|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
3-130 |
4.08e-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: 4.08e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 3 SALAIFTCRPNSHPFQERHVYLDEPVKIGRSVARCRPAQNNATFDCKVLSRNHALIWFDHktGKFYLQDTKSSNGTFINS 82
Cdd:cd22679 1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1952581418 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 |
1.14e-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: 103.53 E-value: 1.14e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952581418 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 |
1.49e-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: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 27 PVKIGRSVARCRPAQNNAT-FDCKVLSRNHALIWfdHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCELLSGDIIQF 105
Cdd:cd22692 38 QIHIGRYTERVRQAIYHPVvFKSKVVSRTHGCIK--VDEGNWYIKDVKSSSGTFLNHQRLSPASRTSKPYPLRDGDILQL 115
|
...
gi 1952581418 106 GVD 108
Cdd:cd22692 116 GMD 118
|
|
| FHA_VPS64-like |
cd22695 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ... |
6-126 |
3.98e-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: 3.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 6 AIFTCRPNSHPFQERHV---YLDEPVKIGRSVARCRPAQN---------------NATFDCKVLSRNHALIWFDHKTGKF 67
Cdd:cd22695 2 HILVLKSLNATFETKFLvvpFKPDGLKLGRPVTNSVNKNNsgskrdlfsqqvrpdNGNFDSRVLSRNHACLSCDPTTGKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581418 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 |
5.43e-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: 5.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 13 NSHPFQERHVYLDEPVKIGRSvarcrpAQNNATFDCKVLSRNHALIWFDHktGKFYLQDTKSSNGTFINSQRLsrgseeS 92
Cdd:cd00060 6 DGDGGGREFPLTKGVVTIGRS------PDCDIVLDDPSVSRRHARIEVDG--GGVYLEDLGSTNGTFVNGKRI------T 71
|
90
....*....|....
gi 1952581418 93 PPCELLSGDIIQFG 106
Cdd:cd00060 72 PPVPLQDGDVIRLG 85
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
28-105 |
8.11e-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: 8.11e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581418 28 VKIGRSvarcrpAQNNATFDCKVLSRNHALIWFDhKTGKFYLQDTKSSNGTFINSQRLSRgseesPPCELLSGDIIQF 105
Cdd:pfam00498 1 VTIGRS------PDCDIVLDDPSVSRRHAEIRYD-GGGRFYLEDLGSTNGTFVNGQRLGP-----EPVRLKDGDVIRL 66
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
203-866 |
2.59e-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: 77.40 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 203 SWQALIDE-DRLLSRLEVMGNQLQAYSKNQTE-----DGIRKELVTLQEDKHSYETT---AKESLRRVLQEKIEVVRKLS 273
Cdd:TIGR02168 233 RLEELREElEELQEELKEAEEELEELTAELQEleeklEELRLEVSELEEEIEELQKElyaLANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 274 EVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQH---RIDEME 350
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETlrsKVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 351 EKEQLLQARIEALQAdndftneRLTALQVRLEQLQEKNIKDHNSIGIQVDDLLPKINGSTDKEHFLLKSGGD-----CSE 425
Cdd:TIGR02168 393 LQIASLNNEIERLEA-------RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELErleeaLEE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 426 LFQQFIECKNKLKAPVEPTQ--NNRISNVEDMFEsHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEE---------- 493
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAqlQARLDSLERLQE-NLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyeaaieaalg 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 494 ---TKLLKENQLEAKE------------------SDMSDTLSPSKDR----SSEDTTDYQMDEQELNESLNKV--SLLKD 546
Cdd:TIGR02168 545 grlQAVVVENLNAAKKaiaflkqnelgrvtflplDSIKGTEIQGNDReilkNIEGFLGVAKDLVKFDPKLRKAlsYLLGG 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 547 LL-------AEARASSRKHESELDHLKYELQCAH-VQTGDSE----------REKQELQQELKEAQELAISSKQKCFEM- 607
Cdd:TIGR02168 625 VLvvddldnALELAKKLRPGYRIVTLDGDLVRPGgVITGGSAktnssilerrREIEELEEKIEELEEKIAELEKALAELr 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 608 --QALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILRE---DKEIEIIETRDQLASTHKEIVALRQTAVEAATGR 682
Cdd:TIGR02168 705 keLEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEEriaQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 683 ESdiaiLQGELHKVQTELEQWRQTASEYESEIFNlqtklqlqtqqqkdkQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQ 762
Cdd:TIGR02168 785 EE----LEAQIEQLKEELKALREALDELRAELTL---------------LNEEAANLRERLESLERRIAATERRLEDLEE 845
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 763 EKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVklahAENETQKFQKQYEADQ 842
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE----LESKRSELRRELEELR 921
|
730 740
....*....|....*....|....
gi 1952581418 843 TMYLELKEKLDKTQKENESITDEL 866
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRIDNLQERL 945
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
174-874 |
2.76e-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: 77.42 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 174 EALHREQMLEQKLATLQRLLAnTQEASDSSWQALIDEDRL-LSRLEVMGNQLQAYSKNQTED---GIRKELVTLQEDKHS 249
Cdd:TIGR02169 227 ELLKEKEALERQKEAIERQLA-SLEEELEKLTEEISELEKrLEEIEQLLEELNKKIKDLGEEeqlRVKEKIGELEAEIAS 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 250 YETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMN---DRTQEELRELANKYNGAVNELKEFTEKLKQAEG 326
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERkrrDKLTEEYAELKEELEDLRAELEEVDKEFAETRD 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 327 KQEEIQQK---ALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKDHNSIGIQVDDLl 403
Cdd:TIGR02169 386 ELKDYREKlekLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL- 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 404 pkinGSTDKEHFLLKSGGD-----CSELFQQFIECKNKLKAPVEPTQNNRisNVEDMFESHLENNQTTEEDLKNDSERFK 478
Cdd:TIGR02169 465 ----SKYEQELYDLKEEYDrvekeLSKLQRELAEAEAQARASEERVRGGR--AVEEVLKASIQGVHGTVAQLGSVGERYA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 479 ATL-----------IAEDDHTKVtEETKLLKE-----------NQLEAKESDMS-------------------------- 510
Cdd:TIGR02169 539 TAIevaagnrlnnvVVEDDAVAK-EAIELLKRrkagratflplNKMRDERRDLSilsedgvigfavdlvefdpkyepafk 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 511 ----DTL----------------------------------SPSKDRSSEDTTDYQMDEQELNESLNKvslLKDLLAEAR 552
Cdd:TIGR02169 618 yvfgDTLvvedieaarrlmgkyrmvtlegelfeksgamtggSRAPRGGILFSRSEPAELQRLRERLEG---LKRELSSLQ 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 553 ASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKcfemQALLEEERKTAKKQVEESTRQIQAL 632
Cdd:TIGR02169 695 SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED----LSSLEQEIENVKSELKELEARIEEL 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 633 QAHLHKLQKDIEILREDKEIEIIETRDQLASTHKEIVA---LRQTAVEAATGRES-DIAILQGELHKVQTELEQWRQTAS 708
Cdd:TIGR02169 771 EEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSrieARLREIEQKLNRLTlEKEYLEKEIQELQEQRIDLKEQIK 850
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 709 EYESEIFNLQTKLQLQTQqqkdkqkgEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKL 788
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEE--------ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 789 TKDASGLEVSRKALEVEVGTLKEQRLQETN--GLRVKLAHAENETQKFQ-------KQYEADQTMYLELKEKLDKTQKEN 859
Cdd:TIGR02169 923 KAKLEALEEELSEIEDPKGEDEEIPEEELSleDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEER 1002
|
810
....*....|....*
gi 1952581418 860 ESITDELENCkENLK 874
Cdd:TIGR02169 1003 KAILERIEEY-EKKK 1016
|
|
| CC1_SLMAP-like |
cd21868 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ... |
167-204 |
2.02e-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: 2.02e-13
10 20 30
....*....|....*....|....*....|....*...
gi 1952581418 167 QLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSW 204
Cdd:cd21868 1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
172-879 |
4.52e-13 |
|
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: 73.55 E-value: 4.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 172 LQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRllsrlevmgnqlqaySKNQTEDGIRKELVTLQEDKHsye 251
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS---------------ELEEEIEELQKELYALANEIS--- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 252 ttAKESLRRVLQEKIE-VVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEE 330
Cdd:TIGR02168 299 --RLEQQKQILRERLAnLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 331 IQQKALSEKKElqhrIDEMEEKEQLLQARIEALQAdndftneRLTALQVRLEQLQEKNIKDHNSIGIQVDDLLPKINGST 410
Cdd:TIGR02168 377 LEEQLETLRSK----VAQLELQIASLNNEIERLEA-------RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 411 DKEHFLLKSGGD-----CSELFQQFIECKNKLKAPVEPTQ--NNRISNVEDMFEsHLENNQTTEEDLKNDSERFKATLIA 483
Cdd:TIGR02168 446 EEELEELQEELErleeaLEELREELEEAEQALDAAERELAqlQARLDSLERLQE-NLEGFSEGVKALLKNQSGLSGILGV 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 484 EDDHTKVTEETKLLKENQLEA---------KESDMSDTLSPSKDRSS------EDTTDYQMDEQELNESLNKVSLLKDLL 548
Cdd:TIGR02168 525 LSELISVDEGYEAAIEAALGGrlqavvvenLNAAKKAIAFLKQNELGrvtflpLDSIKGTEIQGNDREILKNIEGFLGVA 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 549 AEARASSRKHESELDHLkyelqCAHVQTGDSEREKQELQQELKEAQEL------------AISSKQKCFEMQAL-LEEER 615
Cdd:TIGR02168 605 KDLVKFDPKLRKALSYL-----LGGVLVVDDLDNALELAKKLRPGYRIvtldgdlvrpggVITGGSAKTNSSILeRRREI 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 616 KTAKKQVEESTRQIQALQAHLHKLQK---DIEILREDKEIEIIETRDQLASTHKEIVALRQTaVEAATGRESDIAILQGE 692
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKeleELEEELEQLRKELEELSRQISALRKDLARLEAE-VEQLEERIAQLSKELTE 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 693 LHKVQTELEQWRQTASEYESEIfnlqTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQ 772
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEA----EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 773 WFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQR---LQETNGLRVKLAHAENETQKFQKQYEADQTMYLELK 849
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELealLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
730 740 750
....*....|....*....|....*....|
gi 1952581418 850 EKLDKTQKENESITDELENCKENLKLLQQK 879
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
14-106 |
6.30e-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: 6.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 14 SHPFQERHVYLDE-PVKIGRSvarcrpAQNNATFDCKVLSRNHALIWFDHktGKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716 8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
|
90
....*....|....
