|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
3-130 |
9.16e-81 |
|
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and similar proteins; SLMAP, also called sarcolemmal-associated protein (SLAP), is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. It is a cardiac membrane protein that plays an important role in E-C coupling and the adrenergic response of the heart. Overexpression of the SLMAP gene has been associated with diabetes and endothelial dysfunction of macro- and micro-blood vessels. SLMAP contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438731 [Multi-domain] Cd Length: 126 Bit Score: 254.11 E-value: 9.16e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 3 SALAIFTCRPNSHPFQERHVYLDEPIKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHktSKFYLQDTKSSNGTFINS 82
Cdd:cd22679 1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1907106148 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 |
3.76e-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: 101.61 E-value: 3.76e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907106148 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 |
1.23e-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: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 27 PIKIGRSVARCRPAQNNAT-FDCKVLSRNHALVWfdHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQF 105
Cdd:cd22692 38 QIHIGRYTERVRQAIYHPVvFKSKVVSRTHGCIK--VDEGNWYIKDVKSSSGTFLNHQRLSPASRTSKPYPLRDGDILQL 115
|
...
gi 1907106148 106 GVD 108
Cdd:cd22692 116 GMD 118
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
163-757 |
2.47e-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: 80.49 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSlrKELIA 242
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL--EELEA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 243 LQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELA--------NKYNGAVNEI 314
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLkkleeaelKELQAELEEL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 315 KDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQAD----NDFTNERLTALQEKLMVQGHLTKV 390
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLqenlEGFSEGVKALLKNQSGLSGILGVL 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 391 VE----ESKLSK---------------ENQAKAKE------------------SDLSDTLSPSKEKSS------------ 421
Cdd:TIGR02168 526 SElisvDEGYEAaieaalggrlqavvvENLNAAKKaiaflkqnelgrvtflplDSIKGTEIQGNDREIlkniegflgvak 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 422 -----------------------DDTTDAQMDEQDLNEPLAKVSL-----------LKDDLQGTQSETEAKQDIQHLRKE 467
Cdd:TIGR02168 606 dlvkfdpklrkalsyllggvlvvDDLDNALELAKKLRPGYRIVTLdgdlvrpggviTGGSAKTNSSILERRREIEELEEK 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 468 LVEAQELARTSKQkcfELQALlEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDT---EISSTRDKLLSAQD 544
Cdd:TIGR02168 686 IEELEEKIAELEK---ALAEL-RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQleeRIAQLSKELTELEA 761
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 545 EILLLRQA---AAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSF---QLRCQQCEDQQREEATRL- 617
Cdd:TIGR02168 762 EIEELEERleeAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATERRLe 841
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 618 ---------QGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLK 688
Cdd:TIGR02168 842 dleeqieelSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907106148 689 EQHlrdaADLKTLLSKAENQAKDVQkeyektQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 757
Cdd:TIGR02168 922 EKL----AQLELRLEGLEVRIDNLQ------ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| FHA_VPS64-like |
cd22695 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ... |
6-126 |
4.50e-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: 4.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 6 AIFTCRPNSHPFQERHV---YLDEPIKIGRSVARCRPAQN---------------NATFDCKVLSRNHALVWFDHKTSKF 67
Cdd:cd22695 2 HILVLKSLNATFETKFLvvpFKPDGLKLGRPVTNSVNKNNsgskrdlfsqqvrpdNGNFDSRVLSRNHACLSCDPTTGKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907106148 68 YLQDTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFGVDVTEntrKVTHGCIVSTIK 126
Cdd:cd22695 82 YIRDLKSSNGTFVNGQKIRQND-----VELKVGDEVDLGTDIDS---KIEHRKISAYVE 132
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
229-749 |
4.75e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.72 E-value: 4.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 229 KNQTEDSLRKELIALQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYN 308
Cdd:PTZ00121 1249 RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 309 GAVNEIKDLSDKLKVAE--GKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLMVQG- 385
Cdd:PTZ00121 1329 KKADAAKKKAEEAKKAAeaAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAd 1408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 386 HLTKVVEESKLSKENQAKAKESDLSDTL-SPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEAKQDIQHL 464
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAkKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEA 1488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 465 RKELVEAQELARTSKQKCFELQAL-----LEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEE--KDTEISSTRD 537
Cdd:PTZ00121 1489 KKKAEEAKKKADEAKKAAEAKKKAdeakkAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkKAEEKKKAEE 1568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 538 KLLSAQDEILLLRQA--AAEAVSERDTDFVSLQEELKKVRAE----LEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQR 611
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAeeAKKAEEARIEEVMKLYEEEKKMKAEeakkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 612 EEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQH 691
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN 1728
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907106148 692 LRDAADLKTLLSKAENQAKDVQKEYE---KTQTVLSELKLKFEMTEQEKQSITDELKQCKD 749
Cdd:PTZ00121 1729 KIKAEEAKKEAEEDKKKAEEAKKDEEekkKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
13-106 |
2.18e-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: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 13 NSHPFQERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKtsKFYLQDTKSSNGTFINSQRLsrgseeS 92
Cdd:cd00060 6 DGDGGGREFPLTKGVVTIGRS------PDCDIVLDDPSVSRRHARIEVDGG--GVYLEDLGSTNGTFVNGKRI------T 71
|
90
....*....|....
gi 1907106148 93 PPCEILSGDIIQFG 106
Cdd:cd00060 72 PPVPLQDGDVIRLG 85
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
28-105 |
6.03e-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: 6.03e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907106148 28 IKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhKTSKFYLQDTKSSNGTFINSQRLSRgseesPPCEILSGDIIQF 105
Cdd:pfam00498 1 VTIGRS------PDCDIVLDDPSVSRRHAEIRYD-GGGRFYLEDLGSTNGTFVNGQRLGP-----EPVRLKDGDVIRL 66
|
|
| CC1_SLMAP-like |
cd21868 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ... |
167-204 |
1.28e-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: 62.50 E-value: 1.28e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1907106148 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21868 1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
161-727 |
3.05e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 161 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKEL 240
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 241 IALQEDkhsyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDK 320
Cdd:COG1196 298 ARLEQD-----------IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 321 LKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLMVQGHLTKVVEESKLSKEN 400
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 401 QAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQ--DLNEPLAKVSLLKDDLQGTQSETE-------AKQDIQHLRKELVEA 471
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAAlaELLEELAEAAARLLLLLEAEADYEgflegvkAALLLAGLRGLAGAV 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 472 QELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQ 551
Cdd:COG1196 527 AVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVAS 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 552 AAAEAvSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLqssfqlrcqqcedqqREEATRLQGELEKLKKEWDVL 631
Cdd:COG1196 607 DLREA-DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV---------------TLEGEGGSAGGSLTGGSRREL 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 632 ETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTLLSKAENQAKD 711
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
|
570
....*....|....*.
gi 1907106148 712 VQKEYEKTQTVLSELK 727
Cdd:COG1196 751 EALEELPEPPDLEELE 766
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
190-756 |
3.47e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.47 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 190 QRLLAITQEASDTSWQALIDE--------DRLLSRLEVMGNQLQACSKNQTE-----DSLRKELIALQEDKHSYETT--- 253
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLRleelreelEELQEELKEAEEELEELTAELQEleeklEELRLEVSELEEEIEELQKElya 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 254 AKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQ 333
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 334 KGQAEKKELQT---KIDEMEEKEQELQAKIEALQAD--------NDFTNERLTALQEKLMVQGHLTKVVEESKLSKENQA 402
Cdd:TIGR02168 373 RLEELEEQLETlrsKVAQLELQIASLNNEIERLEARlerledrrERLQQEIEELLKKLEEAELKELQAELEELEEELEEL 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 403 KAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEAKQDIQHLRKEL-------------- 468
Cdd:TIGR02168 453 QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgilgvlselisvd 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 469 ------VEA------QELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQ------EEKDT 530
Cdd:TIGR02168 533 egyeaaIEAalggrlQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLgvakdlVKFDP 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 531 EISSTRDKLLS----AQDeillLRQAAAEAVSER-DTDFVSLQEELKKVRAELEGWRKAAS----EYENEIRSLQSSFQL 601
Cdd:TIGR02168 613 KLRKALSYLLGgvlvVDD----LDNALELAKKLRpGYRIVTLDGDLVRPGGVITGGSAKTNssilERRREIEELEEKIEE 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 602 RCQQCEDQQ------REEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSE-------LQRQEKELHNSQKQSFELTS 668
Cdd:TIGR02168 689 LEEKIAELEkalaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEveqleerIAQLSKELTELEAEIEELEE 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 669 DLSILQMTRKELEKQVGSLK---EQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELK 745
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEaqiEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848
|
650
....*....|.
gi 1907106148 746 QCKDNLKLLRE 756
Cdd:TIGR02168 849 ELSEDIESLAA 859
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
52-106 |
2.29e-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: 2.29e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1907106148 52 SRNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQFG 106
Cdd:cd22686 48 SKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPYPLTHGDELKIG 102
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
235-749 |
4.66e-11 |
|
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: 66.58 E-value: 4.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 235 SLRKELIALQEDKHSYETTAKE--SLRRVLQEKIEVVRKLSEVERSLsntEDECTHLKEMNERTQEELRELANKYNGAVN 312
Cdd:TIGR04523 170 ELENELNLLEKEKLNIQKNIDKikNKLLKLELLLSNLKKKIQKNKSL---ESQISELKKQNNQLKDNIEKKQQEINEKTT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 313 EIKDLSDKLKVAEGKQEEIQQKGQAEKKELQT---KIDEMEEKEQELQAKIEAL--QADNDFTNERLTALQEKlmvqgHL 387
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLnnQKEQDWNKELKSELKNQ-----EK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 388 TKVVEESKLSKENQakaKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEA-KQDIQHLRK 466
Cdd:TIGR04523 322 KLEEIQNQISQNNK---IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNlESQINDLES 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 467 ELVEAQELARTSKQKCFELQA---LLEEERKAYRNQVEESAKQIQvlqvqlqklhmDMENLQEEKDTEISSTRDKLLSAQ 543
Cdd:TIGR04523 399 KIQNQEKLNQQKDEQIKKLQQekeLLEKEIERLKETIIKNNSEIK-----------DLTNQDSVKELIIKNLDNTRESLE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 544 DEILLLRQAaaeaVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSL---QSSFQLRCQQCEdqqrEEATRLQGE 620
Cdd:TIGR04523 468 TQLKVLSRS----INKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLtkkISSLKEKIEKLE----SEKKEKESK 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 621 LEKLKKEWDVLETECHSLKKENVLLssELQRQEKELHNSQKqsfELTSDLSILQMTRKELEKQVGSLKEQhlrdAADLKT 700
Cdd:TIGR04523 540 ISDLEDELNKDDFELKKENLEKEID--EKNKEIEELKQTQK---SLKKKQEEKQELIDQKEKEKKDLIKE----IEEKEK 610
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1907106148 701 LLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKD 749
Cdd:TIGR04523 611 KISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
14-106 |
7.10e-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: 7.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 14 SHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktSKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716 8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
|
90
....*....|....
