|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
3-130 |
6.38e-81 |
|
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and similar proteins; SLMAP, also called sarcolemmal-associated protein (SLAP), is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. It is a cardiac membrane protein that plays an important role in E-C coupling and the adrenergic response of the heart. Overexpression of the SLMAP gene has been associated with diabetes and endothelial dysfunction of macro- and micro-blood vessels. SLMAP contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438731 [Multi-domain] Cd Length: 126 Bit Score: 254.11 E-value: 6.38e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 3 SALAIFTCRPNSHPFQERHVYLDEPIKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHktSKFYLQDTKSSNGTFINS 82
Cdd:cd22679 1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1958683074 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 |
1.00e-26 |
|
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal membrane-associated protein (SLMAP), also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. SLMAP contains an N-terminal FHA domain followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409287 [Multi-domain] Cd Length: 63 Bit Score: 103.15 E-value: 1.00e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683074 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 |
1.20e-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: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 27 PIKIGRSVARCRPAQNNAT-FDCKVLSRNHALVWfdHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQF 105
Cdd:cd22692 38 QIHIGRYTERVRQAIYHPVvFKSKVVSRTHGCIK--VDEGNWYIKDVKSSSGTFLNHQRLSPASRTSKPYPLRDGDILQL 115
|
...
gi 1958683074 106 GVD 108
Cdd:cd22692 116 GMD 118
|
|
| FHA_VPS64-like |
cd22695 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ... |
6-126 |
3.57e-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: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 6 AIFTCRPNSHPFQERHV---YLDEPIKIGRSVARCRPAQN---------------NATFDCKVLSRNHALVWFDHKTSKF 67
Cdd:cd22695 2 HILVLKSLNATFETKFLvvpFKPDGLKLGRPVTNSVNKNNsgskrdlfsqqvrpdNGNFDSRVLSRNHACLSCDPTTGKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683074 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 |
2.12e-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: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 13 NSHPFQERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKtsKFYLQDTKSSNGTFINSQRLsrgseeS 92
Cdd:cd00060 6 DGDGGGREFPLTKGVVTIGRS------PDCDIVLDDPSVSRRHARIEVDGG--GVYLEDLGSTNGTFVNGKRI------T 71
|
90
....*....|....
gi 1958683074 93 PPCEILSGDIIQFG 106
Cdd:cd00060 72 PPVPLQDGDVIRLG 85
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
28-105 |
5.88e-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: 5.88e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683074 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 |
7.65e-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: 62.89 E-value: 7.65e-13
10 20 30
....*....|....*....|....*....|....*...
gi 1958683074 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21868 1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-737 |
1.41e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.63 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 156 NTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQA--CSKNQTE 233
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvAQLELQI 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 234 DSLRKELVALQEDKHSYE------TTAKESLRRVLQE--KIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELAN 305
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEdrrerlQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 306 KYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKiddmEEKEQELQAKIEALQADNDFTNERLTALQERLLS-- 383
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ----SGLSGILGVLSELISVDEGYEAAIEAALGGRLQAvv 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 384 ----------------KSGGDCTFI------HQFIE------CQKKLMVQGHLTKVVE-ESKLSK--------------- 419
Cdd:TIGR02168 552 venlnaakkaiaflkqNELGRVTFLpldsikGTEIQgndreiLKNIEGFLGVAKDLVKfDPKLRKalsyllggvlvvddl 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 420 -ENQAKAKESDLS--------DTLSP--------SKEKSSDDTTDAQMDE--QDLNEPLAKVSLLKALL---EEERKAYR 477
Cdd:TIGR02168 632 dNALELAKKLRPGyrivtldgDLVRPggvitggsAKTNSSILERRREIEEleEKIEELEEKIAELEKALaelRKELEELE 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 478 NQVEESAKQIQVLQVQLQRLHMDMENLQEEKDT---EISSTRDKLLSAQDEILLLHQAAAKA---VSERDTDFMSLQEEL 551
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVEQleeRIAQLSKELTELEAEIEELEERLEEAeeeLAEAEAEIEELEAQI 791
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 552 KKVRAELEGWRKAASEYEEEIRSLQSTF---QLRCQQCE----------VQQREEATRLQGELEKLKKEWDVLENECRSL 618
Cdd:TIGR02168 792 EQLKEELKALREALDELRAELTLLNEEAanlRERLESLErriaaterrlEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 619 KKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHlrdeADLKTLLSKAENQAKDVQkeyek 698
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL----AQLELRLEGLEVRIDNLQ----- 942
|
650 660 670
....*....|....*....|....*....|....*....
gi 1958683074 699 tQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 737
Cdd:TIGR02168 943 -ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
163-737 |
5.55e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSlrKELVA 242
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL--EELEA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 243 LQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKY-NGAVNEIKDLSDKL 321
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEEL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 322 KAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQAdndftneRLTALQERLLSKSGGDCTFIHQFIECQKK 401
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA-------RLDSLERLQENLEGFSEGVKALLKNQSGL 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 402 LMVQGHLTKVVEesklSKENQAKAKESDLSDTLspskEKSSDDTTDAQMDEQDLnepLAKVSLLKALLEEERKAYRNQVE 481
Cdd:TIGR02168 519 SGILGVLSELIS----VDEGYEAAIEAALGGRL----QAVVVENLNAAKKAIAF---LKQNELGRVTFLPLDSIKGTEIQ 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 482 ESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDeillLHQAAAKAVSER-DTDFMSLQEELKKVRAELEG 560
Cdd:TIGR02168 588 GNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDD----LDNALELAKKLRpGYRIVTLDGDLVRPGGVITG 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 561 WRKAAS----EYEEEIRSLQstfqlrcQQCEVQQrEEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKEL 636
Cdd:TIGR02168 664 GSAKTNssilERRREIEELE-------EKIEELE-EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDL 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 637 HNSQKQSLELTSDLSILQMTRKELENQMGSLKEQ----------HLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSEL 706
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERleeaeeelaeAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
570 580 590
....*....|....*....|....*....|.
gi 1958683074 707 KLKFEMTEQEKQSITDELKQCKDNLKLLREK 737
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
52-106 |
2.22e-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: 2.22e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1958683074 52 SRNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQFG 106
Cdd:cd22686 48 SKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPYPLTHGDELKIG 102
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
190-740 |
6.05e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.23 E-value: 6.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 190 QRLLAITQEASDTSWQALIDE--------DRLLSRLEVMGNQLQACSKNQTE-----DSLRKELVALQEDKHSYETT--- 253
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLRleelreelEELQEELKEAEEELEELTAELQEleeklEELRLEVSELEEEIEELQKElya 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 254 AKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQ 333
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 334 KGQAEKKELQ---AKIDDMEEKEQELQAKIEALQADNDFTNERLTALQERLLSKSggdctfihQFIECQKKLMVQGHLTK 410
Cdd:TIGR02168 373 RLEELEEQLEtlrSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL--------KKLEEAELKELQAELEE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 411 VVEEsklskENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYR---NQVEESAKQI 487
Cdd:TIGR02168 445 LEEE-----LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEgvkALLKNQSGLS 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 488 QVLQVQLQRLHMDmENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSL--------QEELKKVRAELE 559
Cdd:TIGR02168 520 GILGVLSELISVD-EGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLdsikgteiQGNDREILKNIE 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 560 GWRKAASEYEEEIRSLQSTFQLRCQQCEVQQR-EEATRLQG--------------------------------------E 600
Cdd:TIGR02168 599 GFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDlDNALELAKklrpgyrivtldgdlvrpggvitggsaktnssilerrrE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 601 LEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLKT 680
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683074 681 LLSKAENQAKDVQKEYEKTQTVLSE---LKLKFEMTEQEKQSITDELKQCKDNLKLLREKGNN 740
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEieeLEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
239-739 |
6.86e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 6.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 239 ELVALQEDKHSYETTAKESLRRV--LQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKD 316
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 317 LSDKLKAAEGKQEEIQQKGQAEKK---------ELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQERLLSKSGG 387
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKkaeekkkadEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 388 DCTFIHQFIECQKKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEqdlnEPLAKVSLLKA 467
Cdd:PTZ00121 1442 EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA----EAKKKADEAKK 1517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 468 LLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQE-EKDTEISSTRDKLLSAQDEILLLHQA--AAKAVSERDTDF 544
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElKKAEEKKKAEEAKKAEEDKNMALRKAeeAKKAEEARIEEV 1597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 545 MSLQEELKKVRAE----LEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKK 620
Cdd:PTZ00121 1598 MKLYEEEKKMKAEeakkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 621 ENVLLSSE--------LQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTL--LSKAENQAK 690
Cdd:PTZ00121 1678 EEAKKAEEdekkaaeaLKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAeeAKKDEEEKK 1757
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958683074 691 DVQK------------EYEKTQTVLSELKlkfEMTEQEKQSITDELKQCKDNLKLLREKGN 739
Cdd:PTZ00121 1758 KIAHlkkeeekkaeeiRKEKEAVIEEELD---EEDEKRRMEVDKKIKDIFDNFANIIEGGK 1815
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
14-106 |
6.91e-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: 6.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 14 SHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktSKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716 8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
|
90
....*....|....
gi 1958683074 93 pPCEILSGDIIQFG 106
Cdd:COG1716 75 -PAPLRDGDVIRLG 87
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
161-707 |
1.32e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 161 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKEL 240
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 241 VALQEDKHSYETT----------AKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGA 310
Cdd:COG1196 298 ARLEQDIARLEERrreleerleeLEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 311 VNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQERLLSksggdct 390
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE------- 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 391 fihqfiecQKKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLE 470
Cdd:COG1196 451 --------EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 471 EERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKL-------LSAQDEILLLHQAAAKAVSERDTD 543
Cdd:COG1196 523 AGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratflpLDKIRARAALAAALARGAIGAAVD 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 544 FMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENV 623
Cdd:COG1196 603 LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 624 LLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVL 703
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
....
gi 1958683074 704 SELK 707
Cdd:COG1196 763 EELE 766
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
271-711 |
1.90e-10 |
|
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: 64.43 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 271 KLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAvneIKDLSDKLKaaegKQEEIQQKGQAEKKELQAKIDDME 350
Cdd:pfam01576 149 KLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAM---ISDLEERLK----KEEKGRQELEKAKRKLEGESTDLQ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 351 EKEQELQAKIEALQADNDFTNERLTALQERLLSKSGgdctfihQFIECQKKLM-VQGHLTKVVE--ESKLSKENQAKAKE 427
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAKKEEELQAALARLEEETA-------QKNNALKKIReLEAQISELQEdlESERAARNKAEKQR 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 428 SDLSDTLSPSKEKSSD--DTTDAQMDEQDLNEplAKVSLLKALLEEERKAYRNQVEESAKQIQVLqvqlqrlhmdMENLQ 505
Cdd:pfam01576 295 RDLGEELEALKTELEDtlDTTAAQQELRSKRE--QEVTELKKALEEETRSHEAQLQEMRQKHTQA----------LEELT 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 506 EEKDteiSSTRDKllsaqdeilllhQAAAKAVSERDTDFMSLQEELKKV---RAELEGWRKAASEYEEEirslqstFQLR 582
Cdd:pfam01576 363 EQLE---QAKRNK------------ANLEKAKQALESENAELQAELRTLqqaKQDSEHKRKKLEGQLQE-------LQAR 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 583 CQQCEVQQREEA---TRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLsilqmtrKE 659
Cdd:pfam01576 421 LSESERQRAELAeklSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRL-------RQ 493
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1958683074 660 LENQMGSLKEQhlrdeadlktlLSKAENQAKDVQKEYEKTQTVLSELKLKFE 711
Cdd:pfam01576 494 LEDERNSLQEQ-----------LEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
212-736 |
4.99e-10 |
|
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: 63.14 E-value: 4.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 212 RLLSRLEVMGNQLQACSKNQTEDSLRKELVALQEDKHSYETTAKESLRRVLQEKIEvvrkLSEVERSlSNTEDECTHLRE 291
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE----LDGFERG-PFSERQIKNFHT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 292 MNERTQEELRELANKyngavnEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTN 371
Cdd:TIGR00606 398 LVIERQEDEAKTAAQ------LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 372 ERLTALQErlLSKSGGDCTFIHQ--FIECQKKLMVQGHLTKVVEESKLSKENQAKAK----ESDLSDTLSPSKEKSSDDT 445
Cdd:TIGR00606 472 RILELDQE--LRKAERELSKAEKnsLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQlnhhTTTRTQMEMLTKDKMDKDE 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 446 TDAQMDEQDLNEPLAKVSLL--KALLEEERKAYRNQVEESAKQIQVLQVQLQRLhmdmENLQEEKDTEISSTRDKLLSAQ 523
Cdd:TIGR00606 550 QIRKIKSRHSDELTSLLGYFpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASL----EQNKNHINNELESKEEQLSSYE 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 524 DEILllhqaAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQC------EVQQREEATRL 597
Cdd:TIGR00606 626 DKLF-----DVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCqrvfqtEAELQEFISDL 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 598 QGELEKLKKEWDVLENECRSLKKENVLL-------SSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSL--K 668
Cdd:TIGR00606 701 QSKLRLAPDKLKSTESELKKKEKRRDEMlglapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTImpE 780
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 669 EQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVL--SELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 736
Cdd:TIGR00606 781 EESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLqgSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
211-559 |
8.14e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 8.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 211 DRLLSRLEVMGNQLQACSKNQTEdsLRKELVALQEDkhsyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLR 290
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAE--LRKELEELEEE-----------LEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 291 EMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEgkqeeiqqkgqAEKKELQAKIDDMEEKEQELQAKIEALQADNDFT 370
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAE-----------AEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 371 NERLTALQERLLSksggdctfihqfiECQKKLMVQGHLTKVVEESKLSKENQAKAKESdlSDTLSPSKEKSSDDTTDAQM 450
Cdd:TIGR02168 816 NEEAANLRERLES-------------LERRIAATERRLEDLEEQIEELSEDIESLAAE--IEELEELIEELESELEALLN 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 451 DEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISStrdklLSAQDEILLlh 530
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER-----LSEEYSLTL-- 953
|
330 340
....*....|....*....|....*....
