|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
3-130 |
1.23e-80 |
|
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and similar proteins; SLMAP, also called sarcolemmal-associated protein (SLAP), is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. It is a cardiac membrane protein that plays an important role in E-C coupling and the adrenergic response of the heart. Overexpression of the SLMAP gene has been associated with diabetes and endothelial dysfunction of macro- and micro-blood vessels. SLMAP contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438731 [Multi-domain] Cd Length: 126 Bit Score: 254.11 E-value: 1.23e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 3 SALAIFTCRPNSHPFQERHVYLDEPIKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHktSKFYLQDTKSSNGTFINS 82
Cdd:cd22679 1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1958683057 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 |
5.00e-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: 101.22 E-value: 5.00e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683057 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQ 225
Cdd:cd21911 1 QELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQLS 63
|
|
| FHA_DMA-like |
cd22692 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest ... |
27-108 |
1.26e-17 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest protein 1 (DMA1), 2 (DMA2) and similar proteins; DMA1 (also known as checkpoint forkhead associated with RING domains-containing protein 1, or CHF1) and DMA2 (also known as checkpoint forkhead associated with RING domains-containing protein 2, or CHF2) are E3 ubiquitin-protein ligases which function in cell cycle retarding in conjunction with the UBC4 and UBC13/MMS2 complex, two E2 ubiquitin conjugating enzymes. They are involved in nutritional control of the cell cycle and required for proper spindle positioning, likely regulating septin ring deposition at the bud neck. DMA1 targets the degradation of G1 cyclin PCL1. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438744 [Multi-domain] Cd Length: 139 Bit Score: 79.92 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 27 PIKIGRSVARCRPAQNNAT-FDCKVLSRNHALVWfdHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQF 105
Cdd:cd22692 38 QIHIGRYTERVRQAIYHPVvFKSKVVSRTHGCIK--VDEGNWYIKDVKSSSGTFLNHQRLSPASRTSKPYPLRDGDILQL 115
|
...
gi 1958683057 106 GVD 108
Cdd:cd22692 116 GMD 118
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-774 |
2.30e-15 |
|
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: 80.87 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 156 NTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQA--CSKNQTE 233
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvAQLELQI 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 234 DSLRKELVALQEDKHSYE------TTAKESLRRVLQE--KIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELAN 305
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEdrrerlQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 306 KYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKID---------DMEEKEQELQAKIE-ALQAD-NDFTNERL 374
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlsELISVDEGYEAAIEaALGGRlQAVVVENL 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 375 TALQVRLEPLQEKTLKECSSLEKLMVQGHLTKVVEESKLSKENQAKAKESDLsDTLSPSKEKSSD---------DTTDAQ 445
Cdd:TIGR02168 556 NAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDL-VKFDPKLRKALSyllggvlvvDDLDNA 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 446 MDEQDLNEPLAKVSLLKDDLQG-----TQAETEAKQDTQHLRKELVEAQELARASKQKCFDLQALL---EEERKAYRNQV 517
Cdd:TIGR02168 635 LELAKKLRPGYRIVTLDGDLVRpggviTGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALaelRKELEELEEEL 714
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 518 EESAKQIQVLQVQLQRLHMDMENLQEEKDT---EISSTRDKLLSAQDEILLLHQAAAKA---VSERDTDFMSLQEELKKV 591
Cdd:TIGR02168 715 EQLRKELEELSRQISALRKDLARLEAEVEQleeRIAQLSKELTELEAEIEELEERLEEAeeeLAEAEAEIEELEAQIEQL 794
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 592 RAELEGWRKAASEYEEEIRSLQSTF---QLRCQQCE----------VQQREEATRLQGELEKLKKEWDVLENECRSLKKE 658
Cdd:TIGR02168 795 KEELKALREALDELRAELTLLNEEAanlRERLESLErriaaterrlEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 659 NVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHlrdeADLKTLLSKAENQAKDVQkeyektQT 738
Cdd:TIGR02168 875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL----AQLELRLEGLEVRIDNLQ------ER 944
|
650 660 670
....*....|....*....|....*....|....*.
gi 1958683057 739 VLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 774
Cdd:TIGR02168 945 LSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| FHA_VPS64-like |
cd22695 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ... |
6-126 |
3.91e-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: 3.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 6 AIFTCRPNSHPFQERHV---YLDEPIKIGRSVARCRPAQN---------------NATFDCKVLSRNHALVWFDHKTSKF 67
Cdd:cd22695 2 HILVLKSLNATFETKFLvvpFKPDGLKLGRPVTNSVNKNNsgskrdlfsqqvrpdNGNFDSRVLSRNHACLSCDPTTGKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683057 68 YLQDTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFGVDVTEntrKVTHGCIVSTIK 126
Cdd:cd22695 82 YIRDLKSSNGTFVNGQKIRQND-----VELKVGDEVDLGTDIDS---KIEHRKISAYVE 132
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
239-776 |
1.30e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.64 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 239 ELVALQEDKHSYETTAKESLRRV--LQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKD 316
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 317 LSDKLKAAEGKQEEIQQKGQAEKK--ELQAKIDDMEEKEQELQAKIEALQadndftneRLTALQVRLEPLQEKTlkecss 394
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELK--------KAAAAKKKADEAKKKA------ 1427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 395 lEKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKE--KSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAET 472
Cdd:PTZ00121 1428 -EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEeaKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA 1506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 473 EAKQDTQHLRK--------ELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEE 544
Cdd:PTZ00121 1507 EAKKKADEAKKaeeakkadEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA 1586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 545 KDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTdfmslQEELKKVRAELEGWRKAASEYEEEIRSLQstfQLRCQQCE 624
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK-----AEELKKAEEEKKKVEQLKKKEAEEKKKAE---ELKKAEEE 1658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 625 VQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSI--------LQMTRKE 696
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKaeeenkikAEEAKKE 1738
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 697 LENQMGSLKEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKlkfEMTEQEKQSITDELKQCKDNLKLLREKGN 776
Cdd:PTZ00121 1739 AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD---EEDEKRRMEVDKKIKDIFDNFANIIEGGK 1815
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
190-773 |
1.42e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.09 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 190 QRLLAITQEASDTSWQALIDE--------DRLLSRLEVMGNQLQACSKNQTE-----DSLRKELVALQEDKHSYETT--- 253
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLRleelreelEELQEELKEAEEELEELTAELQEleeklEELRLEVSELEEEIEELQKElya 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 254 AKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQ 333
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 334 KGQAEKKELQ---AKIDDMEEKEQELQAKIEALQAdndftneRLTALQVRLEPLQEKTLKECSSLEKLMVQGHLTKVVEE 410
Cdd:TIGR02168 373 RLEELEEQLEtlrSKVAQLELQIASLNNEIERLEA-------RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 411 SKLskENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEA-KQDTQHLRK------ 483
Cdd:TIGR02168 446 EEE--LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGvKALLKNQSGlsgilg 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 484 ---ELVE----------------AQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQ-- 542
Cdd:TIGR02168 524 vlsELISvdegyeaaieaalggrLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLgv 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 543 ----EEKDTEISSTRDKLLS--------------------------AQDEILLLHQAAAKAVSERDTDFMSLQEELKKVR 592
Cdd:TIGR02168 604 akdlVKFDPKLRKALSYLLGgvlvvddldnalelakklrpgyrivtLDGDLVRPGGVITGGSAKTNSSILERRREIEELE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 593 AELEGWRKAASEYEEEIRSLQSTFQLRcQQCEVQQREEATRLQGELEKLKKEWDVLENECRSlkkenvlLSSELQRQEKE 672
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEEL-EEELEQLRKELEELSRQISALRKDLARLEAEVEQ-------LEERIAQLSKE 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 673 LHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTL---LSKAENQAKDVQKEYEKTQTVLSELKLKFEM 749
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALreaLDELRAELTLLNEEAANLRERLESLERRIAA 835
|
650 660
....*....|....*....|....
gi 1958683057 750 TEQEKQSITDELKQCKDNLKLLRE 773
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAA 859
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
13-106 |
2.23e-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: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 13 NSHPFQERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKtsKFYLQDTKSSNGTFINSQRLsrgseeS 92
Cdd:cd00060 6 DGDGGGREFPLTKGVVTIGRS------PDCDIVLDDPSVSRRHARIEVDGG--GVYLEDLGSTNGTFVNGKRI------T 71
|
90
....*....|....
gi 1958683057 93 PPCEILSGDIIQFG 106
Cdd:cd00060 72 PPVPLQDGDVIRLG 85
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
28-105 |
6.17e-13 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 64.13 E-value: 6.17e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683057 28 IKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhKTSKFYLQDTKSSNGTFINSQRLSRgseesPPCEILSGDIIQF 105
Cdd:pfam00498 1 VTIGRS------PDCDIVLDDPSVSRRHAEIRYD-GGGRFYLEDLGSTNGTFVNGQRLGP-----EPVRLKDGDVIRL 66
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
161-744 |
1.09e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 161 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKEL 240
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 241 VALQEDkhsyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDK 320
Cdd:COG1196 298 ARLEQD-----------IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 321 LKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEKTLKEcssleklmv 400
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE--------- 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 401 qghltkVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQDTQH 480
Cdd:COG1196 438 ------EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 481 LRKELVEAQELARA-----SKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDK 555
Cdd:COG1196 512 AALLLAGLRGLAGAvavliGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAA 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 556 LLS-AQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLqstfqlrcqqcevqqREEATRL 634
Cdd:COG1196 592 LARgAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV---------------TLEGEGG 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 635 QGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEAD 714
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
570 580 590
....*....|....*....|....*....|
gi 1958683057 715 LKTLLSKAENQAKDVQKEYEKTQTVLSELK 744
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEELE 766
|
|
| CC1_SLMAP-like |
cd21868 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ... |
167-204 |
1.51e-12 |
|
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar proteins; The family includes Sarcolemmal membrane-associated protein (SLMAP), its paralog TRAF3-interacting JNK-activating modulator (T3JAM), and similar proteins. SLMAP, also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. T3JAM, also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. SLMAP contains an N-terminal FHA domain, followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409286 [Multi-domain] Cd Length: 38 Bit Score: 62.12 E-value: 1.51e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1958683057 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21868 1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
52-106 |
2.34e-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: 2.34e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1958683057 52 SRNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQFG 106
Cdd:cd22686 48 SKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPYPLTHGDELKIG 102
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
14-106 |
7.26e-11 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 59.20 E-value: 7.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 14 SHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktSKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716 8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
|
90
....*....|....
gi 1958683057 93 pPCEILSGDIIQFG 106
Cdd:COG1716 75 -PAPLRDGDVIRLG 87
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
211-618 |
9.78e-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: 65.85 E-value: 9.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 211 DRLLSRLEVMGNQLQACSKNQTEdsLRKELVALQEDkhsyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLR 290
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAE--LRKELEELEEE-----------LEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 291 EMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEgkqeeiqqkgqAEKKELQAKIDDMEEKEQELQAKIEALQADNDFT 370
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAE-----------AEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 371 NERLTALQVRLEPLQEktlkecsslEKLMVQGHLTKVVEESKLSKENQAKAKESdlSDTLSPSKEKSSDDTTDAQMDEQD 450
Cdd:TIGR02168 816 NEEAANLRERLESLER---------RIAATERRLEDLEEQIEELSEDIESLAAE--IEELEELIEELESELEALLNERAS 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 451 LNEPLAKVSLLKDDLQGTQAETEAKQDTqhLRKELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAkqiqvlqvq 530
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSE--LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL--------- 953
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 531 lqrlhMDMENLQEEKDTEISSTRDKLLSAQDEIL------LLHQAAAKAVSERdTDFMSLQ-EELKKVRAELEgwrKAAS 603
Cdd:TIGR02168 954 -----EEAEALENKIEDDEEEARRRLKRLENKIKelgpvnLAAIEEYEELKER-YDFLTAQkEDLTEAKETLE---EAIE 1024
|
410
....*....|....*.
