|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
3-130 |
1.17e-80 |
|
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: 254.11 E-value: 1.17e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 3 SALAIFTCRPNSHPFQERHVYLDEPIKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHktSKFYLQDTKSSNGTFINS 82
Cdd:cd22679 1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1958683060 83 QRLSRGSEESPPCEILSGDIIQFGVDVTENTRKVTHGCIVSTIKLFLP 130
Cdd:cd22679 79 QRLSKGSEESEPRELHSGDIVQFGVDVVENSRKVTHGCIVATVTLFLP 126
|
|
| CC1_SLMAP |
cd21911 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal ... |
163-225 |
7.05e-27 |
|
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal membrane-associated protein (SLMAP), also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. SLMAP contains an N-terminal FHA domain followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409287 [Multi-domain] Cd Length: 63 Bit Score: 103.92 E-value: 7.05e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683060 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQ 225
Cdd:cd21911 1 QELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQLS 63
|
|
| FHA_DMA-like |
cd22692 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest ... |
27-108 |
1.26e-17 |
|
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: 79.92 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 27 PIKIGRSVARCRPAQNNAT-FDCKVLSRNHALVWfdHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQF 105
Cdd:cd22692 38 QIHIGRYTERVRQAIYHPVvFKSKVVSRTHGCIK--VDEGNWYIKDVKSSSGTFLNHQRLSPASRTSKPYPLRDGDILQL 115
|
...
gi 1958683060 106 GVD 108
Cdd:cd22692 116 GMD 118
|
|
| FHA_VPS64-like |
cd22695 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ... |
6-126 |
3.85e-15 |
|
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: 72.72 E-value: 3.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 6 AIFTCRPNSHPFQERHV---YLDEPIKIGRSVARCRPAQN---------------NATFDCKVLSRNHALVWFDHKTSKF 67
Cdd:cd22695 2 HILVLKSLNATFETKFLvvpFKPDGLKLGRPVTNSVNKNNsgskrdlfsqqvrpdNGNFDSRVLSRNHACLSCDPTTGKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683060 68 YLQDTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFGVDVTEntrKVTHGCIVSTIK 126
Cdd:cd22695 82 YIRDLKSSNGTFVNGQKIRQND-----VELKVGDEVDLGTDIDS---KIEHRKISAYVE 132
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
13-106 |
2.22e-13 |
|
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: 66.53 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 13 NSHPFQERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKtsKFYLQDTKSSNGTFINSQRLsrgseeS 92
Cdd:cd00060 6 DGDGGGREFPLTKGVVTIGRS------PDCDIVLDDPSVSRRHARIEVDGG--GVYLEDLGSTNGTFVNGKRI------T 71
|
90
....*....|....
gi 1958683060 93 PPCEILSGDIIQFG 106
Cdd:cd00060 72 PPVPLQDGDVIRLG 85
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-771 |
3.82e-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: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 156 NTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQA--CSKNQTE 233
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvAQLELQI 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 234 DSLRKELVALQEDKHSYE------TTAKESLRRVLQE--KIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELAN 305
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEdrrerlQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 306 KYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKID---------DMEEKEQELQAKIEALQAdndftnERLTA 376
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlsELISVDEGYEAAIEAALG------GRLQA 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 377 LQVRLEPLQEK---TLKEcSSLG----IQVDDFLPKINGSTEKERLLSKsGGDCTFIHQFIECQKKL--MVQGHL--TKV 445
Cdd:TIGR02168 550 VVVENLNAAKKaiaFLKQ-NELGrvtfLPLDSIKGTEIQGNDREILKNI-EGFLGVAKDLVKFDPKLrkALSYLLggVLV 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 446 VEE--------SKLSKENQAKAKESDL-----SDTLSPSKEKSSDDTTDAQMDE--QDLNEPLAKVSLLKALL---EEER 507
Cdd:TIGR02168 628 VDDldnalelaKKLRPGYRIVTLDGDLvrpggVITGGSAKTNSSILERRREIEEleEKIEELEEKIAELEKALaelRKEL 707
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 508 KAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDT---EISSTRDKLLSAQDEILLLHQAAAKA---VSERDTDFMSL 581
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQleeRIAQLSKELTELEAEIEELEERLEEAeeeLAEAEAEIEEL 787
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 582 QEELKKVRAELEGWRKAASEYEEEIRSLQSTF---QLRCQQCE----------VQQREEATRLQGELEKLKKEWDVLENE 648
Cdd:TIGR02168 788 EAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLErriaaterrlEDLEEQIEELSEDIESLAAEIEELEEL 867
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 649 CRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHlrdeADLKTLLSKAENQAKDVQk 728
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL----AQLELRLEGLEVRIDNLQ- 942
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1958683060 729 eyektQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 771
Cdd:TIGR02168 943 -----ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
28-105 |
6.14e-13 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 64.13 E-value: 6.14e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683060 28 IKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhKTSKFYLQDTKSSNGTFINSQRLSRgseesPPCEILSGDIIQF 105
Cdd:pfam00498 1 VTIGRS------PDCDIVLDDPSVSRRHAEIRYD-GGGRFYLEDLGSTNGTFVNGQRLGP-----EPVRLKDGDVIRL 66
|
|
| CC1_SLMAP-like |
cd21868 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ... |
167-204 |
6.32e-13 |
|
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar proteins; The family includes Sarcolemmal membrane-associated protein (SLMAP), its paralog TRAF3-interacting JNK-activating modulator (T3JAM), and similar proteins. SLMAP, also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. T3JAM, also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. SLMAP contains an N-terminal FHA domain, followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409286 [Multi-domain] Cd Length: 38 Bit Score: 63.27 E-value: 6.32e-13
10 20 30
....*....|....*....|....*....|....*...
gi 1958683060 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21868 1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
52-106 |
2.33e-11 |
|
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 (AGGF1) and similar proteins; AGGF1, also called angiogenic factor VG5Q, or G patch domain-containing protein 7 (GPATC7), or vasculogenesis gene on 5q protein, is an angiogenic factor involved in vascular development, angiogenesis, specification of hemangioblasts, and differentiation of veins. It promotes angiogenesis and the proliferation of endothelial cells. It inhibits inflammatory effect and preserve vascular integrity in non-nervous system diseases. Mutated AGGF1 causes susceptibility to Klippel-Trenaunay syndrome, a vascular disorder. Increased AGGF1 expression is associated with tumor angiogenesis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438738 [Multi-domain] Cd Length: 123 Bit Score: 61.53 E-value: 2.33e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1958683060 52 SRNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQFG 106
Cdd:cd22686 48 SKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPYPLTHGDELKIG 102
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
14-106 |
7.23e-11 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 59.20 E-value: 7.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 14 SHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktSKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716 8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
|
90
....*....|....
gi 1958683060 93 pPCEILSGDIIQFG 106
Cdd:COG1716 75 -PAPLRDGDVIRLG 87
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
239-763 |
8.92e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.93 E-value: 8.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 239 ELVALQEDKHSYETTAKESLRRV--LQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKD 316
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 317 LSDKLKAAEGKQEEIQQKGQAEKK--ELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEKTLKECSS 394
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 395 LGIQVDDFLPKINGSTEKERLLSKSggdctfihqfiecqkklmvqghltkvvEESKLSKENQAKAKESDLSDTLSPSKEK 474
Cdd:PTZ00121 1442 EAKKADEAKKKAEEAKKAEEAKKKA---------------------------EEAKKADEAKKKAEEAKKADEAKKKAEE 1494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 475 SSDDTTDAQMDEqdlnEPLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQE-EKDTEISSTRDKL 553
Cdd:PTZ00121 1495 AKKKADEAKKAA----EAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElKKAEEKKKAEEAK 1570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 554 LSAQDEILLLHQA--AAKAVSERDTDFMSLQEELKKVRAE----LEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQQREE 627
Cdd:PTZ00121 1571 KAEEDKNMALRKAeeAKKAEEARIEEVMKLYEEEKKMKAEeakkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE 1650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 628 ATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLR 707
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKI 1730
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683060 708 DEADLKTLLSKAENQAKDVQKEYE---KTQTVLSELKLKFEMTEQEKQSITDELKQCKD 763
Cdd:PTZ00121 1731 KAEEAKKEAEEDKKKAEEAKKDEEekkKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
190-770 |
2.77e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 190 QRLLAITQEASDTSWQALIDE--------DRLLSRLEVMGNQLQACSKNQTE-----DSLRKELVALQEDKHSYETT--- 253
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLRleelreelEELQEELKEAEEELEELTAELQEleeklEELRLEVSELEEEIEELQKElya 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 254 AKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQ 333
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 334 KGQAEKKELQ---AKIDDMEEKEQELQAKIEALQAdndftneRLTALQVRLEPLQEKTLKECSSLgiQVDDFLPKINGST 410
Cdd:TIGR02168 373 RLEELEEQLEtlrSKVAQLELQIASLNNEIERLEA-------RLERLEDRRERLQQEIEELLKKL--EEAELKELQAELE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 411 EKERLLSKSGGDCTFIHQFIECQKKLMVQGHLTKVVEESKLSK---------------------ENQAKAKESDLSDTLS 469
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQlqarldslerlqenlegfsegVKALLKNQSGLSGILG 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 470 PSKEKSS---------------------DDTTDAQMDEQDLnepLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQL 528
Cdd:TIGR02168 524 VLSELISvdegyeaaieaalggrlqavvVENLNAAKKAIAF---LKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGF 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 529 QRLHMDMenlqEEKDTEISSTRDKLLS--------------------------AQDEILLLHQAAAKAVSERDTDFMSLQ 582
Cdd:TIGR02168 601 LGVAKDL----VKFDPKLRKALSYLLGgvlvvddldnalelakklrpgyrivtLDGDLVRPGGVITGGSAKTNSSILERR 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 583 EELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRcQQCEVQQREEATRLQGELEKLKKEWDVLENECRSlkkenvlLSSE 662
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEEL-EEELEQLRKELEELSRQISALRKDLARLEAEVEQ-------LEER 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 663 LQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTL---LSKAENQAKDVQKEYEKTQTVLSE 739
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALreaLDELRAELTLLNEEAANLRERLES 828
|
650 660 670
....*....|....*....|....*....|.
gi 1958683060 740 LKLKFEMTEQEKQSITDELKQCKDNLKLLRE 770
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
161-741 |
1.08e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 161 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKEL 240
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 241 VALQEDkhsyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDK 320
Cdd:COG1196 298 ARLEQD-----------IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 321 LKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEKTLKEcsslgiqvd 400
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE--------- 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 401 dflpkINGSTEKERLLSKSGGDCTFIHQFIECQKKLMVQGHLTKVVEESKLSKENQAKAKESDL-----SDTLSPSKEKS 475
Cdd:COG1196 438 -----EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLleaeaDYEGFLEGVKA 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 476 SDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQ--VEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKL 553
Cdd:COG1196 513 ALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNivVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 554 LS-AQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLqstfqlrcqqcevqqREEATRLQ 632
Cdd:COG1196 593 ARgAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV---------------TLEGEGGS 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 633 GELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADL 712
Cdd:COG1196 658 AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
570 580
....*....|....*....|....*....