gi 1958683074 531 QAAAKAVSERDTDFMSLQEELKKVRAELE 559
Cdd:TIGR02168 954 EEAEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
235-729 |
1.42e-09 |
|
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: 61.57 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 235 SLRKELVALQEDKHSYETTAKE--SLRRVLQEKIEVVRKLSEVERSLsntEDECTHLREMNERTQEELRELANKYNGAVN 312
Cdd:TIGR04523 170 ELENELNLLEKEKLNIQKNIDKikNKLLKLELLLSNLKKKIQKNKSL---ESQISELKKQNNQLKDNIEKKQQEINEKTT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 313 EIKDLSDKLKAAEGKQEEIQQKGQAEKKELQ---AKIDDMEEKEQELQAKIEAL--QADNDFTNErltalqerllsksgg 387
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQNKIKKQLSEKQKELEqnnKKIKELEKQLNQLKSEISDLnnQKEQDWNKE--------------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 388 dctfIHQFIECQKKlmvqghlTKVVEESKLSKENQakaKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLK- 466
Cdd:TIGR04523 312 ----LKSELKNQEK-------KLEEIQNQISQNNK---IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKk 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 467 --ALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDT---EISSTRDKLLSAQDEIlllhqaaaKAVSERD 541
Cdd:TIGR04523 378 enQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELlekEIERLKETIIKNNSEI--------KDLTNQD 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 542 TDFMSLQEELKKVRAELEgwrKAASEYEEEIRSLQSTFQLRCQQCEVQQRE------EATRLQGELEKLKKEWDVLENEC 615
Cdd:TIGR04523 450 SVKELIIKNLDNTRESLE---TQLKVLSRSINKIKQNLEQKQKELKSKEKElkklneEKKELEEKVKDLTKKISSLKEKI 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 616 RSLKKENVLLSSELQRQEKEL---------HNSQKQSLELTSDLSILQMTRKELENQMGSLKE---------QHLRDEAD 677
Cdd:TIGR04523 527 EKLESEKKEKESKISDLEDELnkddfelkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQElidqkekekKDLIKEIE 606
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1958683074 678 LKT-LLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKD 729
Cdd:TIGR04523 607 EKEkKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
298-737 |
2.93e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 298 EELRELANKYNGAVNEIkdLSDKLKAAEGKQEEIQQKgqaEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTAL 377
Cdd:PRK02224 165 EEYRERASDARLGVERV--LSDQRGSLDQLKAQIEEK---EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 378 QERLlsksggdctfiHQFIECQKKLMVqghLTKVVEESKLSKENQAKAKEsDLSDTLSPSKEKSSD--DTTDAQMDEQDL 455
Cdd:PRK02224 240 DEVL-----------EEHEERREELET---LEAEIEDLRETIAETERERE-ELAEEVRDLRERLEEleEERDDLLAEAGL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 456 NEPLAK-VSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEK----------DTEISSTRDKLLSAQD 524
Cdd:PRK02224 305 DDADAEaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAeelreeaaelESELEEAREAVEDRRE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 525 EILLLH---QAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTF----QLR----CQQCE------ 587
Cdd:PRK02224 385 EIEELEeeiEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVeeaeALLeagkCPECGqpvegs 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 588 ------VQQREEATRLQGELEKLKKEWDVLENECRSLKKenvllSSELQRQEKELHNSQKQSLELTSDlsilqmTRKELE 661
Cdd:PRK02224 465 phvetiEEDRERVEELEAELEDLEEEVEEVEERLERAED-----LVEAEDRIERLEERREDLEELIAE------RRETIE 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 662 NQmgSLKEQHLRDEA-DLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS------ITDELKQCKDNLKLL 734
Cdd:PRK02224 534 EK--RERAEELRERAaELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESlerirtLLAAIADAEDEIERL 611
|
...
gi 1958683074 735 REK 737
Cdd:PRK02224 612 REK 614
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
466-737 |
3.40e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 466 KALLEEERKAyrnQVEESAKQIQVLQVQLQRLHMDMENLQEEKDtEISSTRDKLLSAQDEIL-LLHQAAAKAVSERDTDF 544
Cdd:TIGR02169 214 QALLKEKREY---EGYELLKEKEALERQKEAIERQLASLEEELE-KLTEEISELEKRLEEIEqLLEELNKKIKDLGEEEQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 545 MSLQEELKKVRAELEGWRKAASEYEEEIRSLQStfqlRCQQCEVQ---QREEATRLQGELEKLKKEWDVLENECRSLKKE 621
Cdd:TIGR02169 290 LRVKEKIGELEAEIASLERSIAEKERELEDAEE----RLAKLEAEidkLLAEIEELEREIEEERKRRDKLTEEYAELKEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 622 NVLLSSELQRQEKEL------HNSQKQSLE-LTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTLLSK---AENQAKD 691
Cdd:TIGR02169 366 LEDLRAELEEVDKEFaetrdeLKDYREKLEkLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKineLEEEKED 445
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1958683074 692 VQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 737
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
205-726 |
4.02e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 4.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 205 QALIDEDRLLsRLEVMGNQLQACSKNQTEDSLRKELVALQEDKHSYETTAKESLRRVLQEKIEVVRK--------LSEVE 276
Cdd:COG1196 216 RELKEELKEL-EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELeleeaqaeEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 277 RSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQEL 356
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 357 QAKIEALQADNDFTNERLTALQERLLSKSGGDCTFIHQFIECQKKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLsp 436
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA-- 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 437 sKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTR 516
Cdd:COG1196 453 -ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIG 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 517 DKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAE-----LEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQQR 591
Cdd:COG1196 532 VEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGratflPLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 592 EEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQH 671
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1958683074 672 LRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 726
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
|
| CC1_T3JAM |
cd21912 |
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ... |
164-204 |
7.26e-09 |
|
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; TRAF3-interacting JNK-activating modulator (T3JAM), also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. The model corresponds to a conserved region that shows high sequence similarity with the first CC (CC1) domain of Sarcolemmal membrane-associated protein (SLMAP), which is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409288 [Multi-domain] Cd Length: 45 Bit Score: 51.96 E-value: 7.26e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1958683074 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21912 5 EILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-737 |
9.05e-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: 9.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 197 QEASDTSWQALIDEDRLLSRLEVMGNQLQacsknqtedSLRKELVALQEDKHSYETTAKESLRRVLQEKI---EVVRKLS 273
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIE---------EERKRRDKLTEEYAELKEELEDLRAELEEVDKefaETRDELK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 274 EVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDK--------------LKAAEGKQEEIQQKGQAEK 339
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKineleeekedkaleIKKQEWKLEQLAADLSKYE 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 340 KE---LQAKIDDMEEKEQELQAKIEALQADNDFTNERLT---ALQERLLSKSGGDCTFIHQFIECQKKLMVQ------GH 407
Cdd:TIGR02169 469 QElydLKEEYDRVEKELSKLQRELAEAEAQARASEERVRggrAVEEVLKASIQGVHGTVAQLGSVGERYATAievaagNR 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 408 LTK-VVEESKLSKENQAKAKESDLS-----------DTLSPSKEKSSDDTTDAQMDEQDLNEPLAK-------------- 461
Cdd:TIGR02169 549 LNNvVVEDDAVAKEAIELLKRRKAGratflplnkmrDERRDLSILSEDGVIGFAVDLVEFDPKYEPafkyvfgdtlvved 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 462 -------------VSLLKALLE----------EERKAYRNQVEESAKqiqvlqvqLQRLHMDMENLQEEKDTeISSTRDK 518
Cdd:TIGR02169 629 ieaarrlmgkyrmVTLEGELFEksgamtggsrAPRGGILFSRSEPAE--------LQRLRERLEGLKRELSS-LQSELRR 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 519 LLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEvQQREEATRLQ 598
Cdd:TIGR02169 700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE-ELEEDLHKLE 778
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 599 GELEKLKKE-----WDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLR 673
Cdd:TIGR02169 779 EALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683074 674 DEA---DLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 737
Cdd:TIGR02169 859 LNGkkeELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
416-736 |
1.27e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 416 KLSKENQAKAKESDLSDTLSP------SKEKSSDDTTDAQMDEQ--DLNEPLAKVSLLKALLEEERKAYRNQVEE-SAKQ 486
Cdd:TIGR02169 202 RLRREREKAERYQALLKEKREyegyelLKEKEALERQKEAIERQlaSLEEELEKLTEEISELEKRLEEIEQLLEElNKKI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 487 IQVLQVQLQRLHMDMENLQeekdTEISSTRDKLLSAQDEILLLHQAAAKAVSERDtdfmSLQEELKKVRAELEGWRKAAS 566
Cdd:TIGR02169 282 KDLGEEEQLRVKEKIGELE----AEIASLERSIAEKERELEDAEERLAKLEAEID----KLLAEIEELEREIEEERKRRD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 567 EYEEEIRSLQSTFQLRCQQCEvQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELhnsqkqsLEL 646
Cdd:TIGR02169 354 KLTEEYAELKEELEDLRAELE-EVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL-------ADL 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 647 TSDLSILQMTRKELENQMGSLKEQHLRDEADLKTL---LSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDE 723
Cdd:TIGR02169 426 NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLaadLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
330
....*....|...