gi 1907106148 93 pPCEILSGDIIQFG 106
Cdd:COG1716 75 -PAPLRDGDVIRLG 87
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
233-746 |
1.44e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 233 EDSLRKELIALQEDKhsyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVN 312
Cdd:COG1196 222 LKELEAELLLLKLRE------LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 313 EIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQAdndfTNERLTALQEKLMVQGHLTKVVE 392
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE----AEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 393 ESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEplaKVSLLKDDLQGTQSETEAKQDIQHLRKELVEAQ 472
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER---LERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 473 ELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEIL----- 547
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAgavav 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 548 --------------LLRQAAAEAVSERDTDFVSLQEELKKVRAE-----LEGWRKAASEYENEIRSLQSSFQLRCQQCED 608
Cdd:COG1196 529 ligveaayeaaleaALAAALQNIVVEDDEVAAAAIEYLKAAKAGratflPLDKIRARAALAAALARGAIGAAVDLVASDL 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 609 QQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLK 688
Cdd:COG1196 609 READARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERL 688
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907106148 689 EQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 746
Cdd:COG1196 689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
250-739 |
1.95e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.70 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 250 YETTAKES--LRRVLQEKIEVVRKL----SEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLsDKLKV 323
Cdd:PRK03918 160 YENAYKNLgeVIKEIKRRIERLEKFikrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-EELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 324 AEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQAdndfTNERLTALQEKLMVQGHLTKVVEESKlSKENQAK 403
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE----KVKELKELKEKAEEYIKLSEFYEEYL-DELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 404 AKESDLSDTLSPSKEKSSddttDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEAKQDIQHLRKELVE-AQELARTSKQKC 482
Cdd:PRK03918 314 KRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlKKRLTGLTPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 483 FELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTeiSSTRDKLLSAQDEILLLRQAAAE------A 556
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGK--CPVCGRELTEEHRKELLEEYTAElkriekE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 557 VSERDTDFVSLQEELKKVRAELEGWRKAASEYE--NEIRSLQSSFQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETE 634
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 635 CHS---LKKENVLLSSELQRQEKELHNSQKQSFELT-SDLSILQMTRKELE---------KQVGSLKEQHLRDAADLKTL 701
Cdd:PRK03918 548 LEKleeLKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEpfyneylelKDAEKELEREEKELKKLEEE 627
|
490 500 510
....*....|....*....|....*....|....*...
gi 1907106148 702 LSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 739
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR 665
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
212-756 |
3.82e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 63.91 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 212 RLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHSYETTAKESLRRVLQEKIEvvrkLSEVERSlSNTEDECTHLKE 291
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE----LDGFERG-PFSERQIKNFHT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 292 MNERTQEELRELANKyngavnEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQadndftn 371
Cdd:TIGR00606 398 LVIERQEDEAKTAAQ------LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ------- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 372 eRLTALQEKLMvqghltKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGT 451
Cdd:TIGR00606 465 -QLEGSSDRIL------ELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQM 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 452 QSETEAKQDIQHLRKELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLhmdmENLQEEKDTE 531
Cdd:TIGR00606 538 EMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASL----EQNKNHINNE 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 532 ISSTRDKLLSAQDEILLLRQAAAEavserDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQC----- 606
Cdd:TIGR00606 614 LESKEEQLSSYEDKLFDVCGSQDE-----ESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCqrvfq 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 607 -EDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLL-------SSELQRQEKELHNSQKQSFELTSDLSILQMTRK 678
Cdd:TIGR00606 689 tEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIE 768
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 679 ELEKQVGSL--KEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVL--SELKLKFEMTEQEKQSITDELKQCKDNLKLL 754
Cdd:TIGR00606 769 EQETLLGTImpEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLqgSDLDRTVQQVNQEKQEKQHELDTVVSKIELN 848
|
..
gi 1907106148 755 RE 756
Cdd:TIGR00606 849 RK 850
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
228-757 |
4.81e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 4.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 228 SKNQTEDSLRKELIALQEDKHSYETTA------KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEmNERTQEELR 301
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKELEELKeeieelEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE-KVKELKELK 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 302 ELANKYNgavnEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAkiealqadndfTNERLTALQEKL 381
Cdd:PRK03918 290 EKAEEYI----KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE-----------LKKKLKELEKRL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 382 MVQGHLTKVVEESKLSKEN--QAKAKESDLSdtlspskekssddttdaqmdEQDLNEPLAKVSLLKDDLQGTQSE-TEAK 458
Cdd:PRK03918 355 EELEERHELYEEAKAKKEEleRLKKRLTGLT--------------------PEKLEKELEELEKAKEEIEEEISKiTARI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 459 QDIQHLRKELVEAQELARTSKQKCFELQALLEEERKA-----YRNQVEESAKQIQVLQVQLQKLHMDMENLqeekdteis 533
Cdd:PRK03918 415 GELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKelleeYTAELKRIEKELKEIEEKERKLRKELREL--------- 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 534 strDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFqlrcqqcedqqrEE 613
Cdd:PRK03918 486 ---EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL------------EK 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 614 ATRLQGELEKLKKEWDVLETECHSLKKENVLLS----SELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKE 689
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEELAELLKELEELGfesvEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDK 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 690 QhLRDAADLKTLLSKAENQAKDVQK------------EYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 757
Cdd:PRK03918 631 A-FEELAETEKRLEELRKELEELEKkyseeeyeelreEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
238-756 |
1.08e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 238 KELIALQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDL 317
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 318 SDKLKVAEGKQEEIQQ-KGQAEK-KELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLMVQGHLTKVVEESK 395
Cdd:PRK03918 272 KKEIEELEEKVKELKElKEKAEEyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 396 lSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSE-TEAKQDIQHLRKELVEAQEL 474
Cdd:PRK03918 352 -KRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKiTARIGELKKEIKELKKAIEE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 475 ARTSKQKCFELQALLEEERKA-----YRNQVEESAKQIQVLQVQLQKLHMDMENLqeekdteisstrDKLLSAQDEILLL 549
Cdd:PRK03918 431 LKKAKGKCPVCGRELTEEHRKelleeYTAELKRIEKELKEIEEKERKLRKELREL------------EKVLKKESELIKL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 550 RQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFqlrcqqcedqqrEEATRLQGELEKLKKEWD 629
Cdd:PRK03918 499 KELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL------------EKLEELKKKLAELEKKLD 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 630 VLETECHSLKKENVLLS----SELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQhLRDAADLKTLLSKA 705
Cdd:PRK03918 567 ELEEELAELLKELEELGfesvEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKA-FEELAETEKRLEEL 645
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907106148 706 ENQAKDVQKEY-EKTQTVLSELKLKFEM----TEQEKQSITDELKQCKDNLKLLRE 756
Cdd:PRK03918 646 RKELEELEKKYsEEEYEELREEYLELSRelagLRAELEELEKRREEIKKTLEKLKE 701
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
298-757 |
1.30e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 298 EELRELANKYNGAVNEIkdLSDKLKVAEGKQEEIQQKgqaEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTAL 377
Cdd:PRK02224 165 EEYRERASDARLGVERV--LSDQRGSLDQLKAQIEEK---EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 378 QEklmvqghltkVVEESKLSKENqakakesdlSDTLSPSKEKSSDDTTDAQMDEQDLNEPL----AKVSLLKDDLQGTQS 453
Cdd:PRK02224 240 DE----------VLEEHEERREE---------LETLEAEIEDLRETIAETEREREELAEEVrdlrERLEELEEERDDLLA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 454 ETE---AKQDIQHLRKELVEAQELartskqkcfELQALLEEER---KAYRNQVEESAKQIQVLQVQLQKLHMDMENLqee 527
Cdd:PRK02224 301 EAGlddADAEAVEARREELEDRDE---------ELRDRLEECRvaaQAHNEEAESLREDADDLEERAEELREEAAEL--- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 528 kDTEISSTRDKLLSAQDEILLLR---QAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSF----Q 600
Cdd:PRK02224 369 -ESELEEAREAVEDRREEIEELEeeiEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVeeaeA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 601 LR----CQQCE------------DQQREEATRLQGELEKLKKEWDVLETECHSLKkenvllssELQRQEKELHNSQKQSF 664
Cdd:PRK02224 448 LLeagkCPECGqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAE--------DLVEAEDRIERLEERRE 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 665 ELTSDLSILQMTRKELEKQVGSLKEQhlrdAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS----- 739
Cdd:PRK02224 520 DLEELIAERRETIEEKRERAEELRER----AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESlerir 595
|
490
....*....|....*....
