|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
3-130 |
3.21e-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: 257.58 E-value: 3.21e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 3 SALAIFTCRPNSHPFQERHVYLDEPVKIGRSVARCRPAQNNATFDCKVLSRNHALIWFDHktGKFYLQDTKSSNGTFINS 82
Cdd:cd22679 1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1952581424 83 QRLSRGSEESPPCELLSGDIIQFGVDVTENTRKVTHGCIVSTVKLFMP 130
Cdd:cd22679 79 QRLSKGSEESEPRELHSGDIVQFGVDVVENSRKVTHGCIVATVTLFLP 126
|
|
| CC1_SLMAP |
cd21911 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal ... |
163-225 |
1.95e-26 |
|
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal membrane-associated protein (SLMAP), also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. SLMAP contains an N-terminal FHA domain followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409287 [Multi-domain] Cd Length: 63 Bit Score: 102.76 E-value: 1.95e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952581424 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQ 225
Cdd:cd21911 1 QELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQLS 63
|
|
| FHA_DMA-like |
cd22692 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest ... |
27-108 |
1.46e-18 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest protein 1 (DMA1), 2 (DMA2) and similar proteins; DMA1 (also known as checkpoint forkhead associated with RING domains-containing protein 1, or CHF1) and DMA2 (also known as checkpoint forkhead associated with RING domains-containing protein 2, or CHF2) are E3 ubiquitin-protein ligases which function in cell cycle retarding in conjunction with the UBC4 and UBC13/MMS2 complex, two E2 ubiquitin conjugating enzymes. They are involved in nutritional control of the cell cycle and required for proper spindle positioning, likely regulating septin ring deposition at the bud neck. DMA1 targets the degradation of G1 cyclin PCL1. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438744 [Multi-domain] Cd Length: 139 Bit Score: 83.00 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 27 PVKIGRSVARCRPAQNNAT-FDCKVLSRNHALIWfdHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCELLSGDIIQF 105
Cdd:cd22692 38 QIHIGRYTERVRQAIYHPVvFKSKVVSRTHGCIK--VDEGNWYIKDVKSSSGTFLNHQRLSPASRTSKPYPLRDGDILQL 115
|
...
gi 1952581424 106 GVD 108
Cdd:cd22692 116 GMD 118
|
|
| FHA_VPS64-like |
cd22695 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ... |
6-126 |
3.65e-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: 75.80 E-value: 3.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 6 AIFTCRPNSHPFQERHV---YLDEPVKIGRSVARCRPAQN---------------NATFDCKVLSRNHALIWFDHKTGKF 67
Cdd:cd22695 2 HILVLKSLNATFETKFLvvpFKPDGLKLGRPVTNSVNKNNsgskrdlfsqqvrpdNGNFDSRVLSRNHACLSCDPTTGKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581424 68 YLQDTKSSNGTFINSQRLSRGSeesppCELLSGDIIQFGVDVTEntrKVTHGCIVSTVK 126
Cdd:cd22695 82 YIRDLKSSNGTFVNGQKIRQND-----VELKVGDEVDLGTDIDS---KIEHRKISAYVE 132
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
13-106 |
5.32e-15 |
|
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.
Pssm-ID: 438714 [Multi-domain] Cd Length: 92 Bit Score: 71.15 E-value: 5.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 13 NSHPFQERHVYLDEPVKIGRSvarcrpAQNNATFDCKVLSRNHALIWFDHktGKFYLQDTKSSNGTFINSQRLsrgseeS 92
Cdd:cd00060 6 DGDGGGREFPLTKGVVTIGRS------PDCDIVLDDPSVSRRHARIEVDG--GGVYLEDLGSTNGTFVNGKRI------T 71
|
90
....*....|....
gi 1952581424 93 PPCELLSGDIIQFG 106
Cdd:cd00060 72 PPVPLQDGDVIRLG 85
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
28-105 |
7.95e-15 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 69.91 E-value: 7.95e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581424 28 VKIGRSvarcrpAQNNATFDCKVLSRNHALIWFDhKTGKFYLQDTKSSNGTFINSQRLSRgseesPPCELLSGDIIQF 105
Cdd:pfam00498 1 VTIGRS------PDCDIVLDDPSVSRRHAEIRYD-GGGRFYLEDLGSTNGTFVNGQRLGP-----EPVRLKDGDVIRL 66
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
182-857 |
6.62e-14 |
|
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: 76.26 E-value: 6.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 182 LEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAysknqTEDGIRKELVTLQEDKHSYETTAKESLrrv 261
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA-----EIEELEREIEEERKRRDKLTEEYAELK--- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 262 lQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKAL---SE 338
Cdd:TIGR02169 364 -EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINeleEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 339 KKELQHRIDEMEEKEQLLQA-------RIEALQADNDFTNERLTALQVRLEQLQ------EKNIKDHNSIEHFLLKSGGD 405
Cdd:TIGR02169 443 KEDKALEIKKQEWKLEQLAAdlskyeqELYDLKEEYDRVEKELSKLQRELAEAEaqarasEERVRGGRAVEEVLKASIQG 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 406 CSELFQQFIECKNKLKAPVEPTQNNRISN--VED--------------------------MFESHLENNQTTEE------ 451
Cdd:TIGR02169 523 VHGTVAQLGSVGERYATAIEVAAGNRLNNvvVEDdavakeaiellkrrkagratflplnkMRDERRDLSILSEDgvigfa 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 452 -DLKNDSERFKA--------TLIAEDdhtkvTEETKLLKEN----QLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQELN 518
Cdd:TIGR02169 603 vDLVEFDPKYEPafkyvfgdTLVVED-----IEAARRLMGKyrmvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQ 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 519 ESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKcfemQALLEEER 598
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED----LSSLEQEI 753
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 599 KTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASTHKEIVA---LRQTAVEAATGRES-DIAILQG 674
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSrieARLREIEQKLNRLTlEKEYLEK 833
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 675 ELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQqqkdkqkgEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKL 754
Cdd:TIGR02169 834 EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE--------ELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 755 QWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETN--GLRVKLAHAENETQKFQ-------KQYEADQ 825
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSleDVQAELQRVEEEIRALEpvnmlaiQEYEEVL 985
|
730 740 750
....*....|....*....|....*....|..
gi 1952581424 826 TMYLELKEKLDKTQKENESITDELENCkENLK 857
Cdd:TIGR02169 986 KRLDELKEKRAKLEEERKAILERIEEY-EKKK 1016
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
203-849 |
6.76e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 76.25 E-value: 6.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 203 SWQALIDE-DRLLSRLEVMGNQLQAYSKNQTE-----DGIRKELVTLQEDKHSYETT---AKESLRRVLQEKIEVVRKLS 273
Cdd:TIGR02168 233 RLEELREElEELQEELKEAEEELEELTAELQEleeklEELRLEVSELEEEIEELQKElyaLANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 274 EVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQH---RIDEME 350
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETlrsKVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 351 EKEQLLQARIEALQAdndftneRLTALQVRLEQL-QEKNIKDHNSIEHFLLKSGGDCSEL----------FQQFIECKNK 419
Cdd:TIGR02168 393 LQIASLNNEIERLEA-------RLERLEDRRERLqQEIEELLKKLEEAELKELQAELEELeeeleelqeeLERLEEALEE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 420 LKAPVEPTQ-------------NNRISNVEDMFEsHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEE---------- 476
Cdd:TIGR02168 466 LREELEEAEqaldaaerelaqlQARLDSLERLQE-NLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyeaaieaalg 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 477 ---TKLLKENQLEAKE------------------SDMSDTLSPSKDR----SSEDTTDYQMDEQELNESLNKV--SLLKD 529
Cdd:TIGR02168 545 grlQAVVVENLNAAKKaiaflkqnelgrvtflplDSIKGTEIQGNDReilkNIEGFLGVAKDLVKFDPKLRKAlsYLLGG 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 530 LL-------AEARASSRKHESELDHLKYELQCAH-VQTGDSE----------REKQELQQELKEAQELAISSKQKCFEM- 590
Cdd:TIGR02168 625 VLvvddldnALELAKKLRPGYRIVTLDGDLVRPGgVITGGSAktnssilerrREIEELEEKIEELEEKIAELEKALAELr 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 591 --QALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILRE---DKEIEIIETRDQLASTHKEIVALRQTAVEAATGR 665
Cdd:TIGR02168 705 keLEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEEriaQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 666 ESdiaiLQGELHKVQTELEQWRQTASEYESEIFNlqtklqlqtqqqkdkQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQ 745
Cdd:TIGR02168 785 EE----LEAQIEQLKEELKALREALDELRAELTL---------------LNEEAANLRERLESLERRIAATERRLEDLEE 845
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 746 EKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVklahAENETQKFQKQYEADQ 825
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE----LESKRSELRRELEELR 921
|
730 740
....*....|....*....|....
gi 1952581424 826 TMYLELKEKLDKTQKENESITDEL 849
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRIDNLQERL 945
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
163-862 |
6.99e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 76.25 E-value: 6.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGirKELVT 242
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL--EELEA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 243 LQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKY-NGAVNELKEFTEKL 321
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEEL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 322 KQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQAdndftneRLTALQVRLEQLQEKNIKDHNSIEHFLLK 401
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA-------RLDSLERLQENLEGFSEGVKALLKNQSGL 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 402 SGGDcsELFQQFIECKNKLKAPVEPTQNNRISNVEDmfeshlENNQTTEED---LKNdSERFKATLIAEDD--HTKVTEE 476
Cdd:TIGR02168 519 SGIL--GVLSELISVDEGYEAAIEAALGGRLQAVVV------ENLNAAKKAiafLKQ-NELGRVTFLPLDSikGTEIQGN 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 477 TKLLKENQ---------LEAKESDMSDTLSPSKDRS--SEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESel 545
Cdd:TIGR02168 590 DREILKNIegflgvakdLVKFDPKLRKALSYLLGGVlvVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAK-- 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 546 dhlkyelqcAHVQTGDSEREKQELQQELKEAQELAISSKQKcfemQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKD 625
Cdd:TIGR02168 668 ---------TNSSILERRREIEELEEKIEELEEKIAELEKA----LAELRKELEELEEELEQLRKELEELSRQISALRKD 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 626 IEILRedKEIEIIEtrDQLASTHKEIVALRqtavEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIFnlqtklq 705
Cdd:TIGR02168 735 LARLE--AEVEQLE--ERIAQLSKELTELE----AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK------- 799
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 706 lqtqqqkdkqkgeavQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKAL 785
Cdd:TIGR02168 800 ---------------ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 786 EVEVGTLKEQR---LQETNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQK 862
Cdd:TIGR02168 865 EELIEELESELealLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| CC1_SLMAP-like |
cd21868 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ... |
167-204 |
2.46e-13 |
|
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar proteins; The family includes Sarcolemmal membrane-associated protein (SLMAP), its paralog TRAF3-interacting JNK-activating modulator (T3JAM), and similar proteins. SLMAP, also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. T3JAM, also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. SLMAP contains an N-terminal FHA domain, followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409286 [Multi-domain] Cd Length: 38 Bit Score: 64.81 E-value: 2.46e-13
10 20 30
....*....|....*....|....*....|....*...
gi 1952581424 167 QLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSW 204
Cdd:cd21868 1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
14-106 |
6.17e-13 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 65.36 E-value: 6.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 14 SHPFQERHVYLDE-PVKIGRSvarcrpAQNNATFDCKVLSRNHALIWFDHktGKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716 8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
|
90
....*....|....
gi 1952581424 93 pPCELLSGDIIQFG 106
Cdd:COG1716 75 -PAPLRDGDVIRLG 87
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
52-106 |
1.33e-12 |
|
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 (AGGF1) and similar proteins; AGGF1, also called angiogenic factor VG5Q, or G patch domain-containing protein 7 (GPATC7), or vasculogenesis gene on 5q protein, is an angiogenic factor involved in vascular development, angiogenesis, specification of hemangioblasts, and differentiation of veins. It promotes angiogenesis and the proliferation of endothelial cells. It inhibits inflammatory effect and preserve vascular integrity in non-nervous system diseases. Mutated AGGF1 causes susceptibility to Klippel-Trenaunay syndrome, a vascular disorder. Increased AGGF1 expression is associated with tumor angiogenesis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438738 [Multi-domain] Cd Length: 123 Bit Score: 65.38 E-value: 1.33e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1952581424 52 SRNHALIWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCELLSGDIIQFG 106
Cdd:cd22686 48 SKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPYPLTHGDELKIG 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
539-827 |
3.91e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 539 RKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQkcfemqALLEEERKTAKKQVEESTRQIQALQAH 618
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAEL------AELEAELEELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 619 LHKLQKDIEILREDKE------IEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASE 692
Cdd:COG1196 290 EYELLAELARLEQDIArleerrRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 693 YESEIfNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLT 772
Cdd:COG1196 370 AEAEL-AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1952581424 773 KDASGLEVSRKALEVEVgtlkEQRLQETNGLRVKLAHAENETQKFQKQYEADQTM 827
Cdd:COG1196 449 EEEAELEEEEEALLELL----AELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-786 |
4.09e-12 |
|
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: 70.47 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 156 NSPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALID-EDRLLSRLEVMGNQLQAY-SKNQTE 233
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEElESRLEELEEQLETLRSKVaQLELQI 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 234 DGIRKELVTLQEDKHSyettAKESLRRVLQEKIEVVRKLSEVERSLsnTEDECTHLKEMNDRTQEELRELANKYNGAVNE 313
Cdd:TIGR02168 396 ASLNNEIERLEARLER----LEDRRERLQQEIEELLKKLEEAELKE--LQAELEELEEELEELQEELERLEEALEELREE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 314 LKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQAR----------IEALQADNDFTNERLTALQVRLEQ 383
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQsglsgilgvlSELISVDEGYEAAIEAALGGRLQA 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 384 LQEKNIKDHNSIEHFLLKSG------------------GDCSELFQQFIECKNKLKAPVepTQNNRISNVEDMFESHL-- 443
Cdd:TIGR02168 550 VVVENLNAAKKAIAFLKQNElgrvtflpldsikgteiqGNDREILKNIEGFLGVAKDLV--KFDPKLRKALSYLLGGVlv 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 444 -ENNQTTEEDLKndSERFKATLIAEDDH----------------TKVTEETKLLKEN-----QLEAKESDMSDTLSPSKD 501
Cdd:TIGR02168 628 vDDLDNALELAK--KLRPGYRIVTLDGDlvrpggvitggsaktnSSILERRREIEELeekieELEEKIAELEKALAELRK 705
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 502 RSSEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQcahvqtgDSEREKQELQQELKEAQELAI 581
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT-------ELEAEIEELEERLEEAEEELA 778
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 582 SSKQKcfemQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDK---EIEIIETRDQLASTHKEIVALRQTa 658
Cdd:TIGR02168 779 EAEAE----IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLeslERRIAATERRLEDLEEQIEELSED- 853
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 659 VEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIfnlqTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKN 738
Cdd:TIGR02168 854 IESLAAEIEELEELIEELESELEALLNERASLEEALALL----RSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1952581424 739 DCDSLRQEKVLLTEKL-QWFEEELRCAQQQSVKLTKDASGLEVSRKALE 786
Cdd:TIGR02168 930 RLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
294-851 |
2.73e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 294 DRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALsekkELQHRIDEMEEKEQLLQARIEALQADNDFTNER 373
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE----ELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 374 LTALQVRLEQLQEKNIKDHNSIEhfllksggdcsELFQQFIECKNKLKApveptQNNRISNVEDMFESHLENNQTTEEDL 453
Cdd:COG1196 311 RRELEERLEELEEELAELEEELE-----------ELEEELEELEEELEE-----AEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 454 KNDSERFKATLIAEDDHTKVTEETKLLKENQLEAKEsdmsdtlspskdRSSEDTTDYQMDEQELNESLNKVSLLKDLLAE 533
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEE------------ALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 534 ARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEES----- 608
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAglrgl 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 609 TRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASthKEIVALRQTAVEAAT---------GRESDIAILQGELHKV 679
Cdd:COG1196 523 AGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA--AAIEYLKAAKAGRATflpldkiraRAALAAALARGAIGAA 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 680 QTELEQWRQTASEYESEIFNL---QTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQW 756
Cdd:COG1196 601 VDLVASDLREADARYYVLGDTllgRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 757 FEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYEADQTM---YLELKE 833
Cdd:COG1196 681 LEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEaleELPEPP 760
|
570
....*....|....*...