gi 1958683057 604 EYEEEIRS-LQSTFQL 618
Cdd:TIGR02168 1025 EIDREARErFKDTFDQ 1040
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
204-755 |
1.10e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 204 WQALIDEDRLLSRLEVMGNQLQAcsKNQTEDSLRKELVALQEDKhsyeTTAKESLRRVLQEKIEVVRKLSEVERSLSNTE 283
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEE--LEAELEELEAELAELEAEL----EELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 284 DECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEAL 363
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 364 QADNDFTNERLTALQVRLEPLQEKTLKEcSSLEKLMVQghlTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTD 443
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAE-EALLERLER---LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 444 AQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQDTQHLRKELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAKQ 523
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 524 IQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQdEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEgWRKAAS 603
Cdd:COG1196 538 AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRA-TFLPLDKIRARAALAAALARGAIGAAVDLVASDLR-EADARY 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 604 EYEEEIRSLQSTFQLRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLEL 683
Cdd:COG1196 616 YVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL 695
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683057 684 TSDLSILQMTRKELENQMGSLKEQHLRDEADLKTLLSKAENQAKDVQKEYEKT-QTVLSELKLKFEMTEQEKQ 755
Cdd:COG1196 696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLeEEALEELPEPPDLEELERE 768
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
135-716 |
3.35e-10 |
|
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: 63.98 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 135 ARLRSDVIHAPLpSPVDKVAANTPSMYSQELFQL----SQYLQEALHREQMLEQKLATLQRLLAItqeASDTSWQALIDE 210
Cdd:pfam15921 290 ARSQANSIQSQL-EIIQEQARNQNSMYMRQLSDLestvSQLRSELREAKRMYEDKIEELEKQLVL---ANSELTEARTER 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 211 DRLLSRLEVMGNQLQAC----SKNQTEDSLRKELVALQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNtedec 286
Cdd:pfam15921 366 DQFSQESGNLDDQLQKLladlHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKS----- 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 287 thlrEMNERTQEELRELANKyNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQAD 366
Cdd:pfam15921 441 ----ECQGQMERQMAAIQGK-NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAT 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 367 NDFTNERLTALQVRLEPLQ---------EKTLKECSSLEKLMVQGhlTKVVEESKLSKEN--QAKAKESDLSDTLSPSKE 435
Cdd:pfam15921 516 NAEITKLRSRVDLKLQELQhlknegdhlRNVQTECEALKLQMAEK--DKVIEILRQQIENmtQLVGQHGRTAGAMQVEKA 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 436 KSSDDTTDAQMDEQDLNeplakvsLLKDDLQGTQAETEAKQDTQHLRK-ELVEA-QELARASKQkcfdlqalLEEERKAY 513
Cdd:pfam15921 594 QLEKEINDRRLELQEFK-------ILKDKKDAKIRELEARVSDLELEKvKLVNAgSERLRAVKD--------IKQERDQL 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 514 RNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDEillLHQAAAKAVSERDTDFMSLQEELkkvra 593
Cdd:pfam15921 659 LNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSE---LEQTRNTLKSMEGSDGHAMKVAM----- 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 594 eleGWRKAASEYEEEIRSLQSTFQLrCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKEL 673
Cdd:pfam15921 731 ---GMQKQITAKRGQIDALQSKIQF-LEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKV 806
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1958683057 674 HNSQ----KQSLELTSDLSILQmtRKELENQmgSLKEQHLRDEADLK 716
Cdd:pfam15921 807 ANMEvaldKASLQFAECQDIIQ--RQEQESV--RLKLQHTLDVKELQ 849
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
163-699 |
6.32e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 6.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDtswQALIDEDRLLSRLEVMGNQLQAcsKNQTEDSLRKELVA 242
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRR---ELEERLEELEEELAELEEELEE--LEEELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 243 LQEDkhsyETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLK 322
Cdd:COG1196 349 AEEE----LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 323 AAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEKTLKEcsSLEKLMVQG 402
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL--LLLLEAEAD 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 403 HLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKV-----SLLKDDLQG---------- 467
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVaaaaiEYLKAAKAGratflpldki 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 468 ---TQAETEAKQDTQHLRKELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEE 544
Cdd:COG1196 583 rarAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSL 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 545 KDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCE 624
Cdd:COG1196 663 TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL 742
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 625 VQQREEATRLQGE------LEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHnsqkqslELTSDLSILQMTRKELE 698
Cdd:COG1196 743 EEEELLEEEALEElpeppdLEELERELERLEREIEALGPVNLLAIEEYEELEERYD-------FLSEQREDLEEARETLE 815
|
.
gi 1958683057 699 N 699
Cdd:COG1196 816 E 816
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
448-774 |
7.22e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 7.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 448 EQDLNEPLAKVSLLKDDLQGTQAETEAKQDTQHLRKELVEAQELARASKQKCfdlqalLEEERKAYRNQVEEsakqiqvl 527
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEA------LERQKEAIERQLAS-------- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 528 qvqlqrlhmdMENLQEEKDTEISSTRDKLLSAQDeilLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEE 607
Cdd:TIGR02169 249 ----------LEEELEKLTEEISELEKRLEEIEQ---LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 608 EIRSLQStfqlRCQQCEVQ---QREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKEL------HNSQK 678
Cdd:TIGR02169 316 ELEDAEE----RLAKLEAEidkLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFaetrdeLKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 679 QSLE-LTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTLLSK---AENQAKDVQKEYEKTQTVLSELKLKFEMTEQEK 754
Cdd:TIGR02169 392 EKLEkLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKineLEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL 471
|
330 340
....*....|....*....|
gi 1958683057 755 QSITDELKQCKDNLKLLREK 774
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQRE 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
162-519 |
6.55e-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: 59.70 E-value: 6.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 162 SQELFQLSQY--LQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQacsknQTEDSLRKE 239
Cdd:TIGR02169 664 GGILFSRSEPaeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE-----QEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 240 LVALQEDKHSYE---TTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHlremnertqEELRELANKYNGAVNEIKD 316
Cdd:TIGR02169 739 LEELEEDLSSLEqeiENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH---------SRIPEIQAELSKLEEEVSR 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 317 LSDKLKAAEGKQEEIQQKGQ---AEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEKTLKECS 393
Cdd:TIGR02169 810 IEARLREIEQKLNRLTLEKEyleKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 394 SLEKLMVQGhltKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSL--LKDDLQGTQAE 471
Cdd:TIGR02169 890 ERDELEAQL---RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLedVQAELQRVEEE 966
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958683057 472 TEAKQDTQHLRKELVEAQELARASKQkcfDLQALLEEERKAYRNQVEE 519
Cdd:TIGR02169 967 IRALEPVNMLAIQEYEEVLKRLDELK---EKRAKLEEERKAILERIEE 1011
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
228-698 |
8.54e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 8.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 228 SKNQTEDSLRKELVALQEDKHSYETTA------KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQE--- 298
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKELEELKeeieelEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElke 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 299 ------ELRELANKYNGAVNEIKDLSDKLKA-AEGKQEEIQQkgqAEKKElqAKIDDMEEKEQELQAKIEALQADNDfTN 371
Cdd:PRK03918 291 kaeeyiKLSEFYEEYLDELREIEKRLSRLEEeINGIEERIKE---LEEKE--ERLEELKKKLKELEKRLEELEERHE-LY 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 372 ERLTALQVRLEPLQEKtlKECSSLEKLM-----VQGHLTKVVEESK--LSKENQAKAKESDLSDTLSPSKE-KSSDDTTD 443
Cdd:PRK03918 365 EEAKAKKEELERLKKR--LTGLTPEKLEkeleeLEKAKEEIEEEISkiTARIGELKKEIKELKKAIEELKKaKGKCPVCG 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 444 AQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQdtQHLRKELVEAQ-ELARASK----QKCFDLQALLEEERKAYR-NQV 517
Cdd:PRK03918 443 RELTEEHRKELLEEYTAELKRIEKELKEIEEKE--RKLRKELRELEkVLKKESEliklKELAEQLKELEEKLKKYNlEEL 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 518 EESAKQIQVLQVQLQRLHMDMENLQEE--KDTEISSTRDKLLSAQDEIL-----LLHQAAAKAVSERDTDFMSLQEeLKK 590
Cdd:PRK03918 521 EKKAEEYEKLKEKLIKLKGEIKSLKKEleKLEELKKKLAELEKKLDELEeelaeLLKELEELGFESVEELEERLKE-LEP 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 591 VRAELEGWRKAASEYEEEIRSLQStfqlrCQQCEVQQREEATRLQGELEKLKKEWDVL-----ENECRSLKKENVLLSSE 665
Cdd:PRK03918 600 FYNEYLELKDAEKELEREEKELKK-----LEEELDKAFEELAETEKRLEELRKELEELekkysEEEYEELREEYLELSRE 674
|
490 500 510
....*....|....*....|....*....|...
gi 1958683057 666 LQRQEKELHNSQKQSLELTSDLSILQMTRKELE 698
Cdd:PRK03918 675 LAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
336-679 |
9.71e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 9.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 336 QAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEKTLKECSSLEKLmvqghltkvveeskLSK 415
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL--------------EAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 416 ENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAkqdtqhLRKELVEAQELARAS 495
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA------LREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 496 KQKCFDLQalleEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEkdteisstRDKLLSAQDEILLLHQAAAKAVS 575
Cdd:TIGR02168 816 NEEAANLR----ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE--------IEELEELIEELESELEALLNERA 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 576 ERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQ---STFQLRCQQCEVqqreeatRLQGELEKLKKEWDVLENEC 652
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELRELESKRSELRRELEELReklAQLELRLEGLEV-------RIDNLQERLSEEYSLTLEEA 956
|
330 340
....*....|....*....|....*..
gi 1958683057 653 RSLKKENVLLSSELQRQEKELHNSQKQ 679
Cdd:TIGR02168 957 EALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-646 |
1.05e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 263 QEKIEVVRKLSEVERSLSNTEDEcthLREMNERTQ--EELRELANKYNGAVNEIKDLSDKLKAAEGKQEEiqqkgqAEKK 340
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDI---LNELERQLKslERQAEKAERYKELKAELRELELALLVLRLEELR------EELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 341 ELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEKTLKECSSLEKLMVQghlTKVVEESKLSKENQAK 420
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ---KQILRERLANLERQLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 421 AKESDLsdtlspskekssddttdaQMDEQDLNEPLAKVSLLKDDLQGTQAETEAkqdtqhLRKELVEAQELARASKQKCF 500
Cdd:TIGR02168 320 ELEAQL------------------EELESKLDELAEELAELEEKLEELKEELES------LEAELEELEAELEELESRLE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 501 DLQALLEEERKAY---RNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISS-TRDKLLSAQDEILLLHQAAAKAVSE 576
Cdd:TIGR02168 376 ELEEQLETLRSKVaqlELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEE 455
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 577 RDTdfmsLQEELKKVRAELEGWRKAASEYEEEIRSLQStfqlRCQQCEVQQREEATRLQGELEKLKKEWD 646
Cdd:TIGR02168 456 LER----LEEALEELREELEEAEQALDAAERELAQLQA----RLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| CC1_T3JAM |
cd21912 |
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ... |
164-204 |
1.38e-08 |
|
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: 51.19 E-value: 1.38e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1958683057 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21912 5 EILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
14-110 |
1.70e-08 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine/threonine-protein kinase MEK1 and similar proteins; MEK1 (EC 2.7.11.1), also known as MRE4, is a meiosis-specific protein kinase required for chromosome synapsis and meiotic recombination. The recruitment and activation of MEK1 require the phosphorylation of the chromosome axis protein Hop1 at Thr318 (pT318), which is necessary for recognition by the MEK1 FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438722 [Multi-domain] Cd Length: 105 Bit Score: 53.00 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 14 SHPFQERHV---YLDEPIKIGRSvARCRPAQNNATfdckvLSRNHALVW---FDHKT-SKFYLQDTkSSNGTFINSQRLS 86
Cdd:cd22670 7 SSPGSTDIVlpiYKNQVITIGRS-PSCDIVINDPF-----VSRTHCRIYsvqFDESSaPLVYVEDL-SSNGTYLNGKLIG 79
|
90 100
....*....|....*....|....*
gi 1958683057 87 RGseespPCEILS-GDIIQFGVDVT 110
Cdd:cd22670 80 RN-----NTVLLSdGDVIEIAHSAT 99
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
298-774 |
2.09e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 298 EELRELANKYNGAVNEIkdLSDKLKAAEGKQEEIQQKgqaEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTAL 377
Cdd:PRK02224 165 EEYRERASDARLGVERV--LSDQRGSLDQLKAQIEEK---EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 378 QVRLEPlQEKTLKECSSLEklmvqghltKVVEESKLSKENQAKAKEsDLSDTLSPSKEKSSD--DTTDAQMDEQDLNEPL 455
Cdd:PRK02224 240 DEVLEE-HEERREELETLE---------AEIEDLRETIAETERERE-ELAEEVRDLRERLEEleEERDDLLAEAGLDDAD 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 456 AK-VSLLKDDLQGTQAET-----EAKQDTQHLRKELVEAQELARAskqkcfdlqalLEEERKAYRNQVEEsakqiqvlqv 529
Cdd:PRK02224 309 AEaVEARREELEDRDEELrdrleECRVAAQAHNEEAESLREDADD-----------LEERAEELREEAAE---------- 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 530 qlqrlhmdMENLQEEKDTEISSTRDKLLSAQDEIlllhQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEI 609
Cdd:PRK02224 368 --------LESELEEAREAVEDRREEIEELEEEI----EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 610 RSLQSTF----QLR----CQQCE------------VQQREEATRLQGELEKLKKEWDVLENECRSLKkenvllssELQRQ 669
Cdd:PRK02224 436 RTARERVeeaeALLeagkCPECGqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAE--------DLVEA 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 670 EKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQhlrdEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEM 749
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELRER----AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE 583
|
490 500 510
....*....|....*....|....*....|.