gi 1907106148 740 -ITDELKQCKDNLKLLREK 757
Cdd:PRK02224 596 tLLAAIADAEDEIERLREK 614
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
461-757 |
1.42e-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: 62.01 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 461 IQHLRKELVEAQELARTSKQKCFELQALLEEERKAyrnQVEESAKQIQVLQVQLQKLHMDMENLQEEKDtEISSTRDKLL 540
Cdd:TIGR02169 189 LDLIIDEKRQQLERLRREREKAERYQALLKEKREY---EGYELLKEKEALERQKEAIERQLASLEEELE-KLTEEISELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 541 SAQDEIL-LLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSsfQLRCQQCE-DQQREEATRLQ 618
Cdd:TIGR02169 265 KRLEEIEqLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE--RLAKLEAEiDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 619 GELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLR----- 693
Cdd:TIGR02169 343 REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRlseel 422
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907106148 694 -----DAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 757
Cdd:TIGR02169 423 adlnaAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
238-752 |
1.92e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.70 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 238 KELIALQEDKHSYETTAKESLRRVLQ-EKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELR--ELANKYNGAVNEI 314
Cdd:PTZ00121 1191 EELRKAEDARKAEAARKAEEERKAEEaRKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRkfEEARMAHFARRQA 1270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 315 KDLSDKLKVAE--GKQEEIQQKGQAEKKELQTKIDEMEEKEQElQAKIEALQADNDFTNERLTALQEKlmvqghltkvvE 392
Cdd:PTZ00121 1271 AIKAEEARKADelKKAEEKKKADEAKKAEEKKKADEAKKKAEE-AKKADEAKKKAEEAKKKADAAKKK-----------A 1338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 393 ESKLSKENQAKAKESDLSDTLSPSKEKssddttdAQMDEQDLNEPLAKVSLLKDDLQGTQSETEAKQDIQHLRKELVEAQ 472
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEK-------AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELK 1411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 473 ElARTSKQKCFELQALLEEERKA--YRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLR 550
Cdd:PTZ00121 1412 K-AAAAKKKADEAKKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKK 1490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 551 QaaAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRcqQCEDQQREEATRLQGELEKLKKEWDV 630
Cdd:PTZ00121 1491 K--AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK--KAEEKKKADELKKAEELKKAEEKKKA 1566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 631 LETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLK----EQHLRDAADLKTLLSKAE 706
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkaEEEKKKVEQLKKKEAEEK 1646
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1907106148 707 NQAKDVQKEYEKTQTVLSELKLKfemtEQEKQSITDELKQCKDNLK 752
Cdd:PTZ00121 1647 KKAEELKKAEEENKIKAAEEAKK----AEEDKKKAEEAKKAEEDEK 1688
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
296-624 |
6.00e-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: 59.69 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 296 TQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQ---KGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNE 372
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEeleQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 373 RLTALQEKLMVQghltkvveESKLSKENQAKAKESDLSDTLSPSKEKSSDDttdAQMDEQDLNEPLAKVSLLKDDLQGTQ 452
Cdd:TIGR02168 755 ELTELEAEIEEL--------EERLEEAEEELAEAEAEIEELEAQIEQLKEE---LKALREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 453 SETEA-KQDIQHLRKELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLqEEKDTE 531
Cdd:TIGR02168 824 ERLESlERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL-EELSEE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 532 ISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLqssfqlrcqqcEDQQR 611
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDD-----------EEEAR 971
|
330
....*....|...
gi 1907106148 612 EEATRLQGELEKL 624
Cdd:TIGR02168 972 RRLKRLENKIKEL 984
|
|
| CC1_T3JAM |
cd21912 |
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ... |
164-204 |
1.26e-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: 1.26e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1907106148 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 |
1.66e-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: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 14 SHPFQERHV---YLDEPIKIGRSvARCRPAQNNATfdckvLSRNHALVW---FDHKT-SKFYLQDTkSSNGTFINSQRLS 86
Cdd:cd22670 7 SSPGSTDIVlpiYKNQVITIGRS-PSCDIVINDPF-----VSRTHCRIYsvqFDESSaPLVYVEDL-SSNGTYLNGKLIG 79
|
90 100
....*....|....*....|....*
gi 1907106148 87 RGseespPCEILS-GDIIQFGVDVT 110
Cdd:cd22670 80 RN-----NTVLLSdGDVIEIAHSAT 99
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
246-756 |
2.40e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.82 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 246 DKHSYETTAKESLRRVLQEKIEvvrklsEVERSLSNTEDectHLKEMNERTqEELRELANKYNGAVNEIKDLSDKLKVAE 325
Cdd:pfam15921 131 DIRRRESQSQEDLRNQLQNTVH------ELEAAKCLKED---MLEDSNTQI-EQLRKMMLSHEGVLQEIRSILVDFEEAS 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 326 GKQ---------EEIQQKGQAEKK---ELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLMVQGHLTKVVEE 393
Cdd:pfam15921 201 GKKiyehdsmstMHFRSLGSAISKilrELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEI 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 394 SKLS-KENQAKAKESDLSDTLSPSKEKSSDDTTdaqMDEQDLNEPLAKVSLLKDDLQGTQSETEAKqdIQHLRKELVEAQ 472
Cdd:pfam15921 281 TGLTeKASSARSQANSIQSQLEIIQEQARNQNS---MYMRQLSDLESTVSQLRSELREAKRMYEDK--IEELEKQLVLAN 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 473 -EL--ARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKL-------HMDMENLQEEKDTEISSTRD----- 537
Cdd:pfam15921 356 sELteARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwdrdtgnSITIDHLRRELDDRNMEVQRleall 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 538 KLLSAQDEILLLRQAAA--------EAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRcQQCEDQ 609
Cdd:pfam15921 436 KAMKSECQGQMERQMAAiqgkneslEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK-ERAIEA 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 610 QREEATRLQG-------ELEKLKKEWDVL---ETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKE 679
Cdd:pfam15921 515 TNAEITKLRSrvdlklqELQHLKNEGDHLrnvQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQ 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 680 LEKQVG----SLKE-QHLRDAADLKtlLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLL 754
Cdd:pfam15921 595 LEKEINdrrlELQEfKILKDKKDAK--IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSL 672
|
..
gi 1907106148 755 RE 756
Cdd:pfam15921 673 SE 674
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
310-559 |
4.56e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.99 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 310 AVNEIKDLSDKLKVAEGKQEEIQqkgqAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLmvqghltk 389
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQ----AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 390 vveesklskenqaKAKESDLSDTLSPSKEKSSDDTT-DAQMDEQDLNEPLAKVSLLKddlQGTQSETEAKQDIQHLRKEL 468
Cdd:COG3883 82 -------------EERREELGERARALYRSGGSVSYlDVLLGSESFSDFLDRLSALS---KIADADADLLEELKADKAEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 469 VEAQELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILL 548
Cdd:COG3883 146 EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
250
....*....|.
gi 1907106148 549 LRQAAAEAVSE 559
Cdd:COG3883 226 AAAAAAAAAAA 236
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
28-85 |
4.75e-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: 4.75e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907106148 28 IKIGRSvarcrPAQNNATFDCKVLSRNHALVWFDhKTSKFYLQDTKSSNGTFINSQRL 85
Cdd:smart00240 1 VTIGRS-----SEDCDIQLDGPSISRRHAVIVYD-GGGRFYLIDLGSTNGTFVNGKRI 52
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
449-752 |
5.24e-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: 56.61 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 449 QGTQSETEAKQDIQHLRKELVEAQELARTSKQKCFELQA---LLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQ 525
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEdlsSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 526 EEKDTEISSTRDKLLSAQDEIlllrqaaaeaVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQ 605
Cdd:TIGR02169 786 ARLSHSRIPEIQAELSKLEEE----------VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 606 CEDQQREEAtRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVG 685
Cdd:TIGR02169 856 IENLNGKKE-ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 686 SLKEQHLRDAADLKTLLS----KAENQAKDVQ------------KEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCkD 749
Cdd:TIGR02169 935 EIEDPKGEDEEIPEEELSledvQAELQRVEEEiralepvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY-E 1013
|
...
gi 1907106148 750 NLK 752
Cdd:TIGR02169 1014 KKK 1016
|
|
| FHA_TCF19 |
cd22685 |
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ... |
29-119 |
5.74e-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: 5.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 29 KIGRSVARCRPAQNNATFDcKVLSRNHALVWFDHKTS---KFYLQDTkSSNGTFINSQRLSRGSEEsppcEILSGDIIQF 105
Cdd:cd22685 31 RIGRNPEVCDVFLCSSQHP-NLISREHAEIHAERDGNgnwKVLIEDR-STNGTYVNDVRLQDGQRR----ELSDGDTITF 104
|
90
....*....|....*.
gi 1907106148 106 G--VDVTENTRKVTHG 119
Cdd:cd22685 105 GhkNGRRVKQWPYQKS 120
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
271-752 |
8.03e-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: 55.80 E-value: 8.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 271 KLSEVERSLSNTEDECTHLKEMNERTQEELRELANKyngaVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEME 350
Cdd:TIGR04523 97 KINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQ----KKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 351 EKEQELQAKIEALQADNDFTNERLTALQEKLMVqghLTKVVEESKL--SKENQAKAKESDLSDTLSPSKEKSSDDTTDAQ 428
Cdd:TIGR04523 173 NELNLLEKEKLNIQKNIDKIKNKLLKLELLLSN---LKKKIQKNKSleSQISELKKQNNQLKDNIEKKQQEINEKTTEIS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 429 MDEQDLNEPLAKVSLLKDDLQGTQSETE-AKQDIQHLRKELVEAQ-ELARTSKQKCFELQALLEEERKAYRNQVEESAKQ 506
Cdd:TIGR04523 250 NTQTQLNQLKDEQNKIKKQLSEKQKELEqNNKKIKELEKQLNQLKsEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQ 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 507 IQVLQVQLQKLHMDMENLQEE---KDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDtdfvSLQEELKKVRAELEGWRK 583
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKEltnSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK----NLESQINDLESKIQNQEK 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 584 AASEYENEIRSLQSSFQLRCQQCED------QQREEATRLQGE-------LEKLKKEWDVLETECHSLKKENVLLSSELQ 650
Cdd:TIGR04523 406 LNQQKDEQIKKLQQEKELLEKEIERlketiiKNNSEIKDLTNQdsvkeliIKNLDNTRESLETQLKVLSRSINKIKQNLE 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 651 RQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQhlrdAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKF 730
Cdd:TIGR04523 486 QKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK----IEKLESEKKEKESKISDLEDELNKDDFELKKENLEK 561
|
490 500
....*....|....*....|..