gi 1952581424 834 KLDKTQKENESITDELEN 851
Cdd:COG1196 761 DLEELERELERLEREIEA 778
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
329-864 |
6.98e-11 |
|
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: 66.28 E-value: 6.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 329 EEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQaDNDFTNERLTalqVRLEQLQEKN---IKDHNSIEHF--LLKSG 403
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQ-ELQFENEKVS---LKLEEEIQENkdlIKENNATRHLcnLLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 404 GDCSELFQQFIECKNKLKAPVEPTQNNRISNVEDMFESHL--ENNQTTEEDLKNDSERFKATLIAEDDHTKVTEETK--- 478
Cdd:pfam05483 164 CARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRvqAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKqvs 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 479 --LLKENQLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAH 556
Cdd:pfam05483 244 llLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIAT 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 557 VQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIE---ILREDK 633
Cdd:pfam05483 324 KTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEemtKFKNNK 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 634 EIEIIETRDQLASTHKEIVALRQTA--VEAATGRESDIAIL----QGELHKVQTELEQWRQTASEYESEIfnlqtklqlq 707
Cdd:pfam05483 404 EVELEELKKILAEDEKLLDEKKQFEkiAEELKGKEQELIFLlqarEKEIHDLEIQLTAIKTSEEHYLKEV---------- 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 708 tqqqkDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEV 787
Cdd:pfam05483 474 -----EDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRD 548
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581424 788 EVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQKGN 864
Cdd:pfam05483 549 ELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGS 625
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
157-551 |
2.24e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.70 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 157 SPSMYSQELFQLSQY--LQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEd 234
Cdd:TIGR02169 659 SRAPRGGILFSRSEPaeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE- 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 235 girkelvtLQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQ-EELRELANKYNGAVNE 313
Cdd:TIGR02169 738 --------RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSR 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 314 LKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKnikdhn 393
Cdd:TIGR02169 810 IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR------ 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 394 siehfLLKSGGDCSELFQQFIECKNK---LKAPVEpTQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKATLIAEDdh 470
Cdd:TIGR02169 884 -----LGDLKKERDELEAQLRELERKieeLEAQIE-KKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED-- 955
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 471 tkvteetklLKEnQLEAKESDMSDtLSPSKDRSSEDTTDYQMDEQELNESLNKvsllkdlLAEARASSRKHESELDHLKY 550
Cdd:TIGR02169 956 ---------VQA-ELQRVEEEIRA-LEPVNMLAIQEYEEVLKRLDELKEKRAK-------LEEERKAILERIEEYEKKKR 1017
|
.
gi 1952581424 551 E 551
Cdd:TIGR02169 1018 E 1018
|
|
| FHA_TCF19 |
cd22685 |
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ... |
28-119 |
1.32e-09 |
|
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar proteins; TCF-19, also called transcription factor SC1, was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It also functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. TCF-19 contains an N-terminal fork head association domain (FHA), a proline rich region, and a C-terminal plant homeodomain (PHD) finger. The FHA domain may serve as a nuclear signaling domain or as a phosphoprotein binding domain. The proline rich region is a common characteristic of trans-activating factors. The PHD finger may allow TCF-19 to interact with chromatin via methylated histone H3.
Pssm-ID: 438737 [Multi-domain] Cd Length: 130 Bit Score: 57.04 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 28 VKIGRSVARCRPAQNNATFDcKVLSRNHALIW---FDHKTGKFYLQDTkSSNGTFINSQRLSRGSEEsppcELLSGDIIQ 104
Cdd:cd22685 30 YRIGRNPEVCDVFLCSSQHP-NLISREHAEIHaerDGNGNWKVLIEDR-STNGTYVNDVRLQDGQRR----ELSDGDTIT 103
|
90
....*....|....*..
gi 1952581424 105 FG--VDVTENTRKVTHG 119
Cdd:cd22685 104 FGhkNGRRVKQWPYQKS 120
|
|
| CC1_T3JAM |
cd21912 |
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ... |
164-204 |
1.60e-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: 53.89 E-value: 1.60e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1952581424 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSW 204
Cdd:cd21912 5 EILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
594-861 |
2.00e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 594 LEEERKTAKK----QVEESTRQIQALQAHLHKLQKDIEILRED---KEIEIIETRDQLASTHKEIVALRQTAVEAatgrE 666
Cdd:COG1196 205 LERQAEKAERyrelKEELKELEAELLLLKLRELEAELEELEAEleeLEAELEELEAELAELEAELEELRLELEEL----E 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 667 SDIAILQGELHKVQTELEQWRQTASEYESEIfnlqtklqlqtqqqkDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQE 746
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERR---------------RELEERLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 747 KVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYEADQT 826
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270
....*....|....*....|....*....|....*
gi 1952581424 827 MYLELKEKLDKTQKENESITDELENCKENLKLLQQ 861
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
28-85 |
3.92e-09 |
|
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.
Pssm-ID: 214578 [Multi-domain] Cd Length: 52 Bit Score: 52.95 E-value: 3.92e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581424 28 VKIGRSvarcrPAQNNATFDCKVLSRNHALIWFDhKTGKFYLQDTKSSNGTFINSQRL 85
Cdd:smart00240 1 VTIGRS-----SEDCDIQLDGPSISRRHAVIVYD-GGGRFYLIDLGSTNGTFVNGKRI 52
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
27-106 |
5.43e-09 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 (FKH1), 2 (FKH2) and similar proteins; This family includes FKH1 and FKH2, as well as pre-rRNA-processing protein FHL1. FKH1 and FKH2 are forkhead transcription factors that regulate the expression of the CLB2 cluster of genes during the G2/M phase of the mitotic cell cycle. The CLB2 cluster of genes includes mitotic regulators such as CLB1, CLB2, CDC5 and CDC20, as well as SWI5 and ACE2. FKH1 and FKH2 are involved in HMRa silencing. They associate with the coding regions of active genes and influence, in opposing ways, transcriptional elongation and termination, and coordinate early transcription elongation and pre-mRNA processing. Both FKH1 and FKH2 play a role as regulators of lifespan in collaboration with the anaphase-promoting complex (APC), likely through combined regulation of stress response, genomic stability, and cell cycle regulation. They also function in controlling yeast cell morphology by preventing pseudohyphal growth and act as rate-limiting replication origin activators via their interaction with the origin recognition complex (ORC). FHL1 is a forkhead protein that controls the pre-rRNA processing machinery in conjunction with IFH1. It might act as a transcriptional regulator of genes specifically involved in that process. IFH1 convert FHL1 from a repressor to an activator. This family also includes AtFHA1 and AtFHA2, which may play a role in the control of plant organ development. AtFHA2 is specifically involved in the regulation of stamen development. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438753 [Multi-domain] Cd Length: 106 Bit Score: 54.55 E-value: 5.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 27 PVKIGRSVARcRPAQNNATFDC-----KVLSRNHALIWFDHKTGKFYLQdTKSSNGTFINSQRLSRGseeSPPCELLSGD 101
Cdd:cd22701 18 EVVLGRNSKN-SSSTAADSVDIdlgpsKKISRRHARIFYDFTTQCFELS-VLGRNGVKVDGILVKPG---SPPVPLRSGS 92
|
....*
gi 1952581424 102 IIQFG 106
Cdd:cd22701 93 LIQIG 97
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
254-796 |
1.46e-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: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 254 AKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQ 333
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 334 kalsEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKDHNSIEHFLLKSggdcSELFQQF 413
Cdd:COG1196 317 ----RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL----EELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 414 IECKNKLKApveptQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKvTEETKLLKENQLEAKESDMS 493
Cdd:COG1196 389 LEALRAAAE-----LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE-ALEEAAEEEAELEEEEEALL 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 494 DTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLA--EARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQ- 570
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAdyEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEa 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 571 --------------QELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIE 636
Cdd:COG1196 543 alaaalqnivveddEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 637 IIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQK 716
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 717 GEAVQLQGKLDELQKQSNglkndcDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQR 796
Cdd:COG1196 703 EEEERELAEAEEERLEEE------LEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
14-110 |
2.43e-08 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine/threonine-protein kinase MEK1 and similar proteins; MEK1 (EC 2.7.11.1), also known as MRE4, is a meiosis-specific protein kinase required for chromosome synapsis and meiotic recombination. The recruitment and activation of MEK1 require the phosphorylation of the chromosome axis protein Hop1 at Thr318 (pT318), which is necessary for recognition by the MEK1 FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438722 [Multi-domain] Cd Length: 105 Bit Score: 52.62 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 14 SHPFQERHV---YLDEPVKIGRSvARCRPAQNNATfdckvLSRNHALIW---FDHKTG-KFYLQDTkSSNGTFINSQRLS 86
Cdd:cd22670 7 SSPGSTDIVlpiYKNQVITIGRS-PSCDIVINDPF-----VSRTHCRIYsvqFDESSApLVYVEDL-SSNGTYLNGKLIG 79
|
90 100
....*....|....*....|....*
gi 1952581424 87 RGseespPCELLS-GDIIQFGVDVT 110
Cdd:cd22670 80 RN-----NTVLLSdGDVIEIAHSAT 99
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
479-814 |
3.29e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 479 LLKENQLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQ 558
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 559 TGDSEREKQELQQELKEAQelaisskqkcfEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREdKEIEII 638
Cdd:COG1196 311 RRELEERLEELEEELAELE-----------EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA-ELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 639 ETRDQLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIfNLQTKLQLQTQQQKDKQKGE 718
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE-EEEEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 719 AVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQ--QSVKLTKDASGLEVSRKALEVEVGTLKEQR 796
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGflEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
330
....*....|....*...
gi 1952581424 797 LQETNGLRVKLAHAENET 814
Cdd:COG1196 538 AALEAALAAALQNIVVED 555
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
567-862 |
3.55e-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: 57.37 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 567 QELQQELKEAQeLAISSKQKCFemqalLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEilredkeieiiETRDQLAS 646
Cdd:TIGR02168 216 KELKAELRELE-LALLVLRLEE-----LREELEELQEELKEAEEELEELTAELQELEEKLE-----------ELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 647 THKEIVALrQTAVEAATgreSDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQqqkdkqkgEAVQLQGKL 726
Cdd:TIGR02168 279 LEEEIEEL-QKELYALA---NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE--------ELAELEEKL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 727 DELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLK---EQRLQETNGL 803
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEdrrERLQQEIEEL 426
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581424 804 RVKLahAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQK 862
Cdd:TIGR02168 427 LKKL--EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
563-850 |
4.38e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 4.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 563 EREKQELQQELK-EAQELAisskqkcfemQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEilreDKEIEIIETR 641
Cdd:TIGR02169 206 EREKAERYQALLkEKREYE----------GYELLKEKEALERQKEAIERQLASLEEELEKLTEEIS----ELEKRLEEIE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 642 DQLASTHKEIVALRqtaveaatgrESDIAILQGELHKVQTELEQWRQTASEYESEIfNLQTKLQLQTQQQKDKQKGEAVQ 721
Cdd:TIGR02169 272 QLLEELNKKIKDLG----------EEEQLRVKEKIGELEAEIASLERSIAEKEREL-EDAEERLAKLEAEIDKLLAEIEE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 722 LQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQ--- 798
Cdd:TIGR02169 341 LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRlse 420
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952581424 799 ---------------------ETNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELE 850
Cdd:TIGR02169 421 eladlnaaiagieakineleeEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
516-841 |
5.19e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 5.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 516 ELNESLNKVSLLKDLLAEARA-SSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALL 594
Cdd:TIGR02169 195 EKRQQLERLRREREKAERYQAlLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 595 EEERKTAKKQVEESTRQIqalQAHLHKLQKDIEILrEDKEIEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQG 674
Cdd:TIGR02169 275 EELNKKIKDLGEEEQLRV---KEKIGELEAEIASL-ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 675 ELHKVQTELEQWRQTASEYESEIfnlqtklqLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKL 754
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEDLRAEL--------EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 755 QWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRlqetnglrvklahaenetQKFQKQYEADQTMYLELKEK 834
Cdd:TIGR02169 423 ADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL------------------SKYEQELYDLKEEYDRVEKE 484
|
....*..
gi 1952581424 835 LDKTQKE 841
Cdd:TIGR02169 485 LSKLQRE 491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
337-685 |
6.38e-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: 56.60 E-value: 6.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 337 SEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKDHNSIEHFLLKSGGDCSELFQQFIEC 416
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 417 KNKLKapVEPTQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKATliaEDDHTKVTEETKLLKENQLEAKEsdmsdTL 496
Cdd:TIGR02168 757 TELEA--EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL---REALDELRAELTLLNEEAANLRE-----RL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 497 SPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLkyelqcahvqtgdsEREKQELQQELKEA 576
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL--------------LNERASLEEALALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 577 QELAISskqkcfemqalLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILredkEIEIIETRDQLASTHKeivALRQ 656
Cdd:TIGR02168 893 RSELEE-----------LSEELRELESKRSELRRELEELREKLAQLELRLEGL----EVRIDNLQERLSEEYS---LTLE 954
|
330 340
....*....|....*....|....*....
gi 1952581424 657 TAVEAATGRESDIAILQGELHKVQTELEQ 685
Cdd:TIGR02168 955 EAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
271-861 |
1.09e-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: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 271 KLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKAlsekKELQHRIDEME 350
Cdd:TIGR04523 97 KINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKY----NDLKKQKEELE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 351 EKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKnIKDHNSIEHFLLKSGGDCSELFQQFIECKNKLKApveptQNN 430
Cdd:TIGR04523 173 NELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKK-IQKNKSLESQISELKKQNNQLKDNIEKKQQEINE-----KTT 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 431 RISNVEDmfeshlENNQTTEEDLKNDSERFKATLIAEDDHTKVTEETKLLkeNQLEAKESDM-----SDTLSPSKDRSSE 505
Cdd:TIGR04523 247 EISNTQT------QLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL--NQLKSEISDLnnqkeQDWNKELKSELKN 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 506 DTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAqelaISSKQ 585
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL----ESQIN 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 586 KcfemqalLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREdkeiEIIETRDQLASTHKEIVALRQTAVEAATGR 665
Cdd:TIGR04523 395 D-------LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKE----TIIKNNSEIKDLTNQDSVKELIIKNLDNTR 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 666 ES---DIAILQGELHKVQTELEQWRQTASEYESEIFNLQTklqlqtqqqkdkqkgEAVQLQGKLDELQKQSNGLKNDCDS 742
Cdd:TIGR04523 464 ESletQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE---------------EKKELEEKVKDLTKKISSLKEKIEK 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 743 LRQEKVLLTEKLQWFEEELrcaqqQSVKLTKDASGLEVSRKALEVEVGTLKEQR---LQETNGLRVKLAHAENETQKFQK 819
Cdd:TIGR04523 529 LESEKKEKESKISDLEDEL-----NKDDFELKKENLEKEIDEKNKEIEELKQTQkslKKKQEEKQELIDQKEKEKKDLIK 603
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1952581424 820 QYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQ 861
Cdd:TIGR04523 604 EIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQ 645
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
55-108 |
1.23e-07 |
|
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) family; The Cep170 family includes Cep170 and Cep170B. Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438756 [Multi-domain] Cd Length: 102 Bit Score: 50.40 E-value: 1.23e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1952581424 55 HALIWFDHKTGKFYLQDTKSSNGTFINSQRLSrgseESPPCELLSGDIIQFGVD 108
Cdd:cd22704 39 HAVITYDQIDNEFKIKDLGSLNGTFVNDSRIP----EQTYITLKLGDSIRFGYD 88
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
225-869 |
1.26e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 225 QAYSKNQTEDGIRKELVTLQEDKHSYETTAK-ESLRRV--LQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELR 301
Cdd:PTZ00121 1195 KAEDARKAEAARKAEEERKAEEARKAEDAKKaEAVKKAeeAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA 1274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 302 ELANKyngaVNELKEFTEKLKQAEGKQEEIQQKA--LSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQV 379
Cdd:PTZ00121 1275 EEARK----ADELKKAEEKKKADEAKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKA 1350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 380 RLEQLQEKNIKDHNSIEHFLLKSGgdcselfqqfiecKNKLKAPVEPTQNNRISNVEDMFESHLENNQTTEEDLKNDSER 459
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKE-------------EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAK 1417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 460 FKAtliaeDDHTKVTEETKLLKENQLEAKESDMSDTLSP-SKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLAEARASS 538
Cdd:PTZ00121 1418 KKA-----DEAKKKAEEKKKADEAKKKAEEAKKADEAKKkAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKA 1492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 539 RKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAK-KQVEESTRQIQALQA 617
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElKKAEEKKKAEEAKKA 1572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 618 HLHKLQ--KDIEILREDKEIEIIETRDQLASTHKEIVALRQTAVEAATGREsdiailqgELHKVQTELEQWRQTASEYES 695
Cdd:PTZ00121 1573 EEDKNMalRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE--------ELKKAEEEKKKVEQLKKKEAE 1644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 696 EIFNLQTKLQLQTQQQ--KDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLR---QEKVLLTEKLQWFEEELRCAQQQSVK 770
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKikAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKkeaEEAKKAEELKKKEAEEKKKAEELKKA 1724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 771 LTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELe 850
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDI- 1803
|
650
....*....|....*....