gi 1958683074 724 LKQCKDNLKLLRE 736
Cdd:TIGR02169 506 VRGGRAVEEVLKA 518
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
14-110 |
1.62e-08 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine/threonine-protein kinase MEK1 and similar proteins; MEK1 (EC 2.7.11.1), also known as MRE4, is a meiosis-specific protein kinase required for chromosome synapsis and meiotic recombination. The recruitment and activation of MEK1 require the phosphorylation of the chromosome axis protein Hop1 at Thr318 (pT318), which is necessary for recognition by the MEK1 FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438722 [Multi-domain] Cd Length: 105 Bit Score: 53.00 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 14 SHPFQERHV---YLDEPIKIGRSvARCRPAQNNATfdckvLSRNHALVW---FDHKT-SKFYLQDTkSSNGTFINSQRLS 86
Cdd:cd22670 7 SSPGSTDIVlpiYKNQVITIGRS-PSCDIVINDPF-----VSRTHCRIYsvqFDESSaPLVYVEDL-SSNGTYLNGKLIG 79
|
90 100
....*....|....*....|....*
gi 1958683074 87 RGseespPCEILS-GDIIQFGVDVT 110
Cdd:cd22670 80 RN-----NTVLLSdGDVIEIAHSAT 99
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
228-729 |
2.17e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 228 SKNQTEDSLRKELVALQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERS--LSNTE------------------DECT 287
Cdd:PTZ00121 1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAdeAKKAEekkkadeakkkaeeakkaDEAK 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 288 HLREMNERTQEELRELA----NKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEAL 363
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAeeakKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE 1401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 364 QADNDFTNERLTALQERLLSKSGGDCTFIHQFIECQKKLMVQ---GHLTKVVEESKLSKENQAKAKESDLSDTLSPSKE- 439
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAkkaDEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEe 1481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 440 -KSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYR-------NQVEESAKQIQVLQVQLQRLHMDMENLQE-EKDT 510
Cdd:PTZ00121 1482 aKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEakkadeaKKAEEAKKADEAKKAEEKKKADELKKAEElKKAE 1561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 511 EISSTRDKLLSAQDEILLLHQA--AAKAVSERDTDFMSLQEELKKVRAE----LEGWRKAASEYEEEIRSLQSTFQLRCQ 584
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAeeAKKAEEARIEEVMKLYEEEKKMKAEeakkAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 585 QCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSE--------LQRQEKELHNSQKQSLELTSDLSILQMT 656
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEdekkaaeaLKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683074 657 RKELENQMGSLKEQHLRDEADLKtllsKAENQAKDvQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKD 729
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKK----KAEEAKKD-EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
505-737 |
2.81e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 505 QEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDtdfmSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQL--- 581
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELE----ELEAELAELEAELEELRLELEELELELEEAQAEEYElla 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 582 ---RCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRK 658
Cdd:COG1196 296 elaRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 659 ELENQMGSLKEQHL---RDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLR 735
Cdd:COG1196 376 EAEEELEELAEELLealRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
..
gi 1958683074 736 EK 737
Cdd:COG1196 456 EE 457
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
28-85 |
4.63e-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: 4.63e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683074 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 |
5.58e-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: 5.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 29 KIGRSVARCRPAQNNATFDcKVLSRNHALVWFDHKTS---KFYLQDTkSSNGTFINSQRLSRGSEEsppcEILSGDIIQF 105
Cdd:cd22685 31 RIGRNPEVCDVFLCSSQHP-NLISREHAEIHAERDGNgnwKVLIEDR-STNGTYVNDVRLQDGQRR----ELSDGDTITF 104
|
90
....*....|....*.
gi 1958683074 106 G--VDVTENTRKVTHG 119
Cdd:cd22685 105 GhkNGRRVKQWPYQKS 120
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
236-719 |
8.57e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 8.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 236 LRKELVALQEDKHSY---ETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDEcthlREMNERTQEELRELANKYNGAVN 312
Cdd:PRK03918 170 VIKEIKRRIERLEKFikrTENIEELIKEKEKELEEVLREINEISSELPELREE----LEKLEKEVKELEELKEEIEELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 313 EIKDLSDKLKAAEGKQEEIQQKgqaeKKELQAKIDDMEEKE---QELQAKIEALQADNDFTNERLTALQ--ERLLSKsgg 387
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEER----IEELKKEIEELEEKVkelKELKEKAEEYIKLSEFYEEYLDELReiEKRLSR--- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 388 dctfIHQFIECQKKLMVQGhltkvveESKLSKENQAKAKESDLSDTLSPSKEKSSD-DTTDAQMDE-QDLNEPLAKVSL- 464
Cdd:PRK03918 319 ----LEEEINGIEERIKEL-------EEKEERLEELKKKLKELEKRLEELEERHELyEEAKAKKEElERLKKRLTGLTPe 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 465 -LKALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQE-EKDTEISSTRDKLLSAQDEILLLHQAAA------KA 536
Cdd:PRK03918 388 kLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElKKAKGKCPVCGRELTEEHRKELLEEYTAelkrieKE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 537 VSERDTDFMSLQEELKKVRAELEGWRKAASEYE--EEIRSLQSTFQLRCQQCEVQQREEATRLQGELEKLKKEWDVLENE 614
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 615 CRS---LKKENVLLSSELQRQEKELHNSQKQSLELT-SDLSILQMTRKELE---NQMGSLK--EQHLRDE----ADLKTL 681
Cdd:PRK03918 548 LEKleeLKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEpfyNEYLELKdaEKELEREekelKKLEEE 627
|
490 500 510
....*....|....*....|....*....|....*...
gi 1958683074 682 LSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 719
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR 665
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
135-679 |
9.04e-08 |
|
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: 55.89 E-value: 9.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 135 ARLRSDVIHAPLpSPVDKVAANTPSMYSQELFQL----SQYLQEALHREQMLEQKLATLQRLLAItqeASDTSWQALIDE 210
Cdd:pfam15921 290 ARSQANSIQSQL-EIIQEQARNQNSMYMRQLSDLestvSQLRSELREAKRMYEDKIEELEKQLVL---ANSELTEARTER 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 211 DRLLSRLEVMGNQLQAC----SKNQTEDSLRKELVALQEDKHSYETTAKESLRRVLQEKIEVVRKLS------------E 274
Cdd:pfam15921 366 DQFSQESGNLDDQLQKLladlHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEallkamksecqgQ 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 275 VERSLSNTEDECTHLREMN------ERTQEELR----ELANKYNGAVNEIKDLSDkLKAAEGKQEEIQQKGQAEKKELQA 344
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSsltaqlESTKEMLRkvveELTAKKMTLESSERTVSD-LTASLQEKERAIEATNAEITKLRS 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 345 KIDdmeEKEQELQAkieaLQADNDFTNERLTALQERLLSKSGGD--CTFIHQFIECQKKLMVQGHLTK---VVEESKLSK 419
Cdd:pfam15921 525 RVD---LKLQELQH----LKNEGDHLRNVQTECEALKLQMAEKDkvIEILRQQIENMTQLVGQHGRTAgamQVEKAQLEK 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 420 ENQAKAKESDLSDTLspsKEKSSDDTTDAQMDEQDLNepLAKVSLLKALLE---------EERKAYRNQVEESAKQIQVL 490
Cdd:pfam15921 598 EINDRRLELQEFKIL---KDKKDAKIRELEARVSDLE--LEKVKLVNAGSErlravkdikQERDQLLNEVKTSRNELNSL 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 491 QVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDEillLHQAAAKAVSERDTDFMSLQEELkkvraeleGWRKAASEYEE 570
Cdd:pfam15921 673 SEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSE---LEQTRNTLKSMEGSDGHAMKVAM--------GMQKQITAKRG 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 571 EIRSLQSTFQLrCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQ----KQSLEL 646
Cdd:pfam15921 742 QIDALQSKIQF-LEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEvaldKASLQF 820
|
570 580 590
....*....|....*....|....*....|...
gi 1958683074 647 TSDLSILQmtRKELENQmgSLKEQHLRDEADLK 679
Cdd:pfam15921 821 AECQDIIQ--RQEQESV--RLKLQHTLDVKELQ 849
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
255-621 |
1.33e-07 |
|
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: 55.46 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 255 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQK 334
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 335 GQA---EKKELQAKIDDMEEKEQELQAKIEALQADNDftnerltalqerllsksggdctfiHQFIEcqkklMVQGHLTKV 411
Cdd:TIGR02169 753 IENvksELKELEARIEELEEDLHKLEEALNDLEARLS------------------------HSRIP-----EIQAELSKL 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 412 VE-----ESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQ 486
Cdd:TIGR02169 804 EEevsriEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 487 IQVLQVQLQRLHMDMENLQEEKDtEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEE------LKKVRAELEg 560
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIE-ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsLEDVQAELQ- 961
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683074 561 wrkaasEYEEEIRSLQSTFQLRCQQCEvqqrEEATR---LQGELEKLKKEWDVLE---NECRSLKKE 621
Cdd:TIGR02169 962 ------RVEEEIRALEPVNMLAIQEYE----EVLKRldeLKEKRAKLEEERKAILeriEEYEKKKRE 1018
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
237-661 |
1.36e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 237 RKELVALQEDKHSYETTaKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNER---TQEELRELANKYNgAVNE 313
Cdd:PRK03918 282 VKELKELKEKAEEYIKL-SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERleeLKKKLKELEKRLE-ELEE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 314 IKDLSDKLKAAEGKQEEIQQK-GQAEKKELQAKIDDMEEKEQELQAKIEALQAD----NDFTNERLTALQErlLSKSGGD 388
Cdd:PRK03918 360 RHELYEEAKAKKEELERLKKRlTGLTPEKLEKELEELEKAKEEIEEEISKITARigelKKEIKELKKAIEE--LKKAKGK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 389 CTFIHQFI--ECQKKLMVQGH--LTKVVEESK--LSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEqdLNEPLAKV 462
Cdd:PRK03918 438 CPVCGRELteEHRKELLEEYTaeLKRIEKELKeiEEKERKLRKELRELEKVLKKESELIKLKELAEQLKE--LEEKLKKY 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 463 SLLKalLEEERKAYRNQVEESAKQIQVLQVQLQRLHM--DMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSER 540
Cdd:PRK03918 516 NLEE--LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKleELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEER 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 541 dtdfmslQEELKKVRAELEGWRKAASEYEEEIRSLQStfqlrCQQCEVQQREEATRLQGELEKLKKEWDVL-----ENEC 615
Cdd:PRK03918 594 -------LKELEPFYNEYLELKDAEKELEREEKELKK-----LEEELDKAFEELAETEKRLEELRKELEELekkysEEEY 661
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1958683074 616 RSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELE 661
Cdd:PRK03918 662 EELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
161-736 |
4.22e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.58 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 161 YSQELFQLSQYLQEA--LHREQ--MLEQKLATLQRLLAITQEASDtswqALIDedrlLSRLEvmgNQLQACSKNQTEDSL 236
Cdd:pfam15921 83 YSHQVKDLQRRLNESneLHEKQkfYLRQSVIDLQTKLQEMQMERD----AMAD----IRRRE---SQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 237 RKELVA--LQEDKHSYETTAKESLRR-------VLQEKIEVVRKLSEVERSLSNTEDECT--HLREMNERTQEELRELAN 305
Cdd:pfam15921 152 HELEAAkcLKEDMLEDSNTQIEQLRKmmlshegVLQEIRSILVDFEEASGKKIYEHDSMStmHFRSLGSAISKILRELDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 306 KYNGAVNEIKDLSDKLKAAEGK-QEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQERLLSK 384
Cdd:pfam15921 232 EISYLKGRIFPVEDQLEALKSEsQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 385 sggDCTFIHQFIECQKKLmvqGHLTKVVEESKLSKENQAKAKESDL----SDTLSPSKEKSSDDTTDAQMDEQ------D 454
Cdd:pfam15921 312 ---NSMYMRQLSDLESTV---SQLRSELREAKRMYEDKIEELEKQLvlanSELTEARTERDQFSQESGNLDDQlqkllaD 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 455 LNEPLAKVSLLKallEEERKAYRNQVEESAKQIQVLQVQLQRlHMDMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAA 534
Cdd:pfam15921 386 LHKREKELSLEK---EQNKRLWDRDTGNSITIDHLRRELDDR-NMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLE 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 535 KaVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQQrEEATRLQG-------ELEKLKKE 607
Cdd:pfam15921 462 K-VSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATN-AEITKLRSrvdlklqELQHLKNE 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 608 WDVLEN---ECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMG----SLKE-QHLRDEADLK 679
Cdd:pfam15921 540 GDHLRNvqtECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINdrrlELQEfKILKDKKDAK 619
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683074 680 tlLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 736
Cdd:pfam15921 620 --IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSE 674
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
228-736 |
6.32e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 6.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 228 SKNQTEDSLRKELVALQEDKHSYETTA------KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREmNERTQEELR 301
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKELEELKeeieelEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE-KVKELKELK 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 302 ELANKYNgavnEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKE---QELQAKIEALQadndftnERLTALQ 378
Cdd:PRK03918 290 EKAEEYI----KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEerlEELKKKLKELE-------KRLEELE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 379 ERllsksggdctfiHQFIECQKKLMVQ--GHLTKV----VEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDE 452
Cdd:PRK03918 359 ER------------HELYEEAKAKKEEleRLKKRLtgltPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 453 --QDLNEPLAKVSLLKALLEEERKA-----YRNQVEESAKQIQVLQVQLQRLHMDMENLqeekdteisstrDKLLSAQDE 525
Cdd:PRK03918 427 aiEELKKAKGKCPVCGRELTEEHRKelleeYTAELKRIEKELKEIEEKERKLRKELREL------------EKVLKKESE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 526 ILLLHQAAA--KAVSERDTDFMSlqEELKKVRAELEGWRKAASEYEEEIRSLQSTFqlrcqqcevqqrEEATRLQGELEK 603
Cdd:PRK03918 495 LIKLKELAEqlKELEEKLKKYNL--EELEKKAEEYEKLKEKLIKLKGEIKSLKKEL------------EKLEELKKKLAE 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 604 LKKEWDVLENECRSLKKENVLLS----SELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQhLRDEADLK 679
Cdd:PRK03918 561 LEKKLDELEEELAELLKELEELGfesvEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKA-FEELAETE 639
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958683074 680 TLLSKAENQAKDVQKEY-EKTQTVLSELKLKFEMT----EQEKQSITDELKQCKDNLKLLRE 736
Cdd:PRK03918 640 KRLEELRKELEELEKKYsEEEYEELREEYLELSRElaglRAELEELEKRREEIKKTLEKLKE 701
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
27-106 |
7.46e-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: 7.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 27 PIKIGRSVARcRPAQNNATFDC-----KVLSRNHALVWFDHKTSKFYLQdTKSSNGTFINSQRLSRGseeSPPCEILSGD 101
Cdd:cd22701 18 EVVLGRNSKN-SSSTAADSVDIdlgpsKKISRRHARIFYDFTTQCFELS-VLGRNGVKVDGILVKPG---SPPVPLRSGS 92
|
....*
gi 1958683074 102 IIQFG 106
Cdd:cd22701 93 LIQIG 97
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
26-106 |
1.76e-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: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 26 EPIKIGRSVArcrpaqNNATFDCKVLSRNHALVwfDHKTSKFYLQDTKSSNGTFINSQRLSRGseesppcEILSGDIIQF 105
Cdd:cd22698 21 DEFTIGRSSN------NDIRLNDHSVSRHHARI--VRQGDKCNLTDLGSTNGTFLNGIRVGTH-------ELKHGDRIQL 85
|
.