gi 1958683060 713 KTLLSKAENQAKDVQKEYEKTQTVLSELK 741
Cdd:COG1196 738 LEELLEEEELLEEEALEELPEPPDLEELE 766
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
135-713 |
1.52e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 61.67 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 135 ARLRSDVIHAPLpSPVDKVAANTPSMYSQELFQL----SQYLQEALHREQMLEQKLATLQRLLAItqeASDTSWQALIDE 210
Cdd:pfam15921 290 ARSQANSIQSQL-EIIQEQARNQNSMYMRQLSDLestvSQLRSELREAKRMYEDKIEELEKQLVL---ANSELTEARTER 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 211 DRLLSRLEVMGNQLQAC----SKNQTEDSLRKELVALQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNtedec 286
Cdd:pfam15921 366 DQFSQESGNLDDQLQKLladlHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKS----- 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 287 thlrEMNERTQEELRELANKyNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQAD 366
Cdd:pfam15921 441 ----ECQGQMERQMAAIQGK-NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAT 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 367 NDFTNERLTALQVRLEPLQ---------EKTLKECSSLGIQVddflpkingsTEKERLLSksggdctFIHQFIECQKKLM 437
Cdd:pfam15921 516 NAEITKLRSRVDLKLQELQhlknegdhlRNVQTECEALKLQM----------AEKDKVIE-------ILRQQIENMTQLV 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 438 VQGHLTK---VVEESKLSKENQAKAKESDLSDTLspsKEKSSDDTTDAQMDEQDLNepLAKVSLLKALLE---------E 505
Cdd:pfam15921 579 GQHGRTAgamQVEKAQLEKEINDRRLELQEFKIL---KDKKDAKIRELEARVSDLE--LEKVKLVNAGSErlravkdikQ 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 506 ERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDEillLHQAAAKAVSERDTDFMSLQEEL 585
Cdd:pfam15921 654 ERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSE---LEQTRNTLKSMEGSDGHAMKVAM 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 586 kkvraeleGWRKAASEYEEEIRSLQSTFQLrCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQR 665
Cdd:pfam15921 731 --------GMQKQITAKRGQIDALQSKIQF-LEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERR 801
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1958683060 666 QEKELHNSQ----KQSLELTSDLSILQmtRKELENQmgSLKEQHLRDEADLK 713
Cdd:pfam15921 802 LKEKVANMEvaldKASLQFAECQDIIQ--RQEQESV--RLKLQHTLDVKELQ 849
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-760 |
1.77e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 197 QEASDTSWQALIDEDRLLSRLEVMGNQLQacsknqtedSLRKELVALQEDKHSYETTAKESLRRVLQEKI---EVVRKLS 273
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIE---------EERKRRDKLTEEYAELKEELEDLRAELEEVDKefaETRDELK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 274 EVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKE 353
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 354 QElqakIEALQADNDFTNERLTALQVRLEPL----------------QEKTLKE--------CSSLG------------- 396
Cdd:TIGR02169 469 QE----LYDLKEEYDRVEKELSKLQRELAEAeaqaraseervrggraVEEVLKAsiqgvhgtVAQLGsvgeryataieva 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 397 -------IQVDD--------------------FLPkINGSTEKERLLSKS--GGDCTFIHQFIECQKKL-----MVQGHl 442
Cdd:TIGR02169 545 agnrlnnVVVEDdavakeaiellkrrkagratFLP-LNKMRDERRDLSILseDGVIGFAVDLVEFDPKYepafkYVFGD- 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 443 TKVVEESKLSKENQAKAKESDLS-DTLSPS--------KEKSSDDTTDAQMDE-QDLNEPLAKVSLLKALLEEERKAYRN 512
Cdd:TIGR02169 623 TLVVEDIEAARRLMGKYRMVTLEgELFEKSgamtggsrAPRGGILFSRSEPAElQRLRERLEGLKRELSSLQSELRRIEN 702
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 513 QVEESAKQIQVLQVQLQRLHMDMENLQEEKDT---EISSTRDKLLSAQDEILllhqaaakavserdtdfmSLQEELKKVR 589
Cdd:TIGR02169 703 RLDELSQELSDASRKIGEIEKEIEQLEQEEEKlkeRLEELEEDLSSLEQEIE------------------NVKSELKELE 764
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 590 AELEGWRKAASEYEEEIRSL----------QSTFQLRCQQCEVQQREEATR-LQGELEKLKKEWDVLENECRSLKKENVL 658
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLearlshsripEIQAELSKLEEEVSRIEARLReIEQKLNRLTLEKEYLEKEIQELQEQRID 844
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 659 LSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADlktlLSKAENQAKDVQKEYEKTQTVLS 738
Cdd:TIGR02169 845 LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ----LRELERKIEELEAQIEKKRKRLS 920
|
650 660
....*....|....*....|..
gi 1958683060 739 ELKLKFEMTEQEKQSITDELKQ 760
Cdd:TIGR02169 921 ELKAKLEALEEELSEIEDPKGE 942
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
298-771 |
2.02e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.21 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 298 EELRELANKYNGAVNEIkdLSDKLKAAEGKQEEIQQKgqaEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTAL 377
Cdd:PRK02224 165 EEYRERASDARLGVERV--LSDQRGSLDQLKAQIEEK---EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 378 QVRLEPlQEKTLKECSSLGIQVDDFLPKINGsTEKERLlsksggdcTFIHQFIEcqkklmvqghLTKVVEEskLSKENQA 457
Cdd:PRK02224 240 DEVLEE-HEERREELETLEAEIEDLRETIAE-TERERE--------ELAEEVRD----------LRERLEE--LEEERDD 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 458 KAKESDLSDtlsPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMEN 537
Cdd:PRK02224 298 LLAEAGLDD---ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 538 LQEekdtEISSTRDKLLSAQDEIlllhQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTF---- 613
Cdd:PRK02224 375 ARE----AVEDRREEIEELEEEI----EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVeeae 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 614 QLR----CQQCE------------VQQREEATRLQGELEKLKKEWDVLENECRSLKKenvllSSELQRQEKELHNSQKQS 677
Cdd:PRK02224 447 ALLeagkCPECGqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAED-----LVEAEDRIERLEERREDL 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 678 LELTSDlsilqmTRKELENQmgSLKEQHLRDEA-DLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS--- 753
Cdd:PRK02224 522 EELIAE------RRETIEEK--RERAEELRERAaELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESler 593
|
490 500
....*....|....*....|.
gi 1958683060 754 ---ITDELKQCKDNLKLLREK 771
Cdd:PRK02224 594 irtLLAAIADAEDEIERLREK 614
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
163-771 |
2.54e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSlrKELVA 242
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL--EELEA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 243 LQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKY-NGAVNEIKDLSDKL 321
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEEL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 322 KAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQAdndftneRLTALQVRLEPLQEktlkecsslgiqvdd 401
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA-------RLDSLERLQENLEG--------------- 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 402 flpkiNGSTEKERLLSKSGGDCTF--IHQFIECQKKLmvqghltkvveesklskenqAKAKESDLSDTLspskEKSSDDT 479
Cdd:TIGR02168 504 -----FSEGVKALLKNQSGLSGILgvLSELISVDEGY--------------------EAAIEAALGGRL----QAVVVEN 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 480 TDAQMDEQDLnepLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDe 559
Cdd:TIGR02168 555 LNAAKKAIAF---LKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDD- 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 560 illLHQAAAKAVSER-DTDFMSLQEELKKVRAELEGWRKAAS----EYEEEIRSLQstfqlrcQQCEVQQrEEATRLQGE 634
Cdd:TIGR02168 631 ---LDNALELAKKLRpGYRIVTLDGDLVRPGGVITGGSAKTNssilERRREIEELE-------EKIEELE-EKIAELEKA 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 635 LEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQ---------- 704
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERleeaeeelae 779
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683060 705 HLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 771
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
500-771 |
3.13e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 500 KALLEEERKAyrnQVEESAKQIQVLQVQLQRLHMDMENLQEEKDtEISSTRDKLLSAQDEIL-LLHQAAAKAVSERDTDF 578
Cdd:TIGR02169 214 QALLKEKREY---EGYELLKEKEALERQKEAIERQLASLEEELE-KLTEEISELEKRLEEIEqLLEELNKKIKDLGEEEQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 579 MSLQEELKKVRAELEGWRKAASEYEEEIRSLQStfqlRCQQCEVQ---QREEATRLQGELEKLKKEWDVLENECRSLKKE 655
Cdd:TIGR02169 290 LRVKEKIGELEAEIASLERSIAEKERELEDAEE----RLAKLEAEidkLLAEIEELEREIEEERKRRDKLTEEYAELKEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 656 NVLLSSELQRQEKEL------HNSQKQSLE-LTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTLLSK---AENQAKD 725
Cdd:TIGR02169 366 LEDLRAELEEVDKEFaetrdeLKDYREKLEkLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKineLEEEKED 445
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1958683060 726 VQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 771
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| CC1_T3JAM |
cd21912 |
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ... |
164-204 |
6.55e-09 |
|
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; TRAF3-interacting JNK-activating modulator (T3JAM), also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. The model corresponds to a conserved region that shows high sequence similarity with the first CC (CC1) domain of Sarcolemmal membrane-associated protein (SLMAP), which is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409288 [Multi-domain] Cd Length: 45 Bit Score: 52.35 E-value: 6.55e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1958683060 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21912 5 EILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
162-387 |
7.85e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 7.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 162 SQELFQLSQY--LQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQacsknQTEDSLRKE 239
Cdd:TIGR02169 664 GGILFSRSEPaeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE-----QEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 240 LVALQEDKHSYE---TTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHlremnertqEELRELANKYNGAVNEIKD 316
Cdd:TIGR02169 739 LEELEEDLSSLEqeiENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH---------SRIPEIQAELSKLEEEVSR 809
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958683060 317 LSDKLKAAEGKQEEIQQKGQ---AEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEK 387
Cdd:TIGR02169 810 IEARLREIEQKLNRLTLEKEyleKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
450-770 |
9.80e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 9.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 450 KLSKENQAKAKESDLSDTLSP------SKEKSSDDTTDAQMDEQ--DLNEPLAKVSLLKALLEEERKAYRNQVEE-SAKQ 520
Cdd:TIGR02169 202 RLRREREKAERYQALLKEKREyegyelLKEKEALERQKEAIERQlaSLEEELEKLTEEISELEKRLEEIEQLLEElNKKI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 521 IQVLQVQLQRLHMDMENLQeekdTEISSTRDKLLSAQDEILLLHQAAAKAVSERDtdfmSLQEELKKVRAELEGWRKAAS 600
Cdd:TIGR02169 282 KDLGEEEQLRVKEKIGELE----AEIASLERSIAEKERELEDAEERLAKLEAEID----KLLAEIEELEREIEEERKRRD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 601 EYEEEIRSLQSTFQLRCQQCEvQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELhnsqkqsLEL 680
Cdd:TIGR02169 354 KLTEEYAELKEELEDLRAELE-EVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL-------ADL 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 681 TSDLSILQMTRKELENQMGSLKEQHLRDEADLKTL---LSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDE 757
Cdd:TIGR02169 426 NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLaadLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
330
....*....|...
gi 1958683060 758 LKQCKDNLKLLRE 770
Cdd:TIGR02169 506 VRGGRAVEEVLKA 518
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
14-110 |
1.70e-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: 53.00 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 14 SHPFQERHV---YLDEPIKIGRSvARCRPAQNNATfdckvLSRNHALVW---FDHKT-SKFYLQDTkSSNGTFINSQRLS 86
Cdd:cd22670 7 SSPGSTDIVlpiYKNQVITIGRS-PSCDIVINDPF-----VSRTHCRIYsvqFDESSaPLVYVEDL-SSNGTYLNGKLIG 79
|
90 100
....*....|....*....|....*
gi 1958683060 87 RGseespPCEILS-GDIIQFGVDVT 110
Cdd:cd22670 80 RN-----NTVLLSdGDVIEIAHSAT 99
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
539-771 |
2.36e-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: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 539 QEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDtdfmSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQL--- 615
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELE----ELEAELAELEAELEELRLELEELELELEEAQAEEYElla 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 616 ---RCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRK 692
Cdd:COG1196 296 elaRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 693 ELENQMGSLKEQHL---RDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLR 769
Cdd:COG1196 376 EAEEELEELAEELLealRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
..
gi 1958683060 770 EK 771
Cdd:COG1196 456 EE 457
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
236-753 |
2.90e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 236 LRKELVALQEDKHSY---ETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDEcthlREMNERTQEELRELANKYNGAVN 312
Cdd:PRK03918 170 VIKEIKRRIERLEKFikrTENIEELIKEKEKELEEVLREINEISSELPELREE----LEKLEKEVKELEELKEEIEELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 313 EIKDLSDKLKAAEGKQEEIQQKgqaeKKELQAKIDDMEEKE---QELQAKIEALQADNDFTNERLTALQVrleplQEKTL 389
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEER----IEELKKEIEELEEKVkelKELKEKAEEYIKLSEFYEEYLDELRE-----IEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 390 KECSSLGIQVDDFLPKINGSTEKERLLSKsggdctfihQFIECQKKLMVQGHLTKVVEESKLSKEN--QAKAKESDLsdt 467
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERLEELKK---------KLKELEKRLEELEERHELYEEAKAKKEEleRLKKRLTGL--- 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 468 lspSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQRL-HMDMENLQEEKDTEI 546
Cdd:PRK03918 385 ---TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELtEEHRKELLEEYTAEL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 547 SSTRDKLLSAQDEilllhqaaakavsERDtdfmsLQEELKKVRAELEGWRKAASEYE--EEIRSLQSTFQLRCQQCEVQQ 624
Cdd:PRK03918 462 KRIEKELKEIEEK-------------ERK-----LRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKK 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 625 REEATRLQGELEKLKKEWDVLENECRS---LKKENVLLSSELQRQEKELHNSQKQSLELT-SDLSILQMTRKELE---NQ 697
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKELEKleeLKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEpfyNE 603
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958683060 698 MGSLK--EQHLRDE----ADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 753
Cdd:PRK03918 604 YLELKdaEKELEREekelKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR 665
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
28-85 |
4.84e-08 |
|
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.