gi 1958683057 750 TEQEKQS------ITDELKQCKDNLKLLREK 774
Cdd:PRK02224 584 LKERIESlerirtLLAAIADAEDEIERLREK 614
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
235-766 |
2.24e-08 |
|
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: 57.72 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 235 SLRKELVALQEDKHSYETTAKE--SLRRVLQEKIEVVRKLSEVERSLsntEDECTHLREMNERTQEELRELANKYNGAVN 312
Cdd:TIGR04523 170 ELENELNLLEKEKLNIQKNIDKikNKLLKLELLLSNLKKKIQKNKSL---ESQISELKKQNNQLKDNIEKKQQEINEKTT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 313 EIKDLSDKLKAAEGKQEEIQQKGQAEKKELQ---AKIDDMEEKEQELQAKIEAL--QADNDFTNErltaLQVRLEPLQEK 387
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQNKIKKQLSEKQKELEqnnKKIKELEKQLNQLKSEISDLnnQKEQDWNKE----LKSELKNQEKK 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 388 tlkecssleklmvqghltKVVEESKLSKENQakaKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQG 467
Cdd:TIGR04523 323 ------------------LEEIQNQISQNNK---IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 468 TQAETEA-KQDTQHLRKELVEAQELARASKQKCFDLQA---LLEEERKAYRNQVEESAKQIQvlqvqlqrlhmDMENLQE 543
Cdd:TIGR04523 382 YKQEIKNlESQINDLESKIQNQEKLNQQKDEQIKKLQQekeLLEKEIERLKETIIKNNSEIK-----------DLTNQDS 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 544 EKDTEISSTRDKLLSAQDEILLLhqaaAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLqstfqlrcqqc 623
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVL----SRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL----------- 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 624 eVQQREEATRLQGELEKLKKEwdvLENECRSLKKENVLLSSELQRQ--EKELHNSQKQSLELTSDLSILQMTRKELENQM 701
Cdd:TIGR04523 516 -TKKISSLKEKIEKLESEKKE---KESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELI 591
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683057 702 GSLKEQ--HLRDEADLKT-LLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKD 766
Cdd:TIGR04523 592 DQKEKEkkDLIKEIEEKEkKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
236-773 |
3.90e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 236 LRKELVALQEDKHSY---ETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDEcthlREMNERTQEELRELANKYNGAVN 312
Cdd:PRK03918 170 VIKEIKRRIERLEKFikrTENIEELIKEKEKELEEVLREINEISSELPELREE----LEKLEKEVKELEELKEEIEELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 313 EIKDLSDKLKAAEGKQEEIQQKgqaeKKELQAKIDDMEEKE---QELQAKIEALQADNDFTNERLTALQvRLEPLQEKTL 389
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEER----IEELKKEIEELEEKVkelKELKEKAEEYIKLSEFYEEYLDELR-EIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 390 KECSSLEKLMVQGhltkvveESKLSKENQAKAKESDLSDTLSPSKEKSSD-DTTDAQMDE-------------QDLNEPL 455
Cdd:PRK03918 321 EEINGIEERIKEL-------EEKEERLEELKKKLKELEKRLEELEERHELyEEAKAKKEElerlkkrltgltpEKLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 456 AKVSLLKDDLQGTQAE-TEAKQDTQHLRKELVEAQELARASKQKCFDLQALLEEERKA-----YRNQVEESAKQIQVLQV 529
Cdd:PRK03918 394 EELEKAKEEIEEEISKiTARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKelleeYTAELKRIEKELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 530 QLQRLHMDMENLqeekdteisstrDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEI 609
Cdd:PRK03918 474 KERKLRKELREL------------EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEI 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 610 RSLQSTFqlrcqqcevqqrEEATRLQGELEKLKKEWDVLENECRSLKKENVLLS----SELQRQEKELHNSQKQSLELTS 685
Cdd:PRK03918 542 KSLKKEL------------EKLEELKKKLAELEKKLDELEEELAELLKELEELGfesvEELEERLKELEPFYNEYLELKD 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 686 DLSILQMTRKELENQMGSLKEQhLRDEADLKTLLSKAENQAKDVQKEY-EKTQTVLSELKLKFEM----TEQEKQSITDE 760
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKA-FEELAETEKRLEELRKELEELEKKYsEEEYEELREEYLELSRelagLRAELEELEKR 688
|
570
....*....|...
gi 1958683057 761 LKQCKDNLKLLRE 773
Cdd:PRK03918 689 REEIKKTLEKLKE 701
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-774 |
4.08e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 197 QEASDTSWQALIDEDRLLSRLEVMGNQLQacsknqtedSLRKELVALQEDKHSYETTAKESLRRVLQEKI---EVVRKLS 273
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIE---------EERKRRDKLTEEYAELKEELEDLRAELEEVDKefaETRDELK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 274 EVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKE 353
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 354 QElqakIEALQADNDFTNERLTALQVRLEPLQ------EKTLKECSSLEKLM---VQGHLTKVVEESKLsKENQAKAKES 424
Cdd:TIGR02169 469 QE----LYDLKEEYDRVEKELSKLQRELAEAEaqarasEERVRGGRAVEEVLkasIQGVHGTVAQLGSV-GERYATAIEV 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 425 DLSDTLspsKEKSSDDTTDAQMDEQDLNE---------PLAK--------------------VSLLKDDLQGTQAETEAK 475
Cdd:TIGR02169 544 AAGNRL---NNVVVEDDAVAKEAIELLKRrkagratflPLNKmrderrdlsilsedgvigfaVDLVEFDPKYEPAFKYVF 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 476 QDTQhlrkeLVEAQELARA--SKQKCFDLQALLEE-----------ERKAYRNQVEESAKqiqvlqvqLQRLHMDMENLQ 542
Cdd:TIGR02169 621 GDTL-----VVEDIEAARRlmGKYRMVTLEGELFEksgamtggsraPRGGILFSRSEPAE--------LQRLRERLEGLK 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 543 EEKDTeISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQ 622
Cdd:TIGR02169 688 RELSS-LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 623 CEvQQREEATRLQGELEKLKKE-----WDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKEL 697
Cdd:TIGR02169 767 IE-ELEEDLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 698 ENQMGSLKEQHLRDEA---DLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 774
Cdd:TIGR02169 846 KEQIKSIEKEIENLNGkkeELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
28-85 |
4.86e-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: 4.86e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683057 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 |
5.88e-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: 5.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 29 KIGRSVARCRPAQNNATFDcKVLSRNHALVWFDHKTS---KFYLQDTkSSNGTFINSQRLSRGSEEsppcEILSGDIIQF 105
Cdd:cd22685 31 RIGRNPEVCDVFLCSSQHP-NLISREHAEIHAERDGNgnwKVLIEDR-STNGTYVNDVRLQDGQRR----ELSDGDTITF 104
|
90
....*....|....*.
gi 1958683057 106 G--VDVTENTRKVTHG 119
Cdd:cd22685 105 GhkNGRRVKQWPYQKS 120
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
542-774 |
7.36e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 7.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 542 QEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDtdfmSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQL--- 618
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELE----ELEAELAELEAELEELRLELEELELELEEAQAEEYElla 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 619 ---RCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRK 695
Cdd:COG1196 296 elaRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 696 ELENQMGSLKEQHL---RDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLR 772
Cdd:COG1196 376 EAEEELEELAEELLealRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
..
gi 1958683057 773 EK 774
Cdd:COG1196 456 EE 457
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
276-748 |
7.60e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 56.34 E-value: 7.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 276 ERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKA---------------AEGKQ------------ 328
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAetelcaeaeemrarlAARKQeleeilhelesr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 329 ----EEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVR---LEPLQEKTLKECSSLEKLM-- 399
Cdd:pfam01576 84 leeeEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDillLEDQNSKLSKERKLLEERIse 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 400 VQGHLTKVVEESK-LSK-ENQAKAKESDLSDTL----------SPSKEKSSDDTTDAQMDEQDLNEPLA--KVSLLK--D 463
Cdd:pfam01576 164 FTSNLAEEEEKAKsLSKlKNKHEAMISDLEERLkkeekgrqelEKAKRKLEGESTDLQEQIAELQAQIAelRAQLAKkeE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 464 DLQGTQA--ETEAKQDTQHLRK---------ELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQ 532
Cdd:pfam01576 244 ELQAALArlEEETAQKNNALKKireleaqisELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 533 RLHMDMENLQ----EEK---DTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEY 605
Cdd:pfam01576 324 KREQEVTELKkaleEETrshEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 606 EEEIRSLQST---FQLRCQQCEVQQREEA---TRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQ 679
Cdd:pfam01576 404 EHKRKKLEGQlqeLQARLSESERQRAELAeklSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683057 680 SLELTSDLsilqmtrKELENQMGSLKEQhlrdeadlktlLSKAENQAKDVQKEYEKTQTVLSELKLKFE 748
Cdd:pfam01576 484 KLNLSTRL-------RQLEDERNSLQEQ-----------LEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
212-773 |
1.91e-07 |
|
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: 55.05 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 212 RLLSRLEVMGNQLQACSKNQTEDSLRKELVALQEDKHSYETTAKESLRRVLQEKIEvvrkLSEVERSlSNTEDECTHLRE 291
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE----LDGFERG-PFSERQIKNFHT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 292 MNERTQEELRELANKyngavnEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQadndftn 371
Cdd:TIGR00606 398 LVIERQEDEAKTAAQ------LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ------- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 372 eRLTALQVRLEPLQEKTLKECSSLEKLMVQGHLtkvveESKLSKENQAKAKESDLSDTLSPSKEKssddttdaqMDEQDL 451
Cdd:TIGR00606 465 -QLEGSSDRILELDQELRKAERELSKAEKNSLT-----ETLKKEVKSLQNEKADLDRKLRKLDQE---------MEQLNH 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 452 NEPLAKVSLLKDDLQGTQAETEAKQDTQHLRKELVEAQELARASKqkcfdLQALLEEERKAyRNQVEESAKQIQVLQVQL 531
Cdd:TIGR00606 530 HTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQ-----LEDWLHSKSKE-INQTRDRLAKLNKELASL 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 532 QRLHMDMENLQEEKDTEISSTRDKLLSAQdeilllhqaaakAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRS 611
Cdd:TIGR00606 604 EQNKNHINNELESKEEQLSSYEDKLFDVC------------GSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQ 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 612 LQSTFQLRCQQC------EVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLL-------SSELQRQEKELHNSQK 678
Cdd:TIGR00606 672 LTDENQSCCPVCqrvfqtEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglapgrQSIIDLKEKEIPELRN 751
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 679 QSLELTSDLSILQMTRKELENQMGSL--KEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVL--SELKLKFEMTEQEK 754
Cdd:TIGR00606 752 KLQKVNRDIQRLKNDIEEQETLLGTImpEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLqgSDLDRTVQQVNQEK 831
|
570
....*....|....*....
gi 1958683057 755 QSITDELKQCKDNLKLLRE 773
Cdd:TIGR00606 832 QEKQHELDTVVSKIELNRK 850
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
481-763 |
2.03e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 481 LRKELVEAQELARASKQKcfdlqaLLEEERKAYRNQVEESAKQIQVLQVQLQRLhmdmENLQEEKDTEISSTRDKLLSAQ 560
Cdd:COG1196 218 LKEELKELEAELLLLKLR------ELEAELEELEAELEELEAELEELEAELAEL----EAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 561 DEILLLHQAAAKAVSERD---TDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQstfqlrcqqcevqqrEEATRLQGE 637
Cdd:COG1196 288 AEEYELLAELARLEQDIArleERRRELEERLEELEEELAELEEELEELEEELEELE---------------EELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 638 LEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLKT 717
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1958683057 718 LLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 763
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
339-756 |
2.33e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 54.36 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 339 KKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEKTLKECSSLEKLMVQGHLTKVVEESKLSKENQ 418
Cdd:pfam05557 15 QNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 419 AKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETeakQDTQHLRKELVEAQELARASKQK 498
Cdd:pfam05557 95 KESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKA---SEAEQLRQNLEKQQSSLAEAEQR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 499 CFDLQalleeerkaYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISstrdKLLSAQDEILLLHQAAA--KAVSE 576
Cdd:pfam05557 172 IKELE---------FEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNK----HLNENIENKLLLKEEVEdlKRKLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 577 RDTDFM----SLQEELKKVRAELEGWRKAASEYEEEIRS--LQSTFQLRCQQCEVQQREEATRLQGELEKLKKEWDVLEN 650
Cdd:pfam05557 239 REEKYReeaaTLELEKEKLEQELQSWVKLAQDTGLNLRSpeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 651 ECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDL----SILQMTRKELENQMGSlkEQHLRDEADLKTLLSKAENQA 726
Cdd:pfam05557 319 ELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgyrAILESYDKELTMSNYS--PQLLERIEEAEDMTQKMQAHN 396
|
410 420 430
....*....|....*....|....*....|
gi 1958683057 727 KDVQKEYEKTQTVLSELKLKFEMTEQEKQS 756
Cdd:pfam05557 397 EEMEAQLSVAEEELGGYKQQAQTLERELQA 426
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
251-769 |
3.11e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 251 ETTAKESLRRVLQ-EKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELR-ELANKYNGA--VNEIKDLSDKLKAAE- 325
Cdd:PTZ00121 1114 ARKAEEAKKKAEDaRKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKaEEARKAEDAkkAEAARKAEEVRKAEEl 1193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 326 GKQEEIQQKGQAEKKELQAKIDDMEEKEQElqAKIEALQADNDFTNERLTALQVRLEPLQEKTLKECSSLEKLMVQGHLT 405
Cdd:PTZ00121 1194 RKAEDARKAEAARKAEEERKAEEARKAEDA--KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAA 1271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 406 KVVEESKLSKENQaKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKvsllkddlqgtQAEtEAKQDTQHLRKEL 485
Cdd:PTZ00121 1272 IKAEEARKADELK-KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK-----------KAE-EAKKKADAAKKKA 1338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 486 VEAQ---ELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMEnlQEEKDTEISSTRDKLLSAQDE 562
Cdd:PTZ00121 1339 EEAKkaaEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE--AKKKAEEDKKKADELKKAAAA 1416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 563 ILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQQREEATRLQGELEKLK 642
Cdd:PTZ00121 1417 KKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAK 1496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 643 KEWDVLENECRSLKKENVLLSSELQRQEKELHNSQK----QSLELTSDLSILQMTRKELENQMGSLK---EQHLRDEADL 715
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEakkaDEAKKAEEKKKADELKKAEELKKAEEKkkaEEAKKAEEDK 1576
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683057 716 KTLLSKAENQAKDVQKEYEKTQTVL-SELKLKFEMT--EQEKQSITDELKQCKDNLK 769
Cdd:PTZ00121 1577 NMALRKAEEAKKAEEARIEEVMKLYeEEKKMKAEEAkkAEEAKIKAEELKKAEEEKK 1633
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
229-735 |
4.73e-07 |
|
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: 53.90 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 229 KNQTEDSLRK---ELVALQEDKHSYettakeslRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELA- 304
Cdd:TIGR00606 586 INQTRDRLAKlnkELASLEQNKNHI--------NNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAm 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 305 -----NKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQV 379
Cdd:TIGR00606 658 lagatAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQS 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 380 RLEpLQEKTLKEcssleklmVQGHLTKVVEEskLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQ---DLNEPLA 456
Cdd:TIGR00606 738 IID-LKEKEIPE--------LRNKLQKVNRD--IQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERfqmELKDVER 806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 457 KVSLLKDDLQGTqaetEAKQDTQHLRKELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHM 536
Cdd:TIGR00606 807 KIAQQAAKLQGS----DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQR 882
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 537 --DMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQS 614
Cdd:TIGR00606 883 rqQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIEN 962
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 615 TFQLRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKenvllSSELQRQEKELHNSQKQSLELTSDLSILQMTR 694
Cdd:TIGR00606 963 KIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQ-----DIDTQKIQERWLQDNLTLRKRENELKEVEEEL 1037
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1958683057 695 KELENQMG-----SLKEQHLRDEADLKtLLSKAENQAKDVQKEYEK 735
Cdd:TIGR00606 1038 KQHLKEMGqmqvlQMKQEHQKLEENID-LIKRNHVLALGRQKGYEK 1082
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
161-773 |
6.43e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.20 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 161 YSQELFQLSQYLQEA--LHREQ--MLEQKLATLQRLLAITQEASDtswqALIDedrlLSRLEvmgNQLQACSKNQTEDSL 236
Cdd:pfam15921 83 YSHQVKDLQRRLNESneLHEKQkfYLRQSVIDLQTKLQEMQMERD----AMAD----IRRRE---SQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 237 RKELVA--LQEDKHSYETTAKESLRR-------VLQEKIEVVRKLSEVERSLSNTEDECT--HLREMNERTQEELRELAN 305
Cdd:pfam15921 152 HELEAAkcLKEDMLEDSNTQIEQLRKmmlshegVLQEIRSILVDFEEASGKKIYEHDSMStmHFRSLGSAISKILRELDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 306 kyngavnEIKDLSDKLKAAEGKQEEIQQKGQAEKKEL-QAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPL 384
Cdd:pfam15921 232 -------EISYLKGRIFPVEDQLEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEII 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 385 QEKT-------LKECSSLEKLMVQghLTKVVEESKLSKENQAKAKESDL----SDTLSPSKEKSSDDTTDAQMDEQ---- 449
Cdd:pfam15921 305 QEQArnqnsmyMRQLSDLESTVSQ--LRSELREAKRMYEDKIEELEKQLvlanSELTEARTERDQFSQESGNLDDQlqkl 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 450 --DLNEPLAKVSLLKDDLQGTQAETEAKQDT-QHLRKELVEAQ-ELARaskqkcfdLQALLEEERKAYRNQVEEsakqiq 525
Cdd:pfam15921 383 laDLHKREKELSLEKEQNKRLWDRDTGNSITiDHLRRELDDRNmEVQR--------LEALLKAMKSECQGQMER------ 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 526 vlqvqlqrlHMDMENLQEEKDTEISSTRDKLLSAQDEIlllhqaaAKAVSERDTDFMSLQEELKKVR---AELEGWRKAA 602
Cdd:pfam15921 449 ---------QMAAIQGKNESLEKVSSLTAQLESTKEML-------RKVVEELTAKKMTLESSERTVSdltASLQEKERAI 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 603 SEYEEEIRSLQSTFQLRCQqcevqqreeatrlqgELEKLKKEWDVLEN---ECRSLKKENVLLSSELQRQEKELHNSQKQ 679
Cdd:pfam15921 513 EATNAEITKLRSRVDLKLQ---------------ELQHLKNEGDHLRNvqtECEALKLQMAEKDKVIEILRQQIENMTQL 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 680 SLELTSDLSILQMTRKELENQMG----SLKE-QHLRDEADLKtlLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEK 754
Cdd:pfam15921 578 VGQHGRTAGAMQVEKAQLEKEINdrrlELQEfKILKDKKDAK--IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQER 655
|
650
....*....|....*....