gi 1958683074 106 G 106
Cdd:cd22698 86 G 86
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
256-737 |
1.89e-06 |
|
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: 51.71 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 256 ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQE---ELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQ 332
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETElcaEAEEMRARLAARKQELEEILHELESRLEEEEERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 333 QKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQERLLSKSGGDCTFIHQFIECQKKLM-VQGHLTKV 411
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISeFTSNLAEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 412 VEESK-LSK-ENQAKAKESDLSDTL----------SPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQ 479
Cdd:pfam01576 172 EEKAKsLSKlKNKHEAMISDLEERLkkeekgrqelEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALAR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 480 VEESAKQIQVLQVQLQRLHMDMENLQEEKDTEiSSTRDKlLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVR-AEL 558
Cdd:pfam01576 252 LEEETAQKNNALKKIRELEAQISELQEDLESE-RAARNK-AEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKReQEV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 559 EGWRKAAseyEEEIRSLQSTFQlRCQQCEVQQREEatrLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHN 638
Cdd:pfam01576 330 TELKKAL---EEETRSHEAQLQ-EMRQKHTQALEE---LTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 639 SQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLK---TLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQ 715
Cdd:pfam01576 403 SEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELEsvsSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETR 482
|
490 500
....*....|....*....|..
gi 1958683074 716 EKQSITDELKQCKDNLKLLREK 737
Cdd:pfam01576 483 QKLNLSTRLRQLEDERNSLQEQ 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
413-732 |
1.91e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 413 EESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQM---DEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQV 489
Cdd:TIGR02169 690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQleqEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 490 LQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDEIlllhqaaakaVSERDTDFMSLQEELKKVRAELEGWRKAASEYE 569
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEE----------VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 570 EEIRSLQSTFQLRCQQCEVQQREEAtRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSD 649
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKE-ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 650 LSILQMTRKELENQMGSLKEQHLRDEADLKTLLS----KAENQAKDVQ------------KEYEKTQTVLSELKLKFEMT 713
Cdd:TIGR02169 919 LSELKAKLEALEEELSEIEDPKGEDEEIPEEELSledvQAELQRVEEEiralepvnmlaiQEYEEVLKRLDELKEKRAKL 998
|
330
....*....|....*....
gi 1958683074 714 EQEKQSITDELKQCkDNLK 732
Cdd:TIGR02169 999 EEERKAILERIEEY-EKKK 1016
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
25-114 |
1.94e-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: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 25 DEPIKIGRSVArcrpAQNNATFDC-KVLSRNHALVWFDHKTSKFyLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDII 103
Cdd:cd22663 20 GKEVTVGRGLG----VTYQLVSTCpLMISRNHCVLKKNDEGQWT-IKDNKSLNGVWVNGERI----EPLKPYPLNEGDLI 90
|
90
....*....|.
gi 1958683074 104 QFGVDVTENTR 114
Cdd:cd22663 91 QLGVPPENKEP 101
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
27-117 |
1.97e-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: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 27 PIKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLsrgSEESPPCEILSGDIIQFG 106
Cdd:cd22678 24 PLTIGRIQ------RGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESI---SPNGRPVVLSSGDVITLG 94
|
90
....*....|.
gi 1958683074 107 vdvTENTRKVT 117
Cdd:cd22678 95 ---SETKILVR 102
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
289-737 |
3.03e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 289 LREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKgQAEKKELQAKIDDMEEKEQELQAKIEALQADND 368
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 369 F--TNERLTALQERLlsksggdctfiHQFIECQKKLMVQGHLTKVVEESKLSKENQAKAKESDLsdtlspsKEKSSDDTT 446
Cdd:COG4717 127 LlpLYQELEALEAEL-----------AELPERLEELEERLEELRELEEELEELEAELAELQEEL-------EELLEQLSL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 447 DAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDmENLQEEKDT--------EISSTRDK 518
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-ERLKEARLLlliaaallALLGLGGS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 519 LLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRcQQCEVQQREEATRLQ 598
Cdd:COG4717 268 LLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLP-PDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 599 GELEKLKKEWDVLENE---CRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQ-HLRD 674
Cdd:COG4717 347 EELQELLREAEELEEElqlEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELlEALD 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958683074 675 EADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEK--QSITDELKQCKDNLKLLREK 737
Cdd:COG4717 427 EEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRELAEE 491
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
55-108 |
3.56e-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: 3.56e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1958683074 55 HALVWFDHKTSKFYLQDTKSSNGTFINSQRLSrgseESPPCEILSGDIIQFGVD 108
Cdd:cd22704 39 HAVITYDQIDNEFKIKDLGSLNGTFVNDSRIP----EQTYITLKLGDSIRFGYD 88
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
470-737 |
3.71e-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: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 470 EEERKAY----RNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFM 545
Cdd:pfam17380 304 EKEEKAReverRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 546 SLQEELK--KVRAELEGWRKAASEYEEEIRSLQStfQLRCQQCEVQQREEATrlQGELEKLKKEwdvLENECRSLKKENV 623
Cdd:pfam17380 384 QMERQQKneRVRQELEAARKVKILEEERQRKIQQ--QKVEMEQIRAEQEEAR--QREVRRLEEE---RAREMERVRLEEQ 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 624 LLSSELQRQEKELHNSQKQSLELTSDlsilQMTRKELENQMGSLKEQHLRDEadlKTLLSKAENQAKDVQKEYEKTQTVL 703
Cdd:pfam17380 457 ERQQQVERLRQQEEERKRKKLELEKE----KRDRKRAEEQRRKILEKELEER---KQAMIEEERKRKLLEKEMEERQKAI 529
|
250 260 270
....*....|....*....|....*....|....*
gi 1958683074 704 SELKLKFEMTEQ-EKQSITDELKQCKDNLKLLREK 737
Cdd:pfam17380 530 YEEERRREAEEErRKQQEMEERRRIQEQMRKATEE 564
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
245-722 |
4.75e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.11 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 245 EDKHSYETTAKES-LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKA 323
Cdd:pfam05483 228 EEEYKKEINDKEKqVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 324 AEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAK-------IEALQADNDFTNERLTALQERLLSKsggdctfihqfi 396
Cdd:pfam05483 308 SMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAkaahsfvVTEFEATTCSLEELLRTEQQRLEKN------------ 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 397 ECQKKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAY 476
Cdd:pfam05483 376 EDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDL 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 477 RNQVEESAKQIQVLQVQLQRLHMDMENlQEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRA 556
Cdd:pfam05483 456 EIQLTAIKTSEEHYLKEVEDLKTELEK-EKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLK 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 557 ELEGWRKAASEYEEEIRSLQSTFQLRCQQ--CEVQQREEATR-LQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQE 633
Cdd:pfam05483 535 QIENLEEKEMNLRDELESVREEFIQKGDEvkCKLDKSEENARsIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELH 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 634 KELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSE-LKLKFEM 712
Cdd:pfam05483 615 QENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEaVKLQKEI 694
|
490
....*....|
gi 1958683074 713 TEQEKQSITD 722
Cdd:pfam05483 695 DKRCQHKIAE 704
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
178-365 |
5.40e-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: 5.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 178 REQML--EQKLATLQRLLAITQEAsDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKELVALQEDKhsyetTAK 255
Cdd:COG4913 241 HEALEdaREQIELLEPIRELAERY-AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAEL-----ERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 256 ESLRRVLQEKIEVVR---------KLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEG 326
Cdd:COG4913 315 EARLDALREELDELEaqirgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE 394
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958683074 327 KQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQA 365
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
223-698 |
6.24e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.05 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 223 QLQACSKNQTEDSLRKELVALQEDKHSYE--------TTAKESLRRVLQEKIEVVRK-----------LSEVERSLSNTE 283
Cdd:TIGR00606 597 NKELASLEQNKNHINNELESKEEQLSSYEdklfdvcgSQDEESDLERLKEEIEKSSKqramlagatavYSQFITQLTDEN 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 284 DECTHLREMNERTQEELRE----LANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAK 359
Cdd:TIGR00606 677 QSCCPVCQRVFQTEAELQEfisdLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKV 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 360 IEALQADNDFTNERLTAL-----QERLLSKSGGDCTFIHQFIECQKklmvqghltkvvEESKLSKENQAKAKESDLSDTL 434
Cdd:TIGR00606 757 NRDIQRLKNDIEEQETLLgtimpEEESAKVCLTDVTIMERFQMELK------------DVERKIAQQAAKLQGSDLDRTV 824
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 435 SPSKEKSSDDttdaqmdEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQRLHM--DMENLQEEKDTEI 512
Cdd:TIGR00606 825 QQVNQEKQEK-------QHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRrqQFEEQLVELSTEV 897
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 513 SSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQQRE 592
Cdd:TIGR00606 898 QSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKET 977
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 593 EATRLQGELEKLKKEWDVLENECRSLKKenvllSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMG-----SL 667
Cdd:TIGR00606 978 ELNTVNAQLEECEKHQEKINEDMRLMRQ-----DIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGqmqvlQM 1052
|
490 500 510
....*....|....*....|....*....|.
gi 1958683074 668 KEQHLRDEADLKtLLSKAENQAKDVQKEYEK 698
Cdd:TIGR00606 1053 KQEHQKLEENID-LIKRNHVLALGRQKGYEK 1082
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
310-578 |
7.91e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 7.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 310 AVNEIKDLSDKLKAAEGKQEEIQqkgqAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQERLLSKsggdc 389
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQ----AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 390 tfihqfiecqkklmvqghltkvveESKLSKENQAKAKESDLSDTLspskekssddttDAQMDEQDLNEPLAKVSLLKALL 469
Cdd:COG3883 85 ------------------------REELGERARALYRSGGSVSYL------------DVLLGSESFSDFLDRLSALSKIA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 470 EEERKAYRNQVEESAKQiqvlqvqlqrlhmdmenlqEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQE 549
Cdd:COG3883 129 DADADLLEELKADKAEL-------------------EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189
|
250 260
....*....|....*....|....*....