gi 1952581418 93 pPCELLSGDIIQFG 106
Cdd:COG1716 75 -PAPLRDGDVIRLG 87
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-803 |
7.10e-13 |
|
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: 72.78 E-value: 7.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 156 NSPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALID-EDRLLSRLEVMGNQLQAY-SKNQTE 233
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEElESRLEELEEQLETLRSKVaQLELQI 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 234 DGIRKELVTLQEDKHSyettAKESLRRVLQEKIEVVRKLSEVERSLsnTEDECTHLKEMNDRTQEELRELANKYNGAVNE 313
Cdd:TIGR02168 396 ASLNNEIERLEARLER----LEDRRERLQQEIEELLKKLEEAELKE--LQAELEELEEELEELQEELERLEEALEELREE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 314 LKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQAR----------IEALQADNDFTNERLTALQVRLEQ 383
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQsglsgilgvlSELISVDEGYEAAIEAALGGRLQA 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 384 LQEKNIKDH---------NSIGIQVDDLLPKINGSTDK--EHFLLKSGGDCSELFQQFIECKNKLKAPVEP--------- 443
Cdd:TIGR02168 550 VVVENLNAAkkaiaflkqNELGRVTFLPLDSIKGTEIQgnDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvvd 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 444 --TQNNRISNVEDmfesHLENNQTTEEDLKNdsERFKATLIAEDDHTKVTEETKLLKEN-----QLEAKESDMSDTLSPS 516
Cdd:TIGR02168 630 dlDNALELAKKLR----PGYRIVTLDGDLVR--PGGVITGGSAKTNSSILERRREIEELeekieELEEKIAELEKALAEL 703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 517 KDRSSEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQcahvqtgDSEREKQELQQELKEAQEL 596
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT-------ELEAEIEELEERLEEAEEE 776
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 597 AISSKQKcfemQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDK---EIEIIETRDQLASTHKEIVALRQ 673
Cdd:TIGR02168 777 LAEAEAE----IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLeslERRIAATERRLEDLEEQIEELSE 852
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 674 TaVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIfnlqTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGL 753
Cdd:TIGR02168 853 D-IESLAAEIEELEELIEELESELEALLNERASLEEALALL----RSELEELSEELRELESKRSELRRELEELREKLAQL 927
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1952581418 754 KNDCDSLRQEKVLLTEKL-QWFEEELRCAQQQSVKLTKDASGLEVSRKALE 803
Cdd:TIGR02168 928 ELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
52-106 |
1.35e-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: 1.35e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1952581418 52 SRNHALIWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCELLSGDIIQFG 106
Cdd:cd22686 48 SKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPYPLTHGDELKIG 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
556-844 |
2.74e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 556 RKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQkcfemqALLEEERKTAKKQVEESTRQIQALQAH 635
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAEL------AELEAELEELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 636 LHKLQKDIEILREDKE------IEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASE 709
Cdd:COG1196 290 EYELLAELARLEQDIArleerrRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 710 YESEIfNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLT 789
Cdd:COG1196 370 AEAEL-AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1952581418 790 KDASGLEVSRKALEVEVgtlkEQRLQETNGLRVKLAHAENETQKFQKQYEADQTM 844
Cdd:COG1196 449 EEEAELEEEEEALLELL----AELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
157-387 |
2.06e-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: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 157 SPSMYSQELFQLSQY--LQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEd 234
Cdd:TIGR02169 659 SRAPRGGILFSRSEPaeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE- 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 235 girkelvtLQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQ-EELRELANKYNGAVNE 313
Cdd:TIGR02169 738 --------RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSR 809
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952581418 314 LKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEK 387
Cdd:TIGR02169 810 IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
329-881 |
2.07e-10 |
|
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: 64.74 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 329 EEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQaDNDFTNERLTalqVRLEQLQEKN---IKDHNSIGIQVDDLLPK 405
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQ-ELQFENEKVS---LKLEEEIQENkdlIKENNATRHLCNLLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 406 INGSTDKEHfllKSGGDCSELFQQFIECKNKLKAPVEPTQNNRISNVEDMFESHLENNQTTEEdLKNDSERFKATLIAED 485
Cdd:pfam05483 164 CARSAEKTK---KYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEK-IQHLEEEYKKEINDKE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 486 DHTKVTeetkLLKENQLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHL 565
Cdd:pfam05483 240 KQVSLL----LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKAL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 566 KYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIE- 644
Cdd:pfam05483 316 EEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEe 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 645 --ILREDKEIEIIETRDQLASTHKEIVALRQTA--VEAATGRESDIAIL----QGELHKVQTELEQWRQTASEYESEIfn 716
Cdd:pfam05483 396 mtKFKNNKEVELEELKKILAEDEKLLDEKKQFEkiAEELKGKEQELIFLlqarEKEIHDLEIQLTAIKTSEEHYLKEV-- 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 717 lqtklqlqtqqqkDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLE 796
Cdd:pfam05483 474 -------------EDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 797 VSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLL 876
Cdd:pfam05483 541 EKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAL 620
|
....*
gi 1952581418 877 QQKGN 881
Cdd:pfam05483 621 KKKGS 625
|
|
| CC1_T3JAM |
cd21912 |
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ... |
164-204 |
1.32e-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: 54.28 E-value: 1.32e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1952581418 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSW 204
Cdd:cd21912 5 EILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
|
|
| FHA_TCF19 |
cd22685 |
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ... |
28-119 |
1.34e-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: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 28 VKIGRSVARCRPAQNNATFDcKVLSRNHALIW---FDHKTGKFYLQDTkSSNGTFINSQRLSRGSEEsppcELLSGDIIQ 104
Cdd:cd22685 30 YRIGRNPEVCDVFLCSSQHP-NLISREHAEIHaerDGNGNWKVLIEDR-STNGTYVNDVRLQDGQRR----ELSDGDTIT 103
|
90
....*....|....*..
gi 1952581418 105 FG--VDVTENTRKVTHG 119
Cdd:cd22685 104 FGhkNGRRVKQWPYQKS 120
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
294-868 |
1.56e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 294 DRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALsekkELQHRIDEMEEKEQLLQARIEALQADNDFTNER 373
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE----ELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 374 LTALQVRLEQLQEKNIKDHNSIGIQVDDLLpkingstdkehfllksggdcsELFQQFIECKNKLKApveptqnnrisnVE 453
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELE---------------------ELEEELEEAEEELEE------------AE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 454 DMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEETKLLKENQLEAKEsdmsdtlspskdRSSEDTTDYQMDEQE 533
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE------------ALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 534 LNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEE 613
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 614 ERKTAKKQVEES-----TRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASthKEIVALRQTAVEAAT-------- 680
Cdd:COG1196 506 FLEGVKAALLLAglrglAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA--AAIEYLKAAKAGRATflpldkir 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 681 -GRESDIAILQGELHKVQTELEQWRQTASEYESEIFNL---QTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKND 756
Cdd:COG1196 584 aRAALAAALARGAIGAAVDLVASDLREADARYYVLGDTllgRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 757 CDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQK 836
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
570 580 590
....*....|....*....|....*....|....*
gi 1952581418 837 QYEADQTM---YLELKEKLDKTQKENESITDELEN 868
Cdd:COG1196 744 EEELLEEEaleELPEPPDLEELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
611-878 |
1.57e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 611 LEEERKTAKK----QVEESTRQIQALQAHLHKLQKDIEILRED---KEIEIIETRDQLASTHKEIVALRQTAVEAatgrE 683
Cdd:COG1196 205 LERQAEKAERyrelKEELKELEAELLLLKLRELEAELEELEAEleeLEAELEELEAELAELEAELEELRLELEEL----E 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 684 SDIAILQGELHKVQTELEQWRQTASEYESEIfnlqtklqlqtqqqkDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQE 763
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERR---------------RELEERLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 764 KVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYEADQT 843
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270
....*....|....*....|....*....|....*
gi 1952581418 844 MYLELKEKLDKTQKENESITDELENCKENLKLLQQ 878
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
161-702 |
3.47e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 161 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGIRKEL 240
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 241 VTLQEDKHSyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEK 320
Cdd:COG1196 298 ARLEQDIAR----LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 321 LKQAEGKQEEIQQK---ALSEKKELQHRIDEMEEKEQLLQARIEALQA------------------------DNDFTNER 373
Cdd:COG1196 374 LAEAEEELEELAEElleALRAAAELAAQLEELEEAEEALLERLERLEEeleeleealaeleeeeeeeeealeEAAEEEAE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 374 LTALQVRLEQLQEKNIKDHNSIGIQVDDLLPKINGSTDKEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQNNRISNVE 453
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 454 DMFESHLENnqTTEEDLKNDSERFKATLIAEDDHTKVTEETKL--LKENQLEAKESDMSDTLSPSKDRSSEDTTDYQMDE 531
Cdd:COG1196 534 AAYEAALEA--ALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtfLPLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 532 QELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALL 611
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 612 EEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLAsthkEIVALRQTAVEAATGRESDIAILQG 691
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL----EEEELLEEEALEELPEPPDLEELER 767
|
570
....*....|.
gi 1952581418 692 ELHKVQTELEQ 702
Cdd:COG1196 768 ELERLEREIEA 778
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
28-85 |
4.00e-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: 4.00e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581418 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 |
5.54e-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: 5.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 27 PVKIGRSVARcRPAQNNATFDC-----KVLSRNHALIWFDHKTGKFYLQdTKSSNGTFINSQRLSRGseeSPPCELLSGD 101
Cdd:cd22701 18 EVVLGRNSKN-SSSTAADSVDIdlgpsKKISRRHARIFYDFTTQCFELS-VLGRNGVKVDGILVKPG---SPPVPLRSGS 92
|
....*
gi 1952581418 102 IIQFG 106
Cdd:cd22701 93 LIQIG 97
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
496-831 |
2.46e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 496 LLKENQLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQ 575
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 576 TGDSEREKQELQQELKEAQelaisskqkcfEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREdKEIEII 655
Cdd:COG1196 311 RRELEERLEELEEELAELE-----------EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA-ELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 656 ETRDQLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIfNLQTKLQLQTQQQKDKQKGE 735
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE-EEEEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 736 AVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQ--QSVKLTKDASGLEVSRKALEVEVGTLKEQR 813
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGflEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
330
....*....|....*...
gi 1952581418 814 LQETNGLRVKLAHAENET 831
Cdd:COG1196 538 AALEAALAAALQNIVVED 555
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
14-110 |
2.48e-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: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 14 SHPFQERHV---YLDEPVKIGRSvARCRPAQNNATfdckvLSRNHALIW---FDHKTG-KFYLQDTkSSNGTFINSQRLS 86
Cdd:cd22670 7 SSPGSTDIVlpiYKNQVITIGRS-PSCDIVINDPF-----VSRTHCRIYsvqFDESSApLVYVEDL-SSNGTYLNGKLIG 79
|
90 100
....*....|....*....|....*
gi 1952581418 87 RGseespPCELLS-GDIIQFGVDVT 110
Cdd:cd22670 80 RN-----NTVLLSdGDVIEIAHSAT 99
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
584-879 |
2.57e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 584 QELQQELKEAQeLAISSKQKCFemqalLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEilredkeieiiETRDQLAS 663
Cdd:TIGR02168 216 KELKAELRELE-LALLVLRLEE-----LREELEELQEELKEAEEELEELTAELQELEEKLE-----------ELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 664 THKEIVALrQTAVEAATgreSDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQqqkdkqkgEAVQLQGKL 743
Cdd:TIGR02168 279 LEEEIEEL-QKELYALA---NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE--------ELAELEEKL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 744 DELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLK---EQRLQETNGL 820
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEdrrERLQQEIEEL 426
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581418 821 RVKLahAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQK 879
Cdd:TIGR02168 427 LKKL--EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
580-867 |
3.34e-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: 57.77 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 580 EREKQELQQELK-EAQELAisskqkcfemQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEilreDKEIEIIETR 658
Cdd:TIGR02169 206 EREKAERYQALLkEKREYE----------GYELLKEKEALERQKEAIERQLASLEEELEKLTEEIS----ELEKRLEEIE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 659 DQLASTHKEIVALRqtaveaatgrESDIAILQGELHKVQTELEQWRQTASEYESEIfNLQTKLQLQTQQQKDKQKGEAVQ 738
Cdd:TIGR02169 272 QLLEELNKKIKDLG----------EEEQLRVKEKIGELEAEIASLERSIAEKEREL-EDAEERLAKLEAEIDKLLAEIEE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 739 LQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQ--- 815
Cdd:TIGR02169 341 LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRlse 420
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952581418 816 ---------------------ETNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELE 867
Cdd:TIGR02169 421 eladlnaaiagieakineleeEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
533-858 |
4.16e-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: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 533 ELNESLNKVSLLKDLLAEARA-SSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALL 611
Cdd:TIGR02169 195 EKRQQLERLRREREKAERYQAlLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 612 EEERKTAKKQVEESTRQIqalQAHLHKLQKDIEILrEDKEIEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQG 691
Cdd:TIGR02169 275 EELNKKIKDLGEEEQLRV---KEKIGELEAEIASL-ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 692 ELHKVQTELEQWRQTASEYESEIfnlqtklqLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKL 771
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEDLRAEL--------EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 772 QWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRlqetnglrvklahaenetQKFQKQYEADQTMYLELKEK 851
Cdd:TIGR02169 423 ADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL------------------SKYEQELYDLKEEYDRVEKE 484
|
....*..
gi 1952581418 852 LDKTQKE 858
Cdd:TIGR02169 485 LSKLQRE 491
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
55-108 |
1.35e-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: 1.35e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1952581418 55 HALIWFDHKTGKFYLQDTKSSNGTFINSQRLSrgseESPPCELLSGDIIQFGVD 108
Cdd:cd22704 39 HAVITYDQIDNEFKIKDLGSLNGTFVNDSRIP----EQTYITLKLGDSIRFGYD 88
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
25-114 |
1.38e-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: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 25 DEPVKIGRSVArcrpAQNNATFDC-KVLSRNHALIWFDhKTGKFYLQDTKSSNGTFINSQRLsrgsEESPPCELLSGDII 103
Cdd:cd22663 20 GKEVTVGRGLG----VTYQLVSTCpLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERI----EPLKPYPLNEGDLI 90
|
90
....*....|.
gi 1952581418 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 |
3.87e-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: 3.87e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581418 30 IGRSVArcrpaqNNATFDCKVLSRNHALIwfDHKTGKFYLQDTKSSNGTFINSQRLSRGseesppcELLSGDIIQFG 106
Cdd:cd22698 25 IGRSSN------NDIRLNDHSVSRHHARI--VRQGDKCNLTDLGSTNGTFLNGIRVGTH-------ELKHGDRIQLG 86
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
254-813 |
5.58e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 254 AKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQ 333
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 334 kalsEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKDHNSIGIQVDDLlpkingstdke 413
Cdd:COG1196 317 ----RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL----------- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 414 hfllksggdcSELFQQFIECKNKLKApveptQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKvTEE 493
Cdd:COG1196 382 ----------EELAEELLEALRAAAE-----LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE-ALE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 494 TKLLKENQLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLA--EARASSRKHESELDHLKYELQC 571
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAdyEGFLEGVKAALLLAGLRGLAGA 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 572 AHVQTGDSEREKQELQ---------------QELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHL 636
Cdd:COG1196 526 VAVLIGVEAAYEAALEaalaaalqnivveddEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVA 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 637 HKLQKDIEILREDKEIEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIFN 716
Cdd:COG1196 606 SDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 717 LQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNglkndcDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLE 796
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEERELAEAEEERLEEE------LEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759
|
570
....*....|....*..