Pssm-ID: 214578 [Multi-domain] Cd Length: 52 Bit Score: 49.87 E-value: 4.84e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683060 28 IKIGRSvarcrPAQNNATFDCKVLSRNHALVWFDhKTSKFYLQDTKSSNGTFINSQRL 85
Cdd:smart00240 1 VTIGRS-----SEDCDIQLDGPSISRRHAVIVYD-GGGRFYLIDLGSTNGTFVNGKRI 52
|
|
| FHA_TCF19 |
cd22685 |
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ... |
29-119 |
5.85e-08 |
|
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar proteins; TCF-19, also called transcription factor SC1, was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It also functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. TCF-19 contains an N-terminal fork head association domain (FHA), a proline rich region, and a C-terminal plant homeodomain (PHD) finger. The FHA domain may serve as a nuclear signaling domain or as a phosphoprotein binding domain. The proline rich region is a common characteristic of trans-activating factors. The PHD finger may allow TCF-19 to interact with chromatin via methylated histone H3.
Pssm-ID: 438737 [Multi-domain] Cd Length: 130 Bit Score: 52.03 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 29 KIGRSVARCRPAQNNATFDcKVLSRNHALVWFDHKTS---KFYLQDTkSSNGTFINSQRLSRGSEEsppcEILSGDIIQF 105
Cdd:cd22685 31 RIGRNPEVCDVFLCSSQHP-NLISREHAEIHAERDGNgnwKVLIEDR-STNGTYVNDVRLQDGQRR----ELSDGDTITF 104
|
90
....*....|....*.
gi 1958683060 106 G--VDVTENTRKVTHG 119
Cdd:cd22685 105 GhkNGRRVKQWPYQKS 120
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
336-676 |
6.12e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 6.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 336 QAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQektlKECSSLGIQVDDFLPKINGSTEKERL 415
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS----RQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 416 LSKSggdctfihqfiecQKKLMVQghltKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTT-------DAQMDEQD 488
Cdd:TIGR02168 752 LSKE-------------LTELEAE----IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalrealdELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 489 LNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDtEISSTRDKLLsaqdeilllhqaaa 568
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE-ELESELEALL-------------- 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 569 KAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQ---STFQLRCQQCEVqqreeatRLQGELEKLKKEWDVL 645
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESKRSELRRELEELReklAQLELRLEGLEV-------RIDNLQERLSEEYSLT 952
|
330 340 350
....*....|....*....|....*....|.
gi 1958683060 646 ENECRSLKKENVLLSSELQRQEKELHNSQKQ 676
Cdd:TIGR02168 953 LEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
255-770 |
6.87e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 6.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 255 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNgAVNEIKDLSDKLKAAEGKQEEIQQK 334
Cdd:PRK03918 178 IERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 335 GQAEKKELQAKIDDMEEKEQELQAKIEALQadndfTNERLTALQVRLEPLQEKTLKECSSLGIQVDDFLPKINGSTEK-E 413
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKELK-----ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERiK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 414 RLLSKSGGDCTFIHQFIECQKKLMVQGHLTKVVEESKLSKEN--QAKAKESDLSdtlspsKEKSSDDTTDAQMDEQDLNE 491
Cdd:PRK03918 332 ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEleRLKKRLTGLT------PEKLEKELEELEKAKEEIEE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 492 PLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQRL-HMDMENLQEEKDTEISSTRDKLLSAQDEilllhqaaaka 570
Cdd:PRK03918 406 EISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELtEEHRKELLEEYTAELKRIEKELKEIEEK----------- 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 571 vsERDtdfmsLQEELKKVRAELEGWRKAASEYE--EEIRSLQSTFQLRCQQCEVQQREEATRLQGELEKLKKEWDVLENE 648
Cdd:PRK03918 475 --ERK-----LRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 649 CRS---LKKENVLLSSELQRQEKELHNSQKQSLELT-SDLSILQMTRKELE---NQMGSLK--EQHLRDE----ADLKTL 715
Cdd:PRK03918 548 LEKleeLKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEpfyNEYLELKdaEKELEREekelKKLEEE 627
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958683060 716 LSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEK-------------------QSITDELKQCKDNLKLLRE 770
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEElreeylelsrelaglraelEELEKRREEIKKTLEKLKE 701
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
161-770 |
2.08e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 54.74 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 161 YSQELFQLSQYLQEA--LHREQ--MLEQKLATLQRLLAITQEASDtswqALIDedrlLSRLEvmgNQLQACSKNQTEDSL 236
Cdd:pfam15921 83 YSHQVKDLQRRLNESneLHEKQkfYLRQSVIDLQTKLQEMQMERD----AMAD----IRRRE---SQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 237 RKELVA--LQEDKHSYETTAKESLRR-------VLQEKIEVVRKLSEVERSLSNTEDECT--HLREMNERTQEELRELAN 305
Cdd:pfam15921 152 HELEAAkcLKEDMLEDSNTQIEQLRKmmlshegVLQEIRSILVDFEEASGKKIYEHDSMStmHFRSLGSAISKILRELDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 306 kyngavnEIKDLSDKLKAAEGKQEEIQQKGQAEKKEL-QAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPL 384
Cdd:pfam15921 232 -------EISYLKGRIFPVEDQLEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEII 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 385 QEKTLKECSSLGIQVDDFLPKINGSTEKERLLSKsggdcTFIHQFIECQKKL-MVQGHLTKV-VEESKLSKE--NQAKAK 460
Cdd:pfam15921 305 QEQARNQNSMYMRQLSDLESTVSQLRSELREAKR-----MYEDKIEELEKQLvLANSELTEArTERDQFSQEsgNLDDQL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 461 ESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALleEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQE 540
Cdd:pfam15921 380 QKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRREL--DDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKN 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 541 EKDTEISSTRDKLLSAQDEIlllhqaaAKAVSERDTDFMSLQEELKKVR---AELEGWRKAASEYEEEIRSLQSTFQLRC 617
Cdd:pfam15921 458 ESLEKVSSLTAQLESTKEML-------RKVVEELTAKKMTLESSERTVSdltASLQEKERAIEATNAEITKLRSRVDLKL 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 618 QqcevqqreeatrlqgELEKLKKEWDVLEN---ECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKEL 694
Cdd:pfam15921 531 Q---------------ELQHLKNEGDHLRNvqtECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQL 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 695 ENQMG----SLKE-QHLRDEADLKtlLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLR 769
Cdd:pfam15921 596 EKEINdrrlELQEfKILKDKKDAK--IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLS 673
|
.
gi 1958683060 770 E 770
Cdd:pfam15921 674 E 674
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
267-771 |
2.80e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.26 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 267 EVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKI 346
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 347 DDMEEKEQE---LQAKIEALQADNDFTNERLTALQVRLEPLQEK---TLKECSSLGIQVDDFLPKINgstEKERLLSKSG 420
Cdd:TIGR04523 117 EQKNKLEVElnkLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKyndLKKQKEELENELNLLEKEKL---NIQKNIDKIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 421 gdctfiHQFIECQKKLMVqghLTKVVEESKL--SKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSL 498
Cdd:TIGR04523 194 ------NKLLKLELLLSN---LKKKIQKNKSleSQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 499 LKALLEEERKayrnQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDEILllhQAAAKAVSERDTDF 578
Cdd:TIGR04523 265 IKKQLSEKQK----ELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKL---EEIQNQISQNNKII 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 579 MSLQEELKKVRAELEGWRKAASEYEEEIRSLQstfqlrcQQCEVQQREEATRLQgELEKLKKEWDVLENECRSLKKENVL 658
Cdd:TIGR04523 338 SQLNEQISQLKKELTNSESENSEKQRELEEKQ-------NEIEKLKKENQSYKQ-EIKNLESQINDLESKIQNQEKLNQQ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 659 LSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHlrdeADLKTLLSKAENQAKDVQKEYEKTQTVLS 738
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELII----KNLDNTRESLETQLKVLSRSINKIKQNLE 485
|
490 500 510
....*....|....*....|....*....|...
gi 1958683060 739 ELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 771
Cdd:TIGR04523 486 QKQKELKSKEKELKKLNEEKKELEEKVKDLTKK 518
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
228-695 |
3.09e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 228 SKNQTEDSLRKELVALQEDKHSYETTA------KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQE--- 298
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKELEELKeeieelEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElke 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 299 ------ELRELANKYNGAVNEIKDLSDKLKA-AEGKQEEIQQkgqAEKKElqAKIDDMEEKEQELQAKIEALQADNDfTN 371
Cdd:PRK03918 291 kaeeyiKLSEFYEEYLDELREIEKRLSRLEEeINGIEERIKE---LEEKE--ERLEELKKKLKELEKRLEELEERHE-LY 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 372 ERLTALQVRLEPLQ-----------EKTLKECSSLGIQVDDFLPKING-----STEKERL------LSKSGGDCTFIHQF 429
Cdd:PRK03918 365 EEAKAKKEELERLKkrltgltpeklEKELEELEKAKEEIEEEISKITArigelKKEIKELkkaieeLKKAKGKCPVCGRE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 430 I--ECQKKLMVQGH--LTKVVEESK--LSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEqdLNEPLAKVSLLKalL 503
Cdd:PRK03918 445 LteEHRKELLEEYTaeLKRIEKELKeiEEKERKLRKELRELEKVLKKESELIKLKELAEQLKE--LEEKLKKYNLEE--L 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 504 EEERKAYRNQVEESAKQIQVLQVQLQRLHM--DMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERdtdfmsl 581
Cdd:PRK03918 521 EKKAEEYEKLKEKLIKLKGEIKSLKKELEKleELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEER------- 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 582 QEELKKVRAELEGWRKAASEYEEEIRSLQStfqlrCQQCEVQQREEATRLQGELEKLKKEWDVL-----ENECRSLKKEN 656
Cdd:PRK03918 594 LKELEPFYNEYLELKDAEKELEREEKELKK-----LEEELDKAFEELAETEKRLEELRKELEELekkysEEEYEELREEY 668
|
490 500 510
....*....|....*....|....*....|....*....
gi 1958683060 657 VLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELE 695
Cdd:PRK03918 669 LELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
271-745 |
3.87e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.03 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 271 KLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAvneIKDLSDKLKaaegKQEEIQQKGQAEKKELQAKIDDME 350
Cdd:pfam01576 149 KLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAM---ISDLEERLK----KEEKGRQELEKAKRKLEGESTDLQ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 351 EKEQELQAKIEALQADNDFTNERLTALQVRLEplqektlKECSslgiqvddflpkingstekerllsksggdctfihQFI 430
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAKKEEELQAALARLE-------EETA----------------------------------QKN 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 431 ECQKKLM-VQGHLTKVVE--ESKLSKENQAKAKESDLSDTLSPSKEKSSD--DTTDAQMDEQDLNEplAKVSLLKALLEE 505
Cdd:pfam01576 261 NALKKIReLEAQISELQEdlESERAARNKAEKQRRDLGEELEALKTELEDtlDTTAAQQELRSKRE--QEVTELKKALEE 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 506 ERKAYRNQVEESAKQIQVLqvqlqrlhmdMENLQEEKDteiSSTRDKllsaqdeilllhQAAAKAVSERDTDFMSLQEEL 585
Cdd:pfam01576 339 ETRSHEAQLQEMRQKHTQA----------LEELTEQLE---QAKRNK------------ANLEKAKQALESENAELQAEL 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 586 KKV---RAELEGWRKAASEYEEEirslqstFQLRCQQCEVQQREEA---TRLQGELEKLKKEWDVLENECRSLKKENVLL 659
Cdd:pfam01576 394 RTLqqaKQDSEHKRKKLEGQLQE-------LQARLSESERQRAELAeklSKLQSELESVSSLLNEAEGKNIKLSKDVSSL 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 660 SSELQRQEKELHNSQKQSLELTSDLsilqmtrKELENQMGSLKEQhlrdeadlktlLSKAENQAKDVQKEYEKTQTVLSE 739
Cdd:pfam01576 467 ESQLQDTQELLQEETRQKLNLSTRL-------RQLEDERNSLQEQ-----------LEEEEEAKRNVERQLSTLQAQLSD 528
|
....*.