gi 1958683074 550 ELKKVRAELEGWRKAASEYEEEIRSLQST 578
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
153-381 |
1.11e-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: 48.22 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 153 VAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgNQLQAcsKNQT 232
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE---QELAA--LEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 233 EDSLRKELVALQEDKhsyettakESLRRVLQEKIEVVRKLSEVER--SLSNTEDECTHLR--EMNERTQEELRELANKYN 308
Cdd:COG4942 85 LAELEKEIAELRAEL--------EAQKEELAELLRALYRLGRQPPlaLLLSPEDFLDAVRrlQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683074 309 GAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQERL 381
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
229-740 |
1.22e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.95 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 229 KNQTEDSLRKELVALQEDKHSYETTAK---------ESLRRVLQEKIEVVRKLSEVERSlsnTEDECTHLREMNERTQEE 299
Cdd:pfam05483 94 KVSIEAELKQKENKLQENRKIIEAQRKaiqelqfenEKVSLKLEEEIQENKDLIKENNA---TRHLCNLLKETCARSAEK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 300 LRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEAlQADNDFTNERLTALQE 379
Cdd:pfam05483 171 TKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKK-EINDKEKQVSLLLIQI 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 380 RLLSKSGGDCTFIHQfiECQKKLmvqghlTKVVEESKLSKENQAKAKESdlSDTLSPSKEKSSDDTTDAQMDEQDLNEPL 459
Cdd:pfam05483 250 TEKENKMKDLTFLLE--ESRDKA------NQLEEKTKLQDENLKELIEK--KDHLTKELEDIKMSLQRSMSTQKALEEDL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 460 AKVSLLKALLEEERKAyrnQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEisstRDKLLSAQDEILLLHQAAAKAVSE 539
Cdd:pfam05483 320 QIATKTICQLTEEKEA---QMEELNKAKAAHSFVVTEFEATTCSLEELLRTE----QQRLEKNEDQLKIITMELQKKSSE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 540 RD--TDFMSLQE----ELKKVRAELEGWRKAASEYEEEIRSLQSTFQlrcqqcevqqreeatRLQGELEKLKKEWDVLEN 613
Cdd:pfam05483 393 LEemTKFKNNKEveleELKKILAEDEKLLDEKKQFEKIAEELKGKEQ---------------ELIFLLQAREKEIHDLEI 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 614 ECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSL--------------KEQHLRDEADLK 679
Cdd:pfam05483 458 QLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMtlelkkhqediincKKQEERMLKQIE 537
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958683074 680 TLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREKGNN 740
Cdd:pfam05483 538 NLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN 598
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
234-711 |
1.42e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 234 DSLRKELVALQEDKHSYETtAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNER--TQEELRELANKYNGAV 311
Cdd:COG4717 74 KELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELeaLEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 312 NEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQERLlsksggdctf 391
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL---------- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 392 ihQFIECQKKLMVQGHLTKVVEEsKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMdeqdLNEPLAKVSLLKALLEE 471
Cdd:COG4717 223 --EELEEELEQLENELEAAALEE-RLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV----LFLVLGLLALLFLLLAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 472 ERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDkLLSAQDEILLLHQAAAKAVSERDtdfmslQEEL 551
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLE-LLDRIEELQELLREAEELEEELQ------LEEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 552 KKVRAELegWRKAASEYEEEIRSLQSTFQLRcqqceVQQREEATRLQGELEKLKKEWdvlenecrslkkENVLLSSELQR 631
Cdd:COG4717 369 EQEIAAL--LAEAGVEDEEELRAALEQAEEY-----QELKEELEELEEQLEELLGEL------------EELLEALDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 632 QEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEA--DLKTLLSKAENQAKDVQKeYEKTQTVLSELKLK 709
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELlqELEELKAELRELAEEWAA-LKLALELLEEAREE 508
|
..
gi 1958683074 710 FE 711
Cdd:COG4717 509 YR 510
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
239-707 |
1.56e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.58 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 239 ELVALQEDKHSYETTAK--ESLRRVLQEKIE-----VVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAV 311
Cdd:pfam15921 279 EITGLTEKASSARSQANsiQSQLEIIQEQARnqnsmYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 312 NEIKDLSDKLKAAEGKQEEiqqkgqaekkELQAKIDDMEEKEQELQAKIEalqadndfTNERLTAlqerllSKSGGDCTF 391
Cdd:pfam15921 359 TEARTERDQFSQESGNLDD----------QLQKLLADLHKREKELSLEKE--------QNKRLWD------RDTGNSITI 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 392 IHQFIECQKKLMVQGHLTKVVEESKLSKENQAKAKESDLsdtlspskekssddttdaqmdeQDLNEPLAKVSLLKALLEE 471
Cdd:pfam15921 415 DHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAI----------------------QGKNESLEKVSSLTAQLES 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 472 ERKAYRNQVEE-SAKQIQVLQVQlqRLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDtDFMSLQEE 550
Cdd:pfam15921 473 TKEMLRKVVEElTAKKMTLESSE--RTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGD-HLRNVQTE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 551 LKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQQREEAtRLQGELEKLK---KEWDVLENECRSLKKENVLLSS 627
Cdd:pfam15921 550 CEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKA-QLEKEINDRRlelQEFKILKDKKDAKIRELEARVS 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 628 ELQRQEKELHNSQKQSLELTSD--------LSILQMTRKELEN---QMGSLKEQHLRDEADLKTLLSKAENQAKDVQKEY 696
Cdd:pfam15921 629 DLELEKVKLVNAGSERLRAVKDikqerdqlLNEVKTSRNELNSlseDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSEL 708
|
490
....*....|.
gi 1958683074 697 EKTQTVLSELK 707
Cdd:pfam15921 709 EQTRNTLKSME 719
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
267-737 |
1.59e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 267 EVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKI 346
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 347 DDMEEKEQE---LQAKIEALQADNDFTNERLTALQERLLSKSGGDCTFIHQFIECQKKLmvqgHLTKVVEESKLSKENQA 423
Cdd:TIGR04523 117 EQKNKLEVElnkLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENEL----NLLEKEKLNIQKNIDKI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 424 KAKESDLSDTLSPSKEKSSDDTTDaqmdEQDLNEPLAKVSLLKALLEEERKAYrNQVEESAKQIQVLQVQLQRLHMDMEN 503
Cdd:TIGR04523 193 KNKLLKLELLLSNLKKKIQKNKSL----ESQISELKKQNNQLKDNIEKKQQEI-NEKTTEISNTQTQLNQLKDEQNKIKK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 504 LQEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMS-LQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLR 582
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKeLKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 583 CQQCEVQQREEATrLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELEN 662
Cdd:TIGR04523 348 KKELTNSESENSE-KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 663 QMGSLKEQHLRDEA-----------------DLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELK 725
Cdd:TIGR04523 427 EIERLKETIIKNNSeikdltnqdsvkeliikNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
490
....*....|..
gi 1958683074 726 QCKDNLKLLREK 737
Cdd:TIGR04523 507 ELEEKVKDLTKK 518
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
52-106 |
2.03e-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: 2.03e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683074 52 SRNH-ALVWfdHK-TSKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22674 48 SRVHaALVY--HKhLNRVFLIDLGSTHGTFVGGIRL----EPHKPQQLPIDSTLRFG 98
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
526-737 |
2.32e-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: 47.45 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 526 ILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQStfQLRCQQCEVQQRE-EATRLQGELEKL 604
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER--RIAALARRIRALEqELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 605 KKEWDVLENECRSLKKE-----------------NVLLSSE-LQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGS 666
Cdd:COG4942 89 EKEIAELRAELEAQKEElaellralyrlgrqpplALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958683074 667 LKEQHlrdeADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 737
Cdd:COG4942 169 LEAER----AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
51-106 |
2.33e-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: 2.33e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683074 51 LSRNHALVWF----DHKTSKFYLQDTKSSNGTFINSQRLsrgseesPP---CEILSGDIIQFG 106
Cdd:cd22677 41 ISRYHAVLQYrgdaDDHDGGFYLYDLGSTHGTFLNKQRI-------PPkqyYRLRVGHVLKFG 96
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
28-106 |
2.67e-05 |
|
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438732 [Multi-domain] Cd Length: 96 Bit Score: 43.48 E-value: 2.67e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683074 28 IKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDhkTSKFYLQDTKSSNGTFINSQRlsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22680 23 VSIGRDP------ENVIVIPDPFVSRNHARITVD--SNEIYIEDLGSTNGTFVNDFK-----RIKGPAKLHPNDIIKLG 88
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
231-737 |
2.76e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 231 QTEDSLRKELVALQEDKHSYETTAK-ESLRRV--LQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKy 307
Cdd:PTZ00121 1201 KAEAARKAEEERKAEEARKAEDAKKaEAVKKAeeAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK- 1279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 308 ngaVNEIKDLSDKLKAAEGKQEEIQQKGQAEKK--ELQAKIDDMEEKEQELQAKIEALQADNDftnerltalqerllsks 385
Cdd:PTZ00121 1280 ---ADELKKAEEKKKADEAKKAEEKKKADEAKKkaEEAKKADEAKKKAEEAKKKADAAKKKAE----------------- 1339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 386 ggdctfihqfiECQKKLMVQGhltkvvEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSll 465
Cdd:PTZ00121 1340 -----------EAKKAAEAAK------AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA-- 1400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 466 kalleEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFM 545
Cdd:PTZ00121 1401 -----EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEA 1475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 546 SLQEELKKVRAELegwRKAASEYEEEIRSLQSTFQLRCQQCEVQQREEATRLQgELEKL--KKEWDVLENECRSLKKENV 623
Cdd:PTZ00121 1476 KKKAEEAKKADEA---KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAD-EAKKAeeAKKADEAKKAEEKKKADEL 1551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 624 LLSSELQRQEKELHNSQKQSLELTSDLSILQMTR-KELENQMGSLKEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTV 702
Cdd:PTZ00121 1552 KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE 1631
|
490 500 510
....*....|....*....|....*....|....*
gi 1958683074 703 LSELKLKFEMTEQEKQSiTDELKQCKDNLKLLREK 737
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKK-AEELKKAEEENKIKAAE 1665
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
276-724 |
2.78e-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: 47.86 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 276 ERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAE---GKQEEIQQKGQAEKKELQAKIDDMEEK 352
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETelcAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 353 EQELQAKIEALQADNDFTNERLTALQERLLSKSGGDCTFIHQFIECQKKL--MVQGHLTKVVEESKLSKENQA-KAKESD 429
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIkkLEEDILLLEDQNSKLSKERKLlEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 430 LSDTLSPSKEKSsddttdaqmdeQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQ---E 506
Cdd:pfam01576 164 FTSNLAEEEEKA-----------KSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQaqiA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 507 EKDTEISSTRDKLLSAQ---DEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRC 583
Cdd:pfam01576 233 ELRAQLAKKEEELQAALarlEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 584 QQCEVQQREEATRLQgELEKLKKewdVLENECRslkkenvllSSELQRQEKELHNSQkQSLELTSDLSILQMTRKELENQ 663
Cdd:pfam01576 313 DTTAAQQELRSKREQ-EVTELKK---ALEEETR---------SHEAQLQEMRQKHTQ-ALEELTEQLEQAKRNKANLEKA 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958683074 664 MGSLKEQHLRDEADLKTLlskaeNQAK-DVQKEYEKTQTVLSELKLKFEMTEQEKQSITDEL 724
Cdd:pfam01576 379 KQALESENAELQAELRTL-----QQAKqDSEHKRKKLEGQLQELQARLSESERQRAELAEKL 435
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
14-106 |
2.96e-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: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 14 SHPFQERHvyldepIKIGRSVarcrpaQNNATFDCKVLSRNHALvwFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEesp 93
Cdd:cd22682 14 QFPITEST------IVIGRSV------ESQVQIDDDSVSRYHAK--LAVNPSAVSIIDLGSTNGTIVNGKKIPKLAS--- 76
|
90
....*....|...