gi 1952581418 797 VSRKALEVEVGTLKEQR 813
Cdd:COG1196 760 PDLEELERELERLEREI 776
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
519-803 |
6.81e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 6.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 519 RSSEDTTDYQMDEQELNE-----SLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEA 593
Cdd:TIGR02168 207 RQAEKAERYKELKAELRElelalLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 594 QE--LAISSKQKCFEMQ-ALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKE---IEIIETRDQLASTHKE 667
Cdd:TIGR02168 287 QKelYALANEISRLEQQkQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEelkEELESLEAELEELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 668 IVALRQTAVEAATGRE---SDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKGEavqLQGKLD 744
Cdd:TIGR02168 367 LEELESRLEELEEQLEtlrSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE---LQAELE 443
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581418 745 ELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALE 803
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
297-876 |
9.53e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 9.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 297 QEELRELanKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQH---RIDEMEEKEQLLQARIEALQADNDFTNER 373
Cdd:COG1196 219 KEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAEleaELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 374 LTALQVRLEQLQEKNIkdhnsigiqvddllpkingstDKEHFLLKSGGDCSELFQQFIECKNKLKapveptqnnRISNVE 453
Cdd:COG1196 297 LARLEQDIARLEERRR---------------------ELEERLEELEEELAELEEELEELEEELE---------ELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 454 DMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEETKLLKENQLEAKESDMSDTLSpSKDRSSEDTTDYQMDEQE 533
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE-AEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 534 LNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEE 613
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 614 ERKTAKKQVEES-----TRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASthKEIVALRQTAVEAAT-------- 680
Cdd:COG1196 506 FLEGVKAALLLAglrglAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA--AAIEYLKAAKAGRATflpldkir 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 681 -GRESDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDS 759
Cdd:COG1196 584 aRAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 760 LRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYE 839
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
570 580 590
....*....|....*....|....*....|....*..
gi 1952581418 840 ADQTMYLELKEKLDKTQKENEsITDELENCKENLKLL 876
Cdd:COG1196 744 EEELLEEEALEELPEPPDLEE-LERELERLEREIEAL 779
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
271-878 |
1.06e-06 |
|
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: 52.72 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 271 KLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKAlsekKELQHRIDEME 350
Cdd:TIGR04523 97 KINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKY----NDLKKQKEELE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 351 EKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKnIKDHNSIGIQVDDLLPKINGSTDKehfLLKSGGDCSELFQQF 430
Cdd:TIGR04523 173 NELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKK-IQKNKSLESQISELKKQNNQLKDN---IEKKQQEINEKTTEI 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 431 IECKNKLKAPVEptQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKATlIAEDDHTKVTEETKLLKEnQLEAKESDMS 510
Cdd:TIGR04523 249 SNTQTQLNQLKD--EQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSE-ISDLNNQKEQDWNKELKS-ELKNQEKKLE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 511 DTlspskdrssedttdyqmdEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQEL 590
Cdd:TIGR04523 325 EI------------------QNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 591 KEAqelaISSKQKcfemqalLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREdkeiEIIETRDQLASTHKEIVA 670
Cdd:TIGR04523 387 KNL----ESQIND-------LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKE----TIIKNNSEIKDLTNQDSV 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 671 LRQTAVEAATGRES---DIAILQGELHKVQTELEQWRQTASEYESEIFNLQTklqlqtqqqkdkqkgEAVQLQGKLDELQ 747
Cdd:TIGR04523 452 KELIIKNLDNTRESletQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE---------------EKKELEEKVKDLT 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 748 KQSNGLKNDCDSLRQEKVLLTEKLQWFEEELrcaqqQSVKLTKDASGLEVSRKALEVEVGTLKEQR---LQETNGLRVKL 824
Cdd:TIGR04523 517 KKISSLKEKIEKLESEKKEKESKISDLEDEL-----NKDDFELKKENLEKEIDEKNKEIEELKQTQkslKKKQEEKQELI 591
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1952581418 825 AHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQ 878
Cdd:TIGR04523 592 DQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQ 645
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
246-881 |
1.12e-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: 52.81 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 246 DKHSYETTAKESLRRVLQEKIEvvrklsEVERSLSNTEDectHLKEMNDRTqEELRELANKYNGAVNELKEFTEKLKQAE 325
Cdd:pfam15921 131 DIRRRESQSQEDLRNQLQNTVH------ELEAAKCLKED---MLEDSNTQI-EQLRKMMLSHEGVLQEIRSILVDFEEAS 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 326 GKQ-------------------EEIQQKALSEKKELQHRI----DEMEEKEQLLQARIE-ALQADNDFTNERLTALQVRL 381
Cdd:pfam15921 201 GKKiyehdsmstmhfrslgsaiSKILRELDTEISYLKGRIfpveDQLEALKSESQNKIElLLQQHQDRIEQLISEHEVEI 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 382 EQLQEKNI---KDHNSIGIQVDDLLPKI-NGSTDKEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQNNRISNVEDMFE 457
Cdd:pfam15921 281 TGLTEKASsarSQANSIQSQLEIIQEQArNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 458 SHLENNQTTEEDLKNDSERFKatLIAedDHTKVTEETKLLKENQLEAKESDMSDTLSPSKDRSSEDttDYQMDEQEL--- 534
Cdd:pfam15921 361 ARTERDQFSQESGNLDDQLQK--LLA--DLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELD--DRNMEVQRLeal 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 535 ----------------------NESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELkE 592
Cdd:pfam15921 435 lkamksecqgqmerqmaaiqgkNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAI-E 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 593 AQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDkeieiIETRDQLASTHKEIVALR 672
Cdd:pfam15921 514 ATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQ-----IENMTQLVGQHGRTAGAM 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 673 QtaVEAATgresdiaiLQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKGEAVQLQGKLDeLQKQSNG 752
Cdd:pfam15921 589 Q--VEKAQ--------LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKD-IKQERDQ 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 753 LKNDCDSLRQEKVLLTEKLQWFEEELRC-AQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENET 831
Cdd:pfam15921 658 LLNEVKTSRNELNSLSEDYEVLKRNFRNkSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQIT 737
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1952581418 832 QKfQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQKGN 881
Cdd:pfam15921 738 AK-RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKN 786
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
27-117 |
1.63e-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: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 27 PVKIGRSVarcrpaQNNATFDCKVLSRNHALIWFDHKTGKFYLQDTKSSNGTFINSQRLsrgSEESPPCELLSGDIIQFG 106
Cdd:cd22678 24 PLTIGRIQ------RGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESI---SPNGRPVVLSSGDVITLG 94
|
90
....*....|.
gi 1952581418 107 vdvTENTRKVT 117
Cdd:cd22678 95 ---SETKILVR 102
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
298-852 |
1.64e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 298 EELRELANKYNGAVNELKEftEKLKQAEGKQEEIQQKalsEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTAL 377
Cdd:PRK02224 165 EEYRERASDARLGVERVLS--DQRGSLDQLKAQIEEK---EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 378 QVRLEQLQEKNiKDHNSIGIQVDDLLPKINGS-TDKEHFllksGGDCSELFQQFIECKNKL-----KAPVEPTQNNRISN 451
Cdd:PRK02224 240 DEVLEEHEERR-EELETLEAEIEDLRETIAETeREREEL----AEEVRDLRERLEELEEERddllaEAGLDDADAEAVEA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 452 VEDMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEETKLLKENQLEAKESDMSDTLSPSKDRSSE-DTTDYQMD 530
Cdd:PRK02224 315 RREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEiEELEEEIE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 531 EQE-----LNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQcahvqtgDSEREKQELQ---------QELKEAQEl 596
Cdd:PRK02224 395 ELRerfgdAPVDLGNAEDFLEELREERDELREREAELEATLRTAR-------ERVEEAEALLeagkcpecgQPVEGSPH- 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 597 aISSKQKCFEMQALLEEERKTAKKQVE------ESTRQIQALQAHLHKLQ---KDIEILREDKEIEIIETRDQLASTHKE 667
Cdd:PRK02224 467 -VETIEEDRERVEELEAELEDLEEEVEeveerlERAEDLVEAEDRIERLEerrEDLEELIAERRETIEEKRERAEELRER 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 668 IVALRQTAVEAatgrESDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQkgEAVQLQGKLDELQ 747
Cdd:PRK02224 546 AAELEAEAEEK----REAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAED--EIERLREKREALA 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 748 KQSNGLKNDCDSLRQEKVLLTEKLQWFE-EELRCAQQQSVKLTKDASG----LEVSRKALEVEVGTLkEQRLQETNGLRV 822
Cdd:PRK02224 620 ELNDERRERLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEkldeLREERDDLQAEIGAV-ENELEELEELRE 698
|
570 580 590
....*....|....*....|....*....|...
gi 1952581418 823 KLAHAENETQKFQKQY---EADQTMYLELKEKL 852
Cdd:PRK02224 699 RREALENRVEALEALYdeaEELESMYGDLRAEL 731
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
578-801 |
2.83e-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: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 578 DSEREKQELQQELKEAQELAISSKQKcfemQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREdkeiEIIET 657
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK----EIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 658 RDQLASTHKEIValRQTAVEAATGRESDIAIL--QGELHKVQTELeQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKGE 735
Cdd:COG4942 96 RAELEAQKEELA--ELLRALYRLGRQPPLALLlsPEDFLDAVRRL-QYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952581418 736 AVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKA 801
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
247-886 |
3.00e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 247 KHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTE--DECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQA 324
Cdd:PTZ00121 1207 KAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKkaEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 325 EGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQAdndftNERLTALQVRLEQLQEKnikdhnsigiqvDDLLP 404
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA-----KKKADAAKKKAEEAKKA------------AEAAK 1349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 405 KINGSTDKEHFLLKSGGDCSELFQQfiecKNKLKAPVEPTQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKAtliae 484
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKE----EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKA----- 1420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 485 DDHTKVTEETKLLKENQLEAKESDMSDTLSP-SKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELD 563
Cdd:PTZ00121 1421 DEAKKKAEEKKKADEAKKKAEEAKKADEAKKkAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAD 1500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 564 HLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAK-KQVEESTRQIQALQAHLHKLQ-- 640
Cdd:PTZ00121 1501 EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElKKAEEKKKAEEAKKAEEDKNMal 1580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 641 KDIEILREDKEIEIIETRDQLASTHKEIVALRQTAVEAATGREsdiailqgELHKVQTELEQWRQTASEYESEIFNLQTK 720
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE--------ELKKAEEEKKKVEQLKKKEAEEKKKAEEL 1652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 721 LQLQTQQQ--KDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLR---QEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGL 795
Cdd:PTZ00121 1653 KKAEEENKikAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKkeaEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA 1732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 796 EVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELencKENLKL 875
Cdd:PTZ00121 1733 EEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDI---FDNFAN 1809
|
650
....*....|.