gi 1958683060 740 LKLKFE 745
Cdd:pfam01576 529 MKKKLE 534
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
211-615 |
4.29e-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: 53.91 E-value: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 211 DRLLSRLEVMGNQLQACSKNQTEdsLRKELVALQEDkhsyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLR 290
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAE--LRKELEELEEE-----------LEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 291 EMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEgkqeeiqqkgqAEKKELQAKIDDMEEKEQELQAKIEALQADNDFT 370
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAE-----------AEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 371 NERLTALQVRLEPLQektlKECSSLGIQVDDFLPKINGSTEKERLLSksggdctfiHQFIECQKKLMVQGHLTKVVEESK 450
Cdd:TIGR02168 816 NEEAANLRERLESLE----RRIAATERRLEDLEEQIEELSEDIESLA---------AEIEELEELIEELESELEALLNER 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 451 LSKENQAKAKESDLsDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQvlqvqlqr 530
Cdd:TIGR02168 883 ASLEEALALLRSEL-EELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL-------- 953
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 531 lhMDMENLQEEKDTEISSTRDKLLSAQDEIL------LLHQAAAKAVSERdTDFMSLQ-EELKKVRAELEgwrKAASEYE 603
Cdd:TIGR02168 954 --EEAEALENKIEDDEEEARRRLKRLENKIKelgpvnLAAIEEYEELKER-YDFLTAQkEDLTEAKETLE---EAIEEID 1027
|
410
....*....|...
gi 1958683060 604 EEIRS-LQSTFQL 615
Cdd:TIGR02168 1028 REARErFKDTFDQ 1040
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
27-106 |
7.82e-07 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 (FKH1), 2 (FKH2) and similar proteins; This family includes FKH1 and FKH2, as well as pre-rRNA-processing protein FHL1. FKH1 and FKH2 are forkhead transcription factors that regulate the expression of the CLB2 cluster of genes during the G2/M phase of the mitotic cell cycle. The CLB2 cluster of genes includes mitotic regulators such as CLB1, CLB2, CDC5 and CDC20, as well as SWI5 and ACE2. FKH1 and FKH2 are involved in HMRa silencing. They associate with the coding regions of active genes and influence, in opposing ways, transcriptional elongation and termination, and coordinate early transcription elongation and pre-mRNA processing. Both FKH1 and FKH2 play a role as regulators of lifespan in collaboration with the anaphase-promoting complex (APC), likely through combined regulation of stress response, genomic stability, and cell cycle regulation. They also function in controlling yeast cell morphology by preventing pseudohyphal growth and act as rate-limiting replication origin activators via their interaction with the origin recognition complex (ORC). FHL1 is a forkhead protein that controls the pre-rRNA processing machinery in conjunction with IFH1. It might act as a transcriptional regulator of genes specifically involved in that process. IFH1 convert FHL1 from a repressor to an activator. This family also includes AtFHA1 and AtFHA2, which may play a role in the control of plant organ development. AtFHA2 is specifically involved in the regulation of stamen development. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438753 [Multi-domain] Cd Length: 106 Bit Score: 48.00 E-value: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 27 PIKIGRSVARcRPAQNNATFDC-----KVLSRNHALVWFDHKTSKFYLQdTKSSNGTFINSQRLSRGseeSPPCEILSGD 101
Cdd:cd22701 18 EVVLGRNSKN-SSSTAADSVDIdlgpsKKISRRHARIFYDFTTQCFELS-VLGRNGVKVDGILVKPG---SPPVPLRSGS 92
|
....*
gi 1958683060 102 IIQFG 106
Cdd:cd22701 93 LIQIG 97
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
235-763 |
1.25e-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: 51.94 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 235 SLRKELVALQEDKHSYETTAKE--SLRRVLQEKIEVVRKLSEVERSLsntEDECTHLREMNERTQEELRELANKYNGAVN 312
Cdd:TIGR04523 170 ELENELNLLEKEKLNIQKNIDKikNKLLKLELLLSNLKKKIQKNKSL---ESQISELKKQNNQLKDNIEKKQQEINEKTT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 313 EIKDLSDKLKAAEGKQEEIQQKGQAEKKELQ---AKIDDMEEKEQELQAKIEAL--QADNDFTNERLTALQVrleplQEK 387
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQNKIKKQLSEKQKELEqnnKKIKELEKQLNQLKSEISDLnnQKEQDWNKELKSELKN-----QEK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 388 TLKECSSlgiQVDDFLPKINGSTEKERLLSKSGGDCTFIHQFIECQKKlmvqghlTKVVEESKLSKENQAKAKEsdlSDT 467
Cdd:TIGR04523 322 KLEEIQN---QISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE-------EKQNEIEKLKKENQSYKQE---IKN 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 468 LSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQvlqvqlqrlhmDMENLQEEKDTEIS 547
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK-----------DLTNQDSVKELIIK 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 548 STRDKLLSAQDEILLLhqaaAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLqstfqlrcqqceVQQREE 627
Cdd:TIGR04523 458 NLDNTRESLETQLKVL----SRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL------------TKKISS 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 628 ATRLQGELEKLKKEwdvLENECRSLKKENVLLSSELQRQ--EKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQ- 704
Cdd:TIGR04523 522 LKEKIEKLESEKKE---KESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEk 598
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958683060 705 -HLRDEADLKT-LLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKD 763
Cdd:TIGR04523 599 kDLIKEIEEKEkKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
499-760 |
1.41e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 499 LKALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTdf 578
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR-- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 579 msLQEELKKVRAELEGWRKAASEYEEEIRSLQSTfqlrcQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVL 658
Cdd:COG1196 300 --LEQDIARLEERRRELEERLEELEEELAELEEE-----LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 659 LSSELQRQE----KELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQ 734
Cdd:COG1196 373 ELAEAEEELeelaEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260
....*....|....*....|....*.
gi 1958683060 735 TVLSELKLKFEMTEQEKQSITDELKQ 760
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAA 478
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
26-106 |
1.96e-06 |
|
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438750 [Multi-domain] Cd Length: 93 Bit Score: 46.64 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 26 EPIKIGRSVArcrpaqNNATFDCKVLSRNHALVwfDHKTSKFYLQDTKSSNGTFINSQRLSRGseesppcEILSGDIIQF 105
Cdd:cd22698 21 DEFTIGRSSN------NDIRLNDHSVSRHHARI--VRQGDKCNLTDLGSTNGTFLNGIRVGTH-------ELKHGDRIQL 85
|
.
gi 1958683060 106 G 106
Cdd:cd22698 86 G 86
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
27-117 |
2.06e-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: 46.97 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 27 PIKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLsrgSEESPPCEILSGDIIQFG 106
Cdd:cd22678 24 PLTIGRIQ------RGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESI---SPNGRPVVLSSGDVITLG 94
|
90
....*....|.
gi 1958683060 107 vdvTENTRKVT 117
Cdd:cd22678 95 ---SETKILVR 102
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
25-114 |
2.35e-06 |
|
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: 46.97 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 25 DEPIKIGRSVArcrpAQNNATFDC-KVLSRNHALVWFDHKTSKFyLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDII 103
Cdd:cd22663 20 GKEVTVGRGLG----VTYQLVSTCpLMISRNHCVLKKNDEGQWT-IKDNKSLNGVWVNGERI----EPLKPYPLNEGDLI 90
|
90
....*....|.
gi 1958683060 104 QFGVDVTENTR 114
Cdd:cd22663 91 QLGVPPENKEP 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
578-771 |
2.95e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 578 FMSLQEELKKVRAELegWRKAASEYEEEIRSLQSTFQLRCQQCEVQQREEATrLQGELEKLKKEWDVLENECRSLKKENV 657
Cdd:COG1196 215 YRELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAE-LEAELEELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 658 LLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQhlrdEADLKTLLSKAENQAKDVQKEYEKTQTVL 737
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE----LEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190
....*....|....*....|....*....|....
gi 1958683060 738 SELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 771
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
231-770 |
3.27e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 231 QTEDSLRKELVALQEDKHsyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGA 310
Cdd:COG1196 219 KEELKELEAELLLLKLRE-----LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 311 VNEIKDLSDKLKAAEGKQEEIQQkgqaEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEKTLK 390
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEE----RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 391 ECSSLGIQVDDFlpkingSTEKERLLSKsggdctfIHQFIECQKKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSP 470
Cdd:COG1196 370 AEAELAEAEEEL------EELAEELLEA-------LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 471 SKEKSSDDTTDAQMDEQDLNEPLAkvslLKALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTR 550
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEA----LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 551 DKLLSAQDEIL-LLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFqLRCQQCEVQQREEAT 629
Cdd:COG1196 513 ALLLAGLRGLAgAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATF-LPLDKIRARAALAAA 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 630 RLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRkELENQMGSLKEQHLRDE 709
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG-EGGSAGGSLTGGSRREL 670
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958683060 710 ADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 770
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
504-771 |
3.55e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.51 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 504 EEERKAY----RNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFM 579
Cdd:pfam17380 304 EKEEKAReverRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 580 SLQEELK--KVRAELEGWRKAASEYEEEIRSLQStfQLRCQQCEVQQREEATrlQGELEKLKKEwdvLENECRSLKKENV 657
Cdd:pfam17380 384 QMERQQKneRVRQELEAARKVKILEEERQRKIQQ--QKVEMEQIRAEQEEAR--QREVRRLEEE---RAREMERVRLEEQ 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 658 LLSSELQRQEKELHNSQKQSLELTSDlsilQMTRKELENQMGSLKEQHLRDEadlKTLLSKAENQAKDVQKEYEKTQTVL 737
Cdd:pfam17380 457 ERQQQVERLRQQEEERKRKKLELEKE----KRDRKRAEEQRRKILEKELEER---KQAMIEEERKRKLLEKEMEERQKAI 529
|
250 260 270
....*....|....*....|....*....|....*
gi 1958683060 738 SELKLKFEMTEQ-EKQSITDELKQCKDNLKLLREK 771
Cdd:pfam17380 530 YEEERRREAEEErRKQQEMEERRRIQEQMRKATEE 564
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
581-771 |
3.56e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 581 LQEELKKVRAELEGWRKAASEYeeeiRSLQSTFQLRCQQCEVQQREEatrLQGELEKLKKEWDVLENECRSLKKENVLLS 660
Cdd:COG1196 194 ILGELERQLEPLERQAEKAERY----RELKEELKELEAELLLLKLRE---LEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 661 SELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTLlskaENQAKDVQKEYEKTQTVLSEL 740
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL----EEELAELEEELEELEEELEEL 342
|
170 180 190
....*....|....*....|....*....|.
gi 1958683060 741 KLKFEMTEQEKQSITDELKQCKDNLKLLREK 771
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
55-108 |
3.58e-06 |
|
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) family; The Cep170 family includes Cep170 and Cep170B. Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438756 [Multi-domain] Cd Length: 102 Bit Score: 46.16 E-value: 3.58e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1958683060 55 HALVWFDHKTSKFYLQDTKSSNGTFINSQRLSrgseESPPCEILSGDIIQFGVD 108
Cdd:cd22704 39 HAVITYDQIDNEFKIKDLGSLNGTFVNDSRIP----EQTYITLKLGDSIRFGYD 88
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
178-365 |
4.51e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 178 REQML--EQKLATLQRLLAITQEAsDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKELVALQEDKhsyetTAK 255
Cdd:COG4913 241 HEALEdaREQIELLEPIRELAERY-AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAEL-----ERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 256 ESLRRVLQEKIEVVR---------KLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEG 326
Cdd:COG4913 315 EARLDALREELDELEaqirgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE 394
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958683060 327 KQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQA 365
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
153-388 |
5.70e-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: 49.38 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 153 VAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgNQLQAcsKNQT 232
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE---QELAA--LEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 233 EDSLRKELVALQEDKHSYETTAKESLRRV----LQEKIEVV---RKLSEVERSLSNTEDECTHLREMNERTQEELRELAN 305
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRALyrlgRQPPLALLlspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 306 KyngaVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQ 385
Cdd:COG4942 165 L----RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
...