gi 1958683057 755 QSITDELKQCKDNLKLLRE 773
Cdd:pfam15921 656 DQLLNEVKTSRNELNSLSE 674
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
27-106 |
7.85e-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: 7.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 27 PIKIGRSVARcRPAQNNATFDC-----KVLSRNHALVWFDHKTSKFYLQdTKSSNGTFINSQRLSRGseeSPPCEILSGD 101
Cdd:cd22701 18 EVVLGRNSKN-SSSTAADSVDIdlgpsKKISRRHARIFYDFTTQCFELS-VLGRNGVKVDGILVKPG---SPPVPLRSGS 92
|
....*
gi 1958683057 102 IIQFG 106
Cdd:cd22701 93 LIQIG 97
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
267-769 |
1.22e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.33 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 267 EVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKI 346
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 347 DDMEEKEQE---LQAKIEALQADNDFTNERLTALQVRLEPLQEK---TLKECSSLEKlmvQGHLTKVVEESKLSKENQAK 420
Cdd:TIGR04523 117 EQKNKLEVElnkLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKyndLKKQKEELEN---ELNLLEKEKLNIQKNIDKIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 421 AKESDLSDTLSPSKEKSSDDTTDaqmdEQDLNEPLAKVSLLKDDLQgtqaetEAKQDTQHLRKELVEAQELARASKQKCF 500
Cdd:TIGR04523 194 NKLLKLELLLSNLKKKIQKNKSL----ESQISELKKQNNQLKDNIE------KKQQEINEKTTEISNTQTQLNQLKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 501 DLQALLEEERKayrnQVEESAKQIQVLQVQLQRLHMDMENLQEEKD--------TEISSTRDKLLSAQDEILLLHQAAA- 571
Cdd:TIGR04523 264 KIKKQLSEKQK----ELEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwnkelkSELKNQEKKLEEIQNQISQNNKIISq 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 572 ---------KAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEvQQREEATRLQGELEKLK 642
Cdd:TIGR04523 340 lneqisqlkKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ-NQEKLNQQKDEQIKKLQ 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 643 KEWDVLENECRSLKKENVLLSSE------------------------------------------LQRQEKELHNSQKQS 680
Cdd:TIGR04523 419 QEKELLEKEIERLKETIIKNNSEikdltnqdsvkeliiknldntresletqlkvlsrsinkikqnLEQKQKELKSKEKEL 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 681 LELTSDLSILQMTRKELENQMGSLKEQhlrdEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMteQEKQSITDE 760
Cdd:TIGR04523 499 KKLNEEKKELEEKVKDLTKKISSLKEK----IEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEI--DEKNKEIEE 572
|
....*....
gi 1958683057 761 LKQCKDNLK 769
Cdd:TIGR04523 573 LKQTQKSLK 581
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
310-576 |
1.57e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 310 AVNEIKDLSDKLKAAEGKQEEIQqkgqAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEKtl 389
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQ----AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 390 kecssleklmvqghltkvveeskLSKENQAKAKESDLSDTLspskekssddttDAQMDEQDLNEPLAKVSLLKddlQGTQ 469
Cdd:COG3883 88 -----------------------LGERARALYRSGGSVSYL------------DVLLGSESFSDFLDRLSALS---KIAD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 470 AETEAKQDTQHLRKELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEI 549
Cdd:COG3883 130 ADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
250 260
....*....|....*....|....*..
gi 1958683057 550 SSTRDKLLSAQDEILLLHQAAAKAVSE 576
Cdd:COG3883 210 AAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
26-106 |
1.83e-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: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 26 EPIKIGRSVArcrpaqNNATFDCKVLSRNHALVwfDHKTSKFYLQDTKSSNGTFINSQRLSRGseesppcEILSGDIIQF 105
Cdd:cd22698 21 DEFTIGRSSN------NDIRLNDHSVSRHHARI--VRQGDKCNLTDLGSTNGTFLNGIRVGTH-------ELKHGDRIQL 85
|
.
gi 1958683057 106 G 106
Cdd:cd22698 86 G 86
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
25-114 |
1.89e-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: 47.35 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 25 DEPIKIGRSVArcrpAQNNATFDC-KVLSRNHALVWFDHKTSKFyLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDII 103
Cdd:cd22663 20 GKEVTVGRGLG----VTYQLVSTCpLMISRNHCVLKKNDEGQWT-IKDNKSLNGVWVNGERI----EPLKPYPLNEGDLI 90
|
90
....*....|.
gi 1958683057 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 |
2.07e-06 |
|
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 (AtPP2C70) and similar proteins; AtPP2C70, also called kinase-associated protein phosphatase, or protein ROOT ATTENUATED GROWTH 1, dephosphorylates the serine/threonine receptor-like kinase RLK5. It may function as a signaling component in a pathway involving RLK5. It acts as a negative regulator of the CLAVATA1 signaling in plant development by binding and dephosphorylating CLAVATA1. It is also a component of a signaling pathway which mediates adaptation to NaCl stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438730 [Multi-domain] Cd Length: 102 Bit Score: 46.97 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 27 PIKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLsrgSEESPPCEILSGDIIQFG 106
Cdd:cd22678 24 PLTIGRIQ------RGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESI---SPNGRPVVLSSGDVITLG 94
|
90
....*....|.
gi 1958683057 107 vdvTENTRKVT 117
Cdd:cd22678 95 ---SETKILVR 102
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
299-774 |
3.16e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.79 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 299 ELRELANKYNGAVNEIKDLSDKLKAAEG---KQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNErlt 375
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKnlnKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINS--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 376 alQVRLEPLQEKTLK-ECSSLEK--LMVQGHLTKVVEESKlSKENQAKAKESDLSDT------LSPSKEKSSDDTTDAQM 446
Cdd:TIGR04523 111 --EIKNDKEQKNKLEvELNKLEKqkKENKKNIDKFLTEIK-KKEKELEKLNNKYNDLkkqkeeLENELNLLEKEKLNIQK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 447 DEQDLNEPLAKVSLLKDDLQG---------------TQAETEAKQDTQHLRKELVEAQELARASKQKCFDLQALLEEERK 511
Cdd:TIGR04523 188 NIDKIKNKLLKLELLLSNLKKkiqknkslesqiselKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 512 ---AYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDEILllhQAAAKAVSERDTDFMSLQEEL 588
Cdd:TIGR04523 268 qlsEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKL---EEIQNQISQNNKIISQLNEQI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 589 KKVRAELEGWRKAASEYEEEIRSLQstfqlrcQQCEVQQREEATRLQgELEKLKKEWDVLENECRSLKKENVLLSSELQR 668
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQRELEEKQ-------NEIEKLKKENQSYKQ-EIKNLESQINDLESKIQNQEKLNQQKDEQIKK 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 669 QEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHlrdeADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFE 748
Cdd:TIGR04523 417 LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELII----KNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELK 492
|
490 500
....*....|....*....|....*.
gi 1958683057 749 MTEQEKQSITDELKQCKDNLKLLREK 774
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKK 518
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
55-108 |
3.46e-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: 3.46e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1958683057 55 HALVWFDHKTSKFYLQDTKSSNGTFINSQRLSrgseESPPCEILSGDIIQFGVD 108
Cdd:cd22704 39 HAVITYDQIDNEFKIKDLGSLNGTFVNDSRIP----EQTYITLKLGDSIRFGYD 88
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
152-618 |
4.50e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 152 KVAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDtswqaliDEDRLLSRLEVMGNQLQACSKNQ 231
Cdd:COG4717 60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA-------ELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 232 TEDSLRKELVALQEdkhsyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDEC-THLREMNERTQEELRELANKYNGA 310
Cdd:COG4717 133 ELEALEAELAELPE--------RLEELEERLEELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 311 VNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLqektLK 390
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV----LF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 391 ECSSLEKLMVQGHLTKVVEESKLSKENQAKAKESDLS--------DTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLK 462
Cdd:COG4717 281 LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEeeeleellAALGLPPDLSPEELLELLDRIEELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 463 DDLQGTQAETEAKQDTQHL----RKELVEAQELARASKQkcfdlqalLEEERKAYRNQVEESAKQIQVLQVQLQRlhMDM 538
Cdd:COG4717 361 EELQLEELEQEIAALLAEAgvedEEELRAALEQAEEYQE--------LKEELEELEEQLEELLGELEELLEALDE--EEL 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 539 ENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKAvsERDTDFMSLQEELKKVRAELEgwrkaasEYEEEIRSLQSTFQL 618
Cdd:COG4717 431 EEELEELEEELEELEEELEELREELAELEAELEQL--EEDGELAELLQELEELKAELR-------ELAEEWAALKLALEL 501
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
451-774 |
6.48e-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: 49.74 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 451 LNEPLAKVSLLKDDLQGTQAETEAKQDTQHLRKElveAQELARaskqkcfdlqallEEERkayRNQVEESAKQIQVLQVQ 530
Cdd:pfam17380 271 LNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQE---KEEKAR-------------EVER---RRKLEEAEKARQAEMDR 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 531 LQRLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELK--KVRAELEGWRKAASEYEEE 608
Cdd:pfam17380 332 QAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKneRVRQELEAARKVKILEEER 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 609 IRSLQStfQLRCQQCEVQQREEATrlQGELEKLKKEwdvLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDls 688
Cdd:pfam17380 412 QRKIQQ--QKVEMEQIRAEQEEAR--QREVRRLEEE---RAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE-- 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 689 ilQMTRKELENQMGSLKEQHLRDEadlKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQ-EKQSITDELKQCKDN 767
Cdd:pfam17380 483 --KRDRKRAEEQRRKILEKELEER---KQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEErRKQQEMEERRRIQEQ 557
|
....*..
