562 323 DELEEIMD-EFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELvKE 401
|
....*
gi 1799135504 745 QHLRD 749
Cdd:PHA02562 402 KYHRG 406
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
208-366 |
6.21e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 208 IDEDRLLSRLEVMGNQLQACSKNQTE---DSLRKELIALQED-KHNYETTAKEslrrvLQEKIEVVRKLSEVERSLsnte 283
Cdd:PRK04778 249 LDHLDIEKEIQDLKEQIDENLALLEEldlDEAEEKNEEIQERiDQLYDILERE-----VKARKYVEKNSDTLPDFL---- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 284 decTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKK---ELQHKIDEMEEKEQELQ 357
Cdd:PRK04778 320 ---EHAKEQNKELKEEIDRVKQSYtlnESELESVRQLEKQLESLEKQYDEITERIAEQEIaysELQEELEEILKQLEEIE 396
|
....*....
gi 1799135504 358 AKIEALQAD 366
Cdd:PRK04778 397 KEQEKLSEM 405
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
256-808 |
6.31e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 40.42 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 256 ESLRRVLQEKIEVVRK--LSEVERSLSNTEDECTHLKEMN--ERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEI 331
Cdd:TIGR01612 1058 DEIEKEIGKNIELLNKeiLEEAEINITNFNEIKEKLKHYNfdDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEI 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 332 QQKGQAEKKELQHKI----------------DEMEEKEQELQAKIEALQADNDFTNERLTAL------QVRLEHLQEKTL 389
Cdd:TIGR01612 1138 KKKSENYIDEIKAQIndledvadkaisnddpEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIaeiekdKTSLEEVKGINL 1217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 390 KECSSLGIQvddFLPKINGSTEK-EHL---LSKSGGDCTFI-HQFIECQKKLIVEGHLTKAVEETKLS----KENQTRAK 460
Cdd:TIGR01612 1218 SYGKNLGKL---FLEKIDEEKKKsEHMikaMEAYIEDLDEIkEKSPEIENEMGIEMDIKAEMETFNIShdddKDHHIISK 1294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 461 ESDfsDTLSPSKEKS--------------------SDDTTDAQMDEQDLNEPLAKVS----LLK--------DDLQGAQS 508
Cdd:TIGR01612 1295 KHD--ENISDIREKSlkiiedfseesdindikkelQKNLLDAQKHNSDINLYLNEIAniynILKlnkikkiiDEVKEYTK 1372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 509 EIEAKQeiQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQL--QRLHIDT--ENLREEKD 584
Cdd:TIGR01612 1373 EIEENN--KNIKDELDKSEKLIKKIKDDINLEECKSKIESTLDDKDIDECIKKIKELKNHIlsEESNIDTyfKNADENNE 1450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 585 SEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEEL---KKVRAELERWRKAAS-------EYEKEITSLQNSF 654
Cdd:TIGR01612 1451 NVLLLFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHIdksKGCKDEADKNAKAIEknkelfeQYKKDVTELLNKY 1530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 655 -QLRCQQCEDQQREEATRLQGELEKLRK----EWNALETECHSLKRENVLLSSELQRQEK----------ELHNSQKQSL 719
Cdd:TIGR01612 1531 sALAIKNKFAKTKKDSEIIIKEIKDAHKkfilEAEKSEQKIKEIKKEKFRIEDDAAKNDKsnkaaidiqlSLENFENKFL 1610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 720 ELTSDLSILQMSRKE---LENQVGSL----KEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEmteqek 792
Cdd:TIGR01612 1611 KISDIKKKINDCLKEtesIEKKISSFsidsQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIE------ 1684
|
650
....*....|....*.