gi 1958683060 386 EKT 388
Cdd:COG4942 241 ERT 243
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-643 |
9.24e-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: 49.28 E-value: 9.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 263 QEKIEVVRKLSEVERSLSNTEDEcthLREMnERTQEELR---ELANKYNGAVNEIKDLSDKLKAAEGKQEEiqqkgqAEK 339
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDI---LNEL-ERQLKSLErqaEKAERYKELKAELRELELALLVLRLEELR------EEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 340 KELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEKTLkecsSLGIQVDDFLPKINGSTEKERLLSks 419
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY----ALANEISRLEQQKQILRERLANLE-- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 420 ggdctfihqfiecQKKLMVQGHLTKVveESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEplaKVSLL 499
Cdd:TIGR02168 316 -------------RQLEELEAQLEEL--ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES---RLEEL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 500 KALLEEERKAY---RNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISS-TRDKLLSAQDEILLLHQAAAKAVSERD 575
Cdd:TIGR02168 378 EEQLETLRSKVaqlELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELE 457
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683060 576 TdfmsLQEELKKVRAELEGWRKAASEYEEEIRSLQStfqlRCQQCEVQQREEATRLQGELEKLKKEWD 643
Cdd:TIGR02168 458 R----LEEALEELREELEEAEQALDAAERELAQLQA----RLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
162-749 |
1.35e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 48.66 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 162 SQELFQLSQYLQEALHR----EQMLEQKLATLQRLLAITQEASDTSWQALIDEDRllsRLEVMGNQLQACSKNQTEDSLR 237
Cdd:pfam10174 129 AKELFLLRKTLEEMELRietqKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWER---TRRIAEAEMQLGHLEVLLDQKE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 238 KELVALQEDKHS-YETTAKESLRRVLQEKIEVV-RKLSEVERSLSNTEDECTHLREMNERTQEELRELANKyngaVNEIK 315
Cdd:pfam10174 206 KENIHLREELHRrNQLQPDPAKTKALQTVIEMKdTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQ----MEVYK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 316 DLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQadndftnERLTALQVRLEPLQektlKECSSL 395
Cdd:pfam10174 282 SHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLK-------ESLTAKEQRAAILQ----TEVDAL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 396 GIQVDdflpkingstEKERLLSKSGgdcTFIHQFIECQKKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSpSKEKS 475
Cdd:pfam10174 351 RLRLE----------EKESFLNKKT---KQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLR-DKDKQ 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 476 SDDTTDA--QMDEQDLNEPLAKVSLLKALLEEERKAYRNQvEESAKQIQVLQVQLQRLHMDMENLQEEKDteiSSTRDKL 553
Cdd:pfam10174 417 LAGLKERvkSLQTDSSNTDTALTTLEEALSEKERIIERLK-EQREREDRERLEELESLKKENKDLKEKVS---ALQPELT 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 554 LSAQDEILLLHQAAAKAVS--ERDTDFMSLQEELKKVRAE---LEGWRKAASEYEEEIR-SLQSTFQLRCQQCEVQQ-RE 626
Cdd:pfam10174 493 EKESSLIDLKEHASSLASSglKKDSKLKSLEIAVEQKKEEcskLENQLKKAHNAEEAVRtNPEINDRIRLLEQEVARyKE 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 627 EATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQsleltsdlsiLQMTRKELENQMGSLKEQHL 706
Cdd:pfam10174 573 ESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVAN----------IKHGQQEMKKKGAQLLEEAR 642
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1958683060 707 RDEADLKTllSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQ 749
Cdd:pfam10174 643 RREDNLAD--NSQQLQLEELMGALEKTRQELDATKARLSSTQQ 683
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
234-655 |
1.40e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 234 DSLRKELVALQEDKHSYETtAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNER--TQEELRELANKYNGAV 311
Cdd:COG4717 74 KELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELeaLEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 312 NEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQ-------AKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPL 384
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEqlslateEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 385 QEKTLKECSSLGIQVDDFLPKINGStekerLLSKSGGDCTFIHQFIECQKKLMVQGHLTkVVEESKLSKENQAKAKESDL 464
Cdd:COG4717 233 ENELEAAALEERLKEARLLLLIAAA-----LLALLGLGGSLLSLILTIAGVLFLVLGLL-ALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 465 SDTLSPSKEkssddttdaqMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQRLhmDMENLQEEKDT 544
Cdd:COG4717 307 LQALPALEE----------LEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 545 EISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAEL-----EGWRKAASEYEEEIRSLQSTF-QLRCQ 618
Cdd:COG4717 375 LLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLealdeEELEEELEELEEELEELEEELeELREE 454
|
410 420 430
....*....|....*....|....*....|....*..
gi 1958683060 619 QCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKE 655
Cdd:COG4717 455 LAELEAELEQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
167-696 |
1.55e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 167 QLSQYLQEALHREQMLEQKLATLQRLLAitqeasdtswQALIDEDRLLSRLEVMGNQLQAcsKNQTEDSLRKELVALQED 246
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELE----------ELEEELEEAEEELEEAEAELAE--AEEALLEAEAELAEAEEE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 247 KHSyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEG 326
Cdd:COG1196 381 LEE----LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 327 KQEEIQQKGQAEKKE---LQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEKTLKECSSLGIQVDDFL 403
Cdd:COG1196 457 EEEALLELLAELLEEaalLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 404 PKINGSTEKERLLSKSGGDctfihqfiecqkklmvQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQ 483
Cdd:COG1196 537 EAALEAALAAALQNIVVED----------------DEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAA 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 484 MDEQDLN---EPLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTR-DKLLSAQDE 559
Cdd:COG1196 601 VDLVASDlreADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELlAALLEAEAE 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 560 ILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQcEVQQREEATRLQGELEKLK 639
Cdd:COG1196 681 LEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE-LLEEEELLEEEALEELPEP 759
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958683060 640 KEWDVLENECRSLKKE-------NVLLSSELQRQEKELHnsqkqslELTSDLSILQMTRKELEN 696
Cdd:COG1196 760 PDLEELERELERLEREiealgpvNLLAIEEYEELEERYD-------FLSEQREDLEEARETLEE 816
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
560-771 |
1.67e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 560 ILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQStfQLRCQQCEVQQRE-EATRLQGELEKL 638
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER--RIAALARRIRALEqELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 639 KKEWDVLENECRSLKKE-----------------NVLLSSE-LQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGS 700
Cdd:COG4942 89 EKEIAELRAELEAQKEElaellralyrlgrqpplALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958683060 701 LKEQHlrdeADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 771
Cdd:COG4942 169 LEAER----AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
52-106 |
2.13e-05 |
|
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 (PPP1R8) and similar proteins; PPP1R8, also called nuclear inhibitor of protein phosphatase 1 (NIPP-1), is an inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. It may also be involved in pre-mRNA splicing and binds DNA and might act as a transcriptional repressor. PPP1R8 seems to be required for cell proliferation. PPP1R8 contains an FHA domain that mediates interactions with threonine-phosphorylated maternal embryonic leucine zipper kinase (MELK). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438726 [Multi-domain] Cd Length: 108 Bit Score: 44.18 E-value: 2.13e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683060 52 SRNH-ALVWfdHK-TSKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22674 48 SRVHaALVY--HKhLNRVFLIDLGSTHGTFVGGIRL----EPHKPQQLPIDSTLRFG 98
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
229-732 |
2.13e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.12 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 229 KNQTEDSLRK---ELVALQEDKHSYettakeslRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELA- 304
Cdd:TIGR00606 586 INQTRDRLAKlnkELASLEQNKNHI--------NNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAm 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 305 -----NKYNGAVNEIKD-------LSDKLKAAEGKQEEIQQKGQA-------EKKELQAKIDDMEEKEQELQAKIEALQA 365
Cdd:TIGR00606 658 lagatAVYSQFITQLTDenqsccpVCQRVFQTEAELQEFISDLQSklrlapdKLKSTESELKKKEKRRDEMLGLAPGRQS 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 366 DNDFTNERLTALQVRLEPLQEKTLKECSSLGIQvDDFLPKINGSTEKERLLSKsggDCTFIHQFIECQKklmvqghltkv 445
Cdd:TIGR00606 738 IIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQ-ETLLGTIMPEEESAKVCLT---DVTIMERFQMELK----------- 802
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 446 vEESKLSKENQAKAKESDLSDTLSPSKEKSSDDttdaqmdEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQ 525
Cdd:TIGR00606 803 -DVERKIAQQAAKLQGSDLDRTVQQVNQEKQEK-------QHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKL 874
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 526 VQLQRLHM--DMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYE 603
Cdd:TIGR00606 875 QIGTNLQRrqQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIH 954
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 604 EEIRSLQSTFQLRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKenvllSSELQRQEKELHNSQKQSLELTSD 683
Cdd:TIGR00606 955 GYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQ-----DIDTQKIQERWLQDNLTLRKRENE 1029
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1958683060 684 LSILQMTRKELENQMG-----SLKEQHLRDEADLKtLLSKAENQAKDVQKEYEK 732
Cdd:TIGR00606 1030 LKEVEEELKQHLKEMGqmqvlQMKQEHQKLEENID-LIKRNHVLALGRQKGYEK 1082
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
276-771 |
2.20e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.25 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 276 ERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKA---------------AEGKQ------------ 328
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAetelcaeaeemrarlAARKQeleeilhelesr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 329 ----EEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVR---LEPLQEKTLKECSSLGIQVDD 401
Cdd:pfam01576 84 leeeEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDillLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 402 FLPKINGSTEKERLLSKsggdctfihqfiecqkklmvqghlTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTD 481
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSK------------------------LKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 482 AQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEiSSTRDKlLSAQDEIL 561
Cdd:pfam01576 220 LQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESE-RAARNK-AEKQRRDL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 562 LLHQAAAKAVSERDTDFMSLQEELKKVR-AELEGWRKAAseyEEEIRSLQSTFQlRCQQCEVQQREEatrLQGELEKLKK 640
Cdd:pfam01576 298 GEELEALKTELEDTLDTTAAQQELRSKReQEVTELKKAL---EEETRSHEAQLQ-EMRQKHTQALEE---LTEQLEQAKR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 641 EWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLK---TLLS 717
Cdd:pfam01576 371 NKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELEsvsSLLN 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1958683060 718 KAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 771
Cdd:pfam01576 451 EAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQ 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
162-593 |
2.44e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 162 SQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgNQLQAcsKNQTEDSLRKELV 241
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE---AELAE--AEEELEELAEELL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 242 ALQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKL 321
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 322 KAAEGKQEEIQQKGQAE---KKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEKTLKECSSLGIQ 398
Cdd:COG1196 470 EEAALLEAALAELLEELaeaAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 399 VDDFLPKINGSTEKERLLSKSGGDCTFI-------------------------------HQFIECQKKLMVQGHLTKVVE 447
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKAAKAGRATFLpldkiraraalaaalargaigaavdlvasdlREADARYYVLGDTLLGRTLVA 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 448 ESKLSKENQAKAKESDL------SDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQI 521
Cdd:COG1196 630 ARLEAALRRAVTLAGRLrevtleGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958683060 522 QVLQVQLQRLHMDMENLQEEKDTEisstRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELE 593
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAE----REELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
51-106 |
2.44e-05 |
|
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also called human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP), is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438729 [Multi-domain] Cd Length: 106 Bit Score: 44.08 E-value: 2.44e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683060 51 LSRNHALVWF----DHKTSKFYLQDTKSSNGTFINSQRLsrgseesPP---CEILSGDIIQFG 106
Cdd:cd22677 41 ISRYHAVLQYrgdaDDHDGGFYLYDLGSTHGTFLNKQRI-------PPkqyYRLRVGHVLKFG 96
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
258-387 |
2.64e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 258 LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQ----- 332
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkey 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1958683060 333 QKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEK 387
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
28-106 |
2.99e-05 |
|
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438732 [Multi-domain] Cd Length: 96 Bit Score: 43.48 E-value: 2.99e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683060 28 IKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDhkTSKFYLQDTKSSNGTFINSQRlsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22680 23 VSIGRDP------ENVIVIPDPFVSRNHARITVD--SNEIYIEDLGSTNGTFVNDFK-----RIKGPAKLHPNDIIKLG 88
|
|
| FHA_RAD53-like_rpt2 |
cd22690 |
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
12-103 |
3.11e-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: 43.43 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 12 PNSHPfqerHVYL-DEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTSKF---YLQDTkSSNGTFINSQRLSR 87
Cdd:cd22690 8 NPSYP----DIELtQNTTFIGRS------KDCDEEITDPRISKHHCIITRKRSGKGLddvYVTDT-STNGTFINNNRLGK 76
|
90
....*....|....*.
gi 1958683060 88 GSEesppCEILSGDII 103
Cdd:cd22690 77 GSQ----SLLQDGDEI 88
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
210-518 |
3.13e-05 |
|
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: 47.76 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 210 EDRLLSRLEVMGNQLQacsKNQTEDSLRKELVALQEDKHSYETTAK--------ESLRRVLQEKIEVVRKLSEVERSLSN 281
Cdd:TIGR02169 186 IERLDLIIDEKRQQLE---RLRREREKAERYQALLKEKREYEGYELlkekealeRQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 282 TEDECTH----LREMNER----TQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQ---QKGQAEKKELQAKIDDME 350
Cdd:TIGR02169 263 LEKRLEEieqlLEELNKKikdlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEerlAKLEAEIDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 351 EKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEK---TLKECSSLGIQVDDFLPKINGSTEKERLLSKSGGDCTFIH 427
Cdd:TIGR02169 343 REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEfaeTRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 428 QFIECQKKLMVQGHLTkvVEESKLSKENQAKAKESDLSdTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEER 507
Cdd:TIGR02169 423 ADLNAAIAGIEAKINE--LEEEKEDKALEIKKQEWKLE-QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
|
330
....*....|.