gi 1958683057 768 LKLLREK 774
Cdd:pfam17380 558 MRKATEE 564
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
182-701 |
7.92e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 182 LEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgnqlqacSKNQTEDSLRKELVALQEDKHSYETTaKESLRRV 261
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHE---------ERREELETLEAEIEDLRETIAETERE-REELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 262 LQEKIEVVRKLSE------VERSLSNTEDECTHLR-----EMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEE 330
Cdd:PRK02224 281 VRDLRERLEELEEerddllAEAGLDDADAEAVEARreeleDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 331 IQQKGQAEKKELQA---KIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEktlkecsslEKLMVQGHLTKV 407
Cdd:PRK02224 361 LREEAAELESELEEareAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE---------ERDELREREAEL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 408 VEESKLSKENQAKAKESdLSDTLSPSKEKSSDDTTDAQMDEQDlNEPLAKVSLLKDDLQGTQAETEAKQDTQhlrKELVE 487
Cdd:PRK02224 432 EATLRTARERVEEAEAL-LEAGKCPECGQPVEGSPHVETIEED-RERVEELEAELEDLEEEVEEVEERLERA---EDLVE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 488 AQELARASKQKCFDLQALLEEErkayRNQVEESAKQIQVLQVQLQRLHMDMENLQE---EKDTEISSTRDKLLSAQDEIL 564
Cdd:PRK02224 507 AEDRIERLEERREDLEELIAER----RETIEEKRERAEELRERAAELEAEAEEKREaaaEAEEEAEEAREEVAELNSKLA 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 565 LLHQA--AAKAVSERDTDFMSLQEELKKVRAELEGW-------RKAASEYEEEIRSLQSTFQLRCQQCEVQQREEAT--- 632
Cdd:PRK02224 583 ELKERieSLERIRTLLAAIADAEDEIERLREKREALaelnderRERLAEKRERKRELEAEFDEARIEEAREDKERAEeyl 662
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958683057 633 -RLQGELEKLKKEWDVLENECRSLkkENVLLSSELQRQEKELHNSQKQSLE-LTSDLSILQMTRKELENQM 701
Cdd:PRK02224 663 eQVEEKLDELREERDDLQAEIGAV--ENELEELEELRERREALENRVEALEaLYDEAEELESMYGDLRAEL 731
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
581-774 |
8.46e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 8.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 581 FMSLQEELKKVRAELegWRKAASEYEEEIRSLQSTFQLRCQQCEVQQREEATrLQGELEKLKKEWDVLENECRSLKKENV 660
Cdd:COG1196 215 YRELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAE-LEAELEELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 661 LLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQhlrdEADLKTLLSKAENQAKDVQKEYEKTQTVL 740
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE----LEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190
....*....|....*....|....*....|....
gi 1958683057 741 SELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 774
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
584-774 |
9.78e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 9.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 584 LQEELKKVRAELEGWRKAASEYeeeiRSLQSTFQLRCQQCEVQQREEatrLQGELEKLKKEWDVLENECRSLKKENVLLS 663
Cdd:COG1196 194 ILGELERQLEPLERQAEKAERY----RELKEELKELEAELLLLKLRE---LEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 664 SELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTLlskaENQAKDVQKEYEKTQTVLSEL 743
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL----EEELAELEEELEELEEELEEL 342
|
170 180 190
....*....|....*....|....*....|.
gi 1958683057 744 KLKFEMTEQEKQSITDELKQCKDNLKLLREK 774
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
231-771 |
1.02e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.45 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 231 QTEDSLRKELVALQEDKHSYETTAKEslRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEEL-RELANKYNG 309
Cdd:pfam12128 353 QSELENLEERLKALTGKHQDVTAKYN--RRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALeSELREQLEA 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 310 AVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKEL------QAKIDDMEEKEQELQAKIEALQADN--------------DF 369
Cdd:pfam12128 431 GKLEFNEEEYRLKSRLGELKLRLNQATATPELLlqlenfDERIERAREEQEAANAEVERLQSELrqarkrrdqasealRQ 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 370 TNERLTALQVRLEPLQEKTLKECSSL--------------------EKLMVQGHLTKVVEESKLSKEN----------QA 419
Cdd:pfam12128 511 ASRRLEERQSALDELELQLFPQAGTLlhflrkeapdweqsigkvisPELLHRTDLDPEVWDGSVGGELnlygvkldlkRI 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 420 KAKES-DLSDTLSPSKEKSSDDTTDAQMDEQDLNEPL--AKVSLLKDDLQGTQAETEAKQDTQHLRKELVEAQELARASK 496
Cdd:pfam12128 591 DVPEWaASEEELRERLDKAEEALQSAREKQAAAEEQLvqANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKN 670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 497 QKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKA--- 573
Cdd:pfam12128 671 KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAelk 750
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 574 --VSERDTDFMS----------LQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQQRE---EATRLQGEL 638
Cdd:pfam12128 751 alETWYKRDLASlgvdpdviakLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNierAISELQQQL 830
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 639 EKLKKEwdvlenecrslkkenvllsSELQRQ--EKELHNSQKQSLELTSDLSILqmtrKELENQMGSLKEQHLRDEAD-- 714
Cdd:pfam12128 831 ARLIAD-------------------TKLRRAklEMERKASEKQQVRLSENLRGL----RCEMSKLATLKEDANSEQAQgs 887
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683057 715 -------LKTLLSKAENQAKDVQKEYEKTQTVL-----SELKLKFEMTEQEKQSITDELKQCKDNLKLL 771
Cdd:pfam12128 888 igerlaqLEDLKLKRDYLSESVKKYVEHFKNVIadhsgSGLAETWESLREEDHYQNDKGIRLLDYRKLV 956
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
178-365 |
1.03e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 178 REQML--EQKLATLQRLLAITQEAsDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKELVALQEDKhsyetTAK 255
Cdd:COG4913 241 HEALEdaREQIELLEPIRELAERY-AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAEL-----ERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 256 ESLRRVLQEKIEVVR---------KLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEG 326
Cdd:COG4913 315 EARLDALREELDELEaqirgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE 394
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958683057 327 KQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQA 365
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
153-388 |
1.98e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 153 VAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgNQLQAcsKNQT 232
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE---QELAA--LEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 233 EDSLRKELVALQEDKHSYETTAKESLRRV----LQEKIEVV---RKLSEVERSLSNTEDECTHLREMNERTQEELRELAN 305
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRALyrlgRQPPLALLlspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 306 KyngaVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQ 385
Cdd:COG4942 165 L----RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
...
gi 1958683057 386 EKT 388
Cdd:COG4942 241 ERT 243
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
52-106 |
2.14e-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: 2.14e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683057 52 SRNH-ALVWfdHK-TSKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22674 48 SRVHaALVY--HKhLNRVFLIDLGSTHGTFVGGIRL----EPHKPQQLPIDSTLRFG 98
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
273-596 |
2.27e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 273 SEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAkiddMEEK 352
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR----LEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 353 EQELQAKIEALQADNDFTNERLTALQVRLEPLQEKtLKECS----SLEKLMVQGHLTKVVEESKLSKENQAKAKESDLSD 428
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEE-LAEAEaeieELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 429 TLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQDTQH--------LRKELVEAQELARASKQKCF 500
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELEseleallnERASLEEALALLRSELEELS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 501 DLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEkdteisstrdklLSAQDEILLlhQAAAKAVSERDTD 580
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER------------LSEEYSLTL--EEAEALENKIEDD 966
|
330
....*....|....*.
gi 1958683057 581 FMSLQEELKKVRAELE 596
Cdd:TIGR02168 967 EEEARRRLKRLENKIK 982
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
51-106 |
2.45e-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: 2.45e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683057 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 |
2.81e-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: 2.81e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683057 28 IKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDhkTSKFYLQDTKSSNGTFINSQRlsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22680 23 VSIGRDP------ENVIVIPDPFVSRNHARITVD--SNEIYIEDLGSTNGTFVNDFK-----RIKGPAKLHPNDIIKLG 88
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
14-106 |
2.85e-05 |
|
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.
Pssm-ID: 438734 [Multi-domain] Cd Length: 96 Bit Score: 43.67 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 14 SHPFQERHvyldepIKIGRSVarcrpaQNNATFDCKVLSRNHALvwFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEesp 93
Cdd:cd22682 14 QFPITEST------IVIGRSV------ESQVQIDDDSVSRYHAK--LAVNPSAVSIIDLGSTNGTIVNGKKIPKLAS--- 76
|
90
....*....|...
gi 1958683057 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 |
3.13e-05 |
|
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine/threonine-protein kinase RAD53 and similar proteins; RAD53, also called CHEK2 homolog, or serine-protein kinase 1 (Spk1), is a nuclear protein kinase that phosphorylates proteins on serine, threonine, and tyrosine. It controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints and prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. It may be involved in the phosphorylation of RPH1. RAD53 contains two FHA domains. This model corresponds to the second one. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438742 [Multi-domain] Cd Length: 105 Bit Score: 43.43 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 12 PNSHPfqerHVYL-DEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTSKF---YLQDTkSSNGTFINSQRLSR 87
Cdd:cd22690 8 NPSYP----DIELtQNTTFIGRS------KDCDEEITDPRISKHHCIITRKRSGKGLddvYVTDT-STNGTFINNNRLGK 76
|
90
....*....|....*.
gi 1958683057 88 GSEesppCEILSGDII 103
Cdd:cd22690 77 GSQ----SLLQDGDEI 88
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
258-397 |
3.21e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 258 LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQ----- 332
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkey 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958683057 333 QKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEKTLKECSSLEK 397
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
234-658 |
3.49e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 234 DSLRKELVALQEDKHSYETtAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNER--TQEELRELANKYNGAV 311
Cdd:COG4717 74 KELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELeaLEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 312 NEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEktlkE 391
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE----E 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 392 CSSLEKLMVQGHltkvvEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMdeQDLNEPLAKVSLLKDDLQGTQAE 471
Cdd:COG4717 229 LEQLENELEAAA-----LEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV--LFLVLGLLALLFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 472 TEAKQDTQHLRKELVEAQELARASKQKCFDLQALLEEERKAYRNQVEesaKQIQVLQVQLQRLHMDMENLQEEKDTEISS 551
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE---LQELLREAEELEEELQLEELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 552 TRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAEL-----EGWRKAASEYEEEIRSLQSTF-QLRCQQCEV 625
Cdd:COG4717 379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLealdeEELEEELEELEEELEELEEELeELREELAEL 458
|
410 420 430
....*....|....*....|....*....|...
gi 1958683057 626 QQREEATRLQGELEKLKKEWDVLENECRSLKKE 658
Cdd:COG4717 459 EAELEQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
210-519 |
3.93e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 210 EDRLLSRLEVMGNQLQacsKNQTEDSLRKELVALQEDKHSYETTAK--------ESLRRVLQEKIEVVRKLSEVERSLSN 281
Cdd:TIGR02169 186 IERLDLIIDEKRQQLE---RLRREREKAERYQALLKEKREYEGYELlkekealeRQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 282 TEDECTH----LREMNERTQEELRElankyngavnEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQakidDMEEKEQELQ 357
Cdd:TIGR02169 263 LEKRLEEieqlLEELNKKIKDLGEE----------EQLRVKEKIGELEAEIASLERSIAEKERELE----DAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 358 AKIEALQADNDFTNERLTALQVRLEPLQEKTLKECSSLEKLMVQghLTKVVEESKLSKENQAKAKE--SDLSDTLSPSKE 435
Cdd:TIGR02169 329 AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE--LEEVDKEFAETRDELKDYREklEKLKREINELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 436 KSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQD-TQHLRKELVEAQELARASKQKCFDLQA---LLEEERK 511
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALeIKKQEWKLEQLAADLSKYEQELYDLKEeydRVEKELS 486
|
....*...
gi 1958683057 512 AYRNQVEE 519
Cdd:TIGR02169 487 KLQRELAE 494
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
312-777 |
4.53e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.02 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 312 NEIKDLSDKLKAAEGKQEEIQQKGQAEKKE-------LQAKIDDMEEKEQELQAKIEALQADNDFtneRLTALQVRLEPL 384
Cdd:pfam05483 151 NATRHLCNLLKETCARSAEKTKKYEYEREEtrqvymdLNNNIEKMILAFEELRVQAENARLEMHF---KLKEDHEKIQHL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 385 QEKTLKECSSLEKlMVQGHLTKVVEesklsKENQAKakesDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDD 464
Cdd:pfam05483 228 EEEYKKEINDKEK-QVSLLLIQITE-----KENKMK----DLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 465 LQGTQAETEAKQDTQHLRKElveaqELARASKQKCfdlqaLLEEERKAyrnQVEESAKQIQVLQVQLQRLHMDMENLQEE 544
Cdd:pfam05483 298 LEDIKMSLQRSMSTQKALEE-----DLQIATKTIC-----QLTEEKEA---QMEELNKAKAAHSFVVTEFEATTCSLEEL 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 545 KDTEisstRDKLLSAQDEILLLHQAAAKAVSERD--TDFMSLQE----ELKKVRAELEGWRKAASEYEEEIRSLQSTFQl 618
Cdd:pfam05483 365 LRTE----QQRLEKNEDQLKIITMELQKKSSELEemTKFKNNKEveleELKKILAEDEKLLDEKKQFEKIAEELKGKEQ- 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 619 rcqqcevqqreeatRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELE 698
Cdd:pfam05483 440 --------------ELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELT 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 699 NQMGSL--------------KEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQC 764
Cdd:pfam05483 506 QEASDMtlelkkhqediincKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKK 585
|
490
....*....|...