gi 1952581424 851 ncKENLKLLQQKGNNGGLF 869
Cdd:PTZ00121 1804 --FDNFANIIEGGKEGNLV 1820
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
25-114 |
1.29e-07 |
|
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. Specially, RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438715 [Multi-domain] Cd Length: 110 Bit Score: 50.82 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 25 DEPVKIGRSVArcrpAQNNATFDC-KVLSRNHALIWFDhKTGKFYLQDTKSSNGTFINSQRLsrgsEESPPCELLSGDII 103
Cdd:cd22663 20 GKEVTVGRGLG----VTYQLVSTCpLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERI----EPLKPYPLNEGDLI 90
|
90
....*....|.
gi 1952581424 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 ... |
30-106 |
3.09e-07 |
|
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438750 [Multi-domain] Cd Length: 93 Bit Score: 48.95 E-value: 3.09e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581424 30 IGRSVArcrpaqNNATFDCKVLSRNHALIwfDHKTGKFYLQDTKSSNGTFINSQRLSRGseesppcELLSGDIIQFG 106
Cdd:cd22698 25 IGRSSN------NDIRLNDHSVSRHHARI--VRQGDKCNLTDLGSTNGTFLNGIRVGTH-------ELKHGDRIQLG 86
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
246-864 |
5.85e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.58 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 246 DKHSYETTAKESLRRVLQEKIEvvrklsEVERSLSNTEDectHLKEMNDRTqEELRELANKYNGAVNELKEFTEKLKQAE 325
Cdd:pfam15921 131 DIRRRESQSQEDLRNQLQNTVH------ELEAAKCLKED---MLEDSNTQI-EQLRKMMLSHEGVLQEIRSILVDFEEAS 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 326 GKQ-------------------EEIQQKALSEKKELQHRIDEMEEKEQLL---------------QARIEALQADNDFTN 371
Cdd:pfam15921 201 GKKiyehdsmstmhfrslgsaiSKILRELDTEISYLKGRIFPVEDQLEALksesqnkielllqqhQDRIEQLISEHEVEI 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 372 ERLT-----------ALQVRLEQLQEKNIKDHNSIEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQNNRISNVEDMFE 440
Cdd:pfam15921 281 TGLTekassarsqanSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 441 SHLENNQTTEEDLKNDSERFKatLIAedDHTKVTEETKLLKENQLEAKESDMSDTLSPSKDRSSEDttDYQMDEQEL--- 517
Cdd:pfam15921 361 ARTERDQFSQESGNLDDQLQK--LLA--DLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELD--DRNMEVQRLeal 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 518 ----------------------NESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELkE 575
Cdd:pfam15921 435 lkamksecqgqmerqmaaiqgkNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAI-E 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 576 AQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDkeieiIETRDQLASTHKEIVALR 655
Cdd:pfam15921 514 ATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQ-----IENMTQLVGQHGRTAGAM 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 656 QtaVEAATgresdiaiLQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKGEAVQLQGKLDeLQKQSNG 735
Cdd:pfam15921 589 Q--VEKAQ--------LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKD-IKQERDQ 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 736 LKNDCDSLRQEKVLLTEKLQWFEEELRC-AQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENET 814
Cdd:pfam15921 658 LLNEVKTSRNELNSLSEDYEVLKRNFRNkSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQIT 737
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1952581424 815 QKfQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQKGN 864
Cdd:pfam15921 738 AK-RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKN 786
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
181-673 |
6.32e-07 |
|
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: 53.19 E-value: 6.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 181 MLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQT--EDGIRKELVTLQEDKHSYETTAKESL 258
Cdd:pfam05483 262 LLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKalEEDLQIATKTICQLTEEKEAQMEELN 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 259 RRVLQEKIEVvrklSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQ------ 332
Cdd:pfam05483 342 KAKAAHSFVV----TEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKkilaed 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 333 QKALSEKKELQHRIDEMEEKEQ----LLQAR----------IEALQADNDFTNERLTALQVRLEQLQEKNIKDHNSIEHF 398
Cdd:pfam05483 418 EKLLDEKKQFEKIAEELKGKEQelifLLQARekeihdleiqLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKL 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 399 LLKSggdcSELFQQFIECKNKLKAPVEPTQNNRisNVEDMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKV----T 474
Cdd:pfam05483 498 LLEN----KELTQEASDMTLELKKHQEDIINCK--KQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCkldkS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 475 EETKLLKENQLEAKESDMSDTLSPSKD--RSSEDTTDYQMDEQELNESLNKVSLLKD------------LLAEARASSRK 540
Cdd:pfam05483 572 EENARSIEYEVLKKEKQMKILENKCNNlkKQIENKNKNIEELHQENKALKKKGSAENkqlnayeikvnkLELELASAKQK 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 541 HESELDHLKYELQCAHVQT----GDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQ 616
Cdd:pfam05483 652 FEEIIDNYQKEIEDKKISEekllEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYK 731
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581424 617 AHlhklQKDIEILREDKEIEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQ 673
Cdd:pfam05483 732 NK----EQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILK 784
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
182-836 |
7.61e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.20 E-value: 7.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 182 LEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGIRKELVTLQEDKHSYETTakeslrrv 261
Cdd:pfam15921 243 VEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSM-------- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 262 lqekieVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSekkE 341
Cdd:pfam15921 315 ------YMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLA---D 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 342 LQHRIDEME-EKEQllQARIEALQADNDFTNERLTalqvrlEQLQEKNIKDHNsIEHFLLKSGGDCSELFQQFIECKNKL 420
Cdd:pfam15921 386 LHKREKELSlEKEQ--NKRLWDRDTGNSITIDHLR------RELDDRNMEVQR-LEALLKAMKSECQGQMERQMAAIQGK 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 421 KAPVEptqnnRISNVEDMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEEtkllKENQLEAKESDMSdTLSPSK 500
Cdd:pfam15921 457 NESLE-----KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE----KERAIEATNAEIT-KLRSRV 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 501 DRSSEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKyELQCAH--------VQTGDSEREKQELQQE 572
Cdd:pfam15921 527 DLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMT-QLVGQHgrtagamqVEKAQLEKEINDRRLE 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 573 LKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALqahlhklqKDIEILREDKEIEIIETRDQLASTHKEIV 652
Cdd:pfam15921 606 LQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAV--------KDIKQERDQLLNEVKTSRNELNSLSEDYE 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 653 ALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESeifnlqtklqlqtqqqkdkQKGEAVQLQGKldeLQKQ 732
Cdd:pfam15921 678 VLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEG-------------------SDGHAMKVAMG---MQKQ 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 733 SNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGL--EVSRKALEVEVGTLKEQRLQE-TNGLRVKLAH 809
Cdd:pfam15921 736 ITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVatEKNKMAGELEVLRSQERRLKEkVANMEVALDK 815
|
650 660
....*....|....*....|....*....
gi 1952581424 810 AENETQKFQK--QYEADQTMYLELKEKLD 836
Cdd:pfam15921 816 ASLQFAECQDiiQRQEQESVRLKLQHTLD 844
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
502-786 |
8.22e-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: 53.14 E-value: 8.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 502 RSSEDTTDYQMDEQELNE-----SLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEA 576
Cdd:TIGR02168 207 RQAEKAERYKELKAELRElelalLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 577 QE--LAISSKQKCFEMQ-ALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKE---IEIIETRDQLASTHKE 650
Cdd:TIGR02168 287 QKelYALANEISRLEQQkQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEelkEELESLEAELEELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 651 IVALRQTAVEAATGRE---SDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKGEavqLQGKLD 727
Cdd:TIGR02168 367 LEELESRLEELEEQLEtlrSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE---LQAELE 443
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581424 728 ELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALE 786
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
167-685 |
1.22e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 167 QLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEvmgnqlqaysknQTEDGIRKELVTLQED 246
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE------------EALLEAEAELAEAEEE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 247 KHSyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELAnkyngavNELKEFTEKLKQAEG 326
Cdd:COG1196 381 LEE----LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE-------EEEEEEEEALEEAAE 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 327 KQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQadndftnERLTALQVRLEQLQEKNIKDHNSIEHFLLKSGGDC 406
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELA-------EAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 407 SELFQQFIECKNKLKAPVEPTQNNRISNVedmfeshlenNQTTEEDLKNDSERFKATLIAeddhtKVTEETKLLKENQLE 486
Cdd:COG1196 523 AGAVAVLIGVEAAYEAALEAALAAALQNI----------VVEDDEVAAAAIEYLKAAKAG-----RATFLPLDKIRARAA 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 487 AKESDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREK 566
Cdd:COG1196 588 LAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSR 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 567 QELQQELKEAQELAISSKQKcfemQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLAs 646
Cdd:COG1196 668 RELLAALLEAEAELEELAER----LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL- 742
|
490 500 510
....*....|....*....|....*....|....*....
gi 1952581424 647 thkEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQ 685
Cdd:COG1196 743 ---EEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
27-117 |
1.60e-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: 47.36 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 27 PVKIGRSVarcrpaQNNATFDCKVLSRNHALIWFDHKTGKFYLQDTKSSNGTFINSQRLsrgSEESPPCELLSGDIIQFG 106
Cdd:cd22678 24 PLTIGRIQ------RGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESI---SPNGRPVVLSSGDVITLG 94
|
90
....*....|.
gi 1952581424 107 vdvTENTRKVT 117
Cdd:cd22678 95 ---SETKILVR 102
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
234-762 |
2.33e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 234 DGIRKELVTLQEDKHSYETTAKEsLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEmNDRTQEELRELANKYNgavnE 313
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKE-LESLEGSKRKLEEKIRELEERIEELKKEIEELEE-KVKELKELKEKAEEYI----K 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 314 LKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQL----------LQARIEALQADNDfTNERLTALQVRLEQ 383
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERleelkkklkeLEKRLEELEERHE-LYEEAKAKKEELER 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 384 LQEKniKDHNSIEHF--LLKSGGDCSELFQQFIECKNKLKAPVEPTQNNRISNVEDMFESHLE----NNQTTEEDLKNDS 457
Cdd:PRK03918 377 LKKR--LTGLTPEKLekELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHRKELL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 458 ERFKATLIAEDDHTKVTEEtkllKENQLEAKESDMSDTLSpskdRSSEDTTDYQMDEQ--ELNESLNKVSLLKdlLAEAR 535
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEE----KERKLRKELRELEKVLK----KESELIKLKELAEQlkELEEKLKKYNLEE--LEKKA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 536 ASSRKHESELDHLKYELqcahvqtgdserekQELQQELKEAQELAISSkqkcfemqALLEEERKTAKKQVEESTRQIQAL 615
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEI--------------KSLKKELEKLEELKKKL--------AELEKKLDELEEELAELLKELEEL 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 616 Q-AHLHKLQKDIEILRE--DKEIEIIETRDQLASTHKEIVALRQTAVEAatgrESDIAILQGELHKVQTELEQWRQtasE 692
Cdd:PRK03918 583 GfESVEELEERLKELEPfyNEYLELKDAEKELEREEKELKKLEEELDKA----FEELAETEKRLEELRKELEELEK---K 655
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952581424 693 YESEIFNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQ--EKVLLTEKLQWFEEELR 762
Cdd:PRK03918 656 YSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKakKELEKLEKALERVEELR 727
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
51-106 |
3.05e-06 |
|
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also called human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP), is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438729 [Multi-domain] Cd Length: 106 Bit Score: 46.78 E-value: 3.05e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952581424 51 LSRNHALIWF----DHKTGKFYLQDTKSSNGTFINSQRLsrgseesPP---CELLSGDIIQFG 106
Cdd:cd22677 41 ISRYHAVLQYrgdaDDHDGGFYLYDLGSTHGTFLNKQRI-------PPkqyYRLRVGHVLKFG 96
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
561-784 |
3.12e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 561 DSEREKQELQQELKEAQELAISSKQKcfemQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREdkeiEIIET 640
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK----EIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 641 RDQLASTHKEIValRQTAVEAATGRESDIAIL--QGELHKVQTELeQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKGE 718
Cdd:COG4942 96 RAELEAQKEELA--ELLRALYRLGRQPPLALLlsPEDFLDAVRRL-QYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952581424 719 AVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKA 784
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
121-862 |
5.10e-06 |
|
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: 50.50 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 121 IVSTVKLFMPDGMEGRRRSDVIQAPLPLPVEKVAANspsmYSQELFQLSQYLQEA--LHREQ--MLEQKLATLQRLLANT 196
Cdd:pfam15921 47 TFTQIPIFPKYEVELDSPRKIIAYPGKEHIERVLEE----YSHQVKDLQRRLNESneLHEKQkfYLRQSVIDLQTKLQEM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 197 QEASDsswqALIDedrlLSRLEvmgNQLQAYSKNQTEDGIRK--ELVTLQEDKHSYETTAKESLRRVLQEKIEVVRKLSE 274
Cdd:pfam15921 123 QMERD----AMAD----IRRRE---SQSQEDLRNQLQNTVHEleAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 275 VERSLSNTEDECTHlkEMNDRTQEELRELANKYNGAVNELKEFTEKLK--------QAEGKQEEIQQKALSEKKELQHRI 346
Cdd:pfam15921 192 ILVDFEEASGKKIY--EHDSMSTMHFRSLGSAISKILRELDTEISYLKgrifpvedQLEALKSESQNKIELLLQQHQDRI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 347 DEMEEKEQLlqaRIEALQADNDFTNERLTALQVRLEQLQEKNIKDHNSIEHFLLKSGGDCSELFQQFIECKNKLKAPVEP 426
Cdd:pfam15921 270 EQLISEHEV---EITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 427 TQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKatLIAedDHTKVTEETKLLKENQLEAKESDMSDTLSPSKDRSSED 506
Cdd:pfam15921 347 LEKQLVLANSELTEARTERDQFSQESGNLDDQLQK--LLA--DLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELD 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 507 ttDYQMDEQEL-------------------------NESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGD 561
Cdd:pfam15921 423 --DRNMEVQRLeallkamksecqgqmerqmaaiqgkNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSD 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 562 SEREKQELQQELkEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDkeieiIETR 641
Cdd:pfam15921 501 LTASLQEKERAI-EATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQ-----IENM 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 642 DQLASTHKEIVALRQtaVEAATgresdiaiLQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKGEAVQ 721
Cdd:pfam15921 575 TQLVGQHGRTAGAMQ--VEKAQ--------LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSER 644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 722 LQG------KLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQ-SVKLTKDASGLEVSRK----------- 783
Cdd:pfam15921 645 LRAvkdikqERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKlKMQLKSAQSELEQTRNtlksmegsdgh 724
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 784 ALEVEVGTLKE---------------QRLQET---------------NGLRVKLAHAENETQKFQKQYEADQTMYLELKE 833
Cdd:pfam15921 725 AMKVAMGMQKQitakrgqidalqskiQFLEEAmtnankekhflkeekNKLSQELSTVATEKNKMAGELEVLRSQERRLKE 804
|
810 820
....*....|....*....|....*....