gi 1907106148 731 EMteQEKQSITDELKQCKDNLK 752
Cdd:TIGR04523 562 EI--DEKNKEIEELKQTQKSLK 581
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
162-595 |
1.49e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 162 SQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgNQLQAcsKNQTEDSLRKELI 241
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE---AELAE--AEEELEELAEELL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 242 ALQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKL 321
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 322 KVAEGKQEEIQQKGQAE---KKELQTKIDEMEEKEQELQAKIEALQADN------------DFTNERLTALQEKLMVQGH 386
Cdd:COG1196 470 EEAALLEAALAELLEELaeaAARLLLLLEAEADYEGFLEGVKAALLLAGlrglagavavliGVEAAYEAALEAALAAALQ 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 387 LTKVVEESKLS------KENQAKAKESDLSDTLSPSKEKSSDDTTDAQMD-----EQDLNEPLAKVSLLKDDLQGTQSET 455
Cdd:COG1196 550 NIVVEDDEVAAaaieylKAAKAGRATFLPLDKIRARAALAAALARGAIGAavdlvASDLREADARYYVLGDTLLGRTLVA 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 456 EAKQDIQHLRKELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISST 535
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 536 RDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAE----------LEGWRKAASEYENEIRSL 595
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEaleelpeppdLEELERELERLEREIEAL 779
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
229-718 |
1.71e-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: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 229 KNQTEDSLRKeliaLQEDKHSYETTaKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELA---- 304
Cdd:TIGR00606 586 INQTRDRLAK----LNKELASLEQN-KNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAmlag 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 305 --NKYNGAVNEIKD-------LSDKLKVAEGKQEEIQQKGQA-------EKKELQTKIDEMEEKEQELQAKIEALQADND 368
Cdd:TIGR00606 661 atAVYSQFITQLTDenqsccpVCQRVFQTEAELQEFISDLQSklrlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIID 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 369 FTNERLTALQEKLMvqgHLTKVVEESKLSKENQAKakesdLSDTLSPSKEKSSDDTTDAQMDEQdLNEPLAKVSLLKDDL 448
Cdd:TIGR00606 741 LKEKEIPELRNKLQ---KVNRDIQRLKNDIEEQET-----LLGTIMPEEESAKVCLTDVTIMER-FQMELKDVERKIAQQ 811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 449 QGTQSETEAKQDIQHLRKELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHM--DMENLQE 526
Cdd:TIGR00606 812 AAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRrqQFEEQLV 891
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 527 EKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQC 606
Cdd:TIGR00606 892 ELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDY 971
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 607 EDQQREEATRLQGELEKLKKEWDVLETECHSLKKenvllSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVG- 685
Cdd:TIGR00606 972 LKQKETELNTVNAQLEECEKHQEKINEDMRLMRQ-----DIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGq 1046
|
490 500 510
....*....|....*....|....*....|....*..
gi 1907106148 686 ----SLKEQHLRDAADLKtLLSKAENQAKDVQKEYEK 718
Cdd:TIGR00606 1047 mqvlQMKQEHQKLEENID-LIKRNHVLALGRQKGYEK 1082
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
245-731 |
6.36e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 53.26 E-value: 6.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 245 EDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTH-LKEMNERTQEE---LRELANKYNGAVNEIKDLSDK 320
Cdd:pfam01576 32 EKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEiLHELESRLEEEeerSQQLQNEKKKMQQHIQDLEEQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 321 LKvaegKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLMVQGHLTKVV------EES 394
Cdd:pfam01576 112 LD----EEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLsklknkHEA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 395 KLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLA--KVSLLK--DDLQGTQS--ETEAKQDIQHLRK-- 466
Cdd:pfam01576 188 MISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAelRAQLAKkeEELQAALArlEEETAQKNNALKKir 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 467 -------ELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQ----EEK---DTEI 532
Cdd:pfam01576 268 eleaqisELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKkaleEETrshEAQL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 533 SSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSS---FQLRCQQCEDQ 609
Cdd:pfam01576 348 QEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQlqeLQARLSESERQ 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 610 QREEA---TRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLsilqmtrKELEKQVGS 686
Cdd:pfam01576 428 RAELAeklSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRL-------RQLEDERNS 500
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1907106148 687 LKEQhlrdaadlktlLSKAENQAKDVQKEYEKTQTVLSELKLKFE 731
Cdd:pfam01576 501 LQEQ-----------LEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
239-738 |
7.16e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.20 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 239 ELIALQEDKHSYETTAK--ESLRRVLQEKIE-----VVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAV 311
Cdd:pfam15921 279 EITGLTEKASSARSQANsiQSQLEIIQEQARnqnsmYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 312 NEIKDLSDKLKVAEGKQEEIQQKGQAE--KKE--------------------------LQTKIDEMEEKEQELQAKIEAL 363
Cdd:pfam15921 359 TEARTERDQFSQESGNLDDQLQKLLADlhKREkelslekeqnkrlwdrdtgnsitidhLRRELDDRNMEVQRLEALLKAM 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 364 QADNDFTNER-LTALQEKLMVQGHLTKVVEESKLSKENQAKAKESDLSD--TLSPSKEKSSDDTTDAQMDEQDLNEPLAK 440
Cdd:pfam15921 439 KSECQGQMERqMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKkmTLESSERTVSDLTASLQEKERAIEATNAE 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 441 VSLLKD----DLQGTQSETEAKQDIQHLRKElVEAQELARTSKQKCFEL---------QALLEEERKAYRNQVEesaKQI 507
Cdd:pfam15921 519 ITKLRSrvdlKLQELQHLKNEGDHLRNVQTE-CEALKLQMAEKDKVIEIlrqqienmtQLVGQHGRTAGAMQVE---KAQ 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 508 QVLQVQLQKLHM-DMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAE---AVSERDTDFVSLQEELKKVRAEL----- 578
Cdd:pfam15921 595 LEKEINDRRLELqEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSErlrAVKDIKQERDQLLNEVKTSRNELnslse 674
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 579 ------EGWRKAASEYENEIRSLQssFQLRCQQCEDQQ----------------------REEATRLQGELEKLKKEWDV 630
Cdd:pfam15921 675 dyevlkRNFRNKSEEMETTTNKLK--MQLKSAQSELEQtrntlksmegsdghamkvamgmQKQITAKRGQIDALQSKIQF 752
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 631 LETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVgslkeqhlrdaADLKTLLSKAENQAK 710
Cdd:pfam15921 753 LEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKV-----------ANMEVALDKASLQFA 821
|
570 580
....*....|....*....|....*...
gi 1907106148 711 DVQKEYEKTQTVLSELKLKFEMTEQEKQ 738
Cdd:pfam15921 822 ECQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
27-106 |
7.67e-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: 7.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 27 PIKIGRSVARcRPAQNNATFDC-----KVLSRNHALVWFDHKTSKFYLQdTKSSNGTFINSQRLSRGseeSPPCEILSGD 101
Cdd:cd22701 18 EVVLGRNSKN-SSSTAADSVDIdlgpsKKISRRHARIFYDFTTQCFELS-VLGRNGVKVDGILVKPG---SPPVPLRSGS 92
|
....*
gi 1907106148 102 IIQFG 106
Cdd:cd22701 93 LIQIG 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
162-388 |
1.06e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 162 SQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTED--SLRKE 239
Cdd:TIGR02168 725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEElkALREA 804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 240 LIALQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERtQEELRELANKYNGAVNEIKDLSD 319
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE-IEELEELIEELESELEALLNERA 883
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907106148 320 KLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLMVQGHLT 388
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT 952
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
25-114 |
1.81e-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: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 25 DEPIKIGRSVArcrpAQNNATFDC-KVLSRNHALVWFDHKTSKFyLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDII 103
Cdd:cd22663 20 GKEVTVGRGLG----VTYQLVSTCpLMISRNHCVLKKNDEGQWT-IKDNKSLNGVWVNGERI----EPLKPYPLNEGDLI 90
|
90
....*....|.
gi 1907106148 104 QFGVDVTENTR 114
Cdd:cd22663 91 QLGVPPENKEP 101
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-757 |
1.85e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 197 QEASDTSWQALIDEDRLLSRLEVMGNQLQacsknqtedSLRKELIALQEDKHSYETTAKESLRRVLQEKI---EVVRKLS 273
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIE---------EERKRRDKLTEEYAELKEELEDLRAELEEVDKefaETRDELK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 274 EVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKE 353
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 354 QElqakIEALQADNDFTNERLTALQEKLMvqghltkvveesklSKENQAKAKESDLSDTLSPSKEKSSDDT----TDAQM 429
Cdd:TIGR02169 469 QE----LYDLKEEYDRVEKELSKLQRELA--------------EAEAQARASEERVRGGRAVEEVLKASIQgvhgTVAQL 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 430 DEQDLNEPLAKVSLLKDDLQGTQSETE--AKQDIQHLRKE---------------------------------------- 467
Cdd:TIGR02169 531 GSVGERYATAIEVAAGNRLNNVVVEDDavAKEAIELLKRRkagratflplnkmrderrdlsilsedgvigfavdlvefdp 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 468 --------------LVEAQELAR---------TSKQKCFELQALL----EEERKAYRNQVEESAKqiqvlqvqLQKLHMD 520
Cdd:TIGR02169 611 kyepafkyvfgdtlVVEDIEAARrlmgkyrmvTLEGELFEKSGAMtggsRAPRGGILFSRSEPAE--------LQRLRER 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 521 MENLQEEKDTeISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQ 600
Cdd:TIGR02169 683 LEGLKRELSS-LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 601 lRCQQCEDQQREEATRLQGELEKLKKE-----WDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQM 675
Cdd:TIGR02169 762 -ELEARIEELEEDLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE 840
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 676 TRKELEKQVGSL-KEQHLRDA--ADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLK 752
Cdd:TIGR02169 841 QRIDLKEQIKSIeKEIENLNGkkEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
....*
gi 1907106148 753 LLREK 757
Cdd:TIGR02169 921 ELKAK 925
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
255-641 |
1.88e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 255 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQK 334
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 335 GQAEKKELQTKIDEMEEKEqelqAKIEALQadndftnERLTALQEKLMVQGHLTKVVEESKLSKENQakakesdlsdtls 414
Cdd:TIGR02169 753 IENVKSELKELEARIEELE----EDLHKLE-------EALNDLEARLSHSRIPEIQAELSKLEEEVS------------- 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 415 pSKEKSSDDTtdaqmdEQDLNEPLAKVSLLKDDLQGTQSETEakqDIQHLRKELVEAQELARTSKQKcfelqalLEEERK 494
Cdd:TIGR02169 809 -RIEARLREI------EQKLNRLTLEKEYLEKEIQELQEQRI---DLKEQIKSIEKEIENLNGKKEE-------LEEELE 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 495 AYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDtEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEE---- 570
Cdd:TIGR02169 872 ELEAALRDLESRLGDLKKERDELEAQLRELERKIE-ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeee 950
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907106148 571 --LKKVRAELEgwrkaasEYENEIRSLQSSFQLRCQQCEDQQREEaTRLQGELEKLKKEWDVLE---TECHSLKKE 641
Cdd:TIGR02169 951 lsLEDVQAELQ-------RVEEEIRALEPVNMLAIQEYEEVLKRL-DELKEKRAKLEEERKAILeriEEYEKKKRE 1018
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
26-106 |
1.94e-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: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 26 EPIKIGRSVArcrpaqNNATFDCKVLSRNHALVwfDHKTSKFYLQDTKSSNGTFINSQRLSRGseesppcEILSGDIIQF 105
Cdd:cd22698 21 DEFTIGRSSN------NDIRLNDHSVSRHHARI--VRQGDKCNLTDLGSTNGTFLNGIRVGTH-------ELKHGDRIQL 85
|
.