gi 1958683057 765 KDNLKLLREKGNN 777
Cdd:pfam05483 586 EKQMKILENKCNN 598
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
245-759 |
5.51e-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: 46.64 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 245 EDKHSYETTAKES-LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKA 323
Cdd:pfam05483 228 EEEYKKEINDKEKqVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 324 AEGKQEEIQQkgqaekkELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEKTLKECSSLEKLMVQGH 403
Cdd:pfam05483 308 SMSTQKALEE-------DLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLK 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 404 LtkvveeskLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQDTQHLRK 483
Cdd:pfam05483 381 I--------ITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEI 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 484 ELVEAQELARASKQKcfdlqalleeerkAYRNQVEEsakqiqvlqvqlqrLHMDMENlQEEKDTEISSTRDKLLSAQDEI 563
Cdd:pfam05483 453 HDLEIQLTAIKTSEE-------------HYLKEVED--------------LKTELEK-EKLKNIELTAHCDKLLLENKEL 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 564 LLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQ--CEVQQREEATR-LQGELEK 640
Cdd:pfam05483 505 TQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEvkCKLDKSEENARsIEYEVLK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 641 LKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTLLS 720
Cdd:pfam05483 585 KEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIE 664
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1958683057 721 KAENQAKDVQKEYEKTQTVLSE-LKLKFEMTEQEKQSITD 759
Cdd:pfam05483 665 DKKISEEKLLEEVEKAKAIADEaVKLQKEIDKRCQHKIAE 704
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
563-774 |
5.70e-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: 46.30 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 563 ILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQStfQLRCQQCEVQQRE-EATRLQGELEKL 641
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER--RIAALARRIRALEqELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 642 KKEWDVLENECRSLKKE-----------------NVLLSSE-LQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGS 703
Cdd:COG4942 89 EKEIAELRAELEAQKEElaellralyrlgrqpplALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958683057 704 LKEQHlrdeADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 774
Cdd:COG4942 169 LEAER----AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
177-763 |
6.49e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 177 HREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDslrkELVALQEDKHSYETTAKE 256
Cdd:TIGR00618 304 QIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAH----EVATSIREISCQQHTLTQ 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 257 SLRRvLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQ 336
Cdd:TIGR00618 380 HIHT-LQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEK 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 337 AEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEKTLKECSSLEKLMVQGHLTKVVEESkLSKE 416
Cdd:TIGR00618 459 IHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRG-EQTY 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 417 NQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQD-----TQHLRKELVEAQEL 491
Cdd:TIGR00618 538 AQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDlteklSEAEDMLACEQHAL 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 492 ARASKQKCFDLQALLEEERKAYRNQVEESAkqiqvlqvqlqrLHMDMENLQEEKDTEISstrdkLLSAQDEILLLHQAAA 571
Cdd:TIGR00618 618 LRKLQPEQDLQDVRLHLQQCSQELALKLTA------------LHALQLTLTQERVREHA-----LSIRVLPKELLASRQL 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 572 KAVSERdtdfmSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQQREeatrLQGELEKLKKEWDVLENE 651
Cdd:TIGR00618 681 ALQKMQ-----SEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSD----LAAREDALNQSLKELMHQ 751
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 652 CRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHlrdEADLKTLLSKAENQAKDVQK 731
Cdd:TIGR00618 752 ARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEI---GQEIPSDEDILNLQCETLVQ 828
|
570 580 590
....*....|....*....|....*....|..
gi 1958683057 732 EYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 763
Cdd:TIGR00618 829 EEEQFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
13-110 |
6.77e-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: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 13 NSHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTskFYLQDTKSSNGTFINSQRLSrgsee 91
Cdd:cd22665 7 SQAHGPEKDFPLYEgENVIGRD------PSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRL----- 73
|
90 100
....*....|....*....|.
gi 1958683057 92 SPPC--EILSGDIIQFGvDVT 110
Cdd:cd22665 74 KPNVryELIDGDLLLFG-DVK 93
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
52-107 |
7.17e-05 |
|
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also called cell cycle regulatory protein p95, or Nijmegen breakage syndrome protein 1 (NBS1), is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. Nibrin modulates the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-dependent protein kinase catalytic subunit (DNA-PKcs) to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. Nibrin also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. Nibrin is a major player in the control of intra-S-phase checkpoint. This subfamily also includes Schizosaccharomyces pombe DNA repair and telomere maintenance protein Nbs1 and Arabidopsis thaliana AtNbs1. SpNbs1 is an FHA domain-containing protein required for DNA damage repair and S-phase DNA damage checkpoint. It is involved in telomere length maintenance and maintenance of chromatin structure. AtNbs1 is a component of MRN complex. It also functions in the very early stages of meiosis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438719 [Multi-domain] Cd Length: 108 Bit Score: 42.70 E-value: 7.17e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958683057 52 SRNHALVWFDH---------KTSKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQFGV 107
Cdd:cd22667 40 SRKHATLTVLHpeanlsdpdTRPELTLKDL-SKYGTFVNGEKLKGGSE----VTLKDGDVITFGV 99
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
537-776 |
9.95e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 9.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 537 DMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKaVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQStf 616
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEK-LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE-- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 617 QLRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRK- 695
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKk 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 696 --ELENQMGSLKEQHLRDEaDLKTLLSKAENQAKdvqkeyEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 773
Cdd:PRK03918 347 lkELEKRLEELEERHELYE-EAKAKKEELERLKK------RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
...
gi 1958683057 774 KGN 776
Cdd:PRK03918 420 EIK 422
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
551-747 |
1.03e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 551 STRDKLLSAQDEILLLHQAAAKAVSERDTdfmsLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQcevQQREE 630
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEA----LEAELDALQERREALQRLAEYSWDEIDVASAEREIAELE---AELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 631 ATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLR 710
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958683057 711 DEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKF 747
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRAEEELERAMRAF 796
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
18-86 |
1.39e-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: 1.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683057 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 |
1.57e-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: 1.57e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683057 49 KVLSRNHALVWFDHKTsKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQF 105
Cdd:cd22672 39 KLVSGDHCKIIRDEKG-QVWLEDT-STNGTLVNKVKVVKGQK----VELKHGDVIYL 89
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
569-763 |
1.67e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 569 AAAKAVSERDTDFMSLQEELKKVRAE---LEGWRKAASEYEE------EIRSLQSTFQL--------RCQQCEVQQREEA 631
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQielLEPIRELAERYAAarerlaELEYLRAALRLwfaqrrleLLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 632 TRLQGELEKLKKEWDVLENECRSLKKE------NVL--LSSELQRQEKELHNsqkqsleltsdlsiLQMTRKELENQMGS 703
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQirgnggDRLeqLEREIERLERELEE--------------RERRRARLEALLAA 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 704 LKEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 763
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
162-752 |
1.69e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.20 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 162 SQELFQLSQYLQEALHR----EQMLEQKLATLQRLLAITQEASDTSWQALIDEDRllsRLEVMGNQLQACSKNQTEDSLR 237
Cdd:pfam10174 129 AKELFLLRKTLEEMELRietqKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWER---TRRIAEAEMQLGHLEVLLDQKE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 238 KELVALQEDKHS-YETTAKESLRRVLQEKIEVV-RKLSEVERSLSNTEDECTHLREMNERTQEELRELANKyngaVNEIK 315
Cdd:pfam10174 206 KENIHLREELHRrNQLQPDPAKTKALQTVIEMKdTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQ----MEVYK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 316 DLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEKTLKECSSL 395
Cdd:pfam10174 282 SHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFL 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 396 EKlmvqghltKVVEESKLSKENQAKAKE-SDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQaetea 474
Cdd:pfam10174 362 NK--------KTKQLQDLTEEKSTLAGEiRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQ----- 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 475 kQDTQHLRKELVEAQElARASKQKCfdLQALLEEERKAYRNQVEESAKQIqvlqvqlqrlhmdmENLQEEKDTEISSTRD 554
Cdd:pfam10174 429 -TDSSNTDTALTTLEE-ALSEKERI--IERLKEQREREDRERLEELESLK--------------KENKDLKEKVSALQPE 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 555 KLLSAQDEILLLHQAAAKAVS--ERDTDFMSLQEELKKVRAE---LEGWRKAASEYEEEIR-SLQSTFQLRCQQCEVQQ- 627
Cdd:pfam10174 491 LTEKESSLIDLKEHASSLASSglKKDSKLKSLEIAVEQKKEEcskLENQLKKAHNAEEAVRtNPEINDRIRLLEQEVARy 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 628 REEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQsleltsdlsiLQMTRKELENQMGSLKEQ 707
Cdd:pfam10174 571 KEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVAN----------IKHGQQEMKKKGAQLLEE 640
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1958683057 708 HLRDEADLKTllSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQ 752
Cdd:pfam10174 641 ARRREDNLAD--NSQQLQLEELMGALEKTRQELDATKARLSSTQQ 683
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
563-773 |
2.48e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 563 ILLLHQAAAKAVSERDtdfmSLQEELKKVRAELEGWRKAASEYEEEIRSLQStfQLRcqqcevQQREEATRLQGELEKLK 642
Cdd:COG4942 8 ALLLALAAAAQADAAA----EAEAELEQLQQEIAELEKELAALKKEEKALLK--QLA------ALERRIAALARRIRALE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 643 KEWDVLENECRSLKKENVLLSSELQRQEKELHN------------------SQKQSLELTSDLSILQMTRKELENQMGSL 704
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEELAEllralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683057 705 KEQhLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMT----EQEKQSITDELKQCKDNLKLLRE 773
Cdd:COG4942 156 RAD-LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLlarlEKELAELAAELAELQQEAEELEA 227
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
337-679 |
2.92e-04 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 44.28 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 337 AEKKELQAKIddmEEKEQELQAKIEALQAdndfTNERLTALQVRLEPLQEKTLKECSsleKLMVQGHLTKVV-------- 408
Cdd:pfam13166 89 EESIEIQEKI---AKLKKEIKDHEEKLDA----AEANLQKLDKEKEKLEADFLDECW---KKIKRKKNSALSealngfky 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 409 EESKLSKENQAKAKESDLSDTLSPSKEKSSDDTT---DAQMDEQDLNEPLA------KVSLLKDDLQGTQAETEAKQDTQ 479
Cdd:pfam13166 159 EANFKSRLLREIEKDNFNAGVLLSDEDRKAALATvfsDNKPEIAPLTFNVIdfdaleKAEILIQKVIGKSSAIEELIKNP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 480 HLRKELVEAQELARASKQKCFDLQALLEEERKA-----YRNQVEEsakqiqvlqvqlqrlhmDMENLQEEKDTEISSTRD 554
Cdd:pfam13166 239 DLADWVEQGLELHKAHLDTCPFCGQPLPAERKAaleahFDDEFTE-----------------FQNRLQKLIEKVESAISS 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 555 KL--LSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRK---AASEYE------EEIRSLQST-------- 615
Cdd:pfam13166 302 LLaqLPAVSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRALEAKRKdpfKSIELDsvdakiESINDLVASineliakh 381
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958683057 616 ------FQLRCQQCEVQ-QREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQ 679
Cdd:pfam13166 382 neitdnFEEEKNKAKKKlRLHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQ 452
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
468-707 |
3.12e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 468 TQAETEAKQDTQHLRKELVEAQELARASKQKcfdlQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEekdt 547
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 548 EISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQstfqlrcqqcevQQ 627
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR------------AD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 628 REEATRLQGELEKLKKEWDVLENEcrsLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQ 707
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAE---LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
570-786 |
3.47e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 570 AAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQStfQLRCQQCEVQQ-REEATRLQGELEKLKKEwdvL 648
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA--ELEALQAEIDKlQAEIAEAEAEIEERREE---L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 649 ENECRSLKKE-------NVLLSSE-----LQRQE--KELHNSQKQSLELTSDLsilqmtRKELENQMGSLKEQhlrdEAD 714
Cdd:COG3883 89 GERARALYRSggsvsylDVLLGSEsfsdfLDRLSalSKIADADADLLEELKAD------KAELEAKKAELEAK----LAE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958683057 715 LKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREKGNNPSILQPVPA 786
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
258-522 |
3.69e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 258 LRRVLQEKIEVV---RKLSEVERSLSntEDECTHLREMNERTQ----EELRELANKYNGAVNEIKDLSDKLKAAEGKQ-- 328
Cdd:PRK05771 1 LAPVRMKKVLIVtlkSYKDEVLEALH--ELGVVHIEDLKEELSnerlRKLRSLLTKLSEALDKLRSYLPKLNPLREEKkk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 329 ------EEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDftnerltalqvRLEPlqektLKECSSLEKLMVQG 402
Cdd:PRK05771 79 vsvkslEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIE-----------RLEP-----WGNFDLDLSLLLGF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 403 HLTKVVeESKLSKEnqaKAKESDLSDTLSPSKEKSSDDTTD------AQMDEQDLNEPLAKVSLLKDDLQ--GTQAET-- 472
Cdd:PRK05771 143 KYVSVF-VGTVPED---KLEELKLESDVENVEYISTDKGYVyvvvvvLKELSDEVEEELKKLGFERLELEeeGTPSELir 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1958683057 473 EAKQDTQHLRKELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAK 522
Cdd:PRK05771 219 EIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAEALSK 268
|
|
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
53-106 |
4.80e-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: 4.80e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1958683057 53 RNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPceilsGDIIQFG 106
Cdd:cd22700 36 EQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAP-----GDVLRFG 84
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
25-108 |
4.98e-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: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 25 DEPIKIGRsvarcRPAQNNAT----FDCKVLSRNHALVWFdhKTSKFYLQDTKSSNGTFINSQRLSR-GSEESPPCEILS 99
Cdd:cd22702 31 KQPCIIGS-----DPHQAISGisvvIPSPQVSELHARITC--KNGAFFLTDLGSEHGTWINDNEGRRyRAPPNFPVRLHP 103
|
....*....