gi 1952581424 834 KLDKTQKENESITDELENCKENLKLLQQK 862
Cdd:pfam15921 805 KVANMEVALDKASLQFAECQDIIQRQEQE 833
|
|
| FHA_CHFR |
cd22672 |
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ... |
49-105 |
6.40e-06 |
|
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains protein (CHFR); CHFR, also called RING finger protein 196 (RNF196), is a checkpoint protein that delays entry into mitosis in response to stress. It functions as an E3 ubiquitin ligase that ubiquitinates and degrades its target proteins, such as Aurora-A, Plk1, Kif22 and PARP-1, which are critical for proper mitotic transitions. It also plays an important role in cell cycle progression and tumor suppression and is negatively regulated by SUMOylation-mediated proteasomal ubiquitylation. Moreover, CHFR is involved in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation. CHFR contains a fork head associated-(FHA) domain and a RING-HC finger. The CHFR FHA domain has been crystallized as a segment-swapped dimer. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438724 [Multi-domain] Cd Length: 108 Bit Score: 45.75 E-value: 6.40e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581424 49 KVLSRNHALIWFDHKtGKFYLQDTkSSNGTFINSQRLSRGSEesppCELLSGDIIQF 105
Cdd:cd22672 39 KLVSGDHCKIIRDEK-GQVWLEDT-STNGTLVNKVKVVKGQK----VELKHGDVIYL 89
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
298-854 |
6.87e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 6.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 298 EELRELANKYNGAVNELKEftEKLKQAEGKQEEIQQKalsEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTAL 377
Cdd:PRK02224 165 EEYRERASDARLGVERVLS--DQRGSLDQLKAQIEEK---EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 378 QVRLEQLQEKnikdhnsiehfllksggdcselfQQFIEcknKLKAPVEPTQNNrISNVEDMFESHLENNQTTEEDLKNDS 457
Cdd:PRK02224 240 DEVLEEHEER-----------------------REELE---TLEAEIEDLRET-IAETEREREELAEEVRDLRERLEELE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 458 ERFKATLiAEDDHTKVTEETKLLKENQLEAKESDMSDTLSPSK----------DRSSEDTTDYQMDEQELNEslnKVSLL 527
Cdd:PRK02224 293 EERDDLL-AEAGLDDADAEAVEARREELEDRDEELRDRLEECRvaaqahneeaESLREDADDLEERAEELRE---EAAEL 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 528 KDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKK---- 603
Cdd:PRK02224 369 ESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEaeal 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 604 ---------------------------QVEESTRQIQALQAHLHKLQKDIEILREDKEIEI-IETRDQLASTHKEIVALR 655
Cdd:PRK02224 449 leagkcpecgqpvegsphvetieedreRVEELEAELEDLEEEVEEVEERLERAEDLVEAEDrIERLEERREDLEELIAER 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 656 QTAVEAatgRESDIAILQGELHKVQTELEQWRQTASEYESEIfnlqtklqlqtqqqkDKQKGEAVQLQGKLDELQKQSNG 735
Cdd:PRK02224 529 RETIEE---KRERAEELRERAAELEAEAEEKREAAAEAEEEA---------------EEAREEVAELNSKLAELKERIES 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 736 LKNDCDSL------RQEKVLLTEKLQWFEEElrcAQQQSVKLtkdaSGLEVSRKALEvevGTLKEQRLQEtngLRVKLAH 809
Cdd:PRK02224 591 LERIRTLLaaiadaEDEIERLREKREALAEL---NDERRERL----AEKRERKRELE---AEFDEARIEE---AREDKER 657
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1952581424 810 AEnetqkfqkQYEADQTMYL-ELKEKLDKTQKENESITDELENCKE 854
Cdd:PRK02224 658 AE--------EYLEQVEEKLdELREERDDLQAEIGAVENELEELEE 695
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
150-845 |
7.20e-06 |
|
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: 49.97 E-value: 7.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 150 VEKVAANSPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASdsSWQALIDEdrLLSRLEVMGNQLQAYSK 229
Cdd:TIGR00618 206 LTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQL--KKQQLLKQ--LRARIEELRAQEAVLEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 230 NQTEDGIRKELVTLQEDKhsyettakESLRRVLQEKIEVVRKLSEVERSLSNT-EDECTHLKEMNDrtQEELRELANKYN 308
Cdd:TIGR00618 282 TQERINRARKAAPLAAHI--------KAVTQIEQQAQRIHTELQSKMRSRAKLlMKRAAHVKQQSS--IEEQRRLLQTLH 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 309 GAVNELKEFTEKlkQAEGKQEEIQQKALSEK-KELQHRIDEMEEKEQLLQARIEALQADndftnerltALQVRLEQLQEK 387
Cdd:TIGR00618 352 SQEIHIRDAHEV--ATSIREISCQQHTLTQHiHTLQQQKTTLTQKLQSLCKELDILQRE---------QATIDTRTSAFR 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 388 NIKDHNSIEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQNnrisnveDMFESHLENNQTtEEDLKNDSERFKATliae 467
Cdd:TIGR00618 421 DLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQ-------ESAQSLKEREQQ-LQTKEQIHLQETRK---- 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 468 ddHTKVTEETKLLKENQLEAKESdmsdTLSPSKDRssedttdYQMDEQELNESLnkvsllkdlLAEARASSRKHESELDH 547
Cdd:TIGR00618 489 --KAVVLARLLELQEEPCPLCGS----CIHPNPAR-------QDIDNPGPLTRR---------MQRGEQTYAQLETSEED 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 548 LKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIE 627
Cdd:TIGR00618 547 VYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 628 ILREDKEIEIIETRDQLASTHKEivalrQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQ 707
Cdd:TIGR00618 627 LQDVRLHLQQCSQELALKLTALH-----ALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQ 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 708 TQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDcdsLRQEKVLLTEKLQWFEEELRCAQQQSVkltkdasgLEVSRKALEV 787
Cdd:TIGR00618 702 CQTLLRELETHIEEYDREFNEIENASSSLGSD---LAAREDALNQSLKELMHQARTVLKART--------EAHFNNNEEV 770
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581424 788 evgTLKEQRLQEtnglrvkLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESI 845
Cdd:TIGR00618 771 ---TAALQTGAE-------LSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDI 818
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
52-106 |
7.61e-06 |
|
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 (PPP1R8) and similar proteins; PPP1R8, also called nuclear inhibitor of protein phosphatase 1 (NIPP-1), is an inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. It may also be involved in pre-mRNA splicing and binds DNA and might act as a transcriptional repressor. PPP1R8 seems to be required for cell proliferation. PPP1R8 contains an FHA domain that mediates interactions with threonine-phosphorylated maternal embryonic leucine zipper kinase (MELK). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438726 [Multi-domain] Cd Length: 108 Bit Score: 45.72 E-value: 7.61e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1952581424 52 SRNHALIWFDHKTGKFYLQDTKSSNGTFINSQRLsrgsEESPPCELLSGDIIQFG 106
Cdd:cd22674 48 SRVHAALVYHKHLNRVFLIDLGSTHGTFVGGIRL----EPHKPQQLPIDSTLRFG 98
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
239-634 |
7.72e-06 |
|
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: 49.51 E-value: 7.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 239 ELVTLQEDKHSYE------------TTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRElanK 306
Cdd:pfam07888 5 ELVTLEEESHGEEggtdmllvvpraELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELES---R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 307 YNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQllqaRIEALQADNDFTNERLTALQVRLEQLQE 386
Cdd:pfam07888 82 VAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEA----RIRELEEDIKTLTQRVLERETELERMKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 387 KNIK----------DHNSIEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQnnrisnvedmfesHLENNQTTEEDLKND 456
Cdd:pfam07888 158 RAKKagaqrkeeeaERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVL-------------QLQDTITTLTQKLTT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 457 SERFKATLIAEDDHTKVTEETKLLKENQLEAKESDMSDTLSpSKDRSSEDTTDYQMDEQELNESLNKVSLlkdLLAEARA 536
Cdd:pfam07888 225 AHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAA-QRDRTQAELHQARLQAAQLTLQLADASL---ALREGRA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 537 SSRKHESELdhlkyeLQCAHVQTGDSEREKQELQQELKEAQElAISSKQKcfeMQALLEEERKTAKKQVEESTRQIQALQ 616
Cdd:pfam07888 301 RWAQERETL------QQSAEADKDRIEKLSAELQRLEERLQE-ERMEREK---LEVELGREKDCNRVQLSESRRELQELK 370
|
410
....*....|....*...
gi 1952581424 617 AHLHKLQKDIEILREDKE 634
Cdd:pfam07888 371 ASLRVAQKEKEQLQAEKQ 388
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
264-696 |
7.78e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 7.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 264 EKIEVVR-KLSEVERSLSNTEDECTHLKEMNDRTQEElRELANKYNGAVNELKEFTEKLKQAEgkqeeiQQKALSEKKEL 342
Cdd:TIGR02169 170 RKKEKALeELEEVEENIERLDLIIDEKRQQLERLRRE-REKAERYQALLKEKREYEGYELLKE------KEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 343 QHRIDEMEEKEQLLQARIEALqadndftNERLTALQVRLEQLQEKnIKDHNSIEhfllksggdcselfqqfiecKNKLKA 422
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISEL-------EKRLEEIEQLLEELNKK-IKDLGEEE--------------------QLRVKE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 423 PVEPTQNnRISNVEDMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEETKLLKEnQLeakesdmsdtlspskdr 502
Cdd:TIGR02169 295 KIGELEA-EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD-KL----------------- 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 503 ssedTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAIS 582
Cdd:TIGR02169 356 ----TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAG 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 583 SKQKcfemQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDkeieiietrdqlasthkeivalrqtaveaa 662
Cdd:TIGR02169 432 IEAK----INELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE------------------------------ 477
|
410 420 430
....*....|....*....|....*....|....
gi 1952581424 663 tgresdIAILQGELHKVQTELEQWRQTASEYESE 696
Cdd:TIGR02169 478 ------YDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
233-665 |
8.30e-06 |
|
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: 50.05 E-value: 8.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 233 EDGIRKELVTLQ----EDKHSYETTAK--ESLRRVLQEKIEVVRKLSE------VERSL-SNTEDECTHLKEMNdrtqEE 299
Cdd:TIGR01612 1269 EMDIKAEMETFNishdDDKDHHIISKKhdENISDIREKSLKIIEDFSEesdindIKKELqKNLLDAQKHNSDIN----LY 1344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 300 LRELANKYN-GAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQL--LQARIEALQADNDFTN--ERL 374
Cdd:TIGR01612 1345 LNEIANIYNiLKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLeeCKSKIESTLDDKDIDEciKKI 1424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 375 TALQVRLEQlQEKNIKDH--NSIEHfllksGGDCSELFQQFIECKNKLKAPVEPTQNNRIS----NVEDMFESHLENNQT 448
Cdd:TIGR01612 1425 KELKNHILS-EESNIDTYfkNADEN-----NENVLLLFKNIEMADNKSQHILKIKKDNATNdhdfNINELKEHIDKSKGC 1498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 449 TEEDLKNDSERFKATLIAEDDHTKVTE----ETKLLKENQLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKV 524
Cdd:TIGR01612 1499 KDEADKNAKAIEKNKELFEQYKKDVTEllnkYSALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEK 1578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 525 SLLKDLLAEARASSRKH---ESELDHLKYE-LQCAHVQT--GDSEREKQELQQELK----EAQELAISSKQKCFEMQALL 594
Cdd:TIGR01612 1579 FRIEDDAAKNDKSNKAAidiQLSLENFENKfLKISDIKKkiNDCLKETESIEKKISsfsiDSQDTELKENGDNLNSLQEF 1658
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952581424 595 EEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASTHKEIVALRQTAVEAATGR 665
Cdd:TIGR01612 1659 LESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKEEIESIKELIEPTIEN 1729
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
25-108 |
8.40e-06 |
|
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar proteins; ZEP, also called protein ABA DEFICIENT 1, ABA1, protein IMPAIRED IN BABA-INDUCED STERILITY 3, protein LOW EXPRESSION OF OSMOTIC STRESS-RESPONSIVE GENES 6, or protein NON-PHOTOCHEMICAL QUENCHING 2, plays an important role in the xanthophyll cycle and abscisic acid (ABA) biosynthesis. It converts zeaxanthin into antheraxanthin and subsequently violaxanthin. ZEP is required for resistance to osmotic and drought stresses, ABA-dependent stomatal closure, seed development and dormancy, modulation of defense gene expression, and disease resistance and non-photochemical quencing (NPQ). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438754 [Multi-domain] Cd Length: 123 Bit Score: 45.88 E-value: 8.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 25 DEPVKIGRsvarcRPAQNNAT----FDCKVLSRNHALIWFdhKTGKFYLQDTKSSNGTFINSQRLSR-GSEESPPCELLS 99
Cdd:cd22702 31 KQPCIIGS-----DPHQAISGisvvIPSPQVSELHARITC--KNGAFFLTDLGSEHGTWINDNEGRRyRAPPNFPVRLHP 103
|
....*....
gi 1952581424 100 GDIIQFGVD 108
Cdd:cd22702 104 SDVIEFGSD 112
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
264-835 |
8.42e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 8.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 264 EKIEVVRKLSEVERSLSNTEDECTHLKEmNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQ 343
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEE-QREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 344 HRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKDHNSIEhfllksggDCSELFQQFIECKNKLKAP 423
Cdd:PRK02224 279 EEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLE--------ECRVAAQAHNEEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 424 VE--PTQNNRISNVEDMFESHLENnqtTEEDLkndsERFKATLIAEDDHTKVTEETKLLKENQLEAKEsDMSDTLSPSKD 501
Cdd:PRK02224 351 ADdlEERAEELREEAAELESELEE---AREAV----EDRREEIEELEEEIEELRERFGDAPVDLGNAE-DFLEELREERD 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 502 RSSEDTTDYQMDEQELNESLNKVsllKDLLAEARASSRKHESEldhlkyelQCAHVQTGDSEREK-QELQQELKEAQEla 580
Cdd:PRK02224 423 ELREREAELEATLRTARERVEEA---EALLEAGKCPECGQPVE--------GSPHVETIEEDRERvEELEAELEDLEE-- 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 581 isskqkcfEMQALleEERKTAKKQVEESTRQIQALQAHLhklqKDIEILREDKEIEIIETRDQLASTHKEIVALRQTAVE 660
Cdd:PRK02224 490 --------EVEEV--EERLERAEDLVEAEDRIERLEERR----EDLEELIAERRETIEEKRERAEELRERAAELEAEAEE 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 661 AatgrESDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQkgEAVQLQGKLDELQKQSNGLKNDC 740
Cdd:PRK02224 556 K----REAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAED--EIERLREKREALAELNDERRERL 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 741 DSLRQEKVLLTEKLQWFE-EELRCAQQQSVKLTKDASG----LEVSRKALEVEVGTLkEQRLQETNGLRVKLAHAENETQ 815
Cdd:PRK02224 630 AEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEkldeLREERDDLQAEIGAV-ENELEELEELRERREALENRVE 708
|
570 580
....*....|....*....|...
gi 1952581424 816 KFQKQY---EADQTMYLELKEKL 835
Cdd:PRK02224 709 ALEALYdeaEELESMYGDLRAEL 731
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
211-548 |
1.10e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 211 DRLLSRLEVMGNQLQAYSKNQTEdgIRKELVTLQEDkhsyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLK 290
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAE--LRKELEELEEE-----------LEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 291 EMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQkalsekkelqhRIDEMEEKEQLLQARIEALQADNDFT 370
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA-----------QIEQLKEELKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 371 NERLTALQVRLEQLQEKNIKDHNSIEhFLLKSGGDCSELFQQFIECKNKLKAPveptqnnrISNVEDMFESHLENNQTTE 450
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLE-DLEEQIEELSEDIESLAAEIEELEEL--------IEELESELEALLNERASLE 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 451 EDLKN-DSERFKATLIAEDDHTKVTEETKLLKE-----NQLEAKESDMSDTLSPSKDRSSEdttDYQMDEQELnesLNKV 524
Cdd:TIGR02168 887 EALALlRSELEELSEELRELESKRSELRRELEElreklAQLELRLEGLEVRIDNLQERLSE---EYSLTLEEA---EALE 960
|
330 340
....*....|....*....|....
gi 1952581424 525 SLLKDLLAEARASSRKHESELDHL 548
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKEL 984
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
28-106 |
1.39e-05 |
|
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438732 [Multi-domain] Cd Length: 96 Bit Score: 44.64 E-value: 1.39e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581424 28 VKIGRSVarcrpaQNNATFDCKVLSRNHALIWFDhkTGKFYLQDTKSSNGTFINSQRlsrgsEESPPCELLSGDIIQFG 106
Cdd:cd22680 23 VSIGRDP------ENVIVIPDPFVSRNHARITVD--SNEIYIEDLGSTNGTFVNDFK-----RIKGPAKLHPNDIIKLG 88
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
13-110 |
1.76e-05 |
|
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also called nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438717 [Multi-domain] Cd Length: 97 Bit Score: 44.14 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 13 NSHPFQERHVYLDE-PVKIGRSvarcrpAQNNATFDCKVLSRNHALIWFDHKTgkFYLQDTKSSNGTFINSQRLSrgsee 91
Cdd:cd22665 7 SQAHGPEKDFPLYEgENVIGRD------PSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRL----- 73
|
90 100
....*....|....*....|.