gi 1907106148 106 G 106
Cdd:cd22698 86 G 86
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
27-117 |
2.02e-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: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 27 PIKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLsrgSEESPPCEILSGDIIQFG 106
Cdd:cd22678 24 PLTIGRIQ------RGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESI---SPNGRPVVLSSGDVITLG 94
|
90
....*....|.
gi 1907106148 107 vdvTENTRKVT 117
Cdd:cd22678 95 ---SETKILVR 102
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
162-735 |
2.30e-06 |
|
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: 51.36 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 162 SQELFQLSQYLQEALHR----EQMLEQKLATLQRLLAITQEASDTSWQALIDEDRllsRLEVMGNQLQACSKNQTEDSLR 237
Cdd:pfam10174 129 AKELFLLRKTLEEMELRietqKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWER---TRRIAEAEMQLGHLEVLLDQKE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 238 KELIALQEDKHS-YETTAKESLRRVLQEKIEVV-RKLSEVERSLSNTEDECTHLKEMNERTQEELRElankyngavnEIK 315
Cdd:pfam10174 206 KENIHLREELHRrNQLQPDPAKTKALQTVIEMKdTKISSLERNIRDLEDEVQMLKTNGLLHTEDREE----------EIK 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 316 dlsdKLKVAEGKQEEIQQKGQAEKKELQTKIDEMeekeQELQAKIEALQADNDFTNERLTALQEKLMVQGHLTKVVEESK 395
Cdd:pfam10174 276 ----QMEVYKSHSKFMKNKIDQLKQELSKKESEL----LALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 396 LSKENQAKAKESDL---SDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEAK-QDIQHLRKELVEA 471
Cdd:pfam10174 348 DALRLRLEEKESFLnkkTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKdKQLAGLKERVKSL 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 472 QELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDteiSSTRDKLLSAQDEILLLRQ 551
Cdd:pfam10174 428 QTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVS---ALQPELTEKESSLIDLKEH 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 552 AAAEAVS--ERDTDFVSLQEELKKVRAE---LEGWRKAASEYENEIRSlQSSFQLRCQQCEDQ---QREEATRLQGELEK 623
Cdd:pfam10174 505 ASSLASSglKKDSKLKSLEIAVEQKKEEcskLENQLKKAHNAEEAVRT-NPEINDRIRLLEQEvarYKEESGKAQAEVER 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 624 LKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQsfeltsdlsiLQMTRKELEKQVGSLKEQHLRDAADLKTllS 703
Cdd:pfam10174 584 LLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVAN----------IKHGQQEMKKKGAQLLEEARRREDNLAD--N 651
|
570 580 590
....*....|....*....|....*....|..
gi 1907106148 704 KAENQAKDVQKEYEKTQTVLSELKLKFEMTEQ 735
Cdd:pfam10174 652 SQQLQLEELMGALEKTRQELDATKARLSSTQQ 683
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
251-757 |
2.83e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 251 ETTAKESLRRVLQ-EKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELR-ELANKYNGA--VNEIKDLSDKLKVAE- 325
Cdd:PTZ00121 1114 ARKAEEAKKKAEDaRKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKaEEARKAEDAkkAEAARKAEEVRKAEEl 1193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 326 GKQEEIQQKGQAEKKELQTKIDEMEEKEQElqAKIEALQADNDFTNERLTALQEKLMVQGHLTKVVEESKLS----KENQ 401
Cdd:PTZ00121 1194 RKAEDARKAEAARKAEEERKAEEARKAEDA--KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAhfarRQAA 1271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 402 AKAKESDLSDTLSPSKEKSsddttdaQMDEQDLNEPLAKVSLLKDDLQGTQSETEAKQDIQHLRKELVEAQELARTSKQK 481
Cdd:PTZ00121 1272 IKAEEARKADELKKAEEKK-------KADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 482 CfELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEE---------KDTEISSTRDKLLSAQDEILLLRQA 552
Cdd:PTZ00121 1345 A-EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkkadeakkKAEEDKKKADELKKAAAAKKKADEA 1423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 553 AAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQREEATRLQGELEKLKKEWDVLE 632
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK 1503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 633 TECHSLKKENVLLSSELQRQEKELHNSQKQSfeltsdlsilqmTRKELEKQVGSLKEQHLRDAADLKtllsKAENQAKDV 712
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEAKKAEEAK------------KADEAKKAEEKKKADELKKAEELK----KAEEKKKAE 1567
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1907106148 713 QKEYEKTQTVLSELKLKfEMTEQEKQSITDELKQCKDNLKLLREK 757
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAE-EAKKAEEARIEEVMKLYEEEKKMKAEE 1611
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
55-108 |
3.69e-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: 3.69e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907106148 55 HALVWFDHKTSKFYLQDTKSSNGTFINSQRLSrgseESPPCEILSGDIIQFGVD 108
Cdd:cd22704 39 HAVITYDQIDNEFKIKDLGSLNGTFVNDSRIP----EQTYITLKLGDSIRFGYD 88
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
299-757 |
6.74e-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: 49.63 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 299 ELRELANKYNGAVNEIKDLSDKLKVAEG---KQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERL- 374
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKnlnKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIk 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 375 TALQEKLMVQGHLTKVVEESKLSKENQAKAKE--SDLSDTLSPSKEKSSDDTTDAQMDEQDLNeplakvsLLKDDLQGTQ 452
Cdd:TIGR04523 114 NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTeiKKKEKELEKLNNKYNDLKKQKEELENELN-------LLEKEKLNIQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 453 SETeAKQDIQHLRKELVEAQELARTSKQKCFELQAL-LEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEE---- 527
Cdd:TIGR04523 187 KNI-DKIKNKLLKLELLLSNLKKKIQKNKSLESQISeLKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEqnki 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 528 ------KDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVS-LQEELKKVRAELEGWRKAASEYENEIRSLQSSFQ 600
Cdd:TIGR04523 266 kkqlseKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKeLKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 601 LRCQQCEDQQREEATrLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKEL 680
Cdd:TIGR04523 346 QLKKELTNSESENSE-KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 681 EKQVGSLKEQHLRDAA-----------------DLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDE 743
Cdd:TIGR04523 425 EKEIERLKETIIKNNSeikdltnqdsvkeliikNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE 504
|
490
....*....|....
gi 1907106148 744 LKQCKDNLKLLREK 757
Cdd:TIGR04523 505 KKELEEKVKDLTKK 518
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
289-743 |
7.13e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 289 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKgQAEKKELQTKIDEMEEKEQELQAKIEALQADND 368
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 369 F---------TNERLTALQ---EKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNE 436
Cdd:COG4717 127 LlplyqeleaLEAELAELPerlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 437 plaKVSLLKDDLQGTQSETE-AKQDIQHLRKELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQ 515
Cdd:COG4717 207 ---RLAELEEELEEAQEELEeLEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 516 KLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRsl 595
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE-- 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 596 qssfQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSF--ELTSDLSIL 673
Cdd:COG4717 362 ----ELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEEL 437
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 674 QMTRKELEKQVgslkEQHLRDAADLKTLLSKAENQAKdvqkeyektqtvLSELKLKFEMTEQEKQSITDE 743
Cdd:COG4717 438 EEELEELEEEL----EELREELAELEAELEQLEEDGE------------LAELLQELEELKAELRELAEE 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
210-502 |
1.46e-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: 48.91 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 210 EDRLLSRLEVMGNQLQacsKNQTEDSLRKELIALQEDKHSYETTAK--------ESLRRVLQEKIEVVRKLSEVERSLSN 281
Cdd:TIGR02169 186 IERLDLIIDEKRQQLE---RLRREREKAERYQALLKEKREYEGYELlkekealeRQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 282 TEDECTH----LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQ 357
Cdd:TIGR02169 263 LEKRLEEieqlLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 358 AKIEALQADNDFTNERLTALQEKLMV-QGHLTKVVEESKLSKENQAKAKE--SDLSDTLSPSKEKSSDDTTDAQMDEQDL 434
Cdd:TIGR02169 343 REIEEERKRRDKLTEEYAELKEELEDlRAELEEVDKEFAETRDELKDYREklEKLKREINELKRELDRLQEELQRLSEEL 422
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907106148 435 NEPLAKVSLLKDDLQGTQSETEAKQD-IQHLRKELVEAQELARTSKQKCFELQA---LLEEERKAYRNQVEE 502
Cdd:TIGR02169 423 ADLNAAIAGIEAKINELEEEKEDKALeIKKQEWKLEQLAADLSKYEQELYDLKEeydRVEKELSKLQRELAE 494
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
318-571 |
1.74e-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: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 318 SDKLKVAEGKQEEIQQKGQAEKKEL---QTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLmvqghltKVVEES 394
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELaalKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-------AELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 395 KLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEAkqdIQHLRKELVEAQEL 474
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE---LRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 475 ARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEisstrDKLLSAqdeilLLRQAAA 554
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL-----EALIAR-----LEAEAAA 238
|
250
....*....|....*..