gi 1958683057 100 GDIIQFGVD 108
Cdd:cd22702 104 SDVIEFGSD 112
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
341-644 |
5.72e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 341 ELQAKIDDMEEKEQELQAKIEALQ----ADNDFTNERLT-ALQVRLEPLQEKTLKECSSLEklmvqGHLTKVVEESKLSK 415
Cdd:PRK04863 790 QLRAEREELAERYATLSFDVQKLQrlhqAFSRFIGSHLAvAFEADPEAELRQLNRRRVELE-----RALADHESQEQQQR 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 416 ENQAKAKES-DLSDTLSPSKEKSSDDTTDAQMDEqdLNEPLAKVSLLKDDLQG-----TQAETEA---KQDTQH---LRK 483
Cdd:PRK04863 865 SQLEQAKEGlSALNRLLPRLNLLADETLADRVEE--IREQLDEAEEAKRFVQQhgnalAQLEPIVsvlQSDPEQfeqLKQ 942
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 484 ELVEAQELARASKQKCFDLQALLeeERKAYRNqVEESAKQIQVLQVQLQRLHMDMENLQEEKDTeissTRDKLLSAQDEI 563
Cdd:PRK04863 943 DYQQAQQTQRDAKQQAFALTEVV--QRRAHFS-YEDAAEMLAKNSDLNEKLRQRLEQAEQERTR----AREQLRQAQAQL 1015
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 564 LLLHQAAAKAVSERDTDFMSLQE---ELKK--VRAElEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQ---QREEATRLQ 635
Cdd:PRK04863 1016 AQYNQVLASLKSSYDAKRQMLQElkqELQDlgVPAD-SGAEERARARRDELHARLSANRSRRNQLEKQltfCEAEMDNLT 1094
|
....*....
gi 1958683057 636 GELEKLKKE 644
Cdd:PRK04863 1095 KKLRKLERD 1103
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
16-111 |
6.24e-04 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaB and similar proteins; FhaB, also called FtsZ-interacting protein A (FipA), is a putative virulence factor involved in regulating cell shape. It can interact with polyketide-associated protein PapA5, a putative membrane protein involved in the biosynthesis of virulence enhancing lipids. FhaB regulates growth and cell division. It is probably required for divisomal protein assembly under oxidative stress. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438745 [Multi-domain] Cd Length: 91 Bit Score: 39.59 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 16 PFQERHVYLD-EPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFdhKTSKFYLQDTKSSNGTFINSQRLSRgseespP 94
Cdd:cd22693 7 TLQGQTFPIDkSGITIGRA------DDNDLVLSDDFVSSRHARIYL--QGSSWYLEDLGSTNGTFVNGNRVTQ------P 72
|
90
....*....|....*..
gi 1958683057 95 CEILSGDIIQFGVDVTE 111
Cdd:cd22693 73 VVVQPGDTIRIGATVFE 89
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
297-544 |
6.47e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 297 QEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQkgqaEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTA 376
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK----QLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 377 LQVRLEPLQEKTLKECSSLEKLMVQGHLTKVVeesklskenqakakesdlsdtlspskekSSDDTTDAQMDEQDLNEPLA 456
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLL----------------------------SPEDFLDAVRRLQYLKYLAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 457 KVSLLKDDLQGTQAETEAkqdtqhLRKELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHM 536
Cdd:COG4942 147 ARREQAEELRADLAELAA------LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
....*...
gi 1958683057 537 DMENLQEE 544
Cdd:COG4942 221 EAEELEAL 228
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
163-348 |
7.25e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWqALIDEDRLLSRLEVMGNQLQACSKNQTE-DSLRKELV 241
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-DEIDVASAEREIAELEAELERLDASSDDlAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 242 ALQEDKhsyeTTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDEcthLREMNERTQEELRELANKYNGAVNEIKDLSDKL 321
Cdd:COG4913 696 ELEAEL----EELEEELDELKGEIGRLEKELEQAEEELDELQDR---LEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
170 180
....*....|....*....|....*..
gi 1958683057 322 KAAEGKQEEIQQKGQAEKKELQAKIDD 348
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAMRA 795
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
52-106 |
7.46e-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: 7.46e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958683057 52 SRNHALVWFDHKTSKFYLQ-----------DTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFG 106
Cdd:cd22683 28 SRSCDLVLSDPSISRFHAElrleqnginviDNNSANGTFINGKRIKGKT-----YILKNGDIIVFG 88
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
208-366 |
7.83e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.90 E-value: 7.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 208 IDEDRLLSRLEVMGNQLQACSKNQTE---DSLRKELVALQED-KHSYETTAKEslrrvLQEKIEVVRKLSEVERSLsnte 283
Cdd:PRK04778 249 LDHLDIEKEIQDLKEQIDENLALLEEldlDEAEEKNEEIQERiDQLYDILERE-----VKARKYVEKNSDTLPDFL---- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 284 decTHLREMNERTQEELRELANKY---NGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKK---ELQAKIDDMEEKEQELQ 357
Cdd:PRK04778 320 ---EHAKEQNKELKEEIDRVKQSYtlnESELESVRQLEKQLESLEKQYDEITERIAEQEIaysELQEELEEILKQLEEIE 396
|
....*....
gi 1958683057 358 AKIEALQAD 366
Cdd:PRK04778 397 KEQEKLSEM 405
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
463-673 |
8.16e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 463 DDLQGTQAETE-AKQDTQHLRkELVEAQELARASKQKCFDLQALLEEeRKAYRNQVEesakqiqvlqvqLQRLHMDMENL 541
Cdd:COG4913 235 DDLERAHEALEdAREQIELLE-PIRELAERYAAARERLAELEYLRAA-LRLWFAQRR------------LELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 542 QEEK---DTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDfmsLQEELKKVRAELEGWRKAASEYEEEIRSLQST--- 615
Cdd:COG4913 301 RAELarlEAELERLEARLDALREELDELEAQIRGNGGDRLEQ---LEREIERLERELEERERRRARLEALLAALGLPlpa 377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958683057 616 --------------FQLRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKEL 673
Cdd:COG4913 378 saeefaalraeaaaLLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
163-362 |
8.25e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALID--------EDRLLSRLEVMGNQLQACSKNQTED 234
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekeiaelRAELEAQKEELAELLRALYRLGRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 235 SLrkELVALQEDKHSYETTAK--ESLRRVLQEKIEVVRK-LSEVERSLSNTEDECTHLREMNERTQEELRELANkyngAV 311
Cdd:COG4942 121 PL--ALLLSPEDFLDAVRRLQylKYLAPARREQAEELRAdLAELAALRAELEAERAELEALLAELEEERAALEA----LK 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958683057 312 NEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEA 362
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
586-760 |
1.04e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 586 EELKKVRAELEGWRKAASEYEEEIRSLQSTFQlRCQQCEvQQREEATRLQGELEKLKKEWDVLEnECRSLKKENVLLSSE 665
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEE-ELEELE-AELEELREELEKLEKLLQLLPLYQ-ELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 666 LQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKL 745
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170
....*....|....*
gi 1958683057 746 KFEMTEQEKQSITDE 760
Cdd:COG4717 228 ELEQLENELEAAALE 242
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
630-753 |
1.12e-03 |
|
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: 41.61 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 630 EATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNsQKQSLELTSDLSilqmtrkELENQMGSLKeqhl 709
Cdd:pfam15294 134 EIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGA-KKDVKSNLKEIS-------DLEEKMAALK---- 201
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1958683057 710 rdeADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQE 753
Cdd:pfam15294 202 ---SDLEKTLNASTALQKSLEEDLASTKHELLKVQEQLEMAEKE 242
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
604-774 |
1.13e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 604 EYEEEIRSLQSTFQLRCQQCEVQQR--EEATRLQGE-LEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNsqkqs 680
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKniEEQRKKNGEnIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIED----- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 681 leLTSDLSILQMTRKELENQMGSL-KEQHLRDEADL-----------KTLLSKAENQAKDVQKEYEKTQTVLSELKLKF- 747
Cdd:PHA02562 253 --PSAALNKLNTAAAKIKSKIEQFqKVIKMYEKGGVcptctqqisegPDRITKIKDKLKELQHSLEKLDTAIDELEEIMd 330
|
170 180
....*....|....*....|....*....
gi 1958683057 748 EMTEQEK--QSITDELKQCKDNLKLLREK 774
Cdd:PHA02562 331 EFNEQSKklLELKNKISTNKQSLITLVDK 359
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
586-777 |
1.19e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 586 EELKKVRAELEGWRKAASEYEEEIRSLQstfQLRCQQcevQQREEATRLQGELEKLKKEWDVLENEcrslkKENVLLSSE 665
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLE---PIRELA---ERYAAARERLAELEYLRAALRLWFAQ-----RRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 666 LQRQEKELHNSQKQSLELTSDLSILQMTRKELENQmgsLKEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKL 745
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQ---IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
170 180 190
....*....|....*....|....*....|..
gi 1958683057 746 KFEMTEQEKQSITDELKQCKDNLKLLREKGNN 777
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
312-490 |
1.32e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 42.32 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 312 NEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQE----- 386
Cdd:pfam05667 310 NEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKqykvk 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 387 -KTLKECSSLEKLMVQghLTKVVEESKLSKEN---QAKAKESDLSDTLSPSKEKSSDDTTDAQmdeqdlnEPLAKVSLLK 462
Cdd:pfam05667 390 kKTLDLLPDAEENIAK--LQALVDASAQRLVElagQWEKHRVPLIEEYRALKEAKSNKEDESQ-------RKLEEIKELR 460
|
170 180
....*....|....*....|....*...
gi 1958683057 463 DDLQGTQAETEAKQDtqhLRKELVEAQE 490
Cdd:pfam05667 461 EKIKEVAEEAKQKEE---LYKQLVAEYE 485
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
27-106 |
1.38e-03 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaA and similar proteins; FhaA regulates cell growth and peptidoglycan synthesis by binding to MviN. It may inhibit the late stages of peptidoglycan synthesis. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438720 [Multi-domain] Cd Length: 91 Bit Score: 38.60 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 27 PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTSkfYLQDTKSSNGTFINSQRLsrgseeSPPCEILSGDIIQFG 106
Cdd:cd22668 19 SNIIGRG------SDADFRLPDTGVSRRHAEIRWDGQVA--HLTDLGSTNGTTVNNAPV------TPEWRLADGDVITLG 84
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
256-365 |
1.44e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 256 ESLRRVLQEKI-EVVRKLSEVERSLSNTEDEcthLREMNERTQEELRELANKYNGAVNEIKdlsdklKAAEGKQEEIQQK 334
Cdd:PRK00409 526 EELERELEQKAeEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLEEAEKEAQQAIKEAK------KEADEIIKELRQL 596
|
90 100 110
....*....|....*....|....*....|.
gi 1958683057 335 GQAEKKELQAKidDMEEKEQELQAKIEALQA 365
Cdd:PRK00409 597 QKGGYASVKAH--ELIEARKRLNKANEKKEK 625
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
256-464 |
1.47e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.35 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 256 ESLRRVLQEKIEVVRK--LSEVERSLSNTEDECTHLREMN--ERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEI 331
Cdd:TIGR01612 1058 DEIEKEIGKNIELLNKeiLEEAEINITNFNEIKEKLKHYNfdDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEI 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 332 QQKGQAEKKELQAKIDDMEE----------------KEQELQAKIEALQADNDFTNERLTAL------QVRLEPLQEKTL 389
Cdd:TIGR01612 1138 KKKSENYIDEIKAQINDLEDvadkaisnddpeeiekKIENIVTKIDKKKNIYDEIKKLLNEIaeiekdKTSLEEVKGINL 1217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958683057 390 KECSSLEKLMvqghLTKVVEESKLSkENQAKAKESDLSDtLSPSKEKSSDDTTDAQMdEQDLNEPLAKVSLLKDD 464
Cdd:TIGR01612 1218 SYGKNLGKLF----LEKIDEEKKKS-EHMIKAMEAYIED-LDEIKEKSPEIENEMGI-EMDIKAEMETFNISHDD 1285
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
49-112 |
1.55e-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: 1.55e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683057 49 KVLSRNHALVWFDHKTS--KFYLQDTKSSNGTFINsqrlsrgSEESPPC---EILSGDIIQFGVDVTEN 112
Cdd:cd22681 64 ETCSKQHCVIQFRNVKGilKPYIMDLDSSNGTCLN-------DNVIPSSryvELRSGDVITFSKSNDYE 125
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
300-387 |
1.62e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 300 LRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQV 379
Cdd:COG3883 124 LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
....*...
gi 1958683057 380 RLEPLQEK 387
Cdd:COG3883 204 ELAAAEAA 211
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
628-754 |
2.47e-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: 40.77 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 628 REEATRLQGELEKLKKEWDVLENECRSLKK----ENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGS 703
Cdd:smart00787 164 MKELELLNSIKPKLRDRKDALEEELRQLKQledeLEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIED 243
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1958683057 704 LKEQhlrdEADLKTLLSKAENQAKDVQKeyeKTQTVLSELKLKFEMTEQEK 754
Cdd:smart00787 244 LTNK----KSELNTEIAEAEKKLEQCRG---FTFKEIEKLKEQLKLLQSLT 287
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
234-383 |
2.57e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 234 DSLRKELVALQEDKhsyeTTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLRE--MNERTQEELRELANKYNGAV 311
Cdd:COG1579 27 KELPAELAELEDEL----AALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNNKEYEALQKEIESLK 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958683057 312 NEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEP 383
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
506-679 |
3.11e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 506 LEEERKAYRNQVEESAKQIQVLQVQLQRLhmdmenlqEEKDTEISSTRDKLLSAQDEILLLHQAAA-KAVSERDTDFMSL 584
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEEL--------EELEAELEELREELEKLEKLLQLLPLYQElEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 585 QEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSS 664
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170
....*....|....*
gi 1958683057 665 ELQRQEKELHNSQKQ 679
Cdd:COG4717 228 ELEQLENELEAAALE 242
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
626-774 |
3.12e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 626 QQREEATR----LQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQ--EKELHNSQKQSLELTSDLSILQMTRKELEN 699
Cdd:COG3206 168 LRREEARKalefLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKllLQQLSELESQLAEARAELAEAEARLAALRA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 700 QMGS----------------LKEQHLRDEADLKTLLSK----------AENQAKDVQKEYEK-TQTVLSELKLKFEMTEQ 752
Cdd:COG3206 248 QLGSgpdalpellqspviqqLRAQLAELEAELAELSARytpnhpdviaLRAQIAALRAQLQQeAQRILASLEAELEALQA 327
|
170 180
....*....|....*....|..