gi 1952581424 92 SPPC--ELLSGDIIQFGvDVT 110
Cdd:cd22665 74 KPNVryELIDGDLLLFG-DVK 93
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
52-107 |
1.95e-05 |
|
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also called cell cycle regulatory protein p95, or Nijmegen breakage syndrome protein 1 (NBS1), is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. Nibrin modulates the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-dependent protein kinase catalytic subunit (DNA-PKcs) to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. Nibrin also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. Nibrin is a major player in the control of intra-S-phase checkpoint. This subfamily also includes Schizosaccharomyces pombe DNA repair and telomere maintenance protein Nbs1 and Arabidopsis thaliana AtNbs1. SpNbs1 is an FHA domain-containing protein required for DNA damage repair and S-phase DNA damage checkpoint. It is involved in telomere length maintenance and maintenance of chromatin structure. AtNbs1 is a component of MRN complex. It also functions in the very early stages of meiosis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438719 [Multi-domain] Cd Length: 108 Bit Score: 44.24 E-value: 1.95e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952581424 52 SRNHALIWFDHKTG---------KFYLQDTkSSNGTFINSQRLSRGSEesppCELLSGDIIQFGV 107
Cdd:cd22667 40 SRKHATLTVLHPEAnlsdpdtrpELTLKDL-SKYGTFVNGEKLKGGSE----VTLKDGDVITFGV 99
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
297-579 |
2.02e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 297 QEELRELANKYngAVNELKEFTEKLKQAEGKQEEIQQK---ALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNER 373
Cdd:TIGR02168 219 KAELRELELAL--LVLRLEELREELEELQEELKEAEEEleeLTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 374 LTALQVRLEQLQEKNIKDHNSIEhfllkSGGDCSELFQQFIECKNKLKAPVEPtQNNRISNVEDMFESHLENNQTTEEDL 453
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLE-----ELEAQLEELESKLDELAEELAELEE-KLEELKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 454 KNDSERFKATLIAEDDHTKVTEETKLLKENQLEAKESDMSDtLSPSKDRSSEDTTD--YQMDEQELNESLNKVSLLKDLL 531
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER-LEDRRERLQQEIEEllKKLEEAELKELQAELEELEEEL 449
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1952581424 532 AEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQEL 579
Cdd:TIGR02168 450 EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
256-861 |
2.21e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.51 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 256 ESLRRVLQEKIEVVRK--LSEVERSLSNTEDECTHLKEMN--DRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEI 331
Cdd:TIGR01612 1058 DEIEKEIGKNIELLNKeiLEEAEINITNFNEIKEKLKHYNfdDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEI 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 332 QQKALSEKKELQHRIDEMEEkeqllqariealQADNDFTNERLTALQVRLEQL-----QEKNI---------------KD 391
Cdd:TIGR01612 1138 KKKSENYIDEIKAQINDLED------------VADKAISNDDPEEIEKKIENIvtkidKKKNIydeikkllneiaeieKD 1205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 392 HNSIEHFL---LKSGGDCSELFQQFIECKNKLKAPVEPTQNNRISNVEDMFES--HLENNQTTEEDLKNDSERFKATLIA 466
Cdd:TIGR01612 1206 KTSLEEVKginLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKspEIENEMGIEMDIKAEMETFNISHDD 1285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 467 EDDHTKVTEE---------TKLLKENQLEAKESDMSDTlspsKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLaearas 537
Cdd:TIGR01612 1286 DKDHHIISKKhdenisdirEKSLKIIEDFSEESDINDI----KKELQKNLLDAQKHNSDINLYLNEIANIYNIL------ 1355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 538 srkhesELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQA 617
Cdd:TIGR01612 1356 ------KLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKIESTLDDKDIDECIKKIKELKN 1429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 618 HlhklqkdieILREDKEieiIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQ-----GELHKVQTELEQWRQTASE 692
Cdd:TIGR01612 1430 H---------ILSEESN---IDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKkdnatNDHDFNINELKEHIDKSKG 1497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 693 YESEI--------FNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKlqwFEEELRCA 764
Cdd:TIGR01612 1498 CKDEAdknakaieKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEK---SEQKIKEI 1574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 765 QQQSVKLTKDASGLEVSRKA---LEVEVGTLKEQRLQETNgLRVKLAHAENETQKFQKQ-----YEADQTMYLELKEKLD 836
Cdd:TIGR01612 1575 KKEKFRIEDDAAKNDKSNKAaidIQLSLENFENKFLKISD-IKKKINDCLKETESIEKKissfsIDSQDTELKENGDNLN 1653
|
650 660
....*....|....*....|....*
gi 1952581424 837 KTQKENESITDELENCKENLKLLQQ 861
Cdd:TIGR01612 1654 SLQEFLESLKDQKKNIEDKKKELDE 1678
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
18-86 |
2.24e-05 |
|
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the first FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438746 [Multi-domain] Cd Length: 93 Bit Score: 43.86 E-value: 2.24e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581424 18 QERHVYLDEPVKIGRSvarcrpAQNNATFDCKVLSRNHALIWFDhkTGKFYLQDTKSSNGTFINSQRLS 86
Cdd:cd22694 8 GELRFDPGSSVRIGRD------PDADVRLDDPRVSRRHALLEFD--GDGWVYTDLGSRNGTYLNGRRVQ 68
|
|
| FHA_RAD53-like_rpt2 |
cd22690 |
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
12-103 |
2.91e-05 |
|
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine/threonine-protein kinase RAD53 and similar proteins; RAD53, also called CHEK2 homolog, or serine-protein kinase 1 (Spk1), is a nuclear protein kinase that phosphorylates proteins on serine, threonine, and tyrosine. It controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints and prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. It may be involved in the phosphorylation of RPH1. RAD53 contains two FHA domains. This model corresponds to the second one. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438742 [Multi-domain] Cd Length: 105 Bit Score: 43.82 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 12 PNSHPfqerHVYL-DEPVKIGRSvarcrpAQNNATFDCKVLSRNHALIWFD-HKTGK--FYLQDTkSSNGTFINSQRLSR 87
Cdd:cd22690 8 NPSYP----DIELtQNTTFIGRS------KDCDEEITDPRISKHHCIITRKrSGKGLddVYVTDT-STNGTFINNNRLGK 76
|
90
....*....|....*.
gi 1952581424 88 GSEesppCELLSGDII 103
Cdd:cd22690 77 GSQ----SLLQDGDEI 88
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
30-106 |
3.16e-05 |
|
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.
Pssm-ID: 438734 [Multi-domain] Cd Length: 96 Bit Score: 43.67 E-value: 3.16e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581424 30 IGRSVarcrpaQNNATFDCKVLSRNHALiwFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEesppCELLSGDIIQFG 106
Cdd:cd22682 24 IGRSV------ESQVQIDDDSVSRYHAK--LAVNPSAVSIIDLGSTNGTIVNGKKIPKLAS----CDLQNGDQIKIG 88
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
1-106 |
3.20e-05 |
|
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442679 [Multi-domain] Cd Length: 402 Bit Score: 47.45 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 1 MPSALAIFTCRPNSHPFQERHVYLDEPVKIGRSvARC-----RPAQnnatfdckVLSRNHALIWFDHktGKFYLQDTkSS 75
Cdd:COG3456 1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRS-ADCdwvlpDPDR--------SVSRRHAEIRFRD--GAFCLTDL-ST 68
|
90 100 110
....*....|....*....|....*....|...
gi 1952581424 76 NGTFIN--SQRLSRGSEEsppcELLSGDIIQFG 106
Cdd:COG3456 69 NGTFLNgsDHPLGPGRPV----RLRDGDRLRIG 97
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
49-112 |
3.37e-05 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 (PML1) and similar proteins; PML1 is an FHA domain-containing protein required for efficient splicing and pre-mRNA nuclear retention. It is a component of the pre-mRNA retention and splicing (RES) complex composed of at least BUD13, IST3, and PML1. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438733 [Multi-domain] Cd Length: 129 Bit Score: 44.35 E-value: 3.37e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581424 49 KVLSRNHALIWFDHKTG--KFYLQDTKSSNGTFINsqrlsrgSEESPPC---ELLSGDIIQFGVDVTEN 112
Cdd:cd22681 64 ETCSKQHCVIQFRNVKGilKPYIMDLDSSNGTCLN-------DNVIPSSryvELRSGDVITFSKSNDYE 125
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
267-392 |
4.39e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.16 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 267 EVVRKLSEveRSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLK-QAEGKQEEIQ--QKALSEKKELQ 343
Cdd:COG2433 380 EALEELIE--KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEaELEEKDERIErlERELSEARSEE 457
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1952581424 344 HRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKDH 392
Cdd:COG2433 458 RREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEH 506
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
212-865 |
5.46e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.35 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 212 RLLSRLEVMGNQLQAYSKNQTEDGIRKELVTLQEDKHSYETTAKESLRRVLQEKIEvvrkLSEVERSlSNTEDECTHLKE 291
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE----LDGFERG-PFSERQIKNFHT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 292 MNDRTQEELRELANKyngavnELKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTN 371
Cdd:TIGR00606 398 LVIERQEDEAKTAAQ------LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 372 ERLTALQVRLEQLQEKNIKDHNSIEHFLLKSggDCSELFQQFIECKNKLKAPVEPTQNNRISNVEDMFESHLENNQTTEE 451
Cdd:TIGR00606 472 RILELDQELRKAERELSKAEKNSLTETLKKE--VKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDE 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 452 DLKNDSERFKATLIAEDDH---TKVTEETKLLKENQLEAKESDMSDtLSPSKDRSSEDTTDYQMDEQELNESLNKvslLK 528
Cdd:TIGR00606 550 QIRKIKSRHSDELTSLLGYfpnKKQLEDWLHSKSKEINQTRDRLAK-LNKELASLEQNKNHINNELESKEEQLSS---YE 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 529 DLLAEArASSRKHESELDHLKYELQCAHVQ----TGDSEREKQELQQELKEAQELAISSkQKCFEMQALLEEERKTAKKQ 604
Cdd:TIGR00606 626 DKLFDV-CGSQDEESDLERLKEEIEKSSKQramlAGATAVYSQFITQLTDENQSCCPVC-QRVFQTEAELQEFISDLQSK 703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 605 VEESTRQIQALQAHLHKLQKDIEILR----------EDKEIEIIETRDQLASTHKEIVALRQ-------------TAVEA 661
Cdd:TIGR00606 704 LRLAPDKLKSTESELKKKEKRRDEMLglapgrqsiiDLKEKEIPELRNKLQKVNRDIQRLKNdieeqetllgtimPEEES 783
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 662 ATGRESDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKGEAVQ----LQGKLDELQKQSNGLK 737
Cdd:TIGR00606 784 AKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSkielNRKLIQDQQEQIQHLK 863
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 738 NDCDSLRQEKVLLTEKLQwfeeELRCAQQQSVKLTKDASGL--EVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQ 815
Cdd:TIGR00606 864 SKTNELKSEKLQIGTNLQ----RRQQFEEQLVELSTEVQSLirEIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKA 939
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1952581424 816 KFQKQyeadqtmylELKEKLDKTQKENESITDELENCKENLKllQQKGNN 865
Cdd:TIGR00606 940 QDKVN---------DIKEKVKNIHGYMKDIENKIQDGKDDYL--KQKETE 978
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
517-862 |
5.52e-05 |
|
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: 46.94 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 517 LNESLNKVSLLKDLLAEAR-ASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQAL-L 594
Cdd:TIGR04523 144 LTEIKKKEKELEKLNNKYNdLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISeL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 595 EEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILR----------EDKEIE-------IIETRDQLASTHKEIVALRQT 657
Cdd:TIGR04523 224 KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKdeqnkikkqlSEKQKEleqnnkkIKELEKQLNQLKSEISDLNNQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 658 AVEAATGR-ESDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKgeavQLQGKLDELQKqsngL 736
Cdd:TIGR04523 304 KEQDWNKElKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQR----ELEEKQNEIEK----L 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 737 KNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQ----------ETNGLRVK 806
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKnnseikdltnQDSVKELI 455
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1952581424 807 LAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQK 862
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK 511
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
514-693 |
5.71e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 514 EQELNESLNKVSLLKDLLAEARASSRKHESELDHLK--YELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQ 591
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRqkNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 592 ALLEEERKTAKKQVEEStrQIQALQAHLHKLQKDIEILRE---DKEIEIIETRDQLASTHKEIVALRQTAVEAAtgrESD 668
Cdd:COG3206 247 AQLGSGPDALPELLQSP--VIQQLRAQLAELEAELAELSArytPNHPDVIALRAQIAALRAQLQQEAQRILASL---EAE 321
|
170 180
....*....|....*....|....*
gi 1952581424 669 IAILQGELHKVQTELEQWRQTASEY 693
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAEL 346
|
|
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
53-106 |
7.28e-05 |
|
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 (FHAD1) and similar proteins; FHAD1, also called FHA domain-containing protein 1, is an uncharacterized FHA domain-containing protein. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438752 [Multi-domain] Cd Length: 96 Bit Score: 42.24 E-value: 7.28e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1952581424 53 RNHALIWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSeesppCELLSGDIIQFG 106
Cdd:cd22700 36 EQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAA-----VRLAPGDVLRFG 84
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
239-865 |
7.79e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 7.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 239 ELVTLQEDKHSYETTAKESLRRV--LQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKE 316
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 317 FTEKLKQAEGKQEEIQQKA--LSEKKELQHRIDEMEEKEQLLQARIEALQ----ADNDFTNERLTALQVRLEQLQEKNIK 390
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKAdaAKKKAEEKKKADEAKKKAEEDKKKADELKkaaaAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 391 DHNSIEHfLLKSGGDCSELFQQFIECKNKLKAPVEPTQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKATLIAEDDH 470
Cdd:PTZ00121 1442 EAKKADE-AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE 1520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 471 TKVTEETKLLKENQ-----LEAKESDMSDTLSPSKD-RSSEDTtdyQMDEQELNESLNKVSLLKDLlAEARASSRKHESE 544
Cdd:PTZ00121 1521 AKKADEAKKAEEAKkadeaKKAEEKKKADELKKAEElKKAEEK---KKAEEAKKAEEDKNMALRKA-EEAKKAEEARIEE 1596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 545 LDHLKYELQCAHVQTGDSEREKQELQQELKEAQELaissKQKCFEMQALLEEERKTA---KKQVEESTRQIQALQAHLHK 621
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE----KKKVEQLKKKEAEEKKKAeelKKAEEENKIKAAEEAKKAEE 1672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 622 LQKDIEILREDKEIEiietrdqlasthkeivalrqTAVEAATGRESDIAILQGELHKVQTElEQWRQTASEYESEIFNLQ 701
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDE--------------------KKAAEALKKEAEEAKKAEELKKKEAE-EKKKAEELKKAEEENKIK 1731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 702 TKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEK-VLLTEKLQWFEEELRCAQQQSVKLTKDASG-LE 779
Cdd:PTZ00121 1732 AEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKeAVIEEELDEEDEKRRMEVDKKIKDIFDNFAnII 1811
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 780 VSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENlKLL 859
Cdd:PTZ00121 1812 EGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEA-DEI 1890
|
....*.
gi 1952581424 860 QQKGNN 865
Cdd:PTZ00121 1891 EKIDKD 1896
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
164-688 |
8.64e-05 |
|
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: 46.37 E-value: 8.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRL------------LSRLEVMGNQLQAYSKNQ 231
Cdd:pfam12128 259 RLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGelsaadaavakdRSELEALEDQHGAFLDAD 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 232 TE---------DGIRKELvTLQEDKHSYETTAKESL-----RRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQ 297
Cdd:pfam12128 339 IEtaaadqeqlPSWQSEL-ENLEERLKALTGKHQDVtakynRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 298 EEL-RELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKEL------QHRIDEMEEKEQLLQARIEALQADN--- 367
Cdd:pfam12128 418 QALeSELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLlqlenfDERIERAREEQEAANAEVERLQSELrqa 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 368 -----------DFTNERLTALQVRLEQLQEKNIKDHNSIEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQNNRISNVE 436
Cdd:pfam12128 498 rkrrdqasealRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGE 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 437 DMFES---HLENNQT-----TEEDLKNDSERFKATLIAEDDHTKVTEETKLLKENQLEAKESDMSDTLSPSKDrsSEDTT 508
Cdd:pfam12128 578 LNLYGvklDLKRIDVpewaaSEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKN--ARLDL 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 509 DYQMDEQElNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSERE----KQELQQEL---KEAQELAI 581
Cdd:pfam12128 656 RRLFDEKQ-SEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREarteKQAYWQVVegaLDAQLALL 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 582 SSKQKCFEMQA-----LLEEERKT--AKKQVEESTrqIQALQAHLHKLQKDIEILREDKEiEIIETRDQLASTHKEIVAL 654
Cdd:pfam12128 735 KAAIAARRSGAkaelkALETWYKRdlASLGVDPDV--IAKLKREIRTLERKIERIAVRRQ-EVLRYFDWYQETWLQRRPR 811
|
570 580 590
....*....|....*....|....*....|....