gi 1958683060 508 KAYRNQVEESA 518
Cdd:TIGR02169 500 RASEERVRGGR 510
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
14-106 |
3.70e-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: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 14 SHPFQERHvyldepIKIGRSVarcrpaQNNATFDCKVLSRNHALvwFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEesp 93
Cdd:cd22682 14 QFPITEST------IVIGRSV------ESQVQIDDDSVSRYHAK--LAVNPSAVSIIDLGSTNGTIVNGKKIPKLAS--- 76
|
90
....*....|...
gi 1958683060 94 pCEILSGDIIQFG 106
Cdd:cd22682 77 -CDLQNGDQIKIG 88
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
548-744 |
5.04e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 548 STRDKLLSAQDEILLLHQAAAKAVSERDTdfmsLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQcevQQREE 627
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEA----LEAELDALQERREALQRLAEYSWDEIDVASAEREIAELE---AELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 628 ATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLR 707
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958683060 708 DEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKF 744
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRAEEELERAMRAF 796
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
534-773 |
5.18e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 534 DMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKaVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQStf 613
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEK-LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE-- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 614 QLRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRK- 692
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKk 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 693 --ELENQMGSLKEQHLRDEaDLKTLLSKAENQAKdvqkeyEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 770
Cdd:PRK03918 347 lkELEKRLEELEERHELYE-EAKAKKEELERLKK------RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
...
gi 1958683060 771 KGN 773
Cdd:PRK03918 420 EIK 422
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
167-768 |
5.34e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.14 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 167 QLSQYLQEALHREQMLEQKLATL-----QRLLAITQE--ASDTSWQA------LIDEDRLL---SRLEVMGNQLQACSKN 230
Cdd:pfam12128 273 LIASRQEERQETSAELNQLLRTLddqwkEKRDELNGElsAADAAVAKdrseleALEDQHGAfldADIETAAADQEQLPSW 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 231 QTEDSLRKELVALQEDKHSYETTAKEslRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEEL-RELANKYNG 309
Cdd:pfam12128 353 QSELENLEERLKALTGKHQDVTAKYN--RRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALeSELREQLEA 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 310 AVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKEL------QAKIDDMEEKEQELQAKIEALQAD-------NDFTNERLTA 376
Cdd:pfam12128 431 GKLEFNEEEYRLKSRLGELKLRLNQATATPELLlqlenfDERIERAREEQEAANAEVERLQSElrqarkrRDQASEALRQ 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 377 LQVRLEPLQEktlkECSSLGIQVD-------DFLPKINGSTEKE--RLLSKSGGDCTFIHQFI---ECQKKLMVQG---H 441
Cdd:pfam12128 511 ASRRLEERQS----ALDELELQLFpqagtllHFLRKEAPDWEQSigKVISPELLHRTDLDPEVwdgSVGGELNLYGvklD 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 442 LTKVVEESKLSKENQAKAKESDLSDTLSPSKEK-----SSDDTTDAQMDEQDLNEPLAKVSL----------------LK 500
Cdd:pfam12128 587 LKRIDVPEWAASEEELRERLDKAEEALQSAREKqaaaeEQLVQANGELEKASREETFARTALknarldlrrlfdekqsEK 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 501 ALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMenLQEEKDT-------------EISSTRDKLLSAQDEILLLHQAA 567
Cdd:pfam12128 667 DKKNKALAERKDSANERLNSLEAQLKQLDKKHQAW--LEEQKEQkreartekqaywqVVEGALDAQLALLKAAIAARRSG 744
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 568 AKA-----VSERDTDFMS----------LQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQQRE---EAT 629
Cdd:pfam12128 745 AKAelkalETWYKRDLASlgvdpdviakLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNierAIS 824
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 630 RLQGELEKLKKEwdvlenecrslkkenvllsSELQRQ--EKELHNSQKQSLELTSDLSILqmtrKELENQMGSLKEQHLR 707
Cdd:pfam12128 825 ELQQQLARLIAD-------------------TKLRRAklEMERKASEKQQVRLSENLRGL----RCEMSKLATLKEDANS 881
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958683060 708 DEAD---------LKTLLSKAENQAKDVQKEYEKTQTVL-----SELKLKFEMTEQEKQSITDELKQCKDNLKLL 768
Cdd:pfam12128 882 EQAQgsigerlaqLEDLKLKRDYLSESVKKYVEHFKNVIadhsgSGLAETWESLREEDHYQNDKGIRLLDYRKLV 956
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
566-760 |
5.98e-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: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 566 AAAKAVSERDTDFMSLQEELKKVRAE---LEGWRKAASEYEE------EIRSLQSTFQL--------RCQQCEVQQREEA 628
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQielLEPIRELAERYAAarerlaELEYLRAALRLwfaqrrleLLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 629 TRLQGELEKLKKEWDVLENECRSLKKE------NVL--LSSELQRQEKELHNsqkqsleltsdlsiLQMTRKELENQMGS 700
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQirgnggDRLeqLEREIERLERELEE--------------RERRRARLEALLAA 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 701 LKEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 760
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
560-770 |
6.24e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 560 ILLLHQAAAKAVSERDtdfmSLQEELKKVRAELEGWRKAASEYEEEIRSLQStfQLRcqqcevQQREEATRLQGELEKLK 639
Cdd:COG4942 8 ALLLALAAAAQADAAA----EAEAELEQLQQEIAELEKELAALKKEEKALLK--QLA------ALERRIAALARRIRALE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 640 KEWDVLENECRSLKKENVLLSSELQRQEKELHN------------------SQKQSLELTSDLSILQMTRKELENQMGSL 701
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEELAEllralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683060 702 KEQhLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMT----EQEKQSITDELKQCKDNLKLLRE 770
Cdd:COG4942 156 RAD-LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLlarlEKELAELAAELAELQQEAEELEA 227
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
13-110 |
6.74e-05 |
|
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also called nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438717 [Multi-domain] Cd Length: 97 Bit Score: 42.22 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 13 NSHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTskFYLQDTKSSNGTFINSQRLSrgsee 91
Cdd:cd22665 7 SQAHGPEKDFPLYEgENVIGRD------PSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRL----- 73
|
90 100
....*....|....*....|.
gi 1958683060 92 SPPC--EILSGDIIQFGvDVT 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 |
7.14e-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: 42.70 E-value: 7.14e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958683060 52 SRNHALVWFDH---------KTSKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQFGV 107
Cdd:cd22667 40 SRKHATLTVLHpeanlsdpdTRPELTLKDL-SKYGTFVNGEKLKGGSE----VTLKDGDVITFGV 99
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
182-386 |
1.14e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 182 LEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgnqlqacSKNQTEDSLRKELVALQEDKHSYETTaKESLRRV 261
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHE---------ERREELETLEAEIEDLRETIAETERE-REELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 262 LQEKIEVVRKLSE------VERSLSNTEDECTHLR-----EMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEE 330
Cdd:PRK02224 281 VRDLRERLEELEEerddllAEAGLDDADAEAVEARreeleDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683060 331 IQQKGQAEKKELQA---KIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQE 386
Cdd:PRK02224 361 LREEAAELESELEEareAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
18-86 |
1.38e-04 |
|
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: 41.54 E-value: 1.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683060 18 QERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhkTSKFYLQDTKSSNGTFINSQRLS 86
Cdd:cd22694 8 GELRFDPGSSVRIGRD------PDADVRLDDPRVSRRHALLEFD--GDGWVYTDLGSRNGTYLNGRRVQ 68
|
|
| FHA_CHFR |
cd22672 |
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ... |
49-105 |
1.86e-04 |
|
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: 41.51 E-value: 1.86e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683060 49 KVLSRNHALVWFDHKTsKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQF 105
Cdd:cd22672 39 KLVSGDHCKIIRDEKG-QVWLEDT-STNGTLVNKVKVVKGQK----VELKHGDVIYL 89
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
245-756 |
2.22e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.71 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 245 EDKHSYETTAKES-LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKA 323
Cdd:pfam05483 228 EEEYKKEINDKEKqVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 324 AEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKiealQADNDFTNERLTALQVRLEPLQEktlkecsslgiqvddfl 403
Cdd:pfam05483 308 SMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKA----KAAHSFVVTEFEATTCSLEELLR----------------- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 404 pkingsTEKERLLSKsggdctfihqfiECQKKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQ 483
Cdd:pfam05483 367 ------TEQQRLEKN------------EDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 484 MDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENlQEEKDTEISSTRDKLLSAQDEILLL 563
Cdd:pfam05483 429 KIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK-EKLKNIELTAHCDKLLLENKELTQE 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 564 HQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQ--CEVQQREEATR-LQGELEKLKK 640
Cdd:pfam05483 508 ASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEvkCKLDKSEENARsIEYEVLKKEK 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 641 EWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTLLSKAE 720
Cdd:pfam05483 588 QMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKK 667
|
490 500 510
....*....|....*....|....*....|....*..
gi 1958683060 721 NQAKDVQKEYEKTQTVLSE-LKLKFEMTEQEKQSITD 756
Cdd:pfam05483 668 ISEEKLLEEVEKAKAIADEaVKLQKEIDKRCQHKIAE 704
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
256-774 |
2.48e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.71 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 256 ESLRRVLQEKIEVVRKLSEVERSlsntedECTHLREMNERTQEELRELANKYNGAV---NEIKDLSDKLKAAEGKQEEIQ 332
Cdd:pfam05483 98 EAELKQKENKLQENRKIIEAQRK------AIQELQFENEKVSLKLEEEIQENKDLIkenNATRHLCNLLKETCARSAEKT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 333 QKGQAEKKE-------LQAKIDDMEEKEQELQAKIEALQADNDFtneRLTALQVRLEPLQEKTLKECSSLGIQVDDFLPK 405
Cdd:pfam05483 172 KKYEYEREEtrqvymdLNNNIEKMILAFEELRVQAENARLEMHF---KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQ 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 406 IngsTEKERLLSksggDCTFIHQfiECQKKLmvqghlTKVVEESKLSKENQAKAKESdlSDTLSPSKEKSSDDTTDAQMD 485
Cdd:pfam05483 249 I---TEKENKMK----DLTFLLE--ESRDKA------NQLEEKTKLQDENLKELIEK--KDHLTKELEDIKMSLQRSMST 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 486 EQDLNEPLAKVSLLKALLEEERKAyrnQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEisstRDKLLSAQDEILLLHQ 565
Cdd:pfam05483 312 QKALEEDLQIATKTICQLTEEKEA---QMEELNKAKAAHSFVVTEFEATTCSLEELLRTE----QQRLEKNEDQLKIITM 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 566 AAAKAVSERD--TDFMSLQE----ELKKVRAELEGWRKAASEYEEEIRSLQSTFQlrcqqcevqqreeatRLQGELEKLK 639
Cdd:pfam05483 385 ELQKKSSELEemTKFKNNKEveleELKKILAEDEKLLDEKKQFEKIAEELKGKEQ---------------ELIFLLQARE 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 640 KEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSL--------------KEQH 705
Cdd:pfam05483 450 KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMtlelkkhqediincKKQE 529
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683060 706 LRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREKGNN 774
Cdd:pfam05483 530 ERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN 598
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
163-362 |
2.72e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALID--------EDRLLSRLEVMGNQLQACSKNQTED 234
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekeiaelRAELEAQKEELAELLRALYRLGRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 235 SLrkELVALQEDKHSYETTAK--ESLRRVLQEKIEVVRK-LSEVERSLSNTEDECTHLREMNERTQEELRELANkyngAV 311
Cdd:COG4942 121 PL--ALLLSPEDFLDAVRRLQylKYLAPARREQAEELRAdLAELAALRAELEAERAELEALLAELEEERAALEA----LK 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958683060 312 NEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEA 362
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
163-348 |
3.30e-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: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWqALIDEDRLLSRLEVMGNQLQACSKNQTE-DSLRKELV 241
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-DEIDVASAEREIAELEAELERLDASSDDlAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 242 ALQEDKhsyeTTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDEcthLREMNERTQEELRELANKYNGAVNEIKDLSDKL 321
Cdd:COG4913 696 ELEAEL----EELEEELDELKGEIGRLEKELEQAEEELDELQDR---LEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
170 180
....*....|....*....|....*..
gi 1958683060 322 KAAEGKQEEIQQKGQAEKKELQAKIDD 348
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAMRA 795
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
583-757 |
3.32e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 583 EELKKVRAELEGWRKAASEYEEEIRSLQSTFQlRCQQCEvQQREEATRLQGELEKLKKEWDVLEnECRSLKKENVLLSSE 662
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEE-ELEELE-AELEELREELEKLEKLLQLLPLYQ-ELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 663 LQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKL 742
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170
....*....|....*
gi 1958683060 743 KFEMTEQEKQSITDE 757
Cdd:COG4717 228 ELEQLENELEAAALE 242
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
208-366 |
3.36e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 208 IDEDRLLSRLEVMGNQLQACSKNQTE---DSLRKELVALQED-KHSYETTAKEslrrvLQEKIEVVRKLSEVERSLsnte 283
Cdd:PRK04778 249 LDHLDIEKEIQDLKEQIDENLALLEEldlDEAEEKNEEIQERiDQLYDILERE-----VKARKYVEKNSDTLPDFL---- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 284 decTHLREMNERTQEELRELANKY---NGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKK---ELQAKIDDMEEKEQELQ 357
Cdd:PRK04778 320 ---EHAKEQNKELKEEIDRVKQSYtlnESELESVRQLEKQLESLEKQYDEITERIAEQEIaysELQEELEEILKQLEEIE 396
|
....*....