gi 1799135504 793 qSITDELKQCKNNLKL 808
Cdd:TIGR01612 1685 -KIEIDVDQHKKNYEI 1699
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
163-365 |
6.36e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.06 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEasdtsWQALIDEDRLLSR----LEVMGNQLQACSKNQT--EDSL 236
Cdd:COG0497 172 KELEELRADEAERARELDLLRFQLEELEAAALQPGE-----EEELEEERRRLSNaeklREALQEALEALSGGEGgaLDLL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 237 RKELIALQEDKHnYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERtQEELRELANKYNGAVNEIKD 316
Cdd:COG0497 247 GQALRALERLAE-YDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEER-LALLRRLARKYGVTVEELLA 324
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1799135504 317 LSDKLkvaegkqeeiqqkgQAEKKELQHKIDEMEEKEQELQAKIEALQA 365
Cdd:COG0497 325 YAEEL--------------RAELAELENSDERLEELEAELAEAEAELLE 359
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
52-106 |
6.44e-03 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein kinase DUN1 and similar proteins; DUN1 is a protein kinase that controls the DNA damage response in yeast. It phosphorylates SML1 on serine residues and cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438735 [Multi-domain] Cd Length: 96 Bit Score: 36.70 E-value: 6.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799135504 52 SRNHALVWFDHKTGKFYLQ-----------DTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFG 106
Cdd:cd22683 28 SRSCDLVLSDPSISRFHAElrleqnginviDNNSANGTFINGKRIKGKT-----YILKNGDIIVFG 88
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
216-583 |
7.57e-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: 39.88 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 216 RLEVMGNQLQACSKNQTEdsLRKELIALQEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNER 295
Cdd:pfam07888 28 RAELLQNRLEECLQERAE--LLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 296 TQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELqhkiDEMEEKEQELQAKIEALQADNDFTNERLT 375
Cdd:pfam07888 106 LSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETEL----ERMKERAKKAGAQRKEEEAERKQLQAKLQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 376 ALQVRLEHLQEKTLKECSSLGIQVDDFLPKINGSTEKEHLLSKSggdctfiHQFIECQKKLIVEghlTKAVEETKLSKEN 455
Cdd:pfam07888 182 QTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTA-------HRKEAENEALLEE---LRSLQERLNASER 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 456 QTRAKESDFSDTLSpSKEKSSDDTTDAQMDEQDLNEPLAKVSL--------LKDDLQGAQSEIEAKQE-IQHLRKELIEA 526
Cdd:pfam07888 252 KVEGLGEELSSMAA-QRDRTQAELHQARLQAAQLTLQLADASLalregrarWAQERETLQQSAEADKDrIEKLSAELQRL 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135504 527 QELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEK 583
Cdd:pfam07888 331 EERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEK 387
|
|
| VI_FHA |
TIGR03354 |
type VI secretion system FHA domain protein; Members of this protein family are FHA ... |
49-106 |
7.81e-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: 7.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799135504 49 KVLSRNHALV-WFDhktGKFYLQDTkSSNGTFINS--QRLSRGSEesppcEILS-GDIIQFG 106
Cdd:TIGR03354 43 RHVSGRHARIrYRD---GAYLLTDL-STNGVFLNGsgSPLGRGNP-----VRLEqGDRLRLG 95
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
262-812 |
8.59e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.82 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 262 LQEKIEVVRKLsevERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDlSDKLKVAEGKQEEIQQKGQAEKKe 341
Cdd:pfam12128 246 LQQEFNTLESA---ELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDD-QWKEKRDELNGELSAADAAVAKD- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 342 lQHKIDEMEE-KEQELQAKIEALQADND----------FTNERLTALQVRLEHLQEKTLKECSSLGIQVDDFLPKINGST 410
Cdd:pfam12128 321 -RSELEALEDqHGAFLDADIETAAADQEqlpswqseleNLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKL 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 411 EKEH-LLSKSGGDCTFIHQFIECQKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPS---KEKSSDDTTDAQMDE 486
Cdd:pfam12128 400 AKIReARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPElllQLENFDERIERAREE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 487 QDlnEPLAKVSLLKDDLQGAQSEIEakQEIQHLRKELIEAQELartsKQKCFELQALLEEERKAY----RNQVEESTKQI 562