gi 1952581424 655 RQTAVEAAtgrESDIAILQGELHKVQTELEQWRQ 688
Cdd:pfam12128 812 LATQLSNI---ERAISELQQQLARLIADTKLRRA 842
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
178-359 |
9.35e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 9.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 178 REQML--EQKLATLQRLLANTQEAsDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGIRKELVTLQEDKHSYE---T 252
Cdd:COG4913 241 HEALEdaREQIELLEPIRELAERY-AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEarlD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 253 TAKESLRRV--------------LQEKIE-VVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEF 317
Cdd:COG4913 320 ALREELDELeaqirgnggdrleqLEREIErLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEE 399
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1952581424 318 TEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEK-----EQLLQAR 359
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERRksnipARLLALR 446
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
453-697 |
9.36e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 9.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 453 LKNDSERFKATLIAEDDHTKVTEETKLLKENQLEAKESDMSDTlspsKDRSSEDTTDYQMDEQELNESLNKVS------- 525
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL----RLEVSELEEEIEELQKELYALANEISrleqqkq 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 526 LLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEM---QALLEEERKTAK 602
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELesrLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 603 KQVEESTRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASTHKEIVALRQTAVEaatGRESDIAILQGELHKVQTE 682
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE---ELEEELEELQEELERLEEA 462
|
250
....*....|....*
gi 1952581424 683 LEQWRQTASEYESEI 697
Cdd:TIGR02168 463 LEELREELEEAEQAL 477
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
178-746 |
9.51e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 9.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 178 REQMLEQK--LATLQRLLANTQEASDSSwQALIDEDRLLSRLEVMGNQLQAYSKNqtedgiRKELVTLQEDKHSYETTAK 255
Cdd:COG4913 214 REYMLEEPdtFEAADALVEHFDDLERAH-EALEDAREQIELLEPIRELAERYAAA------RERLAELEYLRAALRLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 256 ESLRRVLQEKIEvvrklsEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGA-VNELKEFTEKLKQAEGKQEEIQQK 334
Cdd:COG4913 287 QRRLELLEAELE------ELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERR 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 335 AlsekKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKDHnsiehfllksggdcSELFQQFI 414
Cdd:COG4913 361 R----ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL--------------RDLRRELR 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 415 ECKNKLKApveptQNNRISNVE-------DMFESHLENnqtTEEDL---------KNDSER-----------FKATLIAE 467
Cdd:COG4913 423 ELEAEIAS-----LERRKSNIParllalrDALAEALGL---DEAELpfvgelievRPEEERwrgaiervlggFALTLLVP 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 468 DDH----TKVTEETKLLKENQLEAKESDMSDTLSPskdRSSEDTTDYQMD----------EQELNESLN--KVSLLKDLL 531
Cdd:COG4913 495 PEHyaaaLRWVNRLHLRGRLVYERVRTGLPDPERP---RLDPDSLAGKLDfkphpfrawlEAELGRRFDyvCVDSPEELR 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 532 AEARA---------SSRKHESELDHLKYELQC----AHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEER 598
Cdd:COG4913 572 RHPRAitragqvkgNGTRHEKDDRRRIRSRYVlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 599 KTAkkQVEESTRQIQALQAHLHKLQKDIEILREDKeIEIIETRDQLASTHKEIVALRQ---TAVEAATGRESDIAILQGE 675
Cdd:COG4913 652 RLA--EYSWDEIDVASAEREIAELEAELERLDASS-DDLAALEEQLEELEAELEELEEeldELKGEIGRLEKELEQAEEE 728
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952581424 676 LHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKgeavQLQGKLDELQKQSNGLKNDCDSLRQE 746
Cdd:COG4913 729 LDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE----NLEERIDALRARLNRAEEELERAMRA 795
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
152-639 |
1.27e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 152 KVAANSPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDsswqaliDEDRLLSRLEVMGNQLQAYSKNQ 231
Cdd:COG4717 60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA-------ELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 232 TEDGIRKELVTLQEdkhsyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMND-RTQEELRELANKYNGA 310
Cdd:COG4717 133 ELEALEAELAELPE--------RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 311 VNELKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLeqlqeknik 390
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTI--------- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 391 dhnsIEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQNNRISNVEDMFESHLENNQTTEEDLkNDSERFKATLIAEDDH 470
Cdd:COG4717 276 ----AGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDL-SPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 471 TKVTEETKLLKENQLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELD--HL 548
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeEL 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 549 KYELQCAHVQTGDSEREKQELQQELKEAQelAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEI 628
Cdd:COG4717 431 EEELEELEEELEELEEELEELREELAELE--AELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREE 508
|
490
....*....|.
gi 1952581424 629 LREDKEIEIIE 639
Cdd:COG4717 509 YREERLPPVLE 519
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
250-799 |
1.29e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 250 YETTAKES--LRRVLQEKIEVVRKL----SEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGA---VNELKEFTEK 320
Cdd:PRK03918 160 YENAYKNLgeVIKEIKRRIERLEKFikrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLekeVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 321 LKQAEGKQEEIQQ--KALSEK-KELQHRIDEMEEKEQLLQARIEALQadndfTNERLTALQVRLEQLQEKNIKDHNSIEh 397
Cdd:PRK03918 240 IEELEKELESLEGskRKLEEKiRELEERIEELKKEIEELEEKVKELK-----ELKEKAEEYIKLSEFYEEYLDELREIE- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 398 fllKSGGDCSELFQQFIEcknklkapveptqnnRISNVEDMfESHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEET 477
Cdd:PRK03918 314 ---KRLSRLEEEINGIEE---------------RIKELEEK-EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 478 KLLKENQLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLAEARASS------------------- 538
Cdd:PRK03918 375 ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteehrkell 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 539 RKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELaISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAH 618
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEL-IKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEK 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 619 LHKLQKDIEILREDK-------------EIEIIETRDQLASTHKEIVALRQTAVEAATGR-----------------ESD 668
Cdd:PRK03918 534 LIKLKGEIKSLKKELekleelkkklaelEKKLDELEEELAELLKELEELGFESVEELEERlkelepfyneylelkdaEKE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 669 IAILQGELHKVQTELEQWRQTASEYESEIfnlQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSL---RQ 745
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKRL---EELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELekrRE 690
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1952581424 746 EKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQE 799
Cdd:PRK03918 691 EIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSK 744
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
596-796 |
1.53e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 596 EERKTAKKQVEESTRQIQALQAHLHKLQKDI-EILREDKEIE--IIETRDQLASTHKEIVALRQTAVEAatgrESDIAIL 672
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEkALLKQLAALErrIAALARRIRALEQELAALEAELAEL----EKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 673 QGELHKVQTELEQ-----WRQTASEYESEIFNLQTKLQLQTQQQKDKQKGEAvqLQGKLDELQKQSNGLKNDCDSLRQEK 747
Cdd:COG4942 96 RAELEAQKEELAEllralYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA--RREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1952581424 748 VLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQR 796
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
178-685 |
1.70e-04 |
|
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: 45.42 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 178 REQMLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEvmgnQLQAYSKNQTEDGIRKELVTLQEDKHSYEttakES 257
Cdd:TIGR00606 445 KKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAER----ELSKAEKNSLTETLKKEVKSLQNEKADLD----RK 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 258 LRRVLQEKIEVVRKLSEVERSLSNTEDECT---HLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQ-- 332
Cdd:TIGR00606 517 LRKLDQEMEQLNHHTTTRTQMEMLTKDKMDkdeQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAkl 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 333 QKALSEKKELQHRIDEMEEKEQLLQARIEalqaDNDFTNERLTALQVRLEQLQEKNIKDHNSIEHFLLKSGgdcseLFQQ 412
Cdd:TIGR00606 597 NKELASLEQNKNHINNELESKEEQLSSYE----DKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATA-----VYSQ 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 413 FIE---CKNKLKAPV-------EPTQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKATLI-AEDDHTKVTEETKLLK 481
Cdd:TIGR00606 668 FITqltDENQSCCPVcqrvfqtEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGlAPGRQSIIDLKEKEIP 747
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 482 E--NQLEAKESDMSdtlspskdrssEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSR-KHESELDHLKYELQCAHVQ 558
Cdd:TIGR00606 748 ElrNKLQKVNRDIQ-----------RLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERfQMELKDVERKIAQQAAKLQ 816
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 559 TGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEE-------------ERKTAKKQVEESTRQIQALQAHLHKLQKD 625
Cdd:TIGR00606 817 GSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDqqeqiqhlksktnELKSEKLQIGTNLQRRQQFEEQLVELSTE 896
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 626 IEILREdkeiEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQ 685
Cdd:TIGR00606 897 VQSLIR----EIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKN 952
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
182-386 |
1.77e-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: 44.75 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 182 LEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEvmgNQLQAYSKNQTEdgIRKELVTLQEDKHSYETtAKESLRRV 261
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALA---RRIRALEQELAA--LEAELAELEKEIAELRA-ELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 262 LQEKIEVVRKLSEVER--SLSNTEDECTHLK--EMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALS 337
Cdd:COG4942 106 LAELLRALYRLGRQPPlaLLLSPEDFLDAVRrlQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1952581424 338 EKKELQHRIDEMEEKEQLLQARIEALQAdndftneRLTALQVRLEQLQE 386
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAA-------ELAELQQEAEELEA 227
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
514-862 |
2.50e-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: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 514 EQELNESLNKVSLLKDLLAEARASSRKHE--------SELDHLKYELQcahvqtgDSEREKQELQQELKEAQELAISSKQ 585
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEaqirgnggDRLEQLEREIE-------RLERELEERERRRARLEALLAALGL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 586 KCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEiEIIETRDQLASTHK----EIVALRQTAVEA 661
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR-ELEAEIASLERRKSnipaRLLALRDALAEA 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 662 ATGRESDIAILqGELHKVQTELEQWRQTA--------------SEYE---SEIFNLQTKLQ-------LQTQQQKDKQKG 717
Cdd:COG4913 453 LGLDEAELPFV-GELIEVRPEEERWRGAIervlggfaltllvpPEHYaaaLRWVNRLHLRGrlvyervRTGLPDPERPRL 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 718 EAVQLQGKL---------------------------DELQ------------KQSNGL--KNDCDSLRQEKVL---LTEK 753
Cdd:COG4913 532 DPDSLAGKLdfkphpfrawleaelgrrfdyvcvdspEELRrhpraitragqvKGNGTRheKDDRRRIRSRYVLgfdNRAK 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 754 LQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLkeQRLQETNGLRVKLAHAENETQKFQKQY---EADQTMYLE 830
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREAL--QRLAEYSWDEIDVASAEREIAELEAELerlDASSDDLAA 689
|
410 420 430
....*....|....*....|....*....|..
gi 1952581424 831 LKEKLDKTQKENESITDELENCKENLKLLQQK 862
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKE 721
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
289-655 |
2.60e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 289 LKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKaLSEKKELQHRIDEMEEKEQLLQARIEALQADND 368
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 369 F---------TNERLTALQVRLEQLQEKnIKDHNSIEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQNNRISNVEDMF 439
Cdd:COG4717 127 LlplyqeleaLEAELAELPERLEELEER-LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 440 ------ESHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEE------------------------------------- 476
Cdd:COG4717 206 qrlaelEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllliaaallallglggsllsliltiagvlflvlgl 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 477 -----TKLLKENQLEAKESDMSDTLSPSKDRSSEDTTDY--------QMDEQELNESLNKVSLLKDLLAEARAssRKHES 543
Cdd:COG4717 286 lallfLLLAREKASLGKEAEELQALPALEELEEEELEELlaalglppDLSPEELLELLDRIEELQELLREAEE--LEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 544 ELDHLKYELQ--CAHVQTGDSE---------REKQELQQELKEAQE------------LAISSKQKCFEMQALLEEERKT 600
Cdd:COG4717 364 QLEELEQEIAalLAEAGVEDEEelraaleqaEEYQELKEELEELEEqleellgeleelLEALDEEELEEELEELEEELEE 443
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1952581424 601 AKKQVEESTRQIQALQAHLHKLQKDIEIlrEDKEIEIIETRDQLASTHKEIVALR 655
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGEL--AELLQELEELKAELRELAEEWAALK 496
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
258-387 |
2.75e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 258 LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEI----QQ 333
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkEY 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1952581424 334 KALS-EKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEK 387
Cdd:COG1579 92 EALQkEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
16-111 |
4.16e-04 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaB and similar proteins; FhaB, also called FtsZ-interacting protein A (FipA), is a putative virulence factor involved in regulating cell shape. It can interact with polyketide-associated protein PapA5, a putative membrane protein involved in the biosynthesis of virulence enhancing lipids. FhaB regulates growth and cell division. It is probably required for divisomal protein assembly under oxidative stress. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438745 [Multi-domain] Cd Length: 91 Bit Score: 39.98 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 16 PFQERHVYLD-EPVKIGRSvarcrpAQNNATFDCKVLSRNHALIWFdhKTGKFYLQDTKSSNGTFINSQRLSRgseespP 94
Cdd:cd22693 7 TLQGQTFPIDkSGITIGRA------DDNDLVLSDDFVSSRHARIYL--QGSSWYLEDLGSTNGTFVNGNRVTQ------P 72
|
90
....*....|....*..