gi 1952581418 876 LQQKGNNGGLF 886
Cdd:PTZ00121 1810 IIEGGKEGNLV 1820
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
51-106 |
3.11e-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: 3.11e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952581418 51 LSRNHALIWF----DHKTGKFYLQDTKSSNGTFINSQRLsrgseesPP---CELLSGDIIQFG 106
Cdd:cd22677 41 ISRYHAVLQYrgdaDDHDGGFYLYDLGSTHGTFLNKQRI-------PPkqyYRLRVGHVLKFG 96
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
211-565 |
4.56e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 211 DRLLSRLEVMGNQLQAYSKNQTEdgIRKELVTLQEDkhsyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLK 290
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAE--LRKELEELEEE-----------LEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 291 EMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQkalsekkelqhRIDEMEEKEQLLQARIEALQADNDFT 370
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA-----------QIEQLKEELKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 371 NERLTALQVRLEQLQekniKDHNSIGIQVDDLLPKINGSTDKEHFLLKSGGDCSELfqqfiecKNKLKAPVEPTQNNRIS 450
Cdd:TIGR02168 816 NEEAANLRERLESLE----RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL-------IEELESELEALLNERAS 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 451 NVEDMfESHLENNQTTEEDLKNDSERFKAtliAEDDHTKVTEetkllKENQLEAKESDMSDTLSPSKDRSSEdttDYQMD 530
Cdd:TIGR02168 885 LEEAL-ALLRSELEELSEELRELESKRSE---LRRELEELRE-----KLAQLELRLEGLEVRIDNLQERLSE---EYSLT 952
|
330 340 350
....*....|....*....|....*....|....*
gi 1952581418 531 EQELnesLNKVSLLKDLLAEARASSRKHESELDHL 565
Cdd:TIGR02168 953 LEEA---EALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
337-702 |
4.92e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 337 SEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQekniKDHNSIGIQVDDLLPKINGSTDKehfl 416
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS----RQISALRKDLARLEAEVEQLEER---- 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 417 lksggdcselfQQFIECKNKLKAPVEPTQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKATliaEDDHTKVTEETKL 496
Cdd:TIGR02168 749 -----------IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL---REALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 497 LKENQLEAKEsdmsdTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLkyelqcahvqt 576
Cdd:TIGR02168 815 LNEEAANLRE-----RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL----------- 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 577 gdsEREKQELQQELKEAQELAISskqkcfemqalLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILredkEIEIIE 656
Cdd:TIGR02168 879 ---LNERASLEEALALLRSELEE-----------LSEELRELESKRSELRRELEELREKLAQLELRLEGL----EVRIDN 940
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1952581418 657 TRDQLASTHKeivALRQTAVEAATGRESDIAILQGELHKVQTELEQ 702
Cdd:TIGR02168 941 LQERLSEEYS---LTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| FHA_CHFR |
cd22672 |
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ... |
49-105 |
7.34e-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: 7.34e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581418 49 KVLSRNHALIWFDHKtGKFYLQDTkSSNGTFINSQRLSRGSEesppCELLSGDIIQF 105
Cdd:cd22672 39 KLVSGDHCKIIRDEK-GQVWLEDT-STNGTLVNKVKVVKGQK----VELKHGDVIYL 89
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
234-779 |
7.47e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 7.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 234 DGIRKELVTLQEDKHSYETTAKEsLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEmNDRTQEELRELANKYNgavnE 313
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKE-LESLEGSKRKLEEKIRELEERIEELKKEIEELEE-KVKELKELKEKAEEYI----K 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 314 LKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEqllqARIEALQADNDFTNERLTALQVRLEQLQE-KNIKDh 392
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE----ERLEELKKKLKELEKRLEELEERHELYEEaKAKKE- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 393 nsigiQVDDLLPKINGST-DKEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQNNRISNVEDMFESHLE----NNQTTE 467
Cdd:PRK03918 373 -----ELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 468 EDLKNDSERFKATLIAEDDHTKVTEEtkllKENQLEAKESDMSDTLSpskdRSSEDTTDYQMDEQ--ELNESLNKVSLLK 545
Cdd:PRK03918 448 EHRKELLEEYTAELKRIEKELKEIEE----KERKLRKELRELEKVLK----KESELIKLKELAEQlkELEEKLKKYNLEE 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 546 dlLAEARASSRKHESELDHLKYELqcahvqtgdserekQELQQELKEAQELAISSkqkcfemqALLEEERKTAKKQVEES 625
Cdd:PRK03918 520 --LEKKAEEYEKLKEKLIKLKGEI--------------KSLKKELEKLEELKKKL--------AELEKKLDELEEELAEL 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 626 TRQIQALQ-AHLHKLQKDIEILRE--DKEIEIIETRDQLASTHKEIVALRQTAVEAatgrESDIAILQGELHKVQTELEQ 702
Cdd:PRK03918 576 LKELEELGfESVEELEERLKELEPfyNEYLELKDAEKELEREEKELKKLEEELDKA----FEELAETEKRLEELRKELEE 651
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581418 703 WRQtasEYESEIFNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQ--EKVLLTEKLQWFEEELR 779
Cdd:PRK03918 652 LEK---KYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKakKELEKLEKALERVEELR 727
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
52-106 |
7.77e-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: 7.77e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1952581418 52 SRNHALIWFDHKTGKFYLQDTKSSNGTFINSQRLsrgsEESPPCELLSGDIIQFG 106
Cdd:cd22674 48 SRVHAALVYHKHLNRVFLIDLGSTHGTFVGGIRL----EPHKPQQLPIDSTLRFG 98
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
297-879 |
8.19e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 8.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 297 QEELRELANKYngAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQ----------HRIDEMEEKEQLLQAR------- 359
Cdd:TIGR02168 219 KAELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQeleekleelrLEVSELEEEIEELQKElyalane 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 360 IEALQADNDFTNERLTALQ-------VRLEQLQEKNIKDH---NSIGIQVDDLLPKINGSTDK------EHFLLKSGGDc 423
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLErqleeleAQLEELESKLDELAeelAELEEKLEELKEELESLEAEleeleaELEELESRLE- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 424 sELFQQFIECKNKLKAPVEP--TQNNRISNVEDMFEsHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEETKLLKEnq 501
Cdd:TIGR02168 376 -ELEEQLETLRSKVAQLELQiaSLNNEIERLEARLE-RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEE-- 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 502 LEAKESDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLaearassRKHESELDHLKYELQCAHVQTGDSER 581
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ-------ENLEGFSEGVKALLKNQSGLSGILGV 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 582 --EKQELQQELKEAQELAISSKqkcfeMQALLEEERKTAKKQVE-----------------ESTRQIQALQAHLHK---- 638
Cdd:TIGR02168 525 lsELISVDEGYEAAIEAALGGR-----LQAVVVENLNAAKKAIAflkqnelgrvtflpldsIKGTEIQGNDREILKnieg 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 639 -------------------------------LQKDIEILREDKEIEIIETRD-QLASTHKEIVALRQTAVEAATGRESDI 686
Cdd:TIGR02168 600 flgvakdlvkfdpklrkalsyllggvlvvddLDNALELAKKLRPGYRIVTLDgDLVRPGGVITGGSAKTNSSILERRREI 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 687 AILQGELHKVQTELEQWRQTASEYESEIFNLQTklqlqtqqqkdkqkgEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVL 766
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEE---------------ELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 767 LTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQ-----------------ETNGLRVKLAHAEN 829
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeelkalrealdelraELTLLNEEAANLRE 824
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1952581418 830 ETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQK 879
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
25-108 |
8.57e-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: 8.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 25 DEPVKIGRsvarcRPAQNNAT----FDCKVLSRNHALIWFdhKTGKFYLQDTKSSNGTFINSQRLSR-GSEESPPCELLS 99
Cdd:cd22702 31 KQPCIIGS-----DPHQAISGisvvIPSPQVSELHARITC--KNGAFFLTDLGSEHGTWINDNEGRRyRAPPNFPVRLHP 103
|
....*....
gi 1952581418 100 GDIIQFGVD 108
Cdd:cd22702 104 SDVIEFGSD 112
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
182-853 |
9.00e-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: 49.73 E-value: 9.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 182 LEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGIRKELVTLQEDKHSYETTakeslrrv 261
Cdd:pfam15921 243 VEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSM-------- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 262 lqekieVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKE 341
Cdd:pfam15921 315 ------YMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 342 LQHRIDEMEEKEQLLQAR-------IEALQADNDFTNERLTALQVRLEQLQEKnikdhnsIGIQVDDLLPKINGSTDkeh 414
Cdd:pfam15921 389 REKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSE-------CQGQMERQMAAIQGKNE--- 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 415 fllkSGGDCSELFQQFIECKNKLKAPVEPTQNNRISnvedmfeshLENNQTTEEDLKNDSERFKATLIAEDdhtkvTEET 494
Cdd:pfam15921 459 ----SLEKVSSLTAQLESTKEMLRKVVEELTAKKMT---------LESSERTVSDLTASLQEKERAIEATN-----AEIT 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 495 KLLKENQLEAKESDMsdtLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKyelqcahV 574
Cdd:pfam15921 521 KLRSRVDLKLQELQH---LKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQ-------V 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 575 QTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALqahlhklqKDIEILREDKEIEI 654
Cdd:pfam15921 591 EKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAV--------KDIKQERDQLLNEV 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 655 IETRDQLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESeifnlqtklqlqtqqqkdkQKG 734
Cdd:pfam15921 663 KTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEG-------------------SDG 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 735 EAVQLQGKldeLQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGL--EVSRKALEVEVGTLKEQ 812
Cdd:pfam15921 724 HAMKVAMG---MQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVatEKNKMAGELEVLRSQER 800
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1952581418 813 RLQE-TNGLRVKLAHAENETQKFQK--QYEADQTMYLELKEKLD 853
Cdd:pfam15921 801 RLKEkVANMEVALDKASLQFAECQDiiQRQEQESVRLKLQHTLD 844
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
181-690 |
1.27e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.95 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 181 MLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQT--EDGIRKELVTLQEDKHSYETTAKESL 258
Cdd:pfam05483 262 LLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKalEEDLQIATKTICQLTEEKEAQMEELN 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 259 RRVLQEKIEVvrklSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQ------ 332
Cdd:pfam05483 342 KAKAAHSFVV----TEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKkilaed 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 333 QKALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRlEQLQEKNIKDHNSIgiQVDDLLPKINGSTDK 412
Cdd:pfam05483 418 EKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTS-EEHYLKEVEDLKTE--LEKEKLKNIELTAHC 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 413 EHFLLKSggdcSELFQQFIECKNKLKAPVEPTQNNRisNVEDMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKV-- 490
Cdd:pfam05483 495 DKLLLEN----KELTQEASDMTLELKKHQEDIINCK--KQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCkl 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 491 --TEETKLLKENQLEAKESDMSDTLSPSKD--RSSEDTTDYQMDEQELNESLNKVSLLKD------------LLAEARAS 554
Cdd:pfam05483 569 dkSEENARSIEYEVLKKEKQMKILENKCNNlkKQIENKNKNIEELHQENKALKKKGSAENkqlnayeikvnkLELELASA 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 555 SRKHESELDHLKYELQCAHVQT----GDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQ 630
Cdd:pfam05483 649 KQKFEEIIDNYQKEIEDKKISEekllEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELG 728
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 631 ALQAHlhklQKDIEILREDKEIEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQ 690
Cdd:pfam05483 729 LYKNK----EQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILK 784
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
28-106 |
1.67e-05 |
|
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438732 [Multi-domain] Cd Length: 96 Bit Score: 44.25 E-value: 1.67e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581418 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 |
1.79e-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: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 13 NSHPFQERHVYLDE-PVKIGRSvarcrpAQNNATFDCKVLSRNHALIWFDHKTgkFYLQDTKSSNGTFINSQRLSrgsee 91
Cdd:cd22665 7 SQAHGPEKDFPLYEgENVIGRD------PSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRL----- 73
|
90 100
....*....|....*....|.
gi 1952581418 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 |
1.99e-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: 1.99e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952581418 52 SRNHALIWFDHKTG---------KFYLQDTkSSNGTFINSQRLSRGSEesppCELLSGDIIQFGV 107
Cdd:cd22667 40 SRKHATLTVLHPEAnlsdpdtrpELTLKDL-SKYGTFVNGEKLKGGSE----VTLKDGDVITFGV 99
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
256-878 |
2.29e-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: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 256 ESLRRVLQEKIEVVRK--LSEVERSLSNTEDECTHLKEMN--DRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEI 331
Cdd:TIGR01612 1058 DEIEKEIGKNIELLNKeiLEEAEINITNFNEIKEKLKHYNfdDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEI 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 332 QQKALSEKKELQHRIDEMEEkeqllqariealQADNDFTNERLTALQVRLEQLQEKnIKDHNSIGIQVDDLLPKINGSTD 411
Cdd:TIGR01612 1138 KKKSENYIDEIKAQINDLED------------VADKAISNDDPEEIEKKIENIVTK-IDKKKNIYDEIKKLLNEIAEIEK 1204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 412 KEHFL-------LKSGGDCSELFQQFIECKNKLKAPVEPTQNNRISNVEDMFES--HLENNQTTEEDLKNDSERFKATLI 482
Cdd:TIGR01612 1205 DKTSLeevkginLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKspEIENEMGIEMDIKAEMETFNISHD 1284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 483 AEDDHTKVTEE---------TKLLKENQLEAKESDMSDTlspsKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLaeara 553
Cdd:TIGR01612 1285 DDKDHHIISKKhdenisdirEKSLKIIEDFSEESDINDI----KKELQKNLLDAQKHNSDINLYLNEIANIYNIL----- 1355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 554 ssrkhesELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQ 633
Cdd:TIGR01612 1356 -------KLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKIESTLDDKDIDECIKKIKELK 1428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 634 AHlhklqkdieILREDKEieiIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQ-----GELHKVQTELEQWRQTAS 708
Cdd:TIGR01612 1429 NH---------ILSEESN---IDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKkdnatNDHDFNINELKEHIDKSK 1496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 709 EYESEI--------FNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKlqwFEEELRC 780
Cdd:TIGR01612 1497 GCKDEAdknakaieKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEK---SEQKIKE 1573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 781 AQQQSVKLTKDASGLEVSRKA---LEVEVGTLKEQRLQETNgLRVKLAHAENETQKFQKQ-----YEADQTMYLELKEKL 852
Cdd:TIGR01612 1574 IKKEKFRIEDDAAKNDKSNKAaidIQLSLENFENKFLKISD-IKKKINDCLKETESIEKKissfsIDSQDTELKENGDNL 1652
|
650 660
....*....|....*....|....*.
gi 1952581418 853 DKTQKENESITDELENCKENLKLLQQ 878
Cdd:TIGR01612 1653 NSLQEFLESLKDQKKNIEDKKKELDE 1678
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
18-86 |
2.29e-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: 2.29e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581418 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 |
2.97e-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: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 12 PNSHPfqerHVYL-DEPVKIGRSvarcrpAQNNATFDCKVLSRNHALIWFD-HKTGK--FYLQDTkSSNGTFINSQRLSR 87
Cdd:cd22690 8 NPSYP----DIELtQNTTFIGRS------KDCDEEITDPRISKHHCIITRKrSGKGLddVYVTDT-STNGTFINNNRLGK 76
|
90
....*....|....*.
gi 1952581418 88 GSEesppCELLSGDII 103
Cdd:cd22690 77 GSQ----SLLQDGDEI 88
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
1-106 |
3.08e-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: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 1 MPSALAIFTCRPNSHPFQERHVYLDEPVKIGRSvARC-----RPAQnnatfdckVLSRNHALIWFDHktGKFYLQDTkSS 75
Cdd:COG3456 1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRS-ADCdwvlpDPDR--------SVSRRHAEIRFRD--GAFCLTDL-ST 68
|
90 100 110
....*....|....*....|....*....|...
gi 1952581418 76 NGTFIN--SQRLSRGSEEsppcELLSGDIIQFG 106
Cdd:COG3456 69 NGTFLNgsDHPLGPGRPV----RLRDGDRLRIG 97
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
30-106 |
3.49e-05 |
|
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.