gi 1907106148 555 EAVSERDTDFVSLQEEL 571
Cdd:COG4942 239 AAERTPAAGFAALKGKL 255
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
317-739 |
2.00e-05 |
|
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: 48.20 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 317 LSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNdftNERLTALQEKLMVQGHLTKVvEESKL 396
Cdd:pfam05557 14 LQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKRE---AEAEEALREQAELNRLKKKY-LEALN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 397 SKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQgtqsETEAK-QDIQHLRKELVEAQELA 475
Cdd:pfam05557 90 KKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLD----LLKAKaSEAEQLRQNLEKQQSSL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 476 RTSKQKCFELQalleeerkaYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISstrdKLLSAQDEILLLR----- 550
Cdd:pfam05557 166 AEAEQRIKELE---------FEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNK----HLNENIENKLLLKeeved 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 551 -QAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRS--LQSSFQLRCQQCEDQQREEATRLQGELEKLKKE 627
Cdd:pfam05557 233 lKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSpeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 628 WDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDL----SILQMTRKEL-EKQVGSLKEQHLRDAADlktLL 702
Cdd:pfam05557 313 RRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgyrAILESYDKELtMSNYSPQLLERIEEAED---MT 389
|
410 420 430
....*....|....*....|....*....|....*..
gi 1907106148 703 SKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 739
Cdd:pfam05557 390 QKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQA 426
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
52-106 |
2.09e-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: 2.09e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907106148 52 SRNH-ALVWfdHK-TSKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22674 48 SRVHaALVY--HKhLNRVFLIDLGSTHGTFVGGIRL----EPHKPQQLPIDSTLRFG 98
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
51-106 |
2.40e-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: 2.40e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907106148 51 LSRNHALVWF----DHKTSKFYLQDTKSSNGTFINSQRLsrgseesPP---CEILSGDIIQFG 106
Cdd:cd22677 41 ISRYHAVLQYrgdaDDHDGGFYLYDLGSTHGTFLNKQRI-------PPkqyYRLRVGHVLKFG 96
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
182-653 |
2.65e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 182 LEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgnqlqacSKNQTEDSLRKELIALQEDKHSYETTaKESLRRV 261
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHE---------ERREELETLEAEIEDLRETIAETERE-REELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 262 LQEKIEVVRKLSEVERSL-----------SNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEE 330
Cdd:PRK02224 281 VRDLRERLEELEEERDDLlaeaglddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 331 IQQKGQAEKKELQ---TKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLmvqghltkvveESKLSKENQAKAKES 407
Cdd:PRK02224 361 LREEAAELESELEearEAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL-----------EELREERDELREREA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 408 DLSDTLS------------------PSKEKSSDDTTDAQMDEQDlNEPLAKVSLLKDDLQGTQSETEAKQDiqhLRKELV 469
Cdd:PRK02224 430 ELEATLRtarerveeaealleagkcPECGQPVEGSPHVETIEED-RERVEELEAELEDLEEEVEEVEERLE---RAEDLV 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 470 EAQELARTSKQKCFELQALLEEErkayRNQVEESAKQIQVLQVQLQKLHMDMenlqEEKDTEISSTRDKLLSAQDEILLL 549
Cdd:PRK02224 506 EAEDRIERLEERREDLEELIAER----RETIEEKRERAEELRERAAELEAEA----EEKREAAAEAEEEAEEAREEVAEL 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 550 RQAAAEAVSERDT--DFVSLQEELKKVRAELEGW---RKAASEYENEIRSLQSSFQLRCQQCED--------QQREEATR 616
Cdd:PRK02224 578 NSKLAELKERIESleRIRTLLAAIADAEDEIERLrekREALAELNDERRERLAEKRERKRELEAefdearieEAREDKER 657
|
490 500 510
....*....|....*....|....*....|....*..
gi 1907106148 617 LQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQE 653
Cdd:PRK02224 658 AEEYLEQVEEKLDELREERDDLQAEIGAVENELEELE 694
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
28-106 |
2.85e-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: 2.85e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907106148 28 IKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDhkTSKFYLQDTKSSNGTFINSQRlsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22680 23 VSIGRDP------ENVIVIPDPFVSRNHARITVD--SNEIYIEDLGSTNGTFVNDFK-----RIKGPAKLHPNDIIKLG 88
|
|
| FHA_RAD53-like_rpt2 |
cd22690 |
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
12-103 |
3.05e-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: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 12 PNSHPfqerHVYL-DEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTSKF---YLQDTkSSNGTFINSQRLSR 87
Cdd:cd22690 8 NPSYP----DIELtQNTTFIGRS------KDCDEEITDPRISKHHCIITRKRSGKGLddvYVTDT-STNGTFINNNRLGK 76
|
90
....*....|....*.
gi 1907106148 88 GSEesppCEILSGDII 103
Cdd:cd22690 77 GSQ----SLLQDGDEI 88
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
546-757 |
3.31e-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: 47.07 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 546 ILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQcEDQQREEATRLQGELEKLK 625
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-IRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 626 KEWDVLETECHSLKKE-----------------NVLLSSE-LQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSL 687
Cdd:COG4942 90 KEIAELRAELEAQKEElaellralyrlgrqpplALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 688 KEQhlrdAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 757
Cdd:COG4942 170 EAE----RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
14-106 |
3.60e-05 |
|
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.
Pssm-ID: 438734 [Multi-domain] Cd Length: 96 Bit Score: 43.29 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 14 SHPFQERHvyldepIKIGRSVarcrpaQNNATFDCKVLSRNHALvwFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEesp 93
Cdd:cd22682 14 QFPITEST------IVIGRSV------ESQVQIDDDSVSRYHAK--LAVNPSAVSIIDLGSTNGTIVNGKKIPKLAS--- 76
|
90
....*....|...
gi 1907106148 94 pCEILSGDIIQFG 106
Cdd:cd22682 77 -CDLQNGDQIKIG 88
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
253-749 |
6.09e-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: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 253 TAKESLR-RVLQEKIEVVRKLSEVERSLSNTEDEctHLKEMNERtQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEI 331
Cdd:pfam05483 197 LAFEELRvQAENARLEMHFKLKEDHEKIQHLEEE--YKKEINDK-EKQVSLLLIQITEKENKMKDLTFLLEESRDKANQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 332 QQKGQAEKKELQtkidEMEEKEQELQAKIEALQADNDFTNERLTALQEKLMVQGHLTKVVEESKLSKENQAKAKESDLSD 411
Cdd:pfam05483 274 EEKTKLQDENLK----ELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSF 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 412 TLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETE--------AKQDIQHLRKELVEAQELARTSKQ--- 480
Cdd:pfam05483 350 VVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEemtkfknnKEVELEELKKILAEDEKLLDEKKQfek 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 481 -------KCFELQALLEEERKAYRN---QVEESAKQIQVLQVQLQKLHMDMENlQEEKDTEISSTRDKLLSAQDEILLLR 550
Cdd:pfam05483 430 iaeelkgKEQELIFLLQAREKEIHDleiQLTAIKTSEEHYLKEVEDLKTELEK-EKLKNIELTAHCDKLLLENKELTQEA 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 551 QAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQCE---DQQREEATRLQGELEKLKKE 627
Cdd:pfam05483 509 SDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKcklDKSEENARSIEYEVLKKEKQ 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 628 WDVLETECHSLKKEnvllsselqrqekeLHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTLLSKAEN 707
Cdd:pfam05483 589 MKILENKCNNLKKQ--------------IENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEE 654
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1907106148 708 QAKDVQKEYEKTQtvLSELKLkFEMTEQEKQSITDELKQCKD 749
Cdd:pfam05483 655 IIDNYQKEIEDKK--ISEEKL-LEEVEKAKAIADEAVKLQKE 693
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
13-110 |
6.62e-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: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 13 NSHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTskFYLQDTKSSNGTFINSQRLSrgsee 91
Cdd:cd22665 7 SQAHGPEKDFPLYEgENVIGRD------PSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRL----- 73
|
90 100
....*....|....*....|.
gi 1907106148 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 |
7.01e-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: 7.01e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907106148 52 SRNHALVWFDH---------KTSKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQFGV 107
Cdd:cd22667 40 SRKHATLTVLHpeanlsdpdTRPELTLKDL-SKYGTFVNGEKLKGGSE----VTLKDGDVITFGV 99
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
329-634 |
8.32e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 8.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 329 EEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQadndftnERLTALQeKLMVQGHLTKVveesklskenqakakesd 408
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAK-------EGLSALN-RLLPRLNLLAD------------------ 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 409 lsDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEakqDIQHLRKELVEAQELARTSKQKCFELQAL 488
Cdd:PRK04863 890 --ETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPE---QFEQLKQDYQQAQQTQRDAKQQAFALTEV 964
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 489 LeeERKAYRNqVEESAKQIQVLQVQLQKLHMDMENLQEEKDTeissTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQ 568
Cdd:PRK04863 965 V--QRRAHFS-YEDAAEMLAKNSDLNEKLRQRLEQAEQERTR----AREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQ 1037
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907106148 569 E---ELKK--VRAElEGWRKAASEYENEIRSLQSSFQLRCQQCEDQ---QREEATRLQGELEKLKKEWDVLETE 634
Cdd:PRK04863 1038 ElkqELQDlgVPAD-SGAEERARARRDELHARLSANRSRRNQLEKQltfCEAEMDNLTKKLRKLERDYHEMREQ 1110
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
229-760 |
8.36e-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: 46.25 E-value: 8.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 229 KNQTEDSLRKELIALQEDKHSYETTAK---------ESLRRVLQEKIEVVRKLSEVERSlsnTEDECTHLKEMNERTQEE 299
Cdd:pfam05483 94 KVSIEAELKQKENKLQENRKIIEAQRKaiqelqfenEKVSLKLEEEIQENKDLIKENNA---TRHLCNLLKETCARSAEK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 300 LRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAkiEALQADNDFTNE---RLTA 376
Cdd:pfam05483 171 TKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEE--EYKKEINDKEKQvslLLIQ 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 377 LQEKLMVQGHLTKVVEESKlSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQgtqsete 456
Cdd:pfam05483 249 ITEKENKMKDLTFLLEESR-DKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQ------- 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 457 akqdiqhlrkelveaqelaRTSKQKCfelqaLLEEERKAyrnQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEisstR 536
Cdd:pfam05483 321 -------------------IATKTIC-----QLTEEKEA---QMEELNKAKAAHSFVVTEFEATTCSLEELLRTE----Q 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 537 DKLLSAQDEILLLRQAAAEAVSERD--TDFVSLQE----ELKKVRAELEGWRKAASEYENEIRSLQSSFQlrcqqcedqq 610
Cdd:pfam05483 370 QRLEKNEDQLKIITMELQKKSSELEemTKFKNNKEveleELKKILAEDEKLLDEKKQFEKIAEELKGKEQ---------- 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 611 reeatRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSL--- 687
Cdd:pfam05483 440 -----ELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMtle 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 688 -----------KEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 756
Cdd:pfam05483 515 lkkhqediincKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILEN 594
|
....