gi 1958683074 94 pCEILSGDIIQFG 106
Cdd:cd22682 77 -CDLQNGDQIKIG 88
|
|
| FHA_RAD53-like_rpt2 |
cd22690 |
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
12-103 |
2.97e-05 |
|
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine/threonine-protein kinase RAD53 and similar proteins; RAD53, also called CHEK2 homolog, or serine-protein kinase 1 (Spk1), is a nuclear protein kinase that phosphorylates proteins on serine, threonine, and tyrosine. It controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints and prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. It may be involved in the phosphorylation of RPH1. RAD53 contains two FHA domains. This model corresponds to the second one. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438742 [Multi-domain] Cd Length: 105 Bit Score: 43.43 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 12 PNSHPfqerHVYL-DEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTSKF---YLQDTkSSNGTFINSQRLSR 87
Cdd:cd22690 8 NPSYP----DIELtQNTTFIGRS------KDCDEEITDPRISKHHCIITRKRSGKGLddvYVTDT-STNGTFINNNRLGK 76
|
90
....*....|....*.
gi 1958683074 88 GSEesppCEILSGDII 103
Cdd:cd22690 77 GSQ----SLLQDGDEI 88
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
167-559 |
4.18e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQAcsKNQTEDSLRKELVALQED 246
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE--LEEAEEALLERLERLEEE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 247 KHSYETTAKESLRRVLQEKievvRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEG 326
Cdd:COG1196 423 LEELEEALAELEEEEEEEE----EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 327 KQEEIQQKGQAEKKELQAK--------IDDMEEKEQELQAKIEA-----LQADNDFTNERLTALQERLLSKSGGDCTFI- 392
Cdd:COG1196 499 AEADYEGFLEGVKAALLLAglrglagaVAVLIGVEAAYEAALEAalaaaLQNIVVEDDEVAAAAIEYLKAAKAGRATFLp 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 393 ------------------------------HQFIECQKKLMVQGHLTKVVEESKLSKENQAKAKESDL------SDTLSP 436
Cdd:COG1196 579 ldkiraraalaaalargaigaavdlvasdlREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLrevtleGEGGSA 658
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 437 SKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEisstR 516
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE----R 734
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1958683074 517 DKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELE 559
Cdd:COG1196 735 EELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
500-739 |
4.82e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 500 DMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKaVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQStf 579
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEK-LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE-- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 580 QLRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRK- 658
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKk 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 659 --ELENQMGSLKEQHLRDEaDLKTLLSKAENQAKdvqkeyEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 736
Cdd:PRK03918 347 lkELEKRLEELEERHELYE-EAKAKKEELERLKK------RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
...
gi 1958683074 737 KGN 739
Cdd:PRK03918 420 EIK 422
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
13-110 |
6.44e-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: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 13 NSHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTskFYLQDTKSSNGTFINSQRLSrgsee 91
Cdd:cd22665 7 SQAHGPEKDFPLYEgENVIGRD------PSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRL----- 73
|
90 100
....*....|....*....|.
gi 1958683074 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 |
6.82e-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: 6.82e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958683074 52 SRNHALVWFDH---------KTSKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQFGV 107
Cdd:cd22667 40 SRKHATLTVLHpeanlsdpdTRPELTLKDL-SKYGTFVNGEKLKGGSE----VTLKDGDVITFGV 99
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
532-726 |
7.67e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 532 AAAKAVSERDTDFMSLQEELKKVRAE---LEGWRKAASEYEE------EIRSLQSTFQL--------RCQQCEVQQREEA 594
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQielLEPIRELAERYAAarerlaELEYLRAALRLwfaqrrleLLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 595 TRLQGELEKLKKEWDVLENECRSLKKE------NVL--LSSELQRQEKELHNsqkqsleltsdlsiLQMTRKELENQMGS 666
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQirgnggDRLeqLEREIERLERELEE--------------RERRRARLEALLAA 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 667 LKEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 726
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
210-553 |
8.79e-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: 46.21 E-value: 8.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 210 EDRLLSRLEVMGNQLQacsKNQTEDSLRKELVALQEDKHSYETTAK--------ESLRRVLQEKIEVVRKLSEVERSLSN 281
Cdd:TIGR02169 186 IERLDLIIDEKRQQLE---RLRREREKAERYQALLKEKREYEGYELlkekealeRQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 282 TEDECTH----LREMNER----TQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQ---QKGQAEKKELQAKIDDME 350
Cdd:TIGR02169 263 LEKRLEEieqlLEELNKKikdlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEerlAKLEAEIDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 351 EKEQELQAKIEALQADNDFTNERLTALQERLLSKSGGDCTFIHQFIECQKKLmvqghltkvveESKLSKENQAKAKESDL 430
Cdd:TIGR02169 343 REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL-----------EKLKREINELKRELDRL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 431 SDTLSPSKEKSSDDTTDAQMDEQDLNEplakvsllkalLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEekdt 510
Cdd:TIGR02169 412 QEELQRLSEELADLNAAIAGIEAKINE-----------LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKE---- 476
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1958683074 511 EISSTRDKLLSAQDEILLLhQAAAKAVSERDTDFMSLQEELKK 553
Cdd:TIGR02169 477 EYDRVEKELSKLQRELAEA-EAQARASEERVRGGRAVEEVLKA 518
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
526-736 |
8.83e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 8.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 526 ILLLHQAAAKAVSERDtdfmSLQEELKKVRAELEGWRKAASEYEEEIRSLQStfQLRcqqcevQQREEATRLQGELEKLK 605
Cdd:COG4942 8 ALLLALAAAAQADAAA----EAEAELEQLQQEIAELEKELAALKKEEKALLK--QLA------ALERRIAALARRIRALE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 606 KEWDVLENECRSLKKENVLLSSELQRQEKELHN------------------SQKQSLELTSDLSILQMTRKELENQMGSL 667
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEELAEllralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683074 668 KEQhLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMT----EQEKQSITDELKQCKDNLKLLRE 736
Cdd:COG4942 156 RAD-LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLlarlEKELAELAAELAELQQEAEELEA 227
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
328-576 |
9.22e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 9.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 328 QEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQERLlsksggdctfihQFIECQKKLMVQGH 407
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI------------RALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 408 LTKVVEESKLskENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKayrnQVEEsakqi 487
Cdd:COG4942 86 AELEKEIAEL--RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARRE----QAEE----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 488 qvlqvqlqrLHMDMENLQEEKDtEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASE 567
Cdd:COG4942 155 ---------LRADLAELAALRA-ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
....*....
gi 1958683074 568 YEEEIRSLQ 576
Cdd:COG4942 225 LEALIARLE 233
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
18-86 |
1.32e-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: 1.32e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683074 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 |
1.69e-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: 1.69e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683074 49 KVLSRNHALVWFDHKTsKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQF 105
Cdd:cd22672 39 KLVSGDHCKIIRDEKG-QVWLEDT-STNGTLVNKVKVVKGQK----VELKHGDVIYL 89
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
238-380 |
2.20e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 238 KELVALQEDKHSYETTAKESLRRV--LQEKIE-VVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEI 314
Cdd:PRK02224 488 EEEVEEVEERLERAEDLVEAEDRIerLEERREdLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEA 567
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683074 315 KDLSDKLKAAEGKQEEIQQKGQAEKK--ELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQER 380
Cdd:PRK02224 568 EEAREEVAELNSKLAELKERIESLERirTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRER 635
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
163-362 |
3.44e-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: 43.60 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALID--------EDRLLSRLEVMGNQLQACSKNQTED 234
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekeiaelRAELEAQKEELAELLRALYRLGRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 235 SLrkELVALQEDKHSYETTAK--ESLRRVLQEKIEVVRK-LSEVERSLSNTEDECTHLREMNERTQEELRELANkyngAV 311
Cdd:COG4942 121 PL--ALLLSPEDFLDAVRRLQylKYLAPARREQAEELRAdLAELAALRAELEAERAELEALLAELEEERAALEA----LK 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958683074 312 NEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEA 362
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
163-348 |
3.64e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWqALIDEDRLLSRLEVMGNQLQACSKNQTE-DSLRKELV 241
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-DEIDVASAEREIAELEAELERLDASSDDlAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 242 ALQEDKhsyeTTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDEcthLREMNERTQEELRELANKYNGAVNEIKDLSDKL 321
Cdd:COG4913 696 ELEAEL----EELEEELDELKGEIGRLEKELEQAEEELDELQDR---LEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
170 180
....*....|....*....|....*..
gi 1958683074 322 KAAEGKQEEIQQKGQAEKKELQAKIDD 348
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAMRA 795
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
208-366 |
3.71e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 208 IDEDRLLSRLEVMGNQLQACSKNQTE---DSLRKELVALQED-KHSYETTAKEslrrvLQEKIEVVRKLSEVERSLsnte 283
Cdd:PRK04778 249 LDHLDIEKEIQDLKEQIDENLALLEEldlDEAEEKNEEIQERiDQLYDILERE-----VKARKYVEKNSDTLPDFL---- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 284 decTHLREMNERTQEELRELANKY---NGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKK---ELQAKIDDMEEKEQELQ 357
Cdd:PRK04778 320 ---EHAKEQNKELKEEIDRVKQSYtlnESELESVRQLEKQLESLEKQYDEITERIAEQEIaysELQEELEEILKQLEEIE 396
|
....*....
gi 1958683074 358 AKIEALQAD 366
Cdd:PRK04778 397 KEQEKLSEM 405
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
212-621 |
3.90e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 212 RLLSRLEVMGNQLQACSKNQTEdsLRKELVALQEDKHSYETTAK-ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLR 290
Cdd:COG4717 92 ELQEELEELEEELEELEAELEE--LREELEKLEKLLQLLPLYQElEALEAELAELPERLEELEERLEELRELEEELEELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 291 EMNERTQEELRELANKYNGAV-NEIKDLSDKLKAAegkqeeiqqkgQAEKKELQAKIDDMEEKEQELQAKIEALQAD--N 367
Cdd:COG4717 170 AELAELQEELEELLEQLSLATeEELQDLAEELEEL-----------QQRLAELEEELEEAQEELEELEEELEQLENEleA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 368 DFTNERLTALQERLLSKSGGDCTFIHQFIECQKKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTlspskEKSSDDTTD 447
Cdd:COG4717 239 AALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA-----EELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 448 AQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQRLhmDMENLQEEKDTEISSTRDKLLSAQDEIL 527
Cdd:COG4717 314 EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAALLAEAGVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 528 LLHQAAAKAVSERDTDFMSLQEELKKVRAEL-----EGWRKAASEYEEEIRSLQSTF-QLRCQQCEVQQREEATRLQGEL 601
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGELEELLealdeEELEEELEELEEELEELEEELeELREELAELEAELEQLEEDGEL 471
|
410 420
....*....|....*....|
gi 1958683074 602 EKLKKEWDVLENECRSLKKE 621
Cdd:COG4717 472 AELLQELEELKAELRELAEE 491
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
182-613 |
4.30e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 182 LEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgnqlqacSKNQTEDSLRKELVALQEDKHSYETTaKESLRRV 261
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHE---------ERREELETLEAEIEDLRETIAETERE-REELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 262 LQEKIEVVRKLSE------VERSLSNTEDECTHLR-----EMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEE 330
Cdd:PRK02224 281 VRDLRERLEELEEerddllAEAGLDDADAEAVEARreeleDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 331 IQQKGQAEKKELQA---KIDDMEEKEQELQAKIEALQADNDFTNERLTALQERLlsksggdctfihqfiecqkklmvqgh 407
Cdd:PRK02224 361 LREEAAELESELEEareAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL-------------------------- 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 408 ltkvveESKLSKENQAKAKESDLSDTLSPSKEKSSDdtTDAQMDEQDLNE---PLAKVSLLKALLEeerkaYRNQVEESA 484
Cdd:PRK02224 415 ------EELREERDELREREAELEATLRTARERVEE--AEALLEAGKCPEcgqPVEGSPHVETIEE-----DRERVEELE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 485 KQIQVLQVQLQRLHMDMENLQEEKDTEisSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKA 564
Cdd:PRK02224 482 AELEDLEEEVEEVEERLERAEDLVEAE--DRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREA 559
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1958683074 565 ASEYEEEIRSlqstfqlrcqqcevqQREEATRLQGELEKLKKEWDVLEN 613
Cdd:PRK02224 560 AAEAEEEAEE---------------AREEVAELNSKLAELKERIESLER 593
|
|
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
53-106 |
4.57e-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: 4.57e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1958683074 53 RNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPceilsGDIIQFG 106
Cdd:cd22700 36 EQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAP-----GDVLRFG 84
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
234-387 |
4.69e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 234 DSLRKELVALQEDKHSYET--TAKESLRRVLQEKIEVVR-KLSEV--ERSLSNTEDECTHLREMNERTQEELRELANKYN 308
Cdd:COG1579 41 AALEARLEAAKTELEDLEKeiKRLELEIEEVEARIKKYEeQLGNVrnNKEYEALQKEIESLKRRISDLEDEILELMERIE 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683074 309 GAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEalqadndftnERLTALQERLLSKSGG 387
Cdd:COG1579 121 ELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP----------PELLALYERIRKRKNG 189
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
25-108 |
4.73e-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: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 25 DEPIKIGRsvarcRPAQNNAT----FDCKVLSRNHALVWFdhKTSKFYLQDTKSSNGTFINSQRLSR-GSEESPPCEILS 99
Cdd:cd22702 31 KQPCIIGS-----DPHQAISGisvvIPSPQVSELHARITC--KNGAFFLTDLGSEHGTWINDNEGRRyRAPPNFPVRLHP 103
|
....*....