gi 1952581424 95 CELLSGDIIQFGVDVTE 111
Cdd:cd22693 73 VVVQPGDTIRIGATVFE 89
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
198-387 |
4.80e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 198 EASDSSWQALIdEDRLLSRLEvmgNQLQAYSKNQTEDGIR--KELVTLQEDKHSYETTAKEsLRRVLQEKIEVVRKLSEV 275
Cdd:COG4717 33 EAGKSTLLAFI-RAMLLERLE---KEADELFKPQGRKPELnlKELKELEEELKEAEEKEEE-YAELQEELEELEEELEEL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 276 ERSLSNTEDECTHLKEMND---------RTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQHRI 346
Cdd:COG4717 108 EAELEELREELEKLEKLLQllplyqeleALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS 187
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1952581424 347 DEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEK 387
Cdd:COG4717 188 LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
569-767 |
5.10e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 569 LQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREdkeiEIIETRDQLASTH 648
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA----ELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 649 KEIVALRQTAVEAATGREsdIAILQGELHKVQTELEQWRQTASEYES---EIFNLQTKLQLQTQQQKDKQKGEAVQLQGK 725
Cdd:COG4717 123 KLLQLLPLYQELEALEAE--LAELPERLEELEERLEELRELEEELEEleaELAELQEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1952581424 726 LDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQ 767
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
258-862 |
5.45e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 258 LRRVLQ-EKIE-VVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQqKA 335
Cdd:PRK03918 151 VRQILGlDDYEnAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLE-KE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 336 LSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKnIKDHNSIEHFllksggdcSELFQQFIE 415
Cdd:PRK03918 230 VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK-VKELKELKEK--------AEEYIKLSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 416 CKNKLKapvepTQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKATLiaeddhTKVTEETKLLKENQLEAKESDMSDT 495
Cdd:PRK03918 301 FYEEYL-----DELREIEKRLSRLEEEINGIEERIKELEEKEERLEELK------KKLKELEKRLEELEERHELYEEAKA 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 496 LSPSKDRSSEDTTDYQMDEqelneslnkvslLKDLLAEARASSRKHESELDHLKYELqcahvqtgdseREKQELQQELKE 575
Cdd:PRK03918 370 KKEELERLKKRLTGLTPEK------------LEKELEELEKAKEEIEEEISKITARI-----------GELKKEIKELKK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 576 AQELAISSKQKCFEMQALLEEERKtaKKQVEESTRQIQALQAHLHKLQKDIEILR-EDKEIEIIETRDqlasthKEIVAL 654
Cdd:PRK03918 427 AIEELKKAKGKCPVCGRELTEEHR--KELLEEYTAELKRIEKELKEIEEKERKLRkELRELEKVLKKE------SELIKL 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 655 RQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIfnlqtKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSN 734
Cdd:PRK03918 499 KELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEI-----KSLKKELEKLEELKKKLAELEKKLDELEEELA 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 735 GLKNDCDSLRQEKVlltEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQR--LQETNGLRVKLAHAEN 812
Cdd:PRK03918 574 ELLKELEELGFESV---EELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFeeLAETEKRLEELRKELE 650
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581424 813 ETQKF--QKQYEADQTMYLEL-------KEKLDKTQKENESITDELENCKENLKLLQQK 862
Cdd:PRK03918 651 ELEKKysEEEYEELREEYLELsrelaglRAELEELEKRREEIKKTLEKLKEELEEREKA 709
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
258-647 |
6.47e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.53 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 258 LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKyngavneLKEFTEKLKQAEGKQEEI-QQKAL 336
Cdd:COG5022 760 LRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGS-------RKEYRSYLACIIKLQKTIkREKKL 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 337 SEKKELQHRIDEMEekeqLLQARIEALQADNDFTNERLTAL----QVRLEQLQEKNIKDHNSIEHFllksggdcSELFQQ 412
Cdd:COG5022 833 RETEEVEFSLKAEV----LIQKFGRSLKAKKRFSLLKKETIylqsAQRVELAERQLQELKIDVKSI--------SSLKLV 900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 413 FIECKNKLkapveptqnnrisnvedmfeshLENNQTTEEDLKNDSErFKATLIaeddhtkvTEETKLLKENQLEakesdm 492
Cdd:COG5022 901 NLELESEI----------------------IELKKSLSSDLIENLE-FKTELI--------ARLKKLLNNIDLE------ 943
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 493 sdtLSPSKDRSSEDTT-DYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQ 571
Cdd:COG5022 944 ---EGPSIEYVKLPELnKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKE 1020
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581424 572 ELKEAQELAISSKQKCFEMQALLeeERKTAKKQVEESTRQIQALQAHLHKLQKDIE-ILREDKEIEIIETRDQLAST 647
Cdd:COG5022 1021 LPVEVAELQSASKIISSESTELS--ILKPLQKLKGLLLLENNQLQARYKALKLRREnSLLDDKQLYQLESTENLLKT 1095
|
|
| FHA_SNIP1_DDL-like |
cd22676 |
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ... |
52-106 |
6.85e-04 |
|
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA domain-containing protein DDL, and similar proteins; SNIP1 is an FHA domain-containing protein required for pre-mRNA splicing as a component of the spliceosome. It inhibits NF-kappaB signaling by competing for its binding to the C/H1 domain of CBP/p300 transcriptional co-activators. It is involved in microRNA (miRNA) biogenesis. SNIP1 is a regulator of the cell cycle and cyclin D1 expression and may be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. This family also includes Arabidopsis thaliana FHA domain-containing protein DDL and similar proteins. DDL, also called protein DAWDLE, is involved in the microRNA (miRNA) and short interfering RNA (siRNA) biogenesis. It may facilitate DCL1 to access or recognize primary miRNAs. DDL binds RNA non-specifically. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438728 [Multi-domain] Cd Length: 111 Bit Score: 39.97 E-value: 6.85e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952581424 52 SRNHALIWF----------DHKTGKFYLQDTKSSNGTFINSQRLsrgsEESPPCELLSGDIIQFG 106
Cdd:cd22676 42 SKQHAVIQFrevekrnegdVIENIRPYIIDLGSTNGTFLNGEKI----EPRRYYELREKDVLKFG 102
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
256-654 |
7.05e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 256 ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRtQEELRELANKYNGAVNELKEFTEKLKQAEGKQE------ 329
Cdd:PRK01156 315 SNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQ-ILELEGYEMDYNSYLKSIESLKKKIEEYSKNIErmsafi 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 330 -EIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNI-----------KDHNSIEH 397
Cdd:PRK01156 394 sEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgttlgeeKSNHIINH 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 398 FLLKSGGDCSELFQQFIECKNKLKAPVEPTQNNRISNVEDMFESHLENNQ--TTEEDLKNDSERFKATLIAEDDHTKVTE 475
Cdd:PRK01156 474 YNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKieSARADLEDIKIKINELKDKHDKYEEIKN 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 476 ETKLLKENQLEAKESDMSDTLSpskDRSSEDTTDYQMDEQELNESLNKV--------SLLKDLLAEARASSRKHESELDH 547
Cdd:PRK01156 554 RYKSLKLEDLDSKRTSWLNALA---VISLIDIETNRSRSNEIKKQLNDLesrlqeieIGFPDDKSYIDKSIREIENEANN 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 548 LKYELQCAHvqtgDSEREKQELQQELKEAQElAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIE 627
Cdd:PRK01156 631 LNNKYNEIQ----ENKILIEKLRGKIDNYKK-QIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIE 705
|
410 420 430
....*....|....*....|....*....|
gi 1952581424 628 ILREDK---EIEIIETRDQLASTHKEIVAL 654
Cdd:PRK01156 706 ILRTRInelSDRINDINETLESMKKIKKAI 735
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
163-362 |
7.56e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.14 E-value: 7.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 163 QELFQLSQYLQEALHREQML----------------EQKLATLQRLLANTQ---EASDSSWQALIDEDR-LLSRLEVMGN 222
Cdd:COG0497 172 KELEELRADEAERARELDLLrfqleeleaaalqpgeEEELEEERRRLSNAEklrEALQEALEALSGGEGgALDLLGQALR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 223 QLQAYSKNQTEdgirkelvtLQEdkhsyettAKESLRRVLQEKIEVVRklsEVERSLSNTEDECTHLKEMNDRtQEELRE 302
Cdd:COG0497 252 ALERLAEYDPS---------LAE--------LAERLESALIELEEAAS---ELRRYLDSLEFDPERLEEVEER-LALLRR 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952581424 303 LANKYNGAVNELKEFTEKLKQaegKQEEIQQKAlSEKKELQHRIDEMEEK-----EQLLQARIEA 362
Cdd:COG0497 311 LARKYGVTVEELLAYAEELRA---ELAELENSD-ERLEELEAELAEAEAElleaaEKLSAARKKA 371
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
514-697 |
7.83e-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: 42.83 E-value: 7.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 514 EQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELqcahvqtGDSEREKQELQQELKEAQELAISSKQKCFEMQAL 593
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-------AALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 594 LEEERKTAKKQV---------------------EESTRQIQALQAHLHKLQKDIEILREDKEI------EIIETRDQLAS 646
Cdd:COG4942 99 LEAQKEELAELLralyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAElaalraELEAERAELEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1952581424 647 THKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEI 697
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
514-657 |
8.53e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 8.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 514 EQELNESLNKVSLLKDLLAEARASSRKHESELDHL-----KYELQCAHVQTgdsEREKQELQQELkEAQELAISskqkcf 588
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVearikKYEEQLGNVRN---NKEYEALQKEI-ESLKRRIS------ 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581424 589 emqaLLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASTHKEIVALRQT 657
Cdd:COG1579 107 ----DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
238-516 |
8.60e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 8.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 238 KELVTLQEDKHSYETTAKESLRRVLQE----KIEVVRKLSEVER---SLSNTEDECTHLKEMNDRTQEELRELANKYNGA 310
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEEnkikAAEEAKKAEEDKKkaeEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 311 VNELKEfTEKLKQAE----GKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQvrlEQLQE 386
Cdd:PTZ00121 1712 AEEKKK-AEELKKAEeenkIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE---EELDE 1787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 387 KNIKDHNSIEhfllKSGGDCSELFQQFIECKNKLKAPVEPTQ-------------NNRISNVEDMFESHLEN-NQTTEED 452
Cdd:PTZ00121 1788 EDEKRRMEVD----KKIKDIFDNFANIIEGGKEGNLVINDSKemedsaikevadsKNMQLEEADAFEKHKFNkNNENGED 1863
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952581424 453 LKNDSERFKATLIAEDDHTKVtEETKLLKENQLEAKESDMSDTLSPSKDRsseDTTDYQMDEQE 516
Cdd:PTZ00121 1864 GNKEADFNKEKDLKEDDEEEI-EEADEIEKIDKDDIEREIPNNNMAGKNN---DIIDDKLDKDE 1923
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
263-865 |
9.62e-04 |
|
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: 43.24 E-value: 9.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 263 QEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGA----------VNELKEFTEKLKQAEGKQEEIQ 332
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAeemrarlaarKQELEEILHELESRLEEEEERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 333 QKALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKDHNsiEHFLLKSggDCSELFQQ 412
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSK--ERKLLEE--RISEFTSN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 413 FIECKNKLKAPveptqnNRISNVEDMFESHLENNQTTEEDLKNDSERFKATLIAE--DDHTKVTEETKLLKE--NQLEAK 488
Cdd:pfam01576 168 LAEEEEKAKSL------SKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGEstDLQEQIAELQAQIAElrAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 489 ESDMSDTLspskDRSSEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSeREKQE 568
Cdd:pfam01576 242 EEELQAAL----ARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDT-LDTTA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 569 LQQELKEAQELAISSKQKCfemqalLEEERKTAKKQVEE-STRQIQALQahlhKLQKDIEILREDKeIEIIETRDQLAST 647
Cdd:pfam01576 317 AQQELRSKREQEVTELKKA------LEEETRSHEAQLQEmRQKHTQALE----ELTEQLEQAKRNK-ANLEKAKQALESE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 648 HKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYEsEIFNLQTKLQLQTQQQKDKQKGEAVQLQGKLD 727
Cdd:pfam01576 386 NAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELA-EKLSKLQSELESVSSLLNEAEGKNIKLSKDVS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 728 ELQKQSnglkNDCDSLRQE----KVLLTEKLQWFEEELRCAQQQsvkltkdASGLEVSRKALEVEVGTLKEQ------RL 797
Cdd:pfam01576 465 SLESQL----QDTQELLQEetrqKLNLSTRLRQLEDERNSLQEQ-------LEEEEEAKRNVERQLSTLQAQlsdmkkKL 533
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581424 798 QETNGlrvKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQKGNN 865
Cdd:pfam01576 534 EEDAG---TLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSN 598
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
172-619 |
9.95e-04 |
|
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: 42.85 E-value: 9.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 172 LQEALHREQMLEQKLATLQRLL---ANTQEASDSSWQALIDEDR------------LLSRLEVMGNQLQAYSKNQTEdgI 236
Cdd:pfam01576 192 LEERLKKEEKGRQELEKAKRKLegeSTDLQEQIAELQAQIAELRaqlakkeeelqaALARLEEETAQKNNALKKIRE--L 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 237 RKELVTLQEDKHSYET--TAKESLRRVLQEKIEVVRklSEVERSLSNT----------EDECTHLK----EMNDRTQEEL 300
Cdd:pfam01576 270 EAQISELQEDLESERAarNKAEKQRRDLGEELEALK--TELEDTLDTTaaqqelrskrEQEVTELKkaleEETRSHEAQL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 301 RELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQ--------------HRIDEMEEKEQLLQARIEALQAD 366
Cdd:pfam01576 348 QEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQaelrtlqqakqdseHKRKKLEGQLQELQARLSESERQ 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 367 NDFTNERLTALQVRLE-------QLQEKNI---KDHNSIEHFLlksgGDCSELFQQFIECKNKLKAPVEPTQNNRISNVE 436
Cdd:pfam01576 428 RAELAEKLSKLQSELEsvssllnEAEGKNIklsKDVSSLESQL----QDTQELLQEETRQKLNLSTRLRQLEDERNSLQE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 437 DM---------FESHLENNQTTEEDLKNDSERFKATL-IAEDDHTKVTEETKLLKEnQLEAKESDMsDTLSPSKDRSSED 506
Cdd:pfam01576 504 QLeeeeeakrnVERQLSTLQAQLSDMKKKLEEDAGTLeALEEGKKRLQRELEALTQ-QLEEKAAAY-DKLEKTKNRLQQE 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 507 TTDYQMDEQELNESLN----KVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQ----- 577
Cdd:pfam01576 582 LDDLLVDLDHQRQLVSnlekKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELErtnkq 661
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1952581424 578 -----ELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHL 619
Cdd:pfam01576 662 lraemEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDEL 708
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
529-762 |
1.02e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 529 DLLAEARASSRKHES---ELDHLKYELQCAHVQTGdsEREKQELQQELKEAQELAISSKQKcfemQALLEEERKTAKKQV 605
Cdd:COG4913 252 ELLEPIRELAERYAAareRLAELEYLRAALRLWFA--QRRLELLEAELEELRAELARLEAE----LERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 606 EESTRQIQALQ-AHLHKLQKDIEILREDKEiEIIETRDQLASthkeivALRQTAVEAATGREsdiailqgELHKVQTELE 684
Cdd:COG4913 326 DELEAQIRGNGgDRLEQLEREIERLERELE-ERERRRARLEA------LLAALGLPLPASAE--------EFAALRAEAA 390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581424 685 QWRQTASEYESEIFNlqtklqlqtqqqkdkqkgEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELR 762
Cdd:COG4913 391 ALLEALEEELEALEE------------------ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
310-387 |
1.07e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581424 310 AVNELKEFTEKLKQAEGKQEEIQQkalsEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEK 387
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQA----ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
50-106 |
1.13e-03 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaA and similar proteins; FhaA regulates cell growth and peptidoglycan synthesis by binding to MviN. It may inhibit the late stages of peptidoglycan synthesis. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438720 [Multi-domain] Cd Length: 91 Bit Score: 38.99 E-value: 1.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581424 50 VLSRNHALIWFDHKTGkfYLQDTKSSNGTFINSQRLsrgseeSPPCELLSGDIIQFG 106
Cdd:cd22668 36 GVSRRHAEIRWDGQVA--HLTDLGSTNGTTVNNAPV------TPEWRLADGDVITLG 84
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
236-856 |
1.54e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.27 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 236 IRKELVTLQEDKHSYETTAKesLRRVLQEKIEVVRKLSEVERSLSNTE----DECTHLKEMNDRTQEELRELANKYNGAV 311
Cdd:pfam02463 158 IEEEAAGSRLKRKKKEALKK--LIEETENLAELIIDLEELKLQELKLKeqakKALEYYQLKEKLELEEEYLLYLDYLKLN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 312 NELKEFTEKLKQAEGKQEEIQ---QKALSEKKELQHRIDEMEEKEQ--------LLQARIEALQADNDFTNERLTALQVR 380
Cdd:pfam02463 236 EERIDLLQELLRDEQEEIESSkqeIEKEEEKLAQVLKENKEEEKEKklqeeelkLLAKEEEELKSELLKLERRKVDDEEK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 381 LEQLQEKNIKDHNSIehfllksggdcsELFQQFIECKNKLKAPVEPTQNNRISNVEDMFESHLENNQTTEEDLKNDSERF 460
Cdd:pfam02463 316 LKESEKEKKKAEKEL------------KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 461 KATLIAEDDHTKVTEETKLLK---ENQLEAKESDMSDTLSPSKDRSSEDTTDyQMDEQELNESLNKVSLLKDLLAEARAS 537
Cdd:pfam02463 384 ERLSSAAKLKEEELELKSEEEkeaQLLLELARQLEDLLKEEKKEELEILEEE-EESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 538 SRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQA 617
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 618 HLHKLQKDIEILREDKEIEIIETR-----DQLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASE 692
Cdd:pfam02463 543 VAISTAVIVEVSATADEVEERQKLvraltELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRA 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 693 YESEIFNLQTKLQLQTQQQKDKQKG--EAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVK 770
Cdd:pfam02463 623 KVVEGILKDTELTKLKESAKAKESGlrKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIK 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 771 LTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELE 850
Cdd:pfam02463 703 KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREK 782
|
....*.
gi 1952581424 851 NCKENL 856
Cdd:pfam02463 783 TEKLKV 788
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
590-839 |
1.58e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 590 MQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIeiIETRDQLASTHKEIVALRQTAVEAatgrESDI 669
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGL--VDLSEEAKLLLQQLSELESQLAEA----RAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 670 AILQGELHKVQTELEQWRQTASEyeseifnlqtklqLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVL 749
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPE-------------LLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 750 LTEKLQwfeeelRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKeQRLQETNGLRVKLAhaenetqKFQKQYEADQTMYL 829
Cdd:COG3206 303 LRAQLQ------QEAQRILASLEAELEALQAREASLQAQLAQLE-ARLAELPELEAELR-------RLEREVEVARELYE 368
|
250
....*....|
gi 1952581424 830 ELKEKLDKTQ 839
Cdd:COG3206 369 SLLQRLEEAR 378
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
163-366 |
1.58e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALID--------EDRLLSRLEVMGNQLQAYSKNQTED 234
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekeiaelRAELEAQKEELAELLRALYRLGRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 235 GIrkELVTLQEDKHSYETTAK--ESLRRVLQEKIEVVRK-LSEVERSLSNTEDECTHLKEMNDRTQEELRELAnkyngav 311
Cdd:COG4942 121 PL--ALLLSPEDFLDAVRRLQylKYLAPARREQAEELRAdLAELAALRAELEAERAELEALLAELEEERAALE------- 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1952581424 312 nelkefteklkQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQAD 366
Cdd:COG4942 192 -----------ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
160-575 |
1.95e-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: 42.02 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 160 MYSQELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGIRKE 239
Cdd:pfam05483 381 IITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLT 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 240 LVTLQEDKHSYETT------AKESLR---------RVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELA 304
Cdd:pfam05483 461 AIKTSEEHYLKEVEdlktelEKEKLKnieltahcdKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 305 NKYNGAVNELKEFTEKLKQaegkqeeiqqkalsEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQl 384
Cdd:pfam05483 541 EKEMNLRDELESVREEFIQ--------------KGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEN- 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 385 QEKNIKDHNSIEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQnNRISNVEDMFESHLENNQTTEEDLKNDSERFKATl 464
Cdd:pfam05483 606 KNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAK-QKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAI- 683
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 465 iaeddhtkVTEETKLLKENQLEAKESDMSDTLSPSKDRSSEDTTdyqmdeqeLNESLNKVSLLKDLLAEARASSRKHESE 544
Cdd:pfam05483 684 --------ADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKI--------IEERDSELGLYKNKEQEQSSAKAALEIE 747
|
410 420 430
....*....|....*....|....*....|.