Pssm-ID: 438734 [Multi-domain] Cd Length: 96 Bit Score: 43.29 E-value: 3.49e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581418 30 IGRSVarcrpaQNNATFDCKVLSRNHALiwFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEesppCELLSGDIIQFG 106
Cdd:cd22682 24 IGRSV------ESQVQIDDDSVSRYHAK--LAVNPSAVSIIDLGSTNGTIVNGKKIPKLAS----CDLQNGDQIKIG 88
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
239-651 |
3.51e-05 |
|
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: 47.20 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 239 ELVTLQEDKHSYE------------TTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRElanK 306
Cdd:pfam07888 5 ELVTLEEESHGEEggtdmllvvpraELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELES---R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 307 YNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQllqaRIEALQADNDFTNERLTALQVRLEQLQE 386
Cdd:pfam07888 82 VAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEA----RIRELEEDIKTLTQRVLERETELERMKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 387 KNIKDHNSIGIQVDDllpkingSTDKEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQnnrisnvedmfesHLENNQTT 466
Cdd:pfam07888 158 RAKKAGAQRKEEEAE-------RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVL-------------QLQDTITT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 467 EEDLKNDSERFKATLIAEDDHTKVTEETKLLKENQLEAKESDMSDTLSpSKDRSSEDTTDYQMDEQELNESLNKVSLlkd 546
Cdd:pfam07888 218 LTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAA-QRDRTQAELHQARLQAAQLTLQLADASL--- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 547 LLAEARASSRKHESELdhlkyeLQCAHVQTGDSEREKQELQQELKEAQElAISSKQKcfeMQALLEEERKTAKKQVEEST 626
Cdd:pfam07888 294 ALREGRARWAQERETL------QQSAEADKDRIEKLSAELQRLEERLQE-ERMEREK---LEVELGREKDCNRVQLSESR 363
|
410 420
....*....|....*....|....*
gi 1952581418 627 RQIQALQAHLHKLQKDIEILREDKE 651
Cdd:pfam07888 364 RELQELKASLRVAQKEKEQLQAEKQ 388
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
49-112 |
3.75e-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: 3.75e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581418 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 |
4.34e-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: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 267 EVVRKLSEveRSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLK-QAEGKQEEIQ--QKALSEKKELQ 343
Cdd:COG2433 380 EALEELIE--KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEaELEEKDERIErlERELSEARSEE 457
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1952581418 344 HRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKDH 392
Cdd:COG2433 458 RREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEH 506
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
534-879 |
4.65e-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: 47.32 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 534 LNESLNKVSLLKDLLAEAR-ASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQAL-L 611
Cdd:TIGR04523 144 LTEIKKKEKELEKLNNKYNdLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISeL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 612 EEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILR----------EDKEIE-------IIETRDQLASTHKEIVALRQT 674
Cdd:TIGR04523 224 KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKdeqnkikkqlSEKQKEleqnnkkIKELEKQLNQLKSEISDLNNQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 675 AVEAATGR-ESDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKgeavQLQGKLDELQKqsngL 753
Cdd:TIGR04523 304 KEQDWNKElKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQR----ELEEKQNEIEK----L 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 754 KNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQ----------ETNGLRVK 823
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKnnseikdltnQDSVKELI 455
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1952581418 824 LAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQK 879
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK 511
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
239-882 |
4.89e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 239 ELVTLQEDKHSYETTAKESLRRV--LQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKE 316
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 317 FTEKLKQAEGKQEEIQQKA--LSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKDHNS 394
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKAdaAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 395 IGIQVDDLLPKINGSTDKEHFLLKSggdcsELFQQFIECKNKLKapvEPTQNNRISNVEDMFESHLENNQTTEEDLKNDS 474
Cdd:PTZ00121 1442 EAKKADEAKKKAEEAKKAEEAKKKA-----EEAKKADEAKKKAE---EAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD 1513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 475 ERFKATLIAEDDHTKVTEETKLLKENQlEAKESDMSDTLSPSKD-RSSEDTtdyQMDEQELNESLNKVSLLKDLlAEARA 553
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAK-KAEEKKKADELKKAEElKKAEEK---KKAEEAKKAEEDKNMALRKA-EEAKK 1588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 554 SSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELaissKQKCFEMQALLEEERKTA---KKQVEESTRQIQ 630
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE----KKKVEQLKKKEAEEKKKAeelKKAEEENKIKAA 1664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 631 ALQAHLHKLQKDIEILREDKEIEiietrdqlasthkeivalrqTAVEAATGRESDIAILQGELHKVQTElEQWRQTASEY 710
Cdd:PTZ00121 1665 EEAKKAEEDKKKAEEAKKAEEDE--------------------KKAAEALKKEAEEAKKAEELKKKEAE-EKKKAEELKK 1723
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 711 ESEIFNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEK-VLLTEKLQWFEEELRCAQQQSVKLT 789
Cdd:PTZ00121 1724 AEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKeAVIEEELDEEDEKRRMEVDKKIKDI 1803
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 790 KDASG-LEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELEN 868
Cdd:PTZ00121 1804 FDNFAnIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEE 1883
|
650
....*....|....
gi 1952581418 869 CKENlKLLQQKGNN 882
Cdd:PTZ00121 1884 IEEA-DEIEKIDKD 1896
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
531-710 |
5.18e-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: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 531 EQELNESLNKVSLLKDLLAEARASSRKHESELDHLK--YELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQ 608
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRqkNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 609 ALLEEERKTAKKQVEEStrQIQALQAHLHKLQKDIEILRE---DKEIEIIETRDQLASTHKEIVALRQTAVEAAtgrESD 685
Cdd:COG3206 247 AQLGSGPDALPELLQSP--VIQQLRAQLAELEAELAELSArytPNHPDVIALRAQIAALRAQLQQEAQRILASL---EAE 321
|
170 180
....*....|....*....|....*
gi 1952581418 686 IAILQGELHKVQTELEQWRQTASEY 710
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAEL 346
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
164-862 |
6.59e-05 |
|
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: 46.89 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 164 ELFQLSQYLQEA---------LHREQMLEQKLATLQRLLANTQeaSDSSWQALIDEDRLLSRLEVMGNQLQaysknQTED 234
Cdd:TIGR00618 171 NLFPLDQYTQLAlmefakkksLHGKAELLTLRSQLLTLCTPCM--PDTYHERKQVLEKELKHLREALQQTQ-----QSHA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 235 GIRKELvTLQEDKHSYETTAKESLRRV------------LQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRE 302
Cdd:TIGR00618 244 YLTQKR-EAQEEQLKKQQLLKQLRARIeelraqeavleeTQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRS 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 303 LANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKK-ELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRL 381
Cdd:TIGR00618 323 RAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAhEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKEL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 382 EQLQEknikdhnsigiQVDDLLPKINGSTDKEHFLLKSGGDCsELFQQFIECKNKLKAPVEPTQNNRISNVEDMFESHLE 461
Cdd:TIGR00618 403 DILQR-----------EQATIDTRTSAFRDLQGQLAHAKKQQ-ELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 462 NNQTtEEDLKNDSERFKATliaeddHTKVTEETKLLKENQLEAKESdmsdTLSPSKDRssedttdYQMDEQELNESLnkv 541
Cdd:TIGR00618 471 REQQ-LQTKEQIHLQETRK------KAVVLARLLELQEEPCPLCGS----CIHPNPAR-------QDIDNPGPLTRR--- 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 542 sllkdlLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQ 621
Cdd:TIGR00618 530 ------MQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKL 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 622 VEESTRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASTHKEivalrQTAVEAATGRESDIAILQGELHKVQTELE 701
Cdd:TIGR00618 604 SEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALH-----ALQLTLTQERVREHALSIRVLPKELLASR 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 702 QWRQTASEYESEIFNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDcdsLRQEKVLLTEKLQWFEEELRCA 781
Cdd:TIGR00618 679 QLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSD---LAAREDALNQSLKELMHQARTV 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 782 QQQSVkltkdasgLEVSRKALEVevgTLKEQRLQEtnglrvkLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENES 861
Cdd:TIGR00618 756 LKART--------EAHFNNNEEV---TAALQTGAE-------LSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDED 817
|
.
gi 1952581418 862 I 862
Cdd:TIGR00618 818 I 818
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
178-359 |
7.17e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 178 REQML--EQKLATLQRLLANTQEAsDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGIRKELVTLQEDKHSYE---T 252
Cdd:COG4913 241 HEALEdaREQIELLEPIRELAERY-AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEarlD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 253 TAKESLRRV--------------LQEKIE-VVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEF 317
Cdd:COG4913 320 ALREELDELeaqirgnggdrleqLEREIErLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEE 399
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1952581418 318 TEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEK-----EQLLQAR 359
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERRksnipARLLALR 446
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
121-879 |
7.38e-05 |
|
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: 46.65 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 121 IVSTVKLFMPDGMEGRRRSDVIQAPLPLPVEKVAANspsmYSQELFQLSQYLQEA--LHREQ--MLEQKLATLQRLLANT 196
Cdd:pfam15921 47 TFTQIPIFPKYEVELDSPRKIIAYPGKEHIERVLEE----YSHQVKDLQRRLNESneLHEKQkfYLRQSVIDLQTKLQEM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 197 QEASDsswqALIDedrlLSRLEvmgNQLQAYSKNQTEDGIRK--ELVTLQEDKHSYETTAKESLRRVLQEKIEVVRKLSE 274
Cdd:pfam15921 123 QMERD----AMAD----IRRRE---SQSQEDLRNQLQNTVHEleAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 275 VERSLSNTEDECTHlkEMNDRTQEELRELANKYNGAVNELKEFTEKLK--------QAEGKQEEIQQKALSEKKELQHRI 346
Cdd:pfam15921 192 ILVDFEEASGKKIY--EHDSMSTMHFRSLGSAISKILRELDTEISYLKgrifpvedQLEALKSESQNKIELLLQQHQDRI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 347 DEMEEKEQLlqaRIEALQADNDFTNERLTALQVRLEQLQEKNIKDHNSIGIQVDDLLPKIngstdkehfllksggdcSEL 426
Cdd:pfam15921 270 EQLISEHEV---EITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTV-----------------SQL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 427 FQQFIECKNKLKAPVEPTQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKatLIAedDHTKVTEETKLLKENQLEAKE 506
Cdd:pfam15921 330 RSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQK--LLA--DLHKREKELSLEKEQNKRLWD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 507 SDMSDTLSPSKDRSSEDttDYQMDEQEL-------------------------NESLNKVSLLKDLLAEARASSRKHESE 561
Cdd:pfam15921 406 RDTGNSITIDHLRRELD--DRNMEVQRLeallkamksecqgqmerqmaaiqgkNESLEKVSSLTAQLESTKEMLRKVVEE 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 562 LDHLKYELQCAHVQTGDSEREKQELQQELkEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQK 641
Cdd:pfam15921 484 LTAKKMTLESSERTVSDLTASLQEKERAI-EATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDK 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 642 DIEILREDkeieiIETRDQLASTHKEIVALRQtaVEAATgresdiaiLQGELHKVQTELEQWRQTASEYESEIFNLQTKL 721
Cdd:pfam15921 563 VIEILRQQ-----IENMTQLVGQHGRTAGAMQ--VEKAQ--------LEKEINDRRLELQEFKILKDKKDAKIRELEARV 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 722 QLQTQQQKDKQKGEAVQLQG------KLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQ-SVKLTKDASG 794
Cdd:pfam15921 628 SDLELEKVKLVNAGSERLRAvkdikqERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKlKMQLKSAQSE 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 795 LEVSRK-----------ALEVEVGTLKE---------------QRLQET---------------NGLRVKLAHAENETQK 833
Cdd:pfam15921 708 LEQTRNtlksmegsdghAMKVAMGMQKQitakrgqidalqskiQFLEEAmtnankekhflkeekNKLSQELSTVATEKNK 787
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 1952581418 834 FQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQK 879
Cdd:pfam15921 788 MAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQE 833
|
|
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
53-106 |
7.65e-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: 7.65e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1952581418 53 RNHALIWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSeesppCELLSGDIIQFG 106
Cdd:cd22700 36 EQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAA-----VRLAPGDVLRFG 84
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
182-386 |
1.26e-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: 45.53 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 182 LEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEvmgNQLQAYSKNQTEdgIRKELVTLQEDKHSYETtAKESLRRV 261
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALA---RRIRALEQELAA--LEAELAELEKEIAELRA-ELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 262 LQEKIEVVRKLSEVER--SLSNTED--ECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALS 337
Cdd:COG4942 106 LAELLRALYRLGRQPPlaLLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1952581418 338 EKKELQHRIDEMEEKEQLLQARIEALQAdndftneRLTALQVRLEQLQE 386
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAA-------ELAELQQEAEELEA 227
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
613-813 |
1.27e-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: 45.53 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 613 EERKTAKKQVEESTRQIQALQAHLHKLQKDI-EILREDKEIE--IIETRDQLASTHKEIVALRQTAVEAatgrESDIAIL 689
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEkALLKQLAALErrIAALARRIRALEQELAALEAELAEL----EKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 690 QGELHKVQTELEQ-----WRQTASEYESEIFNLQTKLQLQTQQQKDKQKGEAvqLQGKLDELQKQSNGLKNDCDSLRQEK 764
Cdd:COG4942 96 RAELEAQKEELAEllralYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA--RREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1952581418 765 VLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQR 813
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
233-682 |
1.28e-04 |
|
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: 46.20 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 233 EDGIRKELVTL---QEDKHSYETTAK---ESLRRVLQEKIEVVRKLSE------VERSL-SNTEDECTHLKEMNdrtqEE 299
Cdd:TIGR01612 1269 EMDIKAEMETFnisHDDDKDHHIISKkhdENISDIREKSLKIIEDFSEesdindIKKELqKNLLDAQKHNSDIN----LY 1344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 300 LRELANKYN-GAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQL--LQARIEALQADNDFTN--ERL 374
Cdd:TIGR01612 1345 LNEIANIYNiLKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLeeCKSKIESTLDDKDIDEciKKI 1424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 375 TALQVRLEQlQEKNIKDHNSigiqvddllpkiNGSTDKEHFLLksggdcseLFQQFIECKNKLKAPVEPTQNNRIS---- 450
Cdd:TIGR01612 1425 KELKNHILS-EESNIDTYFK------------NADENNENVLL--------LFKNIEMADNKSQHILKIKKDNATNdhdf 1483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 451 NVEDMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTE----ETKLLKENQLEAKESDMSDTLSPSKDRSSEDTTD 526
Cdd:TIGR01612 1484 NINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTEllnkYSALAIKNKFAKTKKDSEIIIKEIKDAHKKFILE 1563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 527 YQMDEQELNESLNKVSLLKDLLAEARASSRKH---ESELDHLKYE-LQCAHVQT--GDSEREKQELQQELK----EAQEL 596
Cdd:TIGR01612 1564 AEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAidiQLSLENFENKfLKISDIKKkiNDCLKETESIEKKISsfsiDSQDT 1643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 597 AISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASTHKEIVALRQTAV 676
Cdd:TIGR01612 1644 ELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKEEIESIKELI 1723
|
....*.