gi 1958683074 100 GDIIQFGVD 108
Cdd:cd22702 104 SDVIEFGSD 112
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
550-736 |
4.89e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 550 ELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEvQQREEATRLQGELEKL---KKEWDVLENECRSLKKENVLLS 626
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREIN-EISSELPELREELEKLekeVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 627 SELQRQEKELHNSQKQSLELTSDLSILQMTRKELEN---------QMGSLKEQHLRDEADLKTLLSKAENQAKDVQKEYE 697
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958683074 698 KtqtvLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 736
Cdd:PRK03918 332 E----LEEKEERLEELKKKLKELEKRLEELEERHELYEE 366
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
166-726 |
5.17e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 166 FQLSQYLQEALHREQMLEQKLATLQRLLAitQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTED--SLRKELVAL 243
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVK--QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQqhTLTQHIHTL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 244 QEDKhsyeTTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLsdklKA 323
Cdd:TIGR00618 385 QQQK----TTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCE----KL 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 324 AEGKQEEIQQKGQAEKKELQAK---IDDMEEKEQELQAKIEALQADNDFTNERLTALQERL--LSKSGGDCTFIHQFIEC 398
Cdd:TIGR00618 457 EKIHLQESAQSLKEREQQLQTKeqiHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdIDNPGPLTRRMQRGEQT 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 399 QKKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLakvSLLKALLEEERKAYRN 478
Cdd:TIGR00618 537 YAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQ---DLTEKLSEAEDMLACE 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 479 QVEESAKQIQVLQVQLQRLHmDMENLQEEKDTEISSTRDKLLSAQDEI----LLLHQAAAKAVSERDTDFMSLQEELKKV 554
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLH-LQQCSQELALKLTALHALQLTLTQERVrehaLSIRVLPKELLASRQLALQKMQSEKEQL 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 555 RAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQQREEATrLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEK 634
Cdd:TIGR00618 693 TYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSD-LAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVT 771
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 635 ELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHlrdEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTE 714
Cdd:TIGR00618 772 AALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEI---GQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEIT 848
|
570
....*....|..
gi 1958683074 715 QEKQSITDELKQ 726
Cdd:TIGR00618 849 HQLLKYEECSKQ 860
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
16-111 |
5.93e-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: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 16 PFQERHVYLD-EPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFdhKTSKFYLQDTKSSNGTFINSQRLSRgseespP 94
Cdd:cd22693 7 TLQGQTFPIDkSGITIGRA------DDNDLVLSDDFVSSRHARIYL--QGSSWYLEDLGSTNGTFVNGNRVTQ------P 72
|
90
....*....|....*..
gi 1958683074 95 CEILSGDIIQFGVDVTE 111
Cdd:cd22693 73 VVVQPGDTIRIGATVFE 89
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
593-716 |
6.04e-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: 42.38 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 593 EATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNsQKQSLELTSDLSilqmtrkELENQMGSLKeqhl 672
Cdd:pfam15294 134 EIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGA-KKDVKSNLKEIS-------DLEEKMAALK---- 201
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1958683074 673 rdeADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQE 716
Cdd:pfam15294 202 ---SDLEKTLNASTALQKSLEEDLASTKHELLKVQEQLEMAEKE 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
549-740 |
6.38e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 549 EELKKVRAELEGWRKAASEYEEEIRSLQstfQLRcQQCevQQREEATRLQGELEKLKKEWDVLENEcrslkKENVLLSSE 628
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLE---PIR-ELA--ERYAAARERLAELEYLRAALRLWFAQ-----RRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 629 LQRQEKELHNSQKQSLELTSDLSILQMTRKELENQmgsLKEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKL 708
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQ---IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
170 180 190
....*....|....*....|....*....|..
gi 1958683074 709 KFEMTEQEKQSITDELKQCKDNLKLLREKGNN 740
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
180-385 |
6.40e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 180 QMLEQKLATLQRLLAITQEASDTSWQALideDRLLSRLEVMGNQLQAcsKNQTEDSLRKELVALQEDKHSYETTAKESLR 259
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAEL---EELNEEYNELQAELEA--LQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 260 rVLQEKIEVVRKLSEVERSLSNTE--DECTHLREMNERTQEELRELANkyngAVNEIKDLSDKLKAAEGKQEEIQQKGQA 337
Cdd:COG3883 94 -ALYRSGGSVSYLDVLLGSESFSDflDRLSALSKIADADADLLEELKA----DKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958683074 338 EKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQERLLSKS 385
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
256-702 |
6.50e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 256 ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERtQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKG 335
Cdd:PRK01156 315 SNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQ-ILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 336 QAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQERLLSKSggdctfihqfiecQKKLMVQGHLTKVVEES 415
Cdd:PRK01156 394 SEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELS-------------RNMEMLNGQSVCPVCGT 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 416 KLSKEnqakaKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLE----EERKAYRNQVEESAKQIQVLQ 491
Cdd:PRK01156 461 TLGEE-----KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLEseeiNKSINEYNKIESARADLEDIK 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 492 VQLQRLHmDMENLQEEKDTEISSTRDKLLSAQDEILLlhqaaaKAVSERDT-DFMSLQEELKKVRAELEGWRKAASEYEE 570
Cdd:PRK01156 536 IKINELK-DKHDKYEEIKNRYKSLKLEDLDSKRTSWL------NALAVISLiDIETNRSRSNEIKKQLNDLESRLQEIEI 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 571 EIRSLQSTFQLRCQQCEvqqrEEATRLQ---GELEKLKKEWDVLENECRSLKKEnvllSSELQRQEKELHNSQKQSLELT 647
Cdd:PRK01156 609 GFPDDKSYIDKSIREIE----NEANNLNnkyNEIQENKILIEKLRGKIDNYKKQ----IAEIDSIIPDLKEITSRINDIE 680
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683074 648 SDLsilqmtrKELENQMGSLKEQHLRDEADLKTLLS---KAENQAKDVQKEYEKTQTV 702
Cdd:PRK01156 681 DNL-------KKSRKALDDAKANRARLESTIEILRTrinELSDRINDINETLESMKKI 731
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
52-106 |
7.10e-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: 7.10e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958683074 52 SRNHALVWFDHKTSKFYLQ-----------DTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFG 106
Cdd:cd22683 28 SRSCDLVLSDPSISRFHAElrleqnginviDNNSANGTFINGKRIKGKT-----YILKNGDIIVFG 88
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
274-382 |
8.86e-04 |
|
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: 42.53 E-value: 8.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 274 EVERSLSNTEDECTHLREMNERTQEELRELANKY---NGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEK----------K 340
Cdd:pfam06160 288 YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEvayselqeelE 367
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1958683074 341 ELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQERLL 382
Cdd:pfam06160 368 EILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELR 409
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
256-365 |
1.07e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 256 ESLRRVLQEKI-EVVRKLSEVERSLSNTEDEcthLREMNERTQEELRELANKYNGAVNEIKdlsdklKAAEGKQEEIQQK 334
Cdd:PRK00409 526 EELERELEQKAeEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLEEAEKEAQQAIKEAK------KEADEIIKELRQL 596
|
90 100 110
....*....|....*....|....*....|.
gi 1958683074 335 GQAEKKELQAKidDMEEKEQELQAKIEALQA 365
Cdd:PRK00409 597 QKGGYASVKAH--ELIEARKRLNKANEKKEK 625
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
167-734 |
1.10e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.52 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 167 QLSQYLQEALHREQMLEQKLATL-----QRLLAITQE--ASDTSWQA------LIDEDRLL---SRLEVMGNQLQACSKN 230
Cdd:pfam12128 273 LIASRQEERQETSAELNQLLRTLddqwkEKRDELNGElsAADAAVAKdrseleALEDQHGAfldADIETAAADQEQLPSW 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 231 QTEDSLRKELVALQEDKHSYETTAKEslRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEEL-RELANKYNG 309
Cdd:pfam12128 353 QSELENLEERLKALTGKHQDVTAKYN--RRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALeSELREQLEA 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 310 AVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKEL------QAKIDDMEEKEQELQAKIEALQAD-------NDFTNERLTA 376
Cdd:pfam12128 431 GKLEFNEEEYRLKSRLGELKLRLNQATATPELLlqlenfDERIERAREEQEAANAEVERLQSElrqarkrRDQASEALRQ 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 377 LQERLLSKSGGDCTFIHQFIECQKKLM---------------------------------------------VQGHLTKV 411
Cdd:pfam12128 511 ASRRLEERQSALDELELQLFPQAGTLLhflrkeapdweqsigkvispellhrtdldpevwdgsvggelnlygVKLDLKRI 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 412 VEESKLSKENQAKAKESDLSDTLSPSKEK-----SSDDTTDAQMDEQDLNEPLAKVSL----------------LKALLE 470
Cdd:pfam12128 591 DVPEWAASEEELRERLDKAEEALQSAREKqaaaeEQLVQANGELEKASREETFARTALknarldlrrlfdekqsEKDKKN 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 471 EERKAYRNQVEESAKQIQVLQVQLQRLHMDMenLQEEKDT-------------EISSTRDKLLSAQDEILLLHQAAAKA- 536
Cdd:pfam12128 671 KALAERKDSANERLNSLEAQLKQLDKKHQAW--LEEQKEQkreartekqaywqVVEGALDAQLALLKAAIAARRSGAKAe 748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 537 ----VSERDTDFMS----------LQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQQRE---EATRLQG 599
Cdd:pfam12128 749 lkalETWYKRDLASlgvdpdviakLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNierAISELQQ 828
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 600 ELEKLKKEwdvlenecrslkkenvllsSELQRQ--EKELHNSQKQSLELTSDLSILqmtrKELENQMGSLKEQHLRDEAD 677
Cdd:pfam12128 829 QLARLIAD-------------------TKLRRAklEMERKASEKQQVRLSENLRGL----RCEMSKLATLKEDANSEQAQ 885
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958683074 678 ---------LKTLLSKAENQAKDVQKEYEKTQTVL-----SELKLKFEMTEQEKQSITDELKQCKDNLKLL 734
Cdd:pfam12128 886 gsigerlaqLEDLKLKRDYLSESVKKYVEHFKNVIadhsgSGLAETWESLREEDHYQNDKGIRLLDYRKLV 956
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
589-737 |
1.21e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 589 QQREEATR----LQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQ--EKELHNSQKQSLELTSDLSILQMTRKELEN 662
Cdd:COG3206 168 LRREEARKalefLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKllLQQLSELESQLAEARAELAEAEARLAALRA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 663 QMGS----------------LKEQHLRDEADLKTLLSK----------AENQAKDVQKEYEK-TQTVLSELKLKFEMTEQ 715
Cdd:COG3206 248 QLGSgpdalpellqspviqqLRAQLAELEAELAELSARytpnhpdviaLRAQIAALRAQLQQeAQRILASLEAELEALQA 327
|
170 180
....*....|....*....|..