gi 1952581424 545 LDHLKYELQCAHVQTGDSEREKQELQQELKE 575
Cdd:pfam05483 748 LSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
297-387 |
2.13e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 297 QEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQkalsEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTA 376
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK----QLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90
....*....|.
gi 1952581424 377 LQVRLEQLQEK 387
Cdd:COG4942 95 LRAELEAQKEE 105
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
289-529 |
2.14e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 289 LKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQ-------LLQARIE 361
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKtikaeieELTDELL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 362 ALQADNDFTNERLTALQVRLEQLQEKnIKDHNSIEHFlLKSGGDCSELFQQFIECKNKLKA----PVEPTQ-----NNRI 432
Cdd:PHA02562 245 NLVMDIEDPSAALNKLNTAAAKIKSK-IEQFQKVIKM-YEKGGVCPTCTQQISEGPDRITKikdkLKELQHsleklDTAI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 433 SNVEDMFESHLEnNQTTEEDLKNDSERFKATLIAEDDHTKVTEetKLLKenQLEAKESDMSDTLSPSKDRSSEDTTDYQM 512
Cdd:PHA02562 323 DELEEIMDEFNE-QSKKLLELKNKISTNKQSLITLVDKAKKVK--AAIE--ELQAEFVDNAEELAKLQDELDKIVKTKSE 397
|
250
....*....|....*..
gi 1952581424 513 DEQELNESLNKVSLLKD 529
Cdd:PHA02562 398 LVKEKYHRGIVTDLLKD 414
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
159-325 |
2.73e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 159 SMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIdEDRLLSRLEVMGNQLQAYSKNQTEDGIRk 238
Cdd:COG3206 215 KLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPV-IQQLRAQLAELEAELAELSARYTPNHPD- 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 239 eLVTLQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFT 318
Cdd:COG3206 293 -VIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLL 371
|
....*..
gi 1952581424 319 EKLKQAE 325
Cdd:COG3206 372 QRLEEAR 378
|
|
| prfA |
PRK00591 |
peptide chain release factor 1; Validated |
515-615 |
3.47e-03 |
|
peptide chain release factor 1; Validated
Pssm-ID: 234801 [Multi-domain] Cd Length: 359 Bit Score: 40.83 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 515 QELNESLNKVSLLKDLlAEARASSRKHeSELDHL--KYelqcahvqtgdseREKQELQQELKEAQELAISSKQKcfEMQA 592
Cdd:PRK00591 16 EELEALLSDPEVISDQ-KRFRKLSKEY-AELEPIveAY-------------REYKQAQEDLEEAKEMLEEESDP--EMRE 78
|
90 100
....*....|....*....|...
gi 1952581424 593 LLEEERKTAKKQVEESTRQIQAL 615
Cdd:PRK00591 79 MAKEELKELEERLEELEEELKIL 101
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
440-690 |
4.18e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.88 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 440 ESHLEN--NQTTEEDLKNDSERFKATLIAEDDHTKVTEETKllKENQLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQEL 517
Cdd:pfam05557 8 KARLSQlqNEKKQMELEHKRARIELEKKASALKRQLDRESD--RNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 518 NESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLeEE 597
Cdd:pfam05557 86 EALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQ-SS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 598 RKTAKKQVEESTRQIQ-------------ALQAHLHKLQKDIEILREDKEI--EIIETRDQLasthKEIVALRQTAVEAA 662
Cdd:pfam05557 165 LAEAEQRIKELEFEIQsqeqdseivknskSELARIPELEKELERLREHNKHlnENIENKLLL----KEEVEDLKRKLERE 240
|
250 260
....*....|....*....|....*...
gi 1952581424 663 TGRESDIAILQGELHKVQTELEQWRQTA 690
Cdd:pfam05557 241 EKYREEAATLELEKEKLEQELQSWVKLA 268
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
270-631 |
4.20e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 270 RKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKL----KQAEGKQEEIQqKALSEKKELQHR 345
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIeklkKENQSYKQEIK-NLESQINDLESK 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 346 IDEMEEKEQLLQARIEALQADNDftnerltALQVRLEQLQEKNIKDHNSIehfllksggdcSELFQQFIECKNKLKapve 425
Cdd:TIGR04523 400 IQNQEKLNQQKDEQIKKLQQEKE-------LLEKEIERLKETIIKNNSEI-----------KDLTNQDSVKELIIK---- 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 426 pTQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKatlIAEDDHTKVTEETKLLKENQLEAKesdmsdtlspskDRSSE 505
Cdd:TIGR04523 458 -NLDNTRESLETQLKVLSRSINKIKQNLEQKQKELK---SKEKELKKLNEEKKELEEKVKDLT------------KKISS 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 506 DTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKH--ESELDHLKYELQCAHVQTGDSEREKQELQQEL--KEAQELAI 581
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIdqKEKEKKDL 601
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1952581424 582 SSKQKCFEMQAL-LEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILRE 631
Cdd:TIGR04523 602 IKEIEEKEKKISsLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKE 652
|
|
| FHA_Rv1747-like_rpt2 |
cd22737 |
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
28-106 |
4.21e-03 |
|
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the second FHA domain, which has a circularly permuted FHA domain fold with a conserved pThr-binding interface.
Pssm-ID: 439356 [Multi-domain] Cd Length: 93 Bit Score: 37.47 E-value: 4.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581424 28 VKIGRSvarcrpAQNNATFDCKVLSRNHALIwfDHKTGKFYLQDTKSSNGTFINSQRLSRgseesppCELLSGDIIQFG 106
Cdd:cd22737 23 VRIGRA------SDNDIVIPEGSVSRHHATL--VPTPGGTQIRDLRSTNGTFVNGLRVDA-------ALLHDGDVVTIG 86
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
516-685 |
4.26e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 516 ELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAisskqkcfemqalle 595
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI--------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 596 eERKTAKKQVEESTRQIQALQAHLHKLQKDIEILrEDKEIEIIETRD----QLASTHKEIVALRQTAVEAATGRESDIAI 671
Cdd:COG1579 76 -KKYEEQLGNVRNNKEYEALQKEIESLKRRISDL-EDEILELMERIEeleeELAELEAELAELEAELEEKKAELDEELAE 153
|
170
....*....|....
gi 1952581424 672 LQGELHKVQTELEQ 685
Cdd:COG1579 154 LEAELEELEAEREE 167
|
|
| VI_FHA |
TIGR03354 |
type VI secretion system FHA domain protein; Members of this protein family are FHA ... |
49-106 |
4.31e-03 |
|
type VI secretion system FHA domain protein; Members of this protein family are FHA (forkhead-associated) domain-containing proteins that are part of type VI secretion loci in a considerable number of bacteria, most of which are known pathogens. Species include Pseudomonas aeruginosa PAO1, Aeromonas hydrophila, Yersinia pestis, Burkholderia mallei, etc. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274537 [Multi-domain] Cd Length: 396 Bit Score: 40.43 E-value: 4.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952581424 49 KVLSRNHA-LIWFDhktGKFYLQDTkSSNGTFINS--QRLSRGSEESppceLLSGDIIQFG 106
Cdd:TIGR03354 43 RHVSGRHArIRYRD---GAYLLTDL-STNGVFLNGsgSPLGRGNPVR----LEQGDRLRLG 95
|
|
| FHA_Ki67 |
cd22673 |
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ... |
52-106 |
4.86e-03 |
|
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438725 [Multi-domain] Cd Length: 95 Bit Score: 37.19 E-value: 4.86e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1952581424 52 SRNHALIWFDhKTGKFYLQDTKSSNGTFINsqrlsrGSEESPPCELLSGDIIQFG 106
Cdd:cd22673 41 SREHCRIEVD-ENGKAYLENLSTTNPTLVN------GKAIEKSAELKDGDVITIG 88
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
601-795 |
5.57e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 601 AKKQVEESTRQIQALQAHLHKLQKDIEILREDKEI---EIIETRDQLASTHKEIVALRQTAVEAatgrESDIAILQGELH 677
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKAllkQLAALERRIAALARRIRALEQELAAL----EAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 678 KVQTELEQWRQTASEY-----------------ESEIFNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDC 740
Cdd:COG4942 94 ELRAELEAQKEELAELlralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1952581424 741 DSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQ 795
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
419-843 |
6.38e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 419 KLKAPVEPTQNNRISNVEDMFESHLENNQTTEEDLK---NDSERFKATLIAED-DHTKVTEETKLLKENQLEAKESDMSD 494
Cdd:PTZ00121 1028 KIEELTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKahvGQDEGLKPSYKDFDfDAKEDNRADEATEEAFGKAEEAKKTE 1107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 495 TLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKdlLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQ--- 571
Cdd:PTZ00121 1108 TGKAEEARKAEEAKKKAEDARKAEEARKAEDARK--AEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARkae 1185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 572 ELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQaHLHKLQKDIEILREDKEIEIIETRDQLASTHKEI 651
Cdd:PTZ00121 1186 EVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVK-KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAH 1264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 652 VALRQTAVEAATGRESDiailqgELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKGEavQLQGKLDELQK 731
Cdd:PTZ00121 1265 FARRQAAIKAEEARKAD------ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAE--EAKKKADAAKK 1336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 732 QSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASglEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAE 811
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD--AAKKKAEEKKKADEAKKKAEEDKKKADELKKAA 1414
|
410 420 430
....*....|....*....|....*....|....
gi 1952581424 812 NETQKFQ--KQYEADQTMYLELKEKLDKTQKENE 843
Cdd:PTZ00121 1415 AAKKKADeaKKKAEEKKKADEAKKKAEEAKKADE 1448
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
333-624 |
6.54e-03 |
|
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: 40.06 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 333 QKALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTA-----------------LQVRLEQLQEKNIKDHNSI 395
Cdd:pfam05622 3 SEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQlesgddsgtpggkkyllLQKQLEQLQEENFRLETAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 396 EHFLLKsggdCSELFQQFIECKNK---LKAPVEPTQ------------NNRISNVEDMFES------------------- 441
Cdd:pfam05622 83 DDYRIK----CEELEKEVLELQHRneeLTSLAEEAQalkdemdilresSDKVKKLEATVETykkkledlgdlrrqvklle 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 442 -----HLENNQTTEEDLK------NDSERFKATLiaEDDHTKVTEETKLLKENQLEAKES-DMSDTLSPSKDR--SSEDT 507
Cdd:pfam05622 159 ernaeYMQRTLQLEEELKkanalrGQLETYKRQV--QELHGKLSEESKKADKLEFEYKKLeEKLEALQKEKERliIERDT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 508 TdyqmdeQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVqtgdseREK-QELQQE---LKEAQELaiSS 583
Cdd:pfam05622 237 L------RETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEI------REKlIRLQHEnkmLRLGQEG--SY 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1952581424 584 KQKCFEMQALLEEERKTAKKQVEE---STRQIQALQAHLHKLQK 624
Cdd:pfam05622 303 RERLTELQQLLEDANRRKNELETQnrlANQRILELQQQVEELQK 346
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
256-365 |
7.01e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 256 ESLRRVLQEKI-EVVRKLSEVERSLSNTEDEcthLKEMNDRTQEELRELANKYNGAVNELKE----------FTEKLKQA 324
Cdd:PRK00409 526 EELERELEQKAeEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLEEAEKEAQQAIKEAKKeadeiikelrQLQKGGYA 602
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1952581424 325 EGKQEEIQQKalseKKELQHRIDEMEEKEQLLQARIEALQA 365
Cdd:PRK00409 603 SVKAHELIEA----RKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
255-389 |
7.09e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 39.33 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 255 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEgkqeEIQQK 334
Cdd:COG4026 113 KNAIIRAGLKSLQNIPEYNELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILE----EEFDN 188
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581424 335 ALSEKKELQHRIDEMEEKEQLLQARIEALQAD---NDFTNERLTALQVrlEQLQEKNI 389
Cdd:COG4026 189 IKSEYSDLKSRFEELLKKRLLEVFSLEELWKElfpEELPEEDFIYFAT--ENLKPGKI 244
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
555-699 |
8.10e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.89 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 555 AHVQTGDSEREKQELQQELKEAQElaisskqkcfemQALLEEERKTAKKQVEESTRQIQALQahlhKLQKDIEILRedKE 634
Cdd:PRK11281 27 ARAASNGDLPTEADVQAQLDALNK------------QKLLEAEDKLVQQDLEQTLALLDKID----RQKEETEQLK--QQ 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581424 635 IEiiETRDQLASTHKEIVALRQTAVEAATGRESDIAI--LQGELHKVQTELEQWRQTASEYESEIFN 699
Cdd:PRK11281 89 LA--QAPAKLRQAQAELEALKDDNDEETRETLSTLSLrqLESRLAQTLDQLQNAQNDLAEYNSQLVS 153
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
164-387 |
8.22e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRL-LSRLEVMGNQLQAYSKNQTEdgIRKELVT 242
Cdd:PRK04863 852 ALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRVEEIREqLDEAEEAKRFVQQHGNALAQ--LEPIVSV 929
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 243 LQEDKHSYET------TAKESLRRVLQEkievVRKLSEV------------ERSLSNTEDECTHLKEMNDRTQEELRELA 304
Cdd:PRK04863 930 LQSDPEQFEQlkqdyqQAQQTQRDAKQQ----AFALTEVvqrrahfsyedaAEMLAKNSDLNEKLRQRLEQAEQERTRAR 1005
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 305 NKYNGAVNELKEFTE---KLKQAEGKQEEIQQKALSEKKELQHRIDEMEE------KEQLLQA------RIEALQADNDF 369
Cdd:PRK04863 1006 EQLRQAQAQLAQYNQvlaSLKSSYDAKRQMLQELKQELQDLGVPADSGAEerararRDELHARlsanrsRRNQLEKQLTF 1085
|
250
....*....|....*...
gi 1952581424 370 TNERLTALQVRLEQLQEK 387
Cdd:PRK04863 1086 CEAEMDNLTKKLRKLERD 1103
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
235-758 |
9.17e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 9.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 235 GIRKELVTLQEDKHSYET---TAKESL----------RRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELR 301
Cdd:PRK02224 210 GLESELAELDEEIERYEEqreQARETRdeadevleehEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 302 ELANKYNGAVNELkefteKLKQAEGKQEEIQQKALSEKK-ELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVR 380
Cdd:PRK02224 290 ELEEERDDLLAEA-----GLDDADAEAVEARREELEDRDeELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 381 LEQLQEKNIKDHNSIEhfllKSGGDCSELFQQFIECKNKLK-APVEPtqnnrisnveDMFESHLENNQTTEEDLKNDSER 459
Cdd:PRK02224 365 AAELESELEEAREAVE----DRREEIEELEEEIEELRERFGdAPVDL----------GNAEDFLEELREERDELREREAE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 460 FKATLIAEDDhtKVTEETKLLKENQL-----EAKESDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDLL-AE 533
Cdd:PRK02224 431 LEATLRTARE--RVEEAEALLEAGKCpecgqPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeAE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 534 ARASSRKHESELDHlkyELQCAHVQTGDSEREKqeLQQELKEAQELAISSKQKcfemqallEEERKTAKKQVEESTRQIQ 613
Cdd:PRK02224 509 DRIERLEERREDLE---ELIAERRETIEEKRER--AEELRERAAELEAEAEEK--------REAAAEAEEEAEEAREEVA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 614 ALQAHLHKLQKDIEILRedkeiEIIETRDQLASTHKEIVALRQtaveaatgRESDIAILQGE-LHKVQTELEQWRQTASE 692
Cdd:PRK02224 576 ELNSKLAELKERIESLE-----RIRTLLAAIADAEDEIERLRE--------KREALAELNDErRERLAEKRERKRELEAE 642
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581424 693 YESEIFNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCD---SLRQEKVLLTEKLQWFE 758
Cdd:PRK02224 643 FDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEeleELRERREALENRVEALE 711
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
274-381 |
9.61e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.45 E-value: 9.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581424 274 EVERSLSNTEDECTHLKEMNDRTQEELRELANKY---NGAVNELKEFTEKLKQAEGKQEEIQQKALSEK----------K 340
Cdd:pfam06160 288 YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEvayselqeelE 367
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1952581424 341 ELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRL 381
Cdd:pfam06160 368 EILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLEL 408
|
|
| |