gi 1907106148 757 KGNN 760
Cdd:pfam05483 595 KCNN 598
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
257-505 |
9.52e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.07 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 257 SLRRVLQEKIEVVRKLSEVERslsnteDECTHLKEmNERTqEELRELANKYNGAVNEIKDLSDKLKVAEGKQ-------- 328
Cdd:PRK05771 13 TLKSYKDEVLEALHELGVVHI------EDLKEELS-NERL-RKLRSLLTKLSEALDKLRSYLPKLNPLREEKkkvsvksl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 329 EEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTnERLTALQEKLMVQGHLTKV-VEESKLSKEnqaKAKES 407
Cdd:PRK05771 85 EELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERL-EPWGNFDLDLSLLLGFKYVsVFVGTVPED---KLEEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 408 DLSDTLSPSKEKSSDDTTD------AQMDEQDLNEPLAKVSLLKDDLQ--GTQSET--EAKQDIQHLRKELVEAQELART 477
Cdd:PRK05771 161 KLESDVENVEYISTDKGYVyvvvvvLKELSDEVEEELKKLGFERLELEeeGTPSELirEIKEELEEIEKERESLLEELKE 240
|
250 260
....*....|....*....|....*...
gi 1907106148 478 SKQKCFELQALLEEERKAYRNQVEESAK 505
Cdd:PRK05771 241 LAKKYLEELLALYEYLEIELERAEALSK 268
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
190-757 |
1.14e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.73 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 190 QRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHSYET----TAKESLRRVLQEK 265
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNeeriDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 266 IEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVA-EGKQEEIQQKGQAEKKELQT 344
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDdEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 345 KIDEMEEKEQELQAKIEALQADndftnerltalqeklmvqghltKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDT 424
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAE----------------------EEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 425 TDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEAKQDIQhlrKELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESA 504
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEE---LEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 505 KQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKA 584
Cdd:pfam02463 468 KKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIST 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 585 ASEYENEIRSLQSSFQLRCQQCEDQQREEATRLQGELEKLKKEWDvletecHSLKKENVLLSSELQRQEKELHNSQKQSF 664
Cdd:pfam02463 548 AVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLK------SIAVLEIDPILNLAQLDKATLEADEDDKR 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 665 ELTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDEL 744
Cdd:pfam02463 622 AKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEI 701
|
570
....*....|...
gi 1907106148 745 KQCKDNLKLLREK 757
Cdd:pfam02463 702 KKKEQREKEELKK 714
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
18-86 |
1.36e-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: 1.36e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907106148 18 QERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhkTSKFYLQDTKSSNGTFINSQRLS 86
Cdd:cd22694 8 GELRFDPGSSVRIGRD------PDADVRLDDPRVSRRHALLEFD--GDGWVYTDLGSRNGTYLNGRRVQ 68
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
153-381 |
1.36e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 153 VAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgNQLQAcsKNQT 232
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE---QELAA--LEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 233 EDSLRKELIALQEDKhsyettakESLRRVLQEKIEVVRKLSEVER--SLSNTEDECTHLK--EMNERTQEELRELANKYN 308
Cdd:COG4942 85 LAELEKEIAELRAEL--------EAQKEELAELLRALYRLGRQPPlaLLLSPEDFLDAVRrlQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907106148 309 GAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKL 381
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
530-746 |
1.46e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 530 TEISSTRDKLLSAQDEILLLRQAAAEAvserdTDFVSLQEELKKVRAELEGWR-----KAASEYENEIRSLQSSFQlrcq 604
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELA-----ERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEELRAELA---- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 605 qcedQQREEATRLQGELEKLKKEWDVLETECHSLKKENV-LLSSELQRQEKELHNsqkqsfeltsdlsiLQMTRKELEKQ 683
Cdd:COG4913 306 ----RLEAELERLEARLDALREELDELEAQIRGNGGDRLeQLEREIERLERELEE--------------RERRRARLEAL 367
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907106148 684 VGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 746
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
152-633 |
1.77e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 152 KVAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDtswqaliDEDRLLSRLEVMGNQLQACSKNQ 231
Cdd:COG4717 60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA-------ELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 232 TEDSLRKELIALQEDKHSYETTAKEsLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMN-ERTQEELRELANKYNGA 310
Cdd:COG4717 133 ELEALEAELAELPERLEELEERLEE-LRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 311 VNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKideMEEKEQELQAKIEALQADNDFTNERLTALQEKLMVQGHLTkV 390
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAALEERLK---EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLL-A 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 391 VEESKLSKENQAKAKESDLSDTLsPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLkddlqgtqsetEAKQDIQHLRKELVE 470
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQAL-PALEELEEEELEELLAALGLPPDLSPEELL-----------ELLDRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 471 AQELARTSKQKCF--ELQALLE----EERKAYRNQVEESAKqiqvlqvqlqklhmdmenlQEEKDTEISSTRDKLLSAQD 544
Cdd:COG4717 356 AEELEEELQLEELeqEIAALLAeagvEDEEELRAALEQAEE-------------------YQELKEELEELEEQLEELLG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 545 EILLLRQAAAEAvsERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLrcqqceDQQREEATRLQGELEKL 624
Cdd:COG4717 417 ELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL------AELLQELEELKAELREL 488
|
....*....
gi 1907106148 625 KKEWDVLET 633
Cdd:COG4717 489 AEEWAALKL 497
|
|
| FHA_CHFR |
cd22672 |
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ... |
49-105 |
1.82e-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: 1.82e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907106148 49 KVLSRNHALVWFDHKTsKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQF 105
Cdd:cd22672 39 KLVSGDHCKIIRDEKG-QVWLEDT-STNGTLVNKVKVVKGQK----VELKHGDVIYL 89
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
178-350 |
2.50e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 178 REQML--EQKLATLQRLLAITQEAsDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHSYE---T 252
Cdd:COG4913 241 HEALEdaREQIELLEPIRELAERY-AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEarlD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 253 TAKESLRRV--------------LQEKIE-VVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDL 317
Cdd:COG4913 320 ALREELDELeaqirgnggdrleqLEREIErLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEE 399
|
170 180 190
....*....|....*....|....*....|...
gi 1907106148 318 SDKLKVAEGKQEEIQQKGQAEKKELQTKIDEME 350
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
446-656 |
2.68e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 446 DDLQGTQSETE-AKQDIQHLRkELVEAQELARTSKQKCFELQALLEEeRKAYRNQVEesakqiqvlqvqLQKLHMDMENL 524
Cdd:COG4913 235 DDLERAHEALEdAREQIELLE-PIRELAERYAAARERLAELEYLRAA-LRLWFAQRR------------LELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 525 QEEK---DTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDfvsLQEELKKVRAELEGWRKAASEYENEIRSLQSS--- 598
Cdd:COG4913 301 RAELarlEAELERLEARLDALREELDELEAQIRGNGGDRLEQ---LEREIERLERELEERERRRARLEALLAALGLPlpa 377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907106148 599 --------------FQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKEL 656
Cdd:COG4913 378 saeefaalraeaaaLLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
366-674 |
3.16e-04 |
|
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: 44.34 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 366 DNDFTNERLTALQEKLMV----QGHLTKVVEESKLSKENQAKAKESDLSDTLSPSkEKSSDDTTDAQMDEQDLNEPLAKV 441
Cdd:pfam17380 267 ENEFLNQLLHIVQHQKAVserqQQEKFEKMEQERLRQEKEEKAREVERRRKLEEA-EKARQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 442 SllKDDLQGTQSEtEAKQDIQHLRKE--------LVEAQELARTSKQKCFELQALLEEERKaYRNQVEESAKQIQVLQVQ 513
Cdd:pfam17380 346 R--ERELERIRQE-ERKRELERIRQEeiameisrMRELERLQMERQQKNERVRQELEAARK-VKILEEERQRKIQQQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 514 LQKLHMDMEN--------LQEEKDTEISSTRDKLLSAQDEILLLRQAAAE-----AVSERDTDFVSLQEELKK--VRAEL 578
Cdd:pfam17380 422 MEQIRAEQEEarqrevrrLEEERAREMERVRLEEQERQQQVERLRQQEEErkrkkLELEKEKRDRKRAEEQRRkiLEKEL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 579 EGWRKAASEYENEIRSLQSSFQLRCQQCEDQQR----EEATRLQGELEKLKK--EWDVLETECHSlKKENVLLSSELQRQ 652
Cdd:pfam17380 502 EERKQAMIEEERKRKLLEKEMEERQKAIYEEERrreaEEERRKQQEMEERRRiqEQMRKATEERS-RLEAMEREREMMRQ 580
|
330 340
....*....|....*....|..
gi 1907106148 653 EKELHNSQKQsFELTSDLSILQ 674
Cdd:pfam17380 581 IVESEKARAE-YEATTPITTIK 601
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
233-757 |
3.31e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 233 EDSLRKELIALQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVN 312
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 313 EIKDLSDKLK-VAEGKQEEIQQK---GQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLMvqghlT 388
Cdd:TIGR02169 273 LLEELNKKIKdLGEEEQLRVKEKigeLEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIE-----E 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 389 KVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQ--------DLNEPLAKVSLLKDDLQGTQSETE---- 456
Cdd:TIGR02169 348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRekleklkrEINELKRELDRLQEELQRLSEELAdlna 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 457 ----AKQDIQHLRKELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHmdmenlQEEKDTEI 532
Cdd:TIGR02169 428 aiagIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA------EAEAQARA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 533 SSTRDKLLSAQDEIL---------LLRQ---------AAAEA---------VSERDTDFVSLQEELKKVRA--------- 576
Cdd:TIGR02169 502 SEERVRGGRAVEEVLkasiqgvhgTVAQlgsvgeryaTAIEVaagnrlnnvVVEDDAVAKEAIELLKRRKAgratflpln 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 577 ----------------------------------------------ELEGWRKAASEY-----ENEI------------- 592
Cdd:TIGR02169 582 kmrderrdlsilsedgvigfavdlvefdpkyepafkyvfgdtlvveDIEAARRLMGKYrmvtlEGELfeksgamtggsra 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 593 RSLQSSFQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLK-------KENVLLSSELQRQEKELHNSQKQSFE 665
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSqelsdasRKIGEIEKEIEQLEQEEEKLKERLEE 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 666 LTSDLSILQMTR-------KELEKQVGSLKEQ--HLRDA-ADLKTLLSkaENQAKDVQKEYEKTQTVLSELKLKFEMTEQ 735
Cdd:TIGR02169 742 LEEDLSSLEQEIenvkselKELEARIEELEEDlhKLEEAlNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
|
650 660
....*....|....*....|..