gi 1952581418 677 EAATGR 682
Cdd:TIGR01612 1724 EPTIEN 1729
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
531-879 |
1.94e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 531 EQELNESLNKVSLLKDLLAEARASSRKHE--------SELDHLKYELQcahvqtgDSEREKQELQQELKEAQELAISSKQ 602
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEaqirgnggDRLEQLEREIE-------RLERELEERERRRARLEALLAALGL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 603 KCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEiEIIETRDQLASTHK----EIVALRQTAVEA 678
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR-ELEAEIASLERRKSnipaRLLALRDALAEA 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 679 ATGRESDIAILqGELHKVQTELEQWRQTA--------------SEYE---SEIFNLQTKLQ-------LQTQQQKDKQKG 734
Cdd:COG4913 453 LGLDEAELPFV-GELIEVRPEEERWRGAIervlggfaltllvpPEHYaaaLRWVNRLHLRGrlvyervRTGLPDPERPRL 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 735 EAVQLQGKL---------------------------DELQ------------KQSNGL--KNDCDSLRQEKVL---LTEK 770
Cdd:COG4913 532 DPDSLAGKLdfkphpfrawleaelgrrfdyvcvdspEELRrhpraitragqvKGNGTRheKDDRRRIRSRYVLgfdNRAK 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 771 LQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLkeQRLQETNGLRVKLAHAENETQKFQKQY---EADQTMYLE 847
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREAL--QRLAEYSWDEIDVASAEREIAELEAELerlDASSDDLAA 689
|
410 420 430
....*....|....*....|....*....|..
gi 1952581418 848 LKEKLDKTQKENESITDELENCKENLKLLQQK 879
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKE 721
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
182-674 |
2.32e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 182 LEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEvmgnqlqaySKNQTEDGIRKELVTLQEDKHSYETTaKESLRRV 261
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHE---------ERREELETLEAEIEDLRETIAETERE-REELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 262 LQEKIEVVRKLSEVERSL-----------SNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEE 330
Cdd:PRK02224 281 VRDLRERLEELEEERDDLlaeaglddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 331 IQQKALSEKKELQH---RIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEknikDHNSIGIQVDDLLPKIN 407
Cdd:PRK02224 361 LREEAAELESELEEareAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE----ERDELREREAELEATLR 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 408 GSTDK--EHFLLKSGGDCSELFQQFIEcknklkAPVEPTQNNRISNVEDMfESHLENNQTTEEDLKNDSERFKATLIAED 485
Cdd:PRK02224 437 TARERveEAEALLEAGKCPECGQPVEG------SPHVETIEEDRERVEEL-EAELEDLEEEVEEVEERLERAEDLVEAED 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 486 DHTKVTEETKLLKENQLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQ--------------------------ELNESLN 539
Cdd:PRK02224 510 RIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKreaaaeaeeeaeeareevaelnsklaELKERIE 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 540 KVSLLKDLLAEaRASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEA-QELAISSKQkcfemqalleEERKTA 618
Cdd:PRK02224 590 SLERIRTLLAA-IADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEfDEARIEEAR----------EDKERA 658
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952581418 619 KKQVEESTRQIQALQAHLHKLQKDI----------EILREDKEiEIIETRDQLASTHKEIVALRQT 674
Cdd:PRK02224 659 EEYLEQVEEKLDELREERDDLQAEIgaveneleelEELRERRE-ALENRVEALEALYDEAEELESM 723
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
258-387 |
2.32e-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: 43.76 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 258 LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEI----QQ 333
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkEY 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1952581418 334 KALS-EKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEK 387
Cdd:COG1579 92 EALQkEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
152-365 |
2.63e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 152 KVAANSPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDsswqaliDEDRLLSRLEVMGNQLQAYSKNQ 231
Cdd:COG4717 60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA-------ELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 232 TEDGIRKELVTLQEdkhsyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMND-RTQEELRELANKYNGA 310
Cdd:COG4717 133 ELEALEAELAELPE--------RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEEL 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1952581418 311 VNELKEFTEKLKQAEGKQEEIQQkalsEKKELQHRIDEMEEKEQLLQARIEALQA 365
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEE----ELEQLENELEAAALEERLKEARLLLLIA 255
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
236-879 |
2.79e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.96 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 236 IRKELVTLQEDKHSYETTAKesLRRVLQEKIEVVRKLSEVERSLSNTE----DECTHLKEMNDRTQEELRELANKYNGAV 311
Cdd:pfam02463 158 IEEEAAGSRLKRKKKEALKK--LIEETENLAELIIDLEELKLQELKLKeqakKALEYYQLKEKLELEEEYLLYLDYLKLN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 312 NELKEFTEKLKQAEGKQEEIQ---QKALSEKKELQHRIDEMEEKEQ--------LLQARIEALQADNDFTNERLTALQVR 380
Cdd:pfam02463 236 EERIDLLQELLRDEQEEIESSkqeIEKEEEKLAQVLKENKEEEKEKklqeeelkLLAKEEEELKSELLKLERRKVDDEEK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 381 LEQLQEKN---IKDHNSIGIQVDDLLPKINGSTDKEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQNNRISNVEDMFE 457
Cdd:pfam02463 316 LKESEKEKkkaEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 458 SHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTE---------ETKLLKENQLEAKESDMSDTLSPSKDRSSEDTTDYQ 528
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEileeeeesiELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 529 MDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQ 608
Cdd:pfam02463 476 ETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSA 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 609 ALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAI 688
Cdd:pfam02463 556 TADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELT 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 689 LQGELHKVQTELEQWRQTASEYESEI--FNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVL 766
Cdd:pfam02463 636 KLKESAKAKESGLRKGVSLEEGLAEKseVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKL 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 767 LTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAE-----NETQKFQKQYEAD 841
Cdd:pfam02463 716 KLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAeerekTEKLKVEEEKEEK 795
|
650 660 670
....*....|....*....|....*....|....*...
gi 1952581418 842 QTMYLELKEKLDKTQKENESITDELENCKENLKLLQQK 879
Cdd:pfam02463 796 LKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEE 833
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
198-387 |
3.15e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 198 EASDSSWQALIdEDRLLSRLEvmgNQLQAYSKNQTEDGIR--KELVTLQEDKHSYETTAKEsLRRVLQEKIEVVRKLSEV 275
Cdd:COG4717 33 EAGKSTLLAFI-RAMLLERLE---KEADELFKPQGRKPELnlKELKELEEELKEAEEKEEE-YAELQEELEELEEELEEL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 276 ERSLSNTEDECTHLKEMND---------RTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQHRI 346
Cdd:COG4717 108 EAELEELREELEKLEKLLQllplyqeleALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS 187
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1952581418 347 DEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEK 387
Cdd:COG4717 188 LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
580-763 |
3.39e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 580 EREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAkkQVEESTRQIQALQAHLHKLQKDIEILREDKeIEIIETRD 659
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLA--EYSWDEIDVASAEREIAELEAELERLDASS-DDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 660 QLASTHKEIVALRQ---TAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKgea 736
Cdd:COG4913 693 QLEELEAELEELEEeldELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE--- 769
|
170 180
....*....|....*....|....*..
gi 1952581418 737 vQLQGKLDELQKQSNGLKNDCDSLRQE 763
Cdd:COG4913 770 -NLEERIDALRARLNRAEEELERAMRA 795
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
586-784 |
3.49e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 586 LQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREdkeiEIIETRDQLASTH 665
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA----ELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 666 KEIVALRQTAVEAATGREsdIAILQGELHKVQTELEQWRQTASEYES---EIFNLQTKLQLQTQQQKDKQKGEAVQLQGK 742
Cdd:COG4717 123 KLLQLLPLYQELEALEAE--LAELPERLEELEERLEELRELEEELEEleaELAELQEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1952581418 743 LDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQ 784
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
16-111 |
4.24e-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: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 16 PFQERHVYLD-EPVKIGRSvarcrpAQNNATFDCKVLSRNHALIWFdhKTGKFYLQDTKSSNGTFINSQRLSRgseespP 94
Cdd:cd22693 7 TLQGQTFPIDkSGITIGRA------DDNDLVLSDDFVSSRHARIYL--QGSSWYLEDLGSTNGTFVNGNRVTQ------P 72
|
90
....*....|....*..
gi 1952581418 95 CELLSGDIIQFGVDVTE 111
Cdd:cd22693 73 VVVQPGDTIRIGATVFE 89
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
264-713 |
5.88e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 264 EKIEVVR-KLSEVERSLSNTEDECTHLKEMNDRTQEElRELANKYNGAVNELKEFTEKLKQAEgkqeeiQQKALSEKKEL 342
Cdd:TIGR02169 170 RKKEKALeELEEVEENIERLDLIIDEKRQQLERLRRE-REKAERYQALLKEKREYEGYELLKE------KEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 343 QHRIDEMEEKEQLLQARIEALqadndftNERLTALQVRLEQLQEKnikdhnsigiqvddllpkINGSTDKEhfllksggd 422
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISEL-------EKRLEEIEQLLEELNKK------------------IKDLGEEE--------- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 423 cselfqqfiecKNKLKAPVEPTQNnRISNVEDMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEETKLLKEnQL 502
Cdd:TIGR02169 289 -----------QLRVKEKIGELEA-EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD-KL 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 503 eakesdmsdtlspskdrssedTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSERE 582
Cdd:TIGR02169 356 ---------------------TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 583 KQELQQELKEAQELAISSKQKcfemQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDkeieiietrdqla 662
Cdd:TIGR02169 415 LQRLSEELADLNAAIAGIEAK----INELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE------------- 477
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1952581418 663 sthkeivalrqtaveaatgresdIAILQGELHKVQTELEQWRQTASEYESE 713
Cdd:TIGR02169 478 -----------------------YDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
531-674 |
6.41e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 531 EQELNESLNKVSLLKDLLAEARASSRKHESELDHL-----KYELQCAHVQTgdsEREKQELQQELkEAQELAISskqkcf 605
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVearikKYEEQLGNVRN---NKEYEALQKEI-ESLKRRIS------ 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581418 606 emqaLLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASTHKEIVALRQT 674
Cdd:COG1579 107 ----DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
531-714 |
6.73e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 531 EQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELqcahvqtGDSEREKQELQQELKEAQELAISSKQKCFEMQAL 610
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-------AALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 611 LEEERKTAKKQV---------------------EESTRQIQALQAHLHKLQKDIEILREDKEI------EIIETRDQLAS 663
Cdd:COG4942 99 LEAQKEELAELLralyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAElaalraELEAERAELEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1952581418 664 THKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEI 714
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| FHA_SNIP1_DDL-like |
cd22676 |
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ... |
52-106 |
6.79e-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: 6.79e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952581418 52 SRNHALIWF----------DHKTGKFYLQDTKSSNGTFINSQRLsrgsEESPPCELLSGDIIQFG 106
Cdd:cd22676 42 SKQHAVIQFrevekrnegdVIENIRPYIIDLGSTNGTFLNGEKI----EPRRYYELREKDVLKFG 102
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
289-546 |
6.83e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 289 LKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALqadnd 368
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEEL----- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 369 ftNERLTALQVRLEQlQEKNIKDHNSIGIQVDDLLPKINgstdKEHFLLKSGGDCSELFQQFIECKNKLKA----PVEPT 444
Cdd:PHA02562 240 --TDELLNLVMDIED-PSAALNKLNTAAAKIKSKIEQFQ----KVIKMYEKGGVCPTCTQQISEGPDRITKikdkLKELQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 445 Q-----NNRISNVEDMFESHLEnNQTTEEDLKNDSERFKATLIAEDDHTKVTEetKLLKenQLEAKESDMSDTLSPSKDR 519
Cdd:PHA02562 313 HsleklDTAIDELEEIMDEFNE-QSKKLLELKNKISTNKQSLITLVDKAKKVK--AAIE--ELQAEFVDNAEELAKLQDE 387
|
250 260
....*....|....*....|....*..