gi 1958683057 753 EKQSITDELKQCKDNLKLLREK 774
Cdd:COG3206 328 REASLQAQLAQLEARLAELPEL 349
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
1-106 |
3.20e-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: 40.90 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 1 MPSALAIFTCRPNSHPFQERHVYLDEPIKIGRSvARC-----RPAQnnatfdckVLSRNHALVWFDHktSKFYLQDTkSS 75
Cdd:COG3456 1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRS-ADCdwvlpDPDR--------SVSRRHAEIRFRD--GAFCLTDL-ST 68
|
90 100 110
....*....|....*....|....*....|...
gi 1958683057 76 NGTFIN--SQRLSRGSEEsppcEILSGDIIQFG 106
Cdd:COG3456 69 NGTFLNgsDHPLGPGRPV----RLRDGDRLRIG 97
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
251-774 |
3.35e-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: 41.11 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 251 ETTAKESLRRVLQEKIEVVRKLSEVERSLSNTE----DECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEG 326
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKeqakKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 327 -----------KQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEKTLKECSSL 395
Cdd:pfam02463 251 eeiesskqeieKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 396 EKLMVQGHLTKVVEESKLSKENQAKAKESDLSD--------------TLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLL 461
Cdd:pfam02463 331 KKEKEEIEELEKELKELEIKREAEEEEEEELEKlqekleqleeellaKKKLESERLSSAAKLKEEELELKSEEEKEAQLL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 462 KDDLQGTQAETEAKQDTQ-HLRKELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRlhmdMEN 540
Cdd:pfam02463 411 LELARQLEDLLKEEKKEElEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQ----EQL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 541 LQEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRC 620
Cdd:pfam02463 487 ELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 621 QQCEVQQREEATRLQGELEKLKKEWDvlenecRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQ 700
Cdd:pfam02463 567 VRALTELPLGARKLRLLIPKLKLPLK------SIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKES 640
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958683057 701 MGSLKEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 774
Cdd:pfam02463 641 AKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKK 714
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
274-381 |
3.80e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 40.61 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 274 EVERSLSNTEDECTHLREMNERTQEELRELANKY---NGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEK----------K 340
Cdd:pfam06160 288 YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEvayselqeelE 367
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1958683057 341 ELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRL 381
Cdd:pfam06160 368 EILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLEL 408
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
327-757 |
3.88e-03 |
|
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: 40.72 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 327 KQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIealqadndftnERLTALQVRLEPLQEKTLKECSSLEKLMVQGHLTK 406
Cdd:TIGR00618 236 QQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARI-----------EELRAQEAVLEETQERINRARKAAPLAAHIKAVTQ 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 407 V----------VEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDE---------------------------- 448
Cdd:TIGR00618 305 IeqqaqrihteLQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHirdahevatsireiscqqhtltqhihtl 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 449 -QDLNEPLAKVSLLKDDLQGTQAEtEAKQDTQHLRkELVEAQELARASKQkCFDLQALLEEERKAYRNQVEESAKQIQVL 527
Cdd:TIGR00618 385 qQQKTTLTQKLQSLCKELDILQRE-QATIDTRTSA-FRDLQGQLAHAKKQ-QELQQRYAELCAAAITCTAQCEKLEKIHL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 528 QVQLQRLHMDMENLQE-----EKDTEISSTRDKLLSAQDE--------ILLLHQAAAKA-VSERDTDFM--------SLQ 585
Cdd:TIGR00618 462 QESAQSLKEREQQLQTkeqihLQETRKKAVVLARLLELQEepcplcgsCIHPNPARQDIdNPGPLTRRMqrgeqtyaQLE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 586 EELKKVRAELEGWRKAASEYEEEIRSLQSTFQlRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSE 665
Cdd:TIGR00618 542 TSEEDVYHQLTSERKQRASLKEQMQEIQQSFS-ILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRK 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 666 LQ----RQEKELHNSQKQSLEltsDLSILQMTRKELENQMGSLKEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLS 741
Cdd:TIGR00618 621 LQpeqdLQDVRLHLQQCSQEL---ALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKE 697
|
490
....*....|....*.
gi 1958683057 742 ELKLKFEMTEQEKQSI 757
Cdd:TIGR00618 698 MLAQCQTLLRELETHI 713
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
284-400 |
3.93e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 284 DE-CTHLREMNERTQEELRELANKyngavneIKDLSDKLKAAEGKQEEIQQ----KGQAEKKELQAKIDDME---EKEQE 355
Cdd:COG0542 396 DEaAARVRMEIDSKPEELDELERR-------LEQLEIEKEALKKEQDEASFerlaELRDELAELEEELEALKarwEAEKE 468
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1958683057 356 LQAKIEALQADNDFTNERLTALQVRLEPLQEKtLKECSSLEKLMV 400
Cdd:COG0542 469 LIEEIQELKEELEQRYGKIPELEKELAELEEE-LAELAPLLREEV 512
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
163-365 |
4.09e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.44 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEasdtsWQALIDEDRLLSR----LEVMGNQLQACSKNQT--EDSL 236
Cdd:COG0497 172 KELEELRADEAERARELDLLRFQLEELEAAALQPGE-----EEELEEERRRLSNaeklREALQEALEALSGGEGgaLDLL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 237 ---RKELVALQEDKHSYETTAkESLRRVLQEKIEVVRklsEVERSLSNTEDECTHLREMNERtQEELRELANKYNGAVNE 313
Cdd:COG0497 247 gqaLRALERLAEYDPSLAELA-ERLESALIELEEAAS---ELRRYLDSLEFDPERLEEVEER-LALLRRLARKYGVTVEE 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958683057 314 IKDLSDKLkaaegkqeeiqqkgQAEKKELQAKIDDMEEKEQELQAKIEALQA 365
Cdd:COG0497 322 LLAYAEEL--------------RAELAELENSDERLEELEAELAEAEAELLE 359
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
267-418 |
4.80e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 267 EVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYngavNEIKDlSDKLKAaegkQEEIQQKGQAEKKELQAKI 346
Cdd:PRK00409 520 ELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKL----QEEED-KLLEEA----EKEAQQAIKEAKKEADEII 590
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958683057 347 DDMEEKEQELQAKIEALQADndftnERLTALQVRLEPLQEKTLKEcssleklMVQGHLTKVVEESKLSKENQ 418
Cdd:PRK00409 591 KELRQLQKGGYASVKAHELI-----EARKRLNKANEKKEKKKKKQ-------KEKQEELKVGDEVKYLSLGQ 650
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
236-519 |
5.48e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 236 LRKELVALQEDKHSYETTAK--ESLRRVLQEKIEVVRKLSEVERSLSNTEDecthlremnerTQEELRELANKYNgavnE 313
Cdd:COG4913 615 LEAELAELEEELAEAEERLEalEAELDALQERREALQRLAEYSWDEIDVAS-----------AEREIAELEAELE----R 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 314 IKDLSDKLKAAEgkqeeiqqkgqAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEKTLKECS 393
Cdd:COG4913 680 LDASSDDLAALE-----------EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 394 S-----LEKLMVQGHLTKVVE--ESKLSKENQAKAK-ESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDl 465
Cdd:COG4913 749 AlleerFAAALGDAVERELREnlEERIDALRARLNRaEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEED- 827
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683057 466 qgtqaeteakqdtqhlrkELVEAQE-----LARASKQKCFDLQALLEEERKAYRNQVEE 519
Cdd:COG4913 828 ------------------GLPEYEErfkelLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
266-488 |
5.62e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 266 IEVVRKLSEVERSLSNTEDECTHLremnertqEELRELANKYNGAVNEIKDLSDKLKAAEgkqeeiQQKGQAEKKELQAK 345
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELL--------EPIRELAERYAAARERLAELEYLRAALR------LWFAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 346 IDDMEEKEQELQAKIEALQADNDFTNERLTALQV--------RLEPLQ------EKTLKECS----SLEKLMVQGHLTKV 407
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAqirgnggdRLEQLEreierlERELEERErrraRLEALLAALGLPLP 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 408 VEESKLsKENQAKAKEsdLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQdtQHLRKELVE 487
Cdd:COG4913 377 ASAEEF-AALRAEAAA--LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL--LALRDALAE 451
|
.
gi 1958683057 488 A 488
Cdd:COG4913 452 A 452
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
173-424 |
6.00e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 173 QEALHREQM--LEQKLATLQRLLAITqeasdtswqALIDEDRLLSRLEVMGNQLQACSKNQTE--------DSLRKELVA 242
Cdd:COG3096 858 QEQQLRQQLdqLKEQLQLLNKLLPQA---------NLLADETLADRLEELREELDAAQEAQAFiqqhgkalAQLEPLVAV 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 243 LQEDKHSYETTAKE-----SLRRVLQEKIEVvrkLSEV-ER----SLSNTEDECTHLREMNERTQEELRElankyngAVN 312
Cdd:COG3096 929 LQSDPEQFEQLQADylqakEQQRRLKQQIFA---LSEVvQRrphfSYEDAVGLLGENSDLNEKLRARLEQ-------AEE 998
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 313 EIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQA--------KIEALQADNDFTNERLTALQVRLEPL 384
Cdd:COG3096 999 ARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEElgvqadaeAEERARIRRDELHEELSQNRSRRSQL 1078
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1958683057 385 qEKTLKECSSlEKLMVQGHLTKVVEESKLSKENQAKAKES 424
Cdd:COG3096 1079 -EKQLTRCEA-EMDSLQKRLRKAERDYKQEREQVVQAKAG 1116
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
290-507 |
6.49e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 40.42 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 290 REMNERTQEELRELANKY----------------NGAVNEIKDLSDKLKAAEGKQEeiqQKGQAEKKElqakiddmeeke 353
Cdd:TIGR01612 1513 KELFEQYKKDVTELLNKYsalaiknkfaktkkdsEIIIKEIKDAHKKFILEAEKSE---QKIKEIKKE------------ 1577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 354 qelQAKIEALQADNDFTNERLTALQVRLEPLQEKTLK-------------ECSSLEKLMvqGHLTKVVEESKLSKENQAK 420
Cdd:TIGR01612 1578 ---KFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLKisdikkkindclkETESIEKKI--SSFSIDSQDTELKENGDNL 1652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 421 AKESDLSDTLSPSKEKSSDDTTdaQMDEQDlneplAKVSLLKDDLQgtqaeteakQDTQHLRKELVEA-QELARASKQKC 499
Cdd:TIGR01612 1653 NSLQEFLESLKDQKKNIEDKKK--ELDELD-----SEIEKIEIDVD---------QHKKNYEIGIIEKiKEIAIANKEEI 1716
|
....*...
gi 1958683057 500 FDLQALLE 507
Cdd:TIGR01612 1717 ESIKELIE 1724
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
180-391 |
6.66e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 180 QMLEQKLATLQRLLAITQEASDTSWQALideDRLLSRLEVMGNQLQAcsKNQTEDSLRKELVALQEDKHSYETTAKESLR 259
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAEL---EELNEEYNELQAELEA--LQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 260 rVLQEKIEVVRKLSEVERSLSNTE--DECTHLREMNERTQEELRELANkyngAVNEIKDLSDKLKAAEGKQEEIQQKGQA 337
Cdd:COG3883 94 -ALYRSGGSVSYLDVLLGSESFSDflDRLSALSKIADADADLLEELKA----DKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958683057 338 EKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQVRLEPLQEKTLKE 391
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
223-698 |
7.00e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 223 QLQACSKNQTEDSLRKELVALQEDKHSYE--------TTAKESLRRVLQEKIEVVRK-----------LSEVERSLSNTE 283
Cdd:TIGR00606 597 NKELASLEQNKNHINNELESKEEQLSSYEdklfdvcgSQDEESDLERLKEEIEKSSKqramlagatavYSQFITQLTDEN 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 284 DECTHLREMNERTQEELRE----LANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAK---IDDMEEKEQEL 356
Cdd:TIGR00606 677 QSCCPVCQRVFQTEAELQEfisdLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKekeIPELRNKLQKV 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 357 QAKIEALQADNDFTNERLTALQVRLEpLQEKTLKECSSLEKLMVQghlTKVVEESKLSKENQAKAKESDLSDTLSPSKEK 436
Cdd:TIGR00606 757 NRDIQRLKNDIEEQETLLGTIMPEEE-SAKVCLTDVTIMERFQME---LKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQ 832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 437 SSDDTTDAQMDEQDLNEPLAKVSllKDDLQGTQAET-EAKQDTQHLRKELVEAQELARASKQKCFDLQALLEEERKAyRN 515
Cdd:TIGR00606 833 EKQHELDTVVSKIELNRKLIQDQ--QEQIQHLKSKTnELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDA-KE 909
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 516 QVEESAKQiqvlqvqlqrlhmdMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQE--------- 586
Cdd:TIGR00606 910 QDSPLETF--------------LEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDgkddylkqk 975
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683057 587 --ELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEV----------------------------------QQREE 630
Cdd:TIGR00606 976 etELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWlqdnltlrkrenelkeveeelkqhlkemgqmqvlQMKQE 1055
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683057 631 ATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELqrQEKELHNSQKQSLELTSDLSILQMTRKELE 698
Cdd:TIGR00606 1056 HQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL--REPQFRDAEEKYREMMIVMRTTELVNKDLD 1121
|
|
| |