gi 1958683060 358 AKIEALQAD 366
Cdd:PRK04778 397 KEQEKLSEM 405
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
197-387 |
4.77e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 197 QEASDTSWQALIDEDRLLSRLEVMGNQLQAcsKNQTEDSLRKELVALQEDKHSYETTAKEslrrvLQEKIEVVR-KLSEV 275
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEE--LNEEYNELQAELEALQAEIDKLQAEIAE-----AEAEIEERReELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 276 ERSLSNTEDECTHLR---------EMNERtQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKI 346
Cdd:COG3883 92 ARALYRSGGSVSYLDvllgsesfsDFLDR-LSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958683060 347 DDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEK 387
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
53-106 |
4.78e-04 |
|
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 (FHAD1) and similar proteins; FHAD1, also called FHA domain-containing protein 1, is an uncharacterized FHA domain-containing protein. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438752 [Multi-domain] Cd Length: 96 Bit Score: 39.93 E-value: 4.78e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1958683060 53 RNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPceilsGDIIQFG 106
Cdd:cd22700 36 EQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAP-----GDVLRFG 84
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
584-770 |
4.96e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 584 ELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEvQQREEATRLQGELEKL---KKEWDVLENECRSLKKENVLLS 660
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREIN-EISSELPELREELEKLekeVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 661 SELQRQEKELHNSQKQSLELTSDLSILQMTRKELEN---------QMGSLKEQHLRDEADLKTLLSKAENQAKDVQKEYE 731
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958683060 732 KtqtvLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 770
Cdd:PRK03918 332 E----LEEKEERLEELKKKLKELEKRLEELEERHELYEE 366
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
25-108 |
4.96e-04 |
|
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: 40.49 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 25 DEPIKIGRsvarcRPAQNNAT----FDCKVLSRNHALVWFdhKTSKFYLQDTKSSNGTFINSQRLSR-GSEESPPCEILS 99
Cdd:cd22702 31 KQPCIIGS-----DPHQAISGisvvIPSPQVSELHARITC--KNGAFFLTDLGSEHGTWINDNEGRRyRAPPNFPVRLHP 103
|
....*....
gi 1958683060 100 GDIIQFGVD 108
Cdd:cd22702 104 SDVIEFGSD 112
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
583-774 |
4.96e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 583 EELKKVRAELEGWRKAASEYEEEIRSLQstfQLRcQQCevQQREEATRLQGELEKLKKEWDVLENEcrslkKENVLLSSE 662
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLE---PIR-ELA--ERYAAARERLAELEYLRAALRLWFAQ-----RRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 663 LQRQEKELHNSQKQSLELTSDLSILQMTRKELENQmgsLKEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKL 742
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQ---IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
170 180 190
....*....|....*....|....*....|..
gi 1958683060 743 KFEMTEQEKQSITDELKQCKDNLKLLREKGNN 774
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
238-387 |
5.30e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 238 KELVALQEDKHSYETTAKESLRRV--LQEKIE-VVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEI 314
Cdd:PRK02224 488 EEEVEEVEERLERAEDLVEAEDRIerLEERREdLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEA 567
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958683060 315 KDLSDKLKAAEGKQEEIQQKGQAEKK--ELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEK 387
Cdd:PRK02224 568 EEAREEVAELNSKLAELKERIESLERirTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAE 642
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
627-750 |
5.72e-04 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 42.77 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 627 EATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNsQKQSLELTSDLSilqmtrkELENQMGSLKeqhl 706
Cdd:pfam15294 134 EIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGA-KKDVKSNLKEIS-------DLEEKMAALK---- 201
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1958683060 707 rdeADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQE 750
Cdd:pfam15294 202 ---SDLEKTLNASTALQKSLEEDLASTKHELLKVQEQLEMAEKE 242
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
16-111 |
6.21e-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: 39.59 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 16 PFQERHVYLD-EPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFdhKTSKFYLQDTKSSNGTFINSQRLSRgseespP 94
Cdd:cd22693 7 TLQGQTFPIDkSGITIGRA------DDNDLVLSDDFVSSRHARIYL--QGSSWYLEDLGSTNGTFVNGNRVTQ------P 72
|
90
....*....|....*..
gi 1958683060 95 CEILSGDIIQFGVDVTE 111
Cdd:cd22693 73 VVVQPGDTIRIGATVFE 89
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
52-106 |
7.43e-04 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein kinase DUN1 and similar proteins; DUN1 is a protein kinase that controls the DNA damage response in yeast. It phosphorylates SML1 on serine residues and cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438735 [Multi-domain] Cd Length: 96 Bit Score: 39.40 E-value: 7.43e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958683060 52 SRNHALVWFDHKTSKFYLQ-----------DTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFG 106
Cdd:cd22683 28 SRSCDLVLSDPSISRFHAElrleqnginviDNNSANGTFINGKRIKGKT-----YILKNGDIIVFG 88
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
234-383 |
9.07e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 234 DSLRKELVALQEDKhsyeTTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLRE--MNERTQEELRELANKYNGAV 311
Cdd:COG1579 27 KELPAELAELEDEL----AALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNNKEYEALQKEIESLK 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958683060 312 NEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEP 383
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
623-771 |
9.55e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 623 QQREEATR----LQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQ--EKELHNSQKQSLELTSDLSILQMTRKELEN 696
Cdd:COG3206 168 LRREEARKalefLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKllLQQLSELESQLAEARAELAEAEARLAALRA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 697 QMGS----------------LKEQHLRDEADLKTLLSK----------AENQAKDVQKEYEK-TQTVLSELKLKFEMTEQ 749
Cdd:COG3206 248 QLGSgpdalpellqspviqqLRAQLAELEAELAELSARytpnhpdviaLRAQIAALRAQLQQeAQRILASLEAELEALQA 327
|
170 180
....*....|....*....|..
gi 1958683060 750 EKQSITDELKQCKDNLKLLREK 771
Cdd:COG3206 328 REASLQAQLAQLEARLAELPEL 349
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
256-365 |
1.10e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 256 ESLRRVLQEKI-EVVRKLSEVERSLSNTEDEcthLREMNERTQEELRELANKYNGAVNEIKdlsdklKAAEGKQEEIQQK 334
Cdd:PRK00409 526 EELERELEQKAeEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLEEAEKEAQQAIKEAK------KEADEIIKELRQL 596
|
90 100 110
....*....|....*....|....*....|.
gi 1958683060 335 GQAEKKELQAKidDMEEKEQELQAKIEALQA 365
Cdd:PRK00409 597 QKGGYASVKAH--ELIEARKRLNKANEKKEK 625
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
503-676 |
1.13e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 503 LEEERKAYRNQVEESAKQIQVLQVQLQRLhMDMENLQEEKDTEISSTRdKLLSAQDEILLLHQAaakavSERDTDFMSLQ 582
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEEL-EELEAELEELREELEKLE-KLLQLLPLYQELEAL-----EAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 583 EELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSE 662
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170
....*....|....
gi 1958683060 663 LQRQEKELHNSQKQ 676
Cdd:COG4717 229 LEQLENELEAAALE 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
180-391 |
1.24e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 180 QMLEQKLATLQRLLAITQEASDTSWQALideDRLLSRLEVMGNQLQAcsKNQTEDSLRKELVALQEDKHSYETTAKESLR 259
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAEL---EELNEEYNELQAELEA--LQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 260 rVLQEKIEVVRKLSEVERSLSNTE--DECTHLREMNERTQEELRELANkyngAVNEIKDLSDKLKAAEGKQEEIQQKGQA 337
Cdd:COG3883 94 -ALYRSGGSVSYLDVLLGSESFSDflDRLSALSKIADADADLLEELKA----DKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958683060 338 EKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEKTLKE 391
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
236-386 |
1.35e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 236 LRKELVALQEDKHSYETTAK--ESLRRVLQEKIEVVRKLSEVERSLSNTEDecthlremnerTQEELRELANKYNgavnE 313
Cdd:COG4913 615 LEAELAELEEELAEAEERLEalEAELDALQERREALQRLAEYSWDEIDVAS-----------AEREIAELEAELE----R 679
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683060 314 IKDLSDKLKAAEGKQEEIQqkgqAEKKELQAKIDDMEEKEQELQAKIEALQadndftnERLTALQVRLEPLQE 386
Cdd:COG4913 680 LDASSDDLAALEEQLEELE----AELEELEEELDELKGEIGRLEKELEQAE-------EELDELQDRLEAAED 741
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
27-106 |
1.38e-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: 38.60 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 27 PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTSkfYLQDTKSSNGTFINSQRLsrgseeSPPCEILSGDIIQFG 106
Cdd:cd22668 19 SNIIGRG------SDADFRLPDTGVSRRHAEIRWDGQVA--HLTDLGSTNGTTVNNAPV------TPEWRLADGDVITLG 84
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
625-751 |
1.52e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.54 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 625 REEATRLQGELEKLKKEWDVLENECRSLKK----ENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGS 700
Cdd:smart00787 164 MKELELLNSIKPKLRDRKDALEEELRQLKQledeLEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIED 243
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1958683060 701 LKEQhlrdEADLKTLLSKAENQAKDVQKeyeKTQTVLSELKLKFEMTEQEK 751
Cdd:smart00787 244 LTNK----KSELNTEIAEAEKKLEQCRG---FTFKEIEKLKEQLKLLQSLT 287
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
49-112 |
1.66e-03 |
|
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: 39.34 E-value: 1.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683060 49 KVLSRNHALVWFDHKTS--KFYLQDTKSSNGTFINsqrlsrgSEESPPC---EILSGDIIQFGVDVTEN 112
Cdd:cd22681 64 ETCSKQHCVIQFRNVKGilKPYIMDLDSSNGTCLN-------DNVIPSSryvELRSGDVITFSKSNDYE 125
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
1-106 |
1.69e-03 |
|
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: 41.67 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 1 MPSALAIFTCRPNSHPFQERHVYLDEPIKIGRSvARC-----RPAQnnatfdckVLSRNHALVWFDHktSKFYLQDTkSS 75
Cdd:COG3456 1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRS-ADCdwvlpDPDR--------SVSRRHAEIRFRD--GAFCLTDL-ST 68
|
90 100 110
....*....|....*....|....*....|...