gi 1952581418 520 SSEDTTDYQMDEQELNESLNKVSLLKD 546
Cdd:PHA02562 388 LDKIVKTKSELVKEKYHRGIVTDLLKD 414
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
163-362 |
7.16e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.14 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 163 QELFQLSQYLQEALHREQML----------------EQKLATLQRLLANTQ---EASDSSWQALIDEDR-LLSRLEVMGN 222
Cdd:COG0497 172 KELEELRADEAERARELDLLrfqleeleaaalqpgeEEELEEERRRLSNAEklrEALQEALEALSGGEGgALDLLGQALR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 223 QLQAYSKNQTEdgirkelvtLQEdkhsyettAKESLRRVLQEKIEVVRklsEVERSLSNTEDECTHLKEMNDRtQEELRE 302
Cdd:COG0497 252 ALERLAEYDPS---------LAE--------LAERLESALIELEEAAS---ELRRYLDSLEFDPERLEEVEER-LALLRR 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952581418 303 LANKYNGAVNELKEFTEKLKQaegKQEEIQQKAlSEKKELQHRIDEMEEK-----EQLLQARIEA 362
Cdd:COG0497 311 LARKYGVTVEELLAYAEELRA---ELAELENSD-ERLEELEAELAEAEAElleaaEKLSAARKKA 371
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
546-779 |
7.78e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 546 DLLAEARASSRKHES---ELDHLKYELQCAHVQTGdsEREKQELQQELKEAQELAISSKQKcfemQALLEEERKTAKKQV 622
Cdd:COG4913 252 ELLEPIRELAERYAAareRLAELEYLRAALRLWFA--QRRLELLEAELEELRAELARLEAE----LERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 623 EESTRQIQALQ-AHLHKLQKDIEILREDKEiEIIETRDQLASthkeivALRQTAVEAATGREsdiailqgELHKVQTELE 701
Cdd:COG4913 326 DELEAQIRGNGgDRLEQLEREIERLERELE-ERERRRARLEA------LLAALGLPLPASAE--------EFAALRAEAA 390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581418 702 QWRQTASEYESEIFNlqtklqlqtqqqkdkqkgEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELR 779
Cdd:COG4913 391 ALLEALEEELEALEE------------------ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
310-387 |
9.24e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 9.24e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581418 310 AVNELKEFTEKLKQAEGKQEEIQQkalsEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEK 387
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQA----ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
178-702 |
9.97e-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: 43.11 E-value: 9.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 178 REQMLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEvmgnQLQAYSKNQTEDGIRKELVTLQEDKHSYEttakES 257
Cdd:TIGR00606 445 KKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAER----ELSKAEKNSLTETLKKEVKSLQNEKADLD----RK 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 258 LRRVLQEKIEVVRKLSEVERSLSNTEDECT---HLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQ-- 332
Cdd:TIGR00606 517 LRKLDQEMEQLNHHTTTRTQMEMLTKDKMDkdeQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAkl 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 333 QKALSEKKELQHRIDEMEEKEQLLQARIEalqaDNDFTNERLTALQVRLEQLQE---KNIKDHNSIGIQVDDLLPKINGS 409
Cdd:TIGR00606 597 NKELASLEQNKNHINNELESKEEQLSSYE----DKLFDVCGSQDEESDLERLKEeieKSSKQRAMLAGATAVYSQFITQL 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 410 TDKEHfllksggDCSELFQQFIECKNKLkapveptqNNRISNVEDMFESHLENNQTTEEDLKNDSERFKATLI-AEDDHT 488
Cdd:TIGR00606 673 TDENQ-------SCCPVCQRVFQTEAEL--------QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGlAPGRQS 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 489 KVTEETKLLKE--NQLEAKESDMSdtlspskdrssEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSR-KHESELDHL 565
Cdd:TIGR00606 738 IIDLKEKEIPElrNKLQKVNRDIQ-----------RLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERfQMELKDVER 806
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 566 KYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEE-------------ERKTAKKQVEESTRQIQAL 632
Cdd:TIGR00606 807 KIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDqqeqiqhlksktnELKSEKLQIGTNLQRRQQF 886
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 633 QAHLHKLQKDIEILREdkeiEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQ 702
Cdd:TIGR00606 887 EEQLVELSTEVQSLIR----EIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKN 952
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
50-106 |
1.15e-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: 1.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581418 50 VLSRNHALIWFDHKTGkfYLQDTKSSNGTFINSQRLsrgseeSPPCELLSGDIIQFG 106
Cdd:cd22668 36 GVSRRHAEIRWDGQVA--HLTDLGSTNGTTVNNAPV------TPEWRLADGDVITLG 84
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
163-366 |
1.28e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALID--------EDRLLSRLEVMGNQLQAYSKNQTED 234
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekeiaelRAELEAQKEELAELLRALYRLGRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 235 GIrkELVTLQEDKHSYETTAK--ESLRRVLQEKIEVVRK-LSEVERSLSNTEDECTHLKEMNDRTQEELRELAnkyngav 311
Cdd:COG4942 121 PL--ALLLSPEDFLDAVRRLQylKYLAPARREQAEELRAdLAELAALRAELEAERAELEALLAELEEERAALE------- 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1952581418 312 nelkefteklkQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQAD 366
Cdd:COG4942 192 -----------ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
607-856 |
1.45e-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: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 607 MQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIeiIETRDQLASTHKEIVALRQTAVEAatgrESDI 686
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGL--VDLSEEAKLLLQQLSELESQLAEA----RAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 687 AILQGELHKVQTELEQWRQTASEyeseifnlqtklqLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVL 766
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPE-------------LLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 767 LTEKLQwfeeelRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKeQRLQETNGLRVKLAhaenetqKFQKQYEADQTMYL 846
Cdd:COG3206 303 LRAQLQ------QEAQRILASLEAELEALQAREASLQAQLAQLE-ARLAELPELEAELR-------RLEREVEVARELYE 368
|
250
....*....|
gi 1952581418 847 ELKEKLDKTQ 856
Cdd:COG3206 369 SLLQRLEEAR 378
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
250-816 |
1.63e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 250 YETTAKES--LRRVLQEKIEVVRKL----SEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGA---VNELKEFTEK 320
Cdd:PRK03918 160 YENAYKNLgeVIKEIKRRIERLEKFikrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLekeVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 321 LKQAEGKQEEIQQ--KALSEK-KELQHRIDEMEEKEQLLQARIEALQadndfTNERLTALQVRLEQLQEKNIKDHNSIGI 397
Cdd:PRK03918 240 IEELEKELESLEGskRKLEEKiRELEERIEELKKEIEELEEKVKELK-----ELKEKAEEYIKLSEFYEEYLDELREIEK 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 398 QVDDLLPKINGSTDKEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQnnrisnVEDMFESHLENNQTTEEDLKNDS-ER 476
Cdd:PRK03918 315 RLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHE------LYEEAKAKKEELERLKKRLTGLTpEK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 477 FKATL-IAEDDHTKVTEETKLLKE--NQLEAKESDMSDTLSpskdrssedttdyqmdeqELNESLNKVSLLKDLLAEARA 553
Cdd:PRK03918 389 LEKELeELEKAKEEIEEEISKITAriGELKKEIKELKKAIE------------------ELKKAKGKCPVCGRELTEEHR 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 554 SS--RKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELaISSKQKCFEMQALLEEERKTAKKQVEESTRQIQA 631
Cdd:PRK03918 451 KEllEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEL-IKLKELAEQLKELEEKLKKYNLEELEKKAEEYEK 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 632 LQAHLHKLQKDIEILREDK-------------EIEIIETRDQLASTHKEIVALRQTAVEAATGR---------------- 682
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELekleelkkklaelEKKLDELEEELAELLKELEELGFESVEELEERlkelepfyneylelkd 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 683 -ESDIAILQGELHKVQTELEQWRQTASEYESEIfnlQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSL- 760
Cdd:PRK03918 610 aEKELEREEKELKKLEEELDKAFEELAETEKRL---EELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELe 686
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581418 761 --RQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQE 816
Cdd:PRK03918 687 krREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSK 744
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
297-387 |
1.88e-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: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 297 QEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQkalsEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTA 376
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK----QLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90
....*....|.
gi 1952581418 377 LQVRLEQLQEK 387
Cdd:COG4942 95 LRAELEAQKEE 105
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
159-325 |
2.63e-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: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 159 SMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIdEDRLLSRLEVMGNQLQAYSKNQTEDGIRk 238
Cdd:COG3206 215 KLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPV-IQQLRAQLAELEAELAELSARYTPNHPD- 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 239 eLVTLQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFT 318
Cdd:COG3206 293 -VIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLL 371
|
....*..
gi 1952581418 319 EKLKQAE 325
Cdd:COG3206 372 QRLEEAR 378
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
457-707 |
2.81e-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: 41.26 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 457 ESHLEN--NQTTEEDLKNDSERFKATLIAEDDHTKVTEETKllKENQLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQEL 534
Cdd:pfam05557 8 KARLSQlqNEKKQMELEHKRARIELEKKASALKRQLDRESD--RNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 535 NESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLeEE 614
Cdd:pfam05557 86 EALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQ-SS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 615 RKTAKKQVEESTRQIQ-------------ALQAHLHKLQKDIEILREDKEI--EIIETRDQLasthKEIVALRQTAVEAA 679
Cdd:pfam05557 165 LAEAEQRIKELEFEIQsqeqdseivknskSELARIPELEKELERLREHNKHlnENIENKLLL----KEEVEDLKRKLERE 240
|
250 260
....*....|....*....|....*...
gi 1952581418 680 TGRESDIAILQGELHKVQTELEQWRQTA 707
Cdd:pfam05557 241 EKYREEAATLELEKEKLEQELQSWVKLA 268
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
447-867 |
3.16e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 447 NRISNVEDMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEETKLLKENQLEAKE-SDMSDTLSPSKDRSSEDTT 525
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKlSEFYEEYLDELREIEKRLS 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 526 DYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKyelqcAHVQTGDSEREKQELQQELKEaqELAISSKQKCF 605
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELE-----ERHELYEEAKAKKEELERLKK--RLTGLTPEKLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 606 EMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDK--------EIEIIETRDQLASTHKEIVALRQTAVE 677
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrELTEEHRKELLEEYTAELKRIEKELKE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 678 AatgrESDIAILQGELHKVQTELEQWRQTASEYE--SEIFNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKN 755
Cdd:PRK03918 471 I----EEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKK 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 756 DCDS---LRQEKVLLTEKLQWFEEELRcaqqqsvkltkdasglEVSRKALEVEVGTLKE-----QRLQETNGLRVKLAHA 827
Cdd:PRK03918 547 ELEKleeLKKKLAELEKKLDELEEELA----------------ELLKELEELGFESVEEleerlKELEPFYNEYLELKDA 610
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1952581418 828 ENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELE 867
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE 650
|
|
| prfA |
PRK00591 |
peptide chain release factor 1; Validated |
532-632 |
3.40e-03 |
|
peptide chain release factor 1; Validated
Pssm-ID: 234801 [Multi-domain] Cd Length: 359 Bit Score: 40.83 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 532 QELNESLNKVSLLKDLlAEARASSRKHeSELDHL--KYelqcahvqtgdseREKQELQQELKEAQELAISSKQKcfEMQA 609
Cdd:PRK00591 16 EELEALLSDPEVISDQ-KRFRKLSKEY-AELEPIveAY-------------REYKQAQEDLEEAKEMLEEESDP--EMRE 78
|
90 100
....*....|....*....|...
gi 1952581418 610 LLEEERKTAKKQVEESTRQIQAL 632
Cdd:PRK00591 79 MAKEELKELEERLEELEEELKIL 101
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
533-702 |
3.44e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 533 ELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAisskqkcfemqalle 612
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI--------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 613 eERKTAKKQVEESTRQIQALQAHLHKLQKDIEILrEDKEIEIIETRD----QLASTHKEIVALRQTAVEAATGRESDIAI 688
Cdd:COG1579 76 -KKYEEQLGNVRNNKEYEALQKEIESLKRRISDL-EDEILELMERIEeleeELAELEAELAELEAELEEKKAELDEELAE 153
|
170
....*....|....