Cdd:pfam12128 480 QE--AANAEVERLQSELRQARKRRD--QASEALRQASRRLEER----QSALDELELQLFPQAGTLlhflRKEAPDWEQSI 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 563 QVL--QAQLQRLHIDTENLREEKDSEIT-----------------STRDELLSARDEILLLHQAAAKVASERDTDIASLQ 623
Cdd:pfam12128 552 GKVisPELLHRTDLDPEVWDGSVGGELNlygvkldlkridvpewaASEEELRERLDKAEEALQSAREKQAAAEEQLVQAN 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 624 EELKKVRAELERWRKAaseyekeitsLQNSfQLRCQQCEDQQREEATRLQGELE----KLRKEWNALETECHSLKRENVL 699
Cdd:pfam12128 632 GELEKASREETFARTA----------LKNA-RLDLRRLFDEKQSEKDKKNKALAerkdSANERLNSLEAQLKQLDKKHQA 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 700 LSSELQRQEKEL---HNSQKQSLELTSDLSILQMS------RKELENQVGSLKEQHLRD--------------SADLKTL 756
Cdd:pfam12128 701 WLEEQKEQKREArteKQAYWQVVEGALDAQLALLKaaiaarRSGAKAELKALETWYKRDlaslgvdpdviaklKREIRTL 780
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799135504 757 LSKAENQAKDVQK--EYEKTQ--TVLSE---LKLKFEMTEQEKQSITDELKQCKNNLKLLREK 812
Cdd:pfam12128 781 ERKIERIAVRRQEvlRYFDWYqeTWLQRrprLATQLSNIERAISELQQQLARLIADTKLRRAK 843
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
173-366 |
8.60e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.75 E-value: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 173 QEALHREQMLEQKLATLQRLLAitqeasdtswqalidedRLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYET 252
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLK-----------------ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 253 TAKESLRRVLQEKIEVVRKlsevERSLSNTEDECTHLKEMNERTQEELRELankyngaVNEIKDLSDKLKVAEGKQEEIQ 332
Cdd:COG1579 69 EEVEARIKKYEEQLGNVRN----NKEYEALQKEIESLKRRISDLEDEILEL-------MERIEELEEELAELEAELAELE 137
|
170 180 190
....*....|....*....|....*....|....
gi 1799135504 333 QKGQAEKKELQHKIDEMEEKEQELQAKIEALQAD 366
Cdd:COG1579 138 AELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
487-717 |
9.14e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.94 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 487 QDLNEPLAKVSLLKDDlqgaqseiEAKQEIQHLRKELIEAQELARTSKQKCFELqALLEEERKAYRN---QVEESTKQIQ 563
Cdd:COG3096 874 QLLNKLLPQANLLADE--------TLADRLEELREELDAAQEAQAFIQQHGKAL-AQLEPLVAVLQSdpeQFEQLQADYL 944
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 564 VLQAQLQRLHIDTENLREekdseiTSTRDELLSARDEILLLHQAAAKVASERdTDIASLQEELKKVRAELERWRKAASEY 643
Cdd:COG3096 945 QAKEQQRRLKQQIFALSE------VVQRRPHFSYEDAVGLLGENSDLNEKLR-ARLEQAEEARREAREQLRQAQAQYSQY 1017
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 644 EKEITSLQNSFQLRCQQ------------------CEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQ 705
Cdd:COG3096 1018 NQVLASLKSSRDAKQQTlqeleqeleelgvqadaeAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLR 1097
|
250
....*....|..
gi 1799135504 706 RQEKELHNSQKQ 717
Cdd:COG3096 1098 KAERDYKQEREQ 1109
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
489-801 |
9.33e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 39.72 E-value: 9.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 489 LNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIE-AQELAR--------TSKQKCFELQAL---------LEEERKA 550
Cdd:pfam17380 271 LNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEkAREVERrrkleeaeKARQAEMDRQAAiyaeqermaMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 551 YRNQVEESTKQIQVLQAQLQRLHI----DTENLREEKDSEITSTRDELLSARDEILL--------------LHQAAAKVA 612
Cdd:pfam17380 351 ERIRQEERKRELERIRQEEIAMEIsrmrELERLQMERQQKNERVRQELEAARKVKILeeerqrkiqqqkveMEQIRAEQE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 613 SERDTDIASLQEELKKvraELERWRKAASEYEKEITSLQnsfqlrcqqcedQQREEATRLQGELEKLRKEWNALETEchs 692
Cdd:pfam17380 431 EARQREVRRLEEERAR---EMERVRLEEQERQQQVERLR------------QQEEERKRKKLELEKEKRDRKRAEEQ--- 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135504 693 lkRENVLlsselqrqEKELHNSQKQSLELTSDLSILQmsrKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYE 772
Cdd:pfam17380 493 --RRKIL--------EKELEERKQAMIEEERKRKLLE---KEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMR 559
|
330 340
....*....|....*....|....*....
gi 1799135504 773 KTQTVLSELKLKFEMTEQEKQSITDELKQ 801
Cdd:pfam17380 560 KATEERSRLEAMEREREMMRQIVESEKAR 588
|
|
| |