gi 1958683060 76 NGTFIN--SQRLSRGSEEsppcEILSGDIIQFG 106
Cdd:COG3456 69 NGTFLNgsDHPLGPGRPV----RLRDGDRLRIG 97
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
274-381 |
2.01e-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: 41.38 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 274 EVERSLSNTEDECTHLREMNERTQEELRELANKY---NGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEK----------K 340
Cdd:pfam06160 288 YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEvayselqeelE 367
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1958683060 341 ELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRL 381
Cdd:pfam06160 368 EILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLEL 408
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
475-704 |
2.08e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 475 SSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEE---KDTEISSTRD 551
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaeLEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 552 KLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQstfqlrcqqcevQQREEATRL 631
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR------------ADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683060 632 QGELEKLKKEWDVLENEcrsLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQ 704
Cdd:COG4942 166 RAELEAERAELEALLAE---LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
163-365 |
2.10e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.60 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEasdtsWQALIDEDRLLSR----LEVMGNQLQACSKNQT--EDSL 236
Cdd:COG0497 172 KELEELRADEAERARELDLLRFQLEELEAAALQPGE-----EEELEEERRRLSNaeklREALQEALEALSGGEGgaLDLL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 237 ---RKELVALQEDKHSYETTAkESLRRVLQEKIEVVRklsEVERSLSNTEDECTHLREMNERtQEELRELANKYNGAVNE 313
Cdd:COG0497 247 gqaLRALERLAEYDPSLAELA-ERLESALIELEEAAS---ELRRYLDSLEFDPERLEEVEER-LALLRRLARKYGVTVEE 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958683060 314 IKDLSDKLkaaegkqeeiqqkgQAEKKELQAKIDDMEEKEQELQAKIEALQA 365
Cdd:COG0497 322 LLAYAEEL--------------RAELAELENSDERLEELEAELAEAEAELLE 359
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
289-519 |
2.22e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 289 LREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALqadnd 368
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEEL----- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 369 ftNERLTALQVRLEPlQEKTLKECSSLGIQVDDFLPKINgsteKERLLSKSGGDCTFIHQFIECQKKLMVQGHLTKVVEE 448
Cdd:PHA02562 240 --TDELLNLVMDIED-PSAALNKLNTAAAKIKSKIEQFQ----KVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQ 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958683060 449 SKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAK 519
Cdd:PHA02562 313 HSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAK 383
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
531-670 |
2.65e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 531 LHMDMENLQEEK---DTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDfmsLQEELKKVRAELEGWRKAASEYEEEIR 607
Cdd:COG4913 293 LEAELEELRAELarlEAELERLEARLDALREELDELEAQIRGNGGDRLEQ---LEREIERLERELEERERRRARLEALLA 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 608 SLQST-----------------FQLRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKEL 670
Cdd:COG4913 370 ALGLPlpasaeefaalraeaaaLLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
284-401 |
4.01e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 284 DE-CTHLREMNERTQEELRELANKyngavneIKDLSDKLKAAEGKQEEIQQ----KGQAEKKELQAKIDDME---EKEQE 355
Cdd:COG0542 396 DEaAARVRMEIDSKPEELDELERR-------LEQLEIEKEALKKEQDEASFerlaELRDELAELEEELEALKarwEAEKE 468
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1958683060 356 LQAKIEALQADNDFTNERLTALQVRLEPLQEKTLKECSSLGIQVDD 401
Cdd:COG0542 469 LIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE 514
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
258-365 |
4.06e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.68 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 258 LRRVLQEKIEVV---RKLSEVERSLSntEDECTHLREMNERTQ----EELRELANKYNGAVNEIKDLSDKLKAAEGKQ-- 328
Cdd:PRK05771 1 LAPVRMKKVLIVtlkSYKDEVLEALH--ELGVVHIEDLKEELSnerlRKLRSLLTKLSEALDKLRSYLPKLNPLREEKkk 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1958683060 329 ------EEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQA 365
Cdd:PRK05771 79 vsvkslEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQ 121
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
267-391 |
4.07e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 267 EVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYngavNEIKDlSDKLKAaegkQEEIQQKGQAEKKELQAKI 346
Cdd:PRK00409 520 ELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKL----QEEED-KLLEEA----EKEAQQAIKEAKKEADEII 590
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1958683060 347 DDMEEKEQELQAKIEALQADndftnERLTALQVRLEPLQEKTLKE 391
Cdd:PRK00409 591 KELRQLQKGGYASVKAHELI-----EARKRLNKANEKKEKKKKKQ 630
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
314-771 |
4.44e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 314 IKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQAdndfTNERLTALQVRLEPLQEKtLKECS 393
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREE-LEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 394 slgiQVDDFLPKINGSTEKERLLSksggdctfihQFIECQKKLMVQGHLTKVVEESKLSKENQAKAKESDLsdtlspsKE 473
Cdd:COG4717 123 ----KLLQLLPLYQELEALEAELA----------ELPERLEELEERLEELRELEEELEELEAELAELQEEL-------EE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 474 KSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDmENLQEEKDT--------E 545
Cdd:COG4717 182 LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-ERLKEARLLlliaaallA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 546 ISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRcQQCEVQQR 625
Cdd:COG4717 261 LLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLP-PDLSPEEL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 626 EEATRLQGELEKLKKEWDVLENE---CRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLK 702
Cdd:COG4717 340 LELLDRIEELQELLREAEELEEElqlEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELE 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958683060 703 EQHLR-DEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEK--QSITDELKQCKDNLKLLREK 771
Cdd:COG4717 420 ELLEAlDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRELAEE 491
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
173-392 |
5.08e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.71 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 173 QEALHREQM--LEQKLATLQRLLAITqeasdtswqALIDEDRLLSRLEVMGNQLQACSKNQTE--------DSLRKELVA 242
Cdd:COG3096 858 QEQQLRQQLdqLKEQLQLLNKLLPQA---------NLLADETLADRLEELREELDAAQEAQAFiqqhgkalAQLEPLVAV 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 243 LQEDKHSYETTAKE-----SLRRVLQEKIEVvrkLSEV-ER----SLSNTEDECTHLREMNERTQEELRElankyngAVN 312
Cdd:COG3096 929 LQSDPEQFEQLQADylqakEQQRRLKQQIFA---LSEVvQRrphfSYEDAVGLLGENSDLNEKLRARLEQ-------AEE 998
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 313 EIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQA--------KIEALQADNDFTNERLTALQVRLEPL 384
Cdd:COG3096 999 ARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEElgvqadaeAEERARIRRDELHEELSQNRSRRSQL 1078
|
....*...
gi 1958683060 385 qEKTLKEC 392
Cdd:COG3096 1079 -EKQLTRC 1085
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
253-387 |
5.27e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 253 TAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQ 332
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1958683060 333 QkgqaEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEK 387
Cdd:COG4372 115 E----ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
213-765 |
5.39e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 213 LLSRLEVMGNQLQACSKNQTEdsLRKELVALQEDKHSyETTAK---ESLRRVLQEKIEVVRklSEVERSLSNT------- 282
Cdd:pfam01576 248 ALARLEEETAQKNNALKKIRE--LEAQISELQEDLES-ERAARnkaEKQRRDLGEELEALK--TELEDTLDTTaaqqelr 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 283 ---EDECTHLR----EMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKID-------D 348
Cdd:pfam01576 323 skrEQEVTELKkaleEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRtlqqakqD 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 349 MEEKEQELQAKIEALQADNDFT-------NERLTALQVRLEPLQE----------KTLKECSSLGIQVDDFLPKINGSTE 411
Cdd:pfam01576 403 SEHKRKKLEGQLQELQARLSESerqraelAEKLSKLQSELESVSSllneaegkniKLSKDVSSLESQLQDTQELLQEETR 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 412 KERLLSksggdcTFIHQFIECQKKLMVQghltkvVEESKLSKENQAKaKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNE 491
Cdd:pfam01576 483 QKLNLS------TRLRQLEDERNSLQEQ------LEEEEEAKRNVER-QLSTLQAQLSDMKKKLEEDAGTLEALEEGKKR 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 492 PLAKVSLLKALLEEERKAY------RNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDEillLHQ 565
Cdd:pfam01576 550 LQRELEALTQQLEEKAAAYdklektKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEE---RDR 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 566 AAAKAvSERDTDFMSLQEEL--------------KKVRAELEGW-------RKAASEYEEEIRSLQSTFQ-LRCQQCEVQ 623
Cdd:pfam01576 627 AEAEA-REKETRALSLARALeealeakeelertnKQLRAEMEDLvsskddvGKNVHELERSKRALEQQVEeMKTQLEELE 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 624 QREEAT-----RLQGELEKLKKEWDV-LENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQ 697
Cdd:pfam01576 706 DELQATedaklRLEVNMQALKAQFERdLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQ 785
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683060 698 MGSLKEQhlRDEADLKtlLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNL 765
Cdd:pfam01576 786 IDAANKG--REEAVKQ--LKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDL 849
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
172-370 |
6.39e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 39.24 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 172 LQEALHREQMLEQKLATLQRLLAITQEASDTSwqalidEDRLLSRLEvmgNQLQACSKNQTEDSLRKELvalqEDKHSYE 251
Cdd:pfam00261 24 LEEAEKRAEKAEAEVAALNRRIQLLEEELERT------EERLAEALE---KLEEAEKAADESERGRKVL----ENRALKD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 252 TTAKESLRRVLQEKIEVV----RKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVN--------------- 312
Cdd:pfam00261 91 EEKMEILEAQLKEAKEIAeeadRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNnlksleaseekaser 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958683060 313 ------EIKDLSDKLKAAEGKQEEIQQKGQaekkELQAKIDDMEEKEQELQAKIEALQADNDFT 370
Cdd:pfam00261 171 edkyeeQIRFLTEKLKEAETRAEFAERSVQ----KLEKEVDRLEDELEAEKEKYKAISEELDQT 230
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
290-434 |
6.97e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 40.03 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 290 REMNERTQEELRELANKY----------------NGAVNEIKDLSDKLKAAEGKQEeiqQKGQAEKKElqakiddmeeke 353
Cdd:TIGR01612 1513 KELFEQYKKDVTELLNKYsalaiknkfaktkkdsEIIIKEIKDAHKKFILEAEKSE---QKIKEIKKE------------ 1577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 354 qelQAKIEALQADNDFTNERLTALQVRLEPLQEKTLKeCSSLGIQVDDFLPKINgSTEK----------ERLLSKSGGDC 423
Cdd:TIGR01612 1578 ---KFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLK-ISDIKKKINDCLKETE-SIEKkissfsidsqDTELKENGDNL 1652
|
170
....*....|.
gi 1958683060 424 TFIHQFIECQK 434
Cdd:TIGR01612 1653 NSLQEFLESLK 1663
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
501-722 |
7.09e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 501 ALLEEERKAYRNQVEESAKQIQVLQVqlqrlhmDMENLQEEKD-----TEISSTRDKLLSAQDEILLLhQAAAKAVSERD 575
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEA-------ELDALQERREalqrlAEYSWDEIDVASAEREIAEL-EAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 576 TDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFqlrcQQCEVQQREEATRLQgELEKLKKEWDV--LENECRSLK 653
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL----EQAEEELDELQDRLE-AAEDLARLELRalLEERFAAAL 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 654 KENVL------LSSELQRQEKELHNSQKQ---------------SLELTSDLSILQMTRKELEnqmgSLKEQHL-RDEAD 711
Cdd:COG4913 760 GDAVErelrenLEERIDALRARLNRAEEEleramrafnrewpaeTADLDADLESLPEYLALLD----RLEEDGLpEYEER 835
|
250
....*....|.
gi 1958683060 712 LKTLLSKAENQ 722
Cdd:COG4913 836 FKELLNENSIE 846
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
161-384 |
8.33e-03 |
|
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: 39.65 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 161 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQAL----IDEDRLLSRLEVMGNQLQACSKNQTEDSL 236
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllnEEAANLRERLESLERRIAATERRLEDLEE 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 237 RKELVALQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTedecthLREMNERTQEELRELANKYNGAVNEIKD 316
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL------LRSELEELSEELRELESKRSELRRELEE 919
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683060 317 LSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDftnERLTALQVRLEPL 384
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR---RRLKRLENKIKEL 984
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
600-762 |
8.63e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 39.17 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 600 SEYEEEIRSLQSTFQLRCQQCEVQQREEAtRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKqslE 679
Cdd:pfam09728 28 AELLEEMKRLQKDLKKLKKKQDQLQKEKD-QLQSELSKAILAKSKLEKLCRELQKQNKKLKEESKKLAKEEEEKRK---E 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 680 LTSDlsiLQMTRKELENQM-------GSLKEQHLRDEADLKTLLSKAENQAKDVQKEYEKT--QTVLSELKLKFEMTEQE 750
Cdd:pfam09728 104 LSEK---FQSTLKDIQDKMeekseknNKLREENEELREKLKSLIEQYELRELHFEKLLKTKelEVQLAEAKLQQATEEEE 180
|
170
....*....|..
gi 1958683060 751 KQSITDELKQCK 762
Cdd:pfam09728 181 KKAQEKEVAKAR 192
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
386-667 |
9.14e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.53 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 386 EKTLKECSSLGI-QVDDflPKINGSTEKERLLSKSggdctfihqFIECQKKLmvqGHLTKVVEESKLSKENQAKAKESDL 464
Cdd:PRK05771 19 DEVLEALHELGVvHIED--LKEELSNERLRKLRSL---------LTKLSEAL---DKLRSYLPKLNPLREEKKKVSVKSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 465 SDTLSPSKEKSSDDttdaqmdEQDLNEPLAKVSLLkallEEERKAYRNQVEESAKQIQvlqvqlqrLHMDMENLQEEKDT 544
Cdd:PRK05771 85 EELIKDVEEELEKI-------EKEIKELEEEISEL----ENEIKELEQEIERLEPWGN--------FDLDLSLLLGFKYV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683060 545 EISS---TRDKLLSAQDEILLLHQAAAKAVSERDT-DFMSLQEELKKVRAELE--GWRKAASEYEEEIRslqstfqlrcq 618
Cdd:PRK05771 146 SVFVgtvPEDKLEELKLESDVENVEYISTDKGYVYvVVVVLKELSDEVEEELKklGFERLELEEEGTPS----------- 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683060 619 qcevqqrEEATRLQGELEKLKKEWDVLENECRSLKKENV--------LLSSELQRQE 667
Cdd:PRK05771 215 -------ELIREIKEELEEIEKERESLLEELKELAKKYLeellalyeYLEIELERAE 264
|
|
| |