gi 1952581418 689 LQGELHKVQTELEQ 702
Cdd:COG1579 154 LEAELEELEAEREE 167
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
211-656 |
3.45e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 211 DRLLSRLEVMGNQLQAYSKNQTE-DGIRKELVTLQEDKHsyETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHL 289
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEElEELEEELEELEAELE--ELREELEKLEKLLQLLPLYQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 290 KEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQADNDF 369
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 370 TNERLTALQVRLEQLQEKNIKDHNSIGIQVDDLLPKINGSTDKEHFLLKSGGdcSELFQQFIECKNKLKAPVEPTQNNRI 449
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVL--GLLALLFLLLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 450 SNVEDMFESHLENNQTTEEDLKND---SERFKATLIAEDDHTKVTEETKLLKENQLEAKESDMSDTLSPSKDRSSEDTTD 526
Cdd:COG4717 310 LPALEELEEEELEELLAALGLPPDlspEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRA 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 527 YQMDEQELNESLNKVSLLKDLLAEARASSRKHESELD--HLKYELQCAHVQTGDSEREKQELQQELKEAQelAISSKQKC 604
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEELEELEEELEELREELAELE--AELEQLEE 467
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1952581418 605 FEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIEIIE 656
Cdd:COG4717 468 DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLE 519
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
212-882 |
3.74e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 212 RLLSRLEVMGNQLQAYSKNQTEDGIRKELVTLQEDKHSYETTAKESLRRVLQEKIEvvrkLSEVERSlSNTEDECTHLKE 291
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE----LDGFERG-PFSERQIKNFHT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 292 MNDRTQEELRELANKyngavnELKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTN 371
Cdd:TIGR00606 398 LVIERQEDEAKTAAQ------LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 372 ERLTALQVRLEQLQEKNIKDHNSIgiqVDDLLPKINGSTDKEHFLLKSggdcselfqqfiecknKLKAPVEPTQNNRISN 451
Cdd:TIGR00606 472 RILELDQELRKAERELSKAEKNSL---TETLKKEVKSLQNEKADLDRK----------------LRKLDQEMEQLNHHTT 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 452 VEDMFESHLENNQTTEEDLKNDSERFKATLIAEDDH---TKVTEETKLLKENQLEAKESDMSDtLSPSKDRSSEDTTDYQ 528
Cdd:TIGR00606 533 TRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYfpnKKQLEDWLHSKSKEINQTRDRLAK-LNKELASLEQNKNHIN 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 529 MDEQELNESLNKvslLKDLLAEArASSRKHESELDHLKYELQCAHVQ----TGDSEREKQELQQELKEAQELAISSkQKC 604
Cdd:TIGR00606 612 NELESKEEQLSS---YEDKLFDV-CGSQDEESDLERLKEEIEKSSKQramlAGATAVYSQFITQLTDENQSCCPVC-QRV 686
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 605 FEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILR----------EDKEIEIIETRDQLASTHKEIVALRQ- 673
Cdd:TIGR00606 687 FQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLglapgrqsiiDLKEKEIPELRNKLQKVNRDIQRLKNd 766
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 674 ------------TAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKGEAVQ--- 738
Cdd:TIGR00606 767 ieeqetllgtimPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSkie 846
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 739 -LQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQwfeeELRCAQQQSVKLTKDASGL--EVSRKALEVEVGTLKEQRLQ 815
Cdd:TIGR00606 847 lNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQ----RRQQFEEQLVELSTEVQSLirEIKDAKEQDSPLETFLEKDQ 922
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581418 816 ETNGLRVKLAHAENETQKFQKQyeadqtmylELKEKLDKTQKENESITDELENCKENLKllQQKGNN 882
Cdd:TIGR00606 923 QEKEELISSKETSNKKAQDKVN---------DIKEKVKNIHGYMKDIENKIQDGKDDYL--KQKETE 978
|
|
| VI_FHA |
TIGR03354 |
type VI secretion system FHA domain protein; Members of this protein family are FHA ... |
49-106 |
4.19e-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: 4.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952581418 49 KVLSRNHA-LIWFDhktGKFYLQDTkSSNGTFINS--QRLSRGSEESppceLLSGDIIQFG 106
Cdd:TIGR03354 43 RHVSGRHArIRYRD---GAYLLTDL-STNGVFLNGsgSPLGRGNPVR----LEQGDRLRLG 95
|
|
| FHA_Rv1747-like_rpt2 |
cd22737 |
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
28-106 |
4.30e-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: 4.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581418 28 VKIGRSvarcrpAQNNATFDCKVLSRNHALIwfDHKTGKFYLQDTKSSNGTFINSQRLSRgseesppCELLSGDIIQFG 106
Cdd:cd22737 23 VRIGRA------SDNDIVIPEGSVSRHHATL--VPTPGGTQIRDLRSTNGTFVNGLRVDA-------ALLHDGDVVTIG 86
|
|
| FHA_Ki67 |
cd22673 |
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ... |
52-106 |
4.95e-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: 4.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1952581418 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, ... |
618-812 |
4.96e-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: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 618 AKKQVEESTRQIQALQAHLHKLQKDIEILREDKEI---EIIETRDQLASTHKEIVALRQTAVEAatgrESDIAILQGELH 694
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKAllkQLAALERRIAALARRIRALEQELAAL----EAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 695 KVQTELEQWRQTASEY-----------------ESEIFNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDC 757
Cdd:COG4942 94 ELRAELEAQKEELAELlralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1952581418 758 DSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQ 812
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
270-387 |
5.21e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 270 RKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNgAVNELKEFTEKLKQAEGKQEEIQQ---------KALSEKK 340
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAEYSWDEIDVASAEREIAEleaelerldASSDDLA 688
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1952581418 341 ELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEK 387
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
436-860 |
5.46e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 436 KLKAPVEPTQNNRISNVEDMFESHLENNQTTEEDLK---NDSERFKATLIAED-DHTKVTEETKLLKENQLEAKESDMSD 511
Cdd:PTZ00121 1028 KIEELTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKahvGQDEGLKPSYKDFDfDAKEDNRADEATEEAFGKAEEAKKTE 1107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 512 TLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKdlLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQ--- 588
Cdd:PTZ00121 1108 TGKAEEARKAEEAKKKAEDARKAEEARKAEDARK--AEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARkae 1185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 589 ELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQaHLHKLQKDIEILREDKEIEIIETRDQLASTHKEI 668
Cdd:PTZ00121 1186 EVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVK-KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAH 1264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 669 VALRQTAVEAATGRESDiailqgELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKGEavQLQGKLDELQK 748
Cdd:PTZ00121 1265 FARRQAAIKAEEARKAD------ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAE--EAKKKADAAKK 1336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 749 QSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASglEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAE 828
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD--AAKKKAEEKKKADEAKKKAEEDKKKADELKKAA 1414
|
410 420 430
....*....|....*....|....*....|....
gi 1952581418 829 NETQKFQ--KQYEADQTMYLELKEKLDKTQKENE 860
Cdd:PTZ00121 1415 AAKKKADeaKKKAEEKKKADEAKKKAEEAKKADE 1448
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
164-387 |
6.63e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRL-LSRLEVMGNQLQAYSKNQTEdgIRKELVT 242
Cdd:PRK04863 852 ALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRVEEIREqLDEAEEAKRFVQQHGNALAQ--LEPIVSV 929
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 243 LQEDKHSYET------TAKESLRRVLQEkievVRKLSEV------------ERSLSNTEDECTHLKEMNDRTQEELRELA 304
Cdd:PRK04863 930 LQSDPEQFEQlkqdyqQAQQTQRDAKQQ----AFALTEVvqrrahfsyedaAEMLAKNSDLNEKLRQRLEQAEQERTRAR 1005
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 305 NKYNGAVNELKEFTE---KLKQAEGKQEEIQQKALSEKKELQHRIDEMEE------KEQLLQA------RIEALQADNDF 369
Cdd:PRK04863 1006 EQLRQAQAQLAQYNQvlaSLKSSYDAKRQMLQELKQELQDLGVPADSGAEerararRDELHARlsanrsRRNQLEKQLTF 1085
|
250
....*....|....*...
gi 1952581418 370 TNERLTALQVRLEQLQEK 387
Cdd:PRK04863 1086 CEAEMDNLTKKLRKLERD 1103
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
532-649 |
6.95e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 532 QELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALL 611
Cdd:COG4913 678 ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA 757
|
90 100 110
....*....|....*....|....*....|....*...
gi 1952581418 612 EEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILRED 649
Cdd:COG4913 758 ALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
256-365 |
7.11e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 256 ESLRRVLQEKI-EVVRKLSEVERSLSNTEDEcthLKEMNDRTQEELRELANKYNGAVNELKE----------FTEKLKQA 324
Cdd:PRK00409 526 EELERELEQKAeEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLEEAEKEAQQAIKEAKKeadeiikelrQLQKGGYA 602
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1952581418 325 EGKQEEIQQKalseKKELQHRIDEMEEKEQLLQARIEALQA 365
Cdd:PRK00409 603 SVKAHELIEA----RKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
255-389 |
7.18e-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: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 255 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEgkqeEIQQK 334
Cdd:COG4026 113 KNAIIRAGLKSLQNIPEYNELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILE----EEFDN 188
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581418 335 ALSEKKELQHRIDEMEEKEQLLQARIEALQAD---NDFTNERLTALQVrlEQLQEKNI 389
Cdd:COG4026 189 IKSEYSDLKSRFEELLKKRLLEVFSLEELWKElfpEELPEEDFIYFAT--ENLKPGKI 244
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
256-671 |
7.93e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 256 ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRtQEELRELANKYNGAVNELKEFTEKLKQAEGKQE------ 329
Cdd:PRK01156 315 SNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQ-ILELEGYEMDYNSYLKSIESLKKKIEEYSKNIErmsafi 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 330 -EIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQeknikDHNSIGIQVDDLlpkinG 408
Cdd:PRK01156 394 sEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLN-----GQSVCPVCGTTL-----G 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 409 STDKEHFLLKSGGDCSELFQQFIECKNKLKAPVEPT--QNNRISNVEDMFESHLENNQTTEEDLKNDSERFKATLIA-ED 485
Cdd:PRK01156 464 EEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIvdLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINElKD 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 486 DHTKVTEETKLLKENQLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKV--------SLLKDLLAEARASSRK 557
Cdd:PRK01156 544 KHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLesrlqeieIGFPDDKSYIDKSIRE 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 558 HESELDHLKYELQCAHvqtgDSEREKQELQQELKEAQElAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLH 637
Cdd:PRK01156 624 IENEANNLNNKYNEIQ----ENKILIEKLRGKIDNYKK-QIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRA 698
|
410 420 430
....*....|....*....|....*....|....*..
gi 1952581418 638 KLQKDIEILREDK---EIEIIETRDQLASTHKEIVAL 671
Cdd:PRK01156 699 RLESTIEILRTRInelSDRINDINETLESMKKIKKAI 735
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
572-716 |
8.07e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.89 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 572 AHVQTGDSEREKQELQQELKEAQElaisskqkcfemQALLEEERKTAKKQVEESTRQIQALQahlhKLQKDIEILRedKE 651
Cdd:PRK11281 27 ARAASNGDLPTEADVQAQLDALNK------------QKLLEAEDKLVQQDLEQTLALLDKID----RQKEETEQLK--QQ 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581418 652 IEiiETRDQLASTHKEIVALRQTAVEAATGRESDIAI--LQGELHKVQTELEQWRQTASEYESEIFN 716
Cdd:PRK11281 89 LA--QAPAKLRQAQAELEALKDDNDEETRETLSTLSLrqLESRLAQTLDQLQNAQNDLAEYNSQLVS 153
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
274-381 |
8.57e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.84 E-value: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 274 EVERSLSNTEDECTHLKEMNDRTQEELRELANKY---NGAVNELKEFTEKLKQAEGKQEEIQQKALSEK----------K 340
Cdd:pfam06160 288 YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEvayselqeelE 367
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1952581418 341 ELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRL 381
Cdd:pfam06160 368 EILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLEL 408
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
238-533 |
9.46e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 238 KELVTLQEDKHSYETTAKESLRRVLQE----KIEVVRKLSEVER---SLSNTEDECTHLKEMNDRTQEELRELANKYNGA 310
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEEnkikAAEEAKKAEEDKKkaeEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 311 VNELKEfTEKLKQAE----GKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQvrlEQLQE 386
Cdd:PTZ00121 1712 AEEKKK-AEELKKAEeenkIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE---EELDE 1787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581418 387 KNIKDHNSIGIQVDDLLpkingstDKEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQNNRIsNVEDMFESHLEN-NQT 465
Cdd:PTZ00121 1788 EDEKRRMEVDKKIKDIF-------DNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQL-EEADAFEKHKFNkNNE 1859
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581418 466 TEEDLKNDSERFKATLIAEDDHTKVtEETKLLKENQLEAKESDMSDTLSPSKDrssEDTTDYQMDEQE 533
Cdd:PTZ00121 1860 NGEDGNKEADFNKEKDLKEDDEEEI-EEADEIEKIDKDDIEREIPNNNMAGKN---NDIIDDKLDKDE 1923
|
|
| |