gi 1958683074 716 EKQSITDELKQCKDNLKLLREK 737
Cdd:COG3206 328 REASLQAQLAQLEARLAELPEL 349
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
27-106 |
1.31e-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: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 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 ... |
591-717 |
1.51e-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: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 591 REEATRLQGELEKLKKEWDVLENECRSLKK----ENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGS 666
Cdd:smart00787 164 MKELELLNSIKPKLRDRKDALEEELRQLKQledeLEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIED 243
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1958683074 667 LKEQhlrdEADLKTLLSKAENQAKDVQKeyeKTQTVLSELKLKFEMTEQEK 717
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 |
1.57e-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: 1.57e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683074 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 |
1.97e-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: 41.29 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 1 MPSALAIFTCRPNSHPFQERHVYLDEPIKIGRSvARC-----RPAQnnatfdckVLSRNHALVWFDHktSKFYLQDTkSS 75
Cdd:COG3456 1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRS-ADCdwvlpDPDR--------SVSRRHAEIRFRD--GAFCLTDL-ST 68
|
90 100 110
....*....|....*....|....*....|...
gi 1958683074 76 NGTFIN--SQRLSRGSEEsppcEILSGDIIQFG 106
Cdd:COG3456 69 NGTFLNgsDHPLGPGRPV----RLRDGDRLRIG 97
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
441-670 |
2.29e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 441 SSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEE---KDTEISSTRD 517
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaeLEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 518 KLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQstfqlrcqqcevQQREEATRL 597
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR------------ADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683074 598 QGELEKLKKEWDVLENEcrsLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQ 670
Cdd:COG4942 166 RAELEAERAELEALLAE---LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
163-365 |
2.40e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.21 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEasdtsWQALIDEDRLLSR----LEVMGNQLQACSKNQT--EDSL 236
Cdd:COG0497 172 KELEELRADEAERARELDLLRFQLEELEAAALQPGE-----EEELEEERRRLSNaeklREALQEALEALSGGEGgaLDLL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 237 ---RKELVALQEDKHSYETTAkESLRRVLQEKIEVVRklsEVERSLSNTEDECTHLREMNERtQEELRELANKYNGAVNE 313
Cdd:COG0497 247 gqaLRALERLAEYDPSLAELA-ERLESALIELEEAAS---ELRRYLDSLEFDPERLEEVEER-LALLRRLARKYGVTVEE 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958683074 314 IKDLSDKLkaaegkqeeiqqkgQAEKKELQAKIDDMEEKEQELQAKIEALQA 365
Cdd:COG0497 322 LLAYAEEL--------------RAELAELENSDERLEELEAELAEAEAELLE 359
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
236-381 |
2.51e-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: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 236 LRKELVALQEDKHSYETTAK--ESLRRVLQEKIEVVRKLSE----------VERSLSNTEDECTHLREMN---------- 293
Cdd:COG4913 615 LEAELAELEEELAEAEERLEalEAELDALQERREALQRLAEyswdeidvasAEREIAELEAELERLDASSddlaaleeql 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 294 ERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQK----GQAEKKELQAKIDDM--EEKEQELQAKI-EALQAD 366
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRleaaEDLARLELRALLEERfaAALGDAVERELrENLEER 774
|
170
....*....|....*
gi 1958683074 367 NDFTNERLTALQERL 381
Cdd:COG4913 775 IDALRARLNRAEEEL 789
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
266-731 |
2.73e-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: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 266 IEVVRKLSEVERSLSNTEDECTHLremnertqEELRELANKYNGAVNEIKDLSDKLKAAEgkqeeiQQKGQAEKKELQAK 345
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELL--------EPIRELAERYAAARERLAELEYLRAALR------LWFAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 346 IDDMEEKEQELQAKIEALQADNDFTNERLTALQERLLSkSGGDctfihQFIECQKKLmvqghltkvveESKLSKENQAKA 425
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQIRG-NGGD-----RLEQLEREI-----------ERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 426 KESDLSDTLSPSKEKSSDDttdaqmdEQDLNEPLAKVSLLKALLEEERKAYRNQVEEsakqiqvlqvqLQRLHMDMENLQ 505
Cdd:COG4913 360 RRARLEALLAALGLPLPAS-------AEEFAALRAEAAALLEALEEELEALEEALAE-----------AEAALRDLRREL 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 506 EEKDTEISS--TRDKLLSAQDEILLLHQAAAKAVSERDTDFMSlqeELKKVRAELEGWRKAA--------------SEYE 569
Cdd:COG4913 422 RELEAEIASleRRKSNIPARLLALRDALAEALGLDEAELPFVG---ELIEVRPEEERWRGAIervlggfaltllvpPEHY 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 570 EE----IRSLQSTFQLRCQQCEVQQREEATR------LQGELE------------KLKKEWDV--------LENECRSL- 618
Cdd:COG4913 499 AAalrwVNRLHLRGRLVYERVRTGLPDPERPrldpdsLAGKLDfkphpfrawleaELGRRFDYvcvdspeeLRRHPRAIt 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 619 --------------------KKENVL----------LSSELQRQEKELHNSQKQSLELTSDLSILQmTRKELENQ----- 663
Cdd:COG4913 579 ragqvkgngtrhekddrrriRSRYVLgfdnraklaaLEAELAELEEELAEAEERLEALEAELDALQ-ERREALQRlaeys 657
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683074 664 -----MGSLKEQHLRDEADLKTL------LSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNL 731
Cdd:COG4913 658 wdeidVASAEREIAELEAELERLdassddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
258-365 |
3.53e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.68 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 258 LRRVLQEKIEVV---RKLSEVERSLSntEDECTHLREMNERTQ----EELRELANKYNGAVNEIKDLSDKLKAAEGKQ-- 328
Cdd:PRK05771 1 LAPVRMKKVLIVtlkSYKDEVLEALH--ELGVVHIEDLKEELSnerlRKLRSLLTKLSEALDKLRSYLPKLNPLREEKkk 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1958683074 329 ------EEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQA 365
Cdd:PRK05771 79 vsvkslEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQ 121
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
465-736 |
5.73e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.34 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 465 LKALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDEI----------LLLHQAAA 534
Cdd:pfam02463 199 ELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIekeeeklaqvLKENKEEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 535 KAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQStfQLRCQQCEVQQREEAtrlQGELEKLKKEWD----V 610
Cdd:pfam02463 279 KEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK--EKKKAEKELKKEKEE---IEELEKELKELEikreA 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 611 LENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTLLSKAENQAK 690
Cdd:pfam02463 354 EEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILE 433
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1958683074 691 DVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 736
Cdd:pfam02463 434 EEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQL 479
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
150-734 |
5.99e-03 |
|
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: 40.10 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 150 VDKVAANTPSMYSQELFqLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACsK 229
Cdd:pfam15921 460 LEKVSSLTAQLESTKEM-LRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL-K 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 230 NQtEDSLRKelVALQEDKHSYETTAKESLRRVLQEKIEVVRKL---------------SEVERSLSNTEDECTHLREMNE 294
Cdd:pfam15921 538 NE-GDHLRN--VQTECEALKLQMAEKDKVIEILRQQIENMTQLvgqhgrtagamqvekAQLEKEINDRRLELQEFKILKD 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 295 RTQEELRELANKYNG-----------------AVNEIKDLSDKL----KAAEGKQEEIQQKGQAEKKELQAKIDDMEEKE 353
Cdd:pfam15921 615 KKDAKIRELEARVSDlelekvklvnagserlrAVKDIKQERDQLlnevKTSRNELNSLSEDYEVLKRNFRNKSEEMETTT 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 354 QELQAKIEALQADNDFTNERLTAL--------------QERLLSKSGgdctfihQFIECQKKL-MVQGHLTKVVEESKLS 418
Cdd:pfam15921 695 NKLKMQLKSAQSELEQTRNTLKSMegsdghamkvamgmQKQITAKRG-------QIDALQSKIqFLEEAMTNANKEKHFL 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 419 KENqaKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLA--KVSLLKALLE--EERKAYRNQVEESAKQIQVLQvql 494
Cdd:pfam15921 768 KEE--KNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVAnmEVALDKASLQfaECQDIIQRQEQESVRLKLQHT--- 842
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 495 qrlhMDMENLQEEKDTEISSTRDKLL-------------SAQDEILLL--HQAAAKAVSERDT-DFMSLQEELKKV---- 554
Cdd:pfam15921 843 ----LDVKELQGPGYTSNSSMKPRLLqpasftrthsnvpSSQSTASFLshHSRKTNALKEDPTrDLKQLLQELRSVinee 918
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 555 ------RAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQQREEATRLQGELEKLKKE-----WDVLENECRSLKKENV 623
Cdd:pfam15921 919 ptvqlsKAEDKGRAPSLGALDDRVRDCIIESSLRSDICHSSSNSLQTEGSKSSETCSREpvllhAGELEDPSSCFTFPST 998
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 624 LLSSELQRQEKELHNSQKQSlELTSDLSILQMTRKELENQMGSLKEQHLRDEA-DLKTL-LSKAENQAKDVQKEYEKTQT 701
Cdd:pfam15921 999 ASPSVKNSASRSFHSSPKKS-PVHSLLTSSAEGSIGSSSQYRSAKTIHSPDSVkDSQSLpIETTGKTCRKLQNRLESLQT 1077
|
650 660 670
....*....|....*....|....*....|...
gi 1958683074 702 VLSELKLKFEMTEQEKQSITDELKQCKDNLKLL 734
Cdd:pfam15921 1078 LVEDLQLKNQAMSSMIRNQEKRIQKVKDQEKML 1110
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
289-485 |
6.36e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 289 LREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQAD-- 366
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDEll 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 367 -------------NDFTNER-LTALQERLLSK------SGGDCTFIHQFIECQKKLMVQGHLTKVVEESKLSKENQAKAK 426
Cdd:PHA02562 245 nlvmdiedpsaalNKLNTAAaKIKSKIEQFQKvikmyeKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDE 324
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683074 427 ESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAK 485
Cdd:PHA02562 325 LEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAK 383
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
172-380 |
8.10e-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: 38.86 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 172 LQEALHREQMLEQKLATLQRLLAITQEASDTSwqalidEDRLLSRLEvmgNQLQACSKNQTEDSLRKELvalqEDKHSYE 251
Cdd:pfam00261 24 LEEAEKRAEKAEAEVAALNRRIQLLEEELERT------EERLAEALE---KLEEAEKAADESERGRKVL----ENRALKD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 252 TTAKESLRRVLQEKIEVV----RKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDlsdkLKAAEGK 327
Cdd:pfam00261 91 EEKMEILEAQLKEAKEIAeeadRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKS----LEASEEK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958683074 328 QEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQER 380
Cdd:pfam00261 167 ASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEK 219
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
173-358 |
8.29e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.94 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 173 QEALHREQM--LEQKLATLQRLLAITqeasdtswqALIDEDRLLSRLEVMGNQLQACSKNQTE--------DSLRKELVA 242
Cdd:COG3096 858 QEQQLRQQLdqLKEQLQLLNKLLPQA---------NLLADETLADRLEELREELDAAQEAQAFiqqhgkalAQLEPLVAV 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 243 LQEDKHSYETTAKE-----SLRRVLQEKIEVvrkLSEV-ER----SLSNTEDECTHLREMNERTQEELRElankyngAVN 312
Cdd:COG3096 929 LQSDPEQFEQLQADylqakEQQRRLKQQIFA---LSEVvQRrphfSYEDAVGLLGENSDLNEKLRARLEQ-------AEE 998
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958683074 313 EIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQA 358
Cdd:COG3096 999 ARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEE 1044
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
566-728 |
9.60e-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: 38.78 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 566 SEYEEEIRSLQSTFQLRCQQCEVQQREEAtRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKqslE 645
Cdd:pfam09728 28 AELLEEMKRLQKDLKKLKKKQDQLQKEKD-QLQSELSKAILAKSKLEKLCRELQKQNKKLKEESKKLAKEEEEKRK---E 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683074 646 LTSDlsiLQMTRKELENQM-------GSLKEQHLRDEADLKTLLSKAENQAKDVQKEYEKT--QTVLSELKLKFEMTEQE 716
Cdd:pfam09728 104 LSEK---FQSTLKDIQDKMeekseknNKLREENEELREKLKSLIEQYELRELHFEKLLKTKelEVQLAEAKLQQATEEEE 180
|
170
....*....|..
gi 1958683074 717 KQSITDELKQCK 728
Cdd:pfam09728 181 KKAQEKEVAKAR 192
|
|
| |