gi 1907106148 736 EKQSITDELKQCKDNLKLLREK 757
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQ 841
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
289-539 |
3.52e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 289 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALqadnd 368
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEEL----- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 369 ftNERLTALQEKLMVQghltkvveESKLSKENQAKAKESDLSDTLSpSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDL 448
Cdd:PHA02562 240 --TDELLNLVMDIEDP--------SAALNKLNTAAAKIKSKIEQFQ-KVIKMYEKGGVCPTCTQQISEGPDRITKIKDKL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 449 -QGTQSETEAKQDIQHLRKELVEAQELARTSKqkcfELQALLEEERKAYRNQVEEsAKQIQVLQVQLQKLHMD----MEN 523
Cdd:PHA02562 309 kELQHSLEKLDTAIDELEEIMDEFNEQSKKLL----ELKNKISTNKQSLITLVDK-AKKVKAAIEELQAEFVDnaeeLAK 383
|
250
....*....|....*.
gi 1907106148 524 LQEEKDtEISSTRDKL 539
Cdd:PHA02562 384 LQDELD-KIVKTKSEL 398
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
327-704 |
4.59e-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: 43.90 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 327 KQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTalqeKLMVQGHLTKVV--------EESKLSK 398
Cdd:pfam13166 90 ESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDECW----KKIKRKKNSALSealngfkyEANFKSR 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 399 ENQAKAKESDLSDTLSPSKEKSSDDTT---DAQMDEQDLNEPLA------KVSLLKDDLQGTQSETEAKQDIQHLRKELV 469
Cdd:pfam13166 166 LLREIEKDNFNAGVLLSDEDRKAALATvfsDNKPEIAPLTFNVIdfdaleKAEILIQKVIGKSSAIEELIKNPDLADWVE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 470 EAQELARTSKQKC-F---ELQALLEEERKAYRNQ-VEEsakqiqvlqvqlqklhmDMENLQEEKDTEISSTRDKL--LSA 542
Cdd:pfam13166 246 QGLELHKAHLDTCpFcgqPLPAERKAALEAHFDDeFTE-----------------FQNRLQKLIEKVESAISSLLaqLPA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 543 QDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRK---AASEYE------NEIRSLQSS--------------F 599
Cdd:pfam13166 309 VSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRALEAKRKdpfKSIELDsvdakiESINDLVASineliakhneitdnF 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 600 QLRCQQCEDQ-QREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELhnsqkqsfeltsdlsilqmtrK 678
Cdd:pfam13166 389 EEEKNKAKKKlRLHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEI---------------------K 447
|
410 420
....*....|....*....|....*.
gi 1907106148 679 ELEKQVGslkeQHLRDAADLKTLLSK 704
Cdd:pfam13166 448 ELEAQLR----DHKPGADEINKLLKA 469
|
|
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
53-106 |
4.70e-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: 4.70e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907106148 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 |
4.87e-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: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 25 DEPIKIGRsvarcRPAQNNAT----FDCKVLSRNHALVWFdhKTSKFYLQDTKSSNGTFINSQRLSR-GSEESPPCEILS 99
Cdd:cd22702 31 KQPCIIGS-----DPHQAISGisvvIPSPQVSELHARITC--KNGAFFLTDLGSEHGTWINDNEGRRyRAPPNFPVRLHP 103
|
....*....
gi 1907106148 100 GDIIQFGVD 108
Cdd:cd22702 104 SDVIEFGSD 112
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
300-428 |
4.96e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 300 LRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQE 379
Cdd:COG3883 124 LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1907106148 380 KLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQ 428
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
534-725 |
5.02e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 534 STRDKLLSAQDEILLLRQAAAEAVSERDTdfvsLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQcedQQREE 613
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEA----LEAELDALQERREALQRLAEYSWDEIDVASAEREIAELE---AELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 614 ATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQsfeltsdlsiLQMTRKELEkQVGSLKEQHLR 693
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE----------LDELQDRLE-AAEDLARLELR 748
|
170 180 190
....*....|....*....|....*....|..
gi 1907106148 694 DAADLKTLLSKAENQAKDVQKEYEKTQTVLSE 725
Cdd:COG4913 749 ALLEERFAAALGDAVERELRENLEERIDALRA 780
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
520-759 |
5.10e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 520 DMENLQEEKDTEISSTRDKLLSAQDEILLLRqAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSsf 599
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELR-EELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE-- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 600 QLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRK- 678
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKk 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 679 --ELEKQVGSLKEQHlRDAADLKTLLSKAENQAKdvqkeyEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 756
Cdd:PRK03918 347 lkELEKRLEELEERH-ELYEEAKAKKEELERLKK------RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
...
gi 1907106148 757 KGN 759
Cdd:PRK03918 420 EIK 422
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
16-111 |
6.10e-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: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 16 PFQERHVYLD-EPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFdhKTSKFYLQDTKSSNGTFINSQRLSRgseespP 94
Cdd:cd22693 7 TLQGQTFPIDkSGITIGRA------DDNDLVLSDDFVSSRHARIYL--QGSSWYLEDLGSTNGTFVNGNRVTQ------P 72
|
90
....*....|....*..
gi 1907106148 95 CEILSGDIIQFGVDVTE 111
Cdd:cd22693 73 VVVQPGDTIRIGATVFE 89
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
522-757 |
6.20e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 522 ENLQEEK--DTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSF 599
Cdd:PHA02562 178 ELNQQIQtlDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 600 QlrcqqcedQQREEATRLQGELEKLKKEWDVLE--TECHSLKkenvllsSELQRQEKELHNSQKQSFELTSDLSILQMTR 677
Cdd:PHA02562 258 N--------KLNTAAAKIKSKIEQFQKVIKMYEkgGVCPTCT-------QQISEGPDRITKIKDKLKELQHSLEKLDTAI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 678 KELEKQVGSLKEQHLR------DAADLKTLLSKAENQAKDVQKEYEKTQTvlselklkfemteqEKQSITDELKQCKDNL 751
Cdd:PHA02562 323 DELEEIMDEFNEQSKKllelknKISTNKQSLITLVDKAKKVKAAIEELQA--------------EFVDNAEELAKLQDEL 388
|
....*.
gi 1907106148 752 KLLREK 757
Cdd:PHA02562 389 DKIVKT 394
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
256-689 |
6.83e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 256 ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERtQEELRELANKYNGAVNEIKDLSDKLKVAEGKQE------ 329
Cdd:PRK01156 315 SNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQ-ILELEGYEMDYNSYLKSIESLKKKIEEYSKNIErmsafi 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 330 -EIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKL-MVQGHLTKVVEESKLSKEnqakaKES 407
Cdd:PRK01156 394 sEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMeMLNGQSVCPVCGTTLGEE-----KSN 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 408 DLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQG---TQSETEAKQdIQHLRKELVEAQELARTSKQKCFE 484
Cdd:PRK01156 469 HIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESeeiNKSINEYNK-IESARADLEDIKIKINELKDKHDK 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 485 LQALLEEERKAYRNQVEesAKQIQVLQVQLQKLHMDMENLQEEKDtEISSTRDKLLSAQDEILLlrqaaaeavserdtdf 564
Cdd:PRK01156 548 YEEIKNRYKSLKLEDLD--SKRTSWLNALAVISLIDIETNRSRSN-EIKKQLNDLESRLQEIEI---------------- 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 565 vslqeELKKVRAELEgwrKAASEYENEIRSLQSSFQLrcQQCEDQQREEatrLQGELEKLKKEWDVLETECHSLKKENVL 644
Cdd:PRK01156 609 -----GFPDDKSYID---KSIREIENEANNLNNKYNE--IQENKILIEK---LRGKIDNYKKQIAEIDSIIPDLKEITSR 675
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1907106148 645 LS---SELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKE 689
Cdd:PRK01156 676 INdieDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINE 723
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
52-106 |
7.30e-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: 7.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907106148 52 SRNHALVWFDHKTSKFYLQ-----------DTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFG 106
Cdd:cd22683 28 SRSCDLVLSDPSISRFHAElrleqnginviDNNSANGTFINGKRIKGKT-----YILKNGDIIVFG 88
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
570-756 |
7.42e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 570 ELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQCeDQQREEATRLQGELEKL---KKEWDVLETECHSLKKENVLLS 646
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREI-NEISSELPELREELEKLekeVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 647 SELQRQEKELHNSQKQSFELTSDLSILQMTRKELEK---------QVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYE 717
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907106148 718 KtqtvLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 756
Cdd:PRK03918 332 E----LEEKEERLEELKKKLKELEKRLEELEERHELYEE 366
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
274-381 |
7.84e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.92 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 274 EVERSLSNTEDECTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEK----------K 340
Cdd:pfam06160 288 YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEvayselqeelE 367
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1907106148 341 ELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKL 381
Cdd:pfam06160 368 EILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLEL 408
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
517-743 |
9.16e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 9.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 517 LHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAvSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQ 596
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEA-EEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 597 SSFQLRcqqcedQQREEATRLQGELEKLKKEWDVLETECHSLKkenvllssELQRQEKELHNSqkqsfeltsdlsiLQMT 676
Cdd:COG4717 123 KLLQLL------PLYQELEALEAELAELPERLEELEERLEELR--------ELEEELEELEAE-------------LAEL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907106148 677 RKELEKQVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDE 743
Cdd:COG4717 176 QEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
473-729 |
1.14e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.19 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 473 ELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQA 552
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 553 AAEAVSERDTdfVSLQEELKKVR-AELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQREEatrlQGELEKLKKEWDVL 631
Cdd:pfam07888 110 SEELSEEKDA--LLAQRAAHEARiRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEE----EAERKQLQAKLQQT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 632 ETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELE---KQVGSLKEQ---HLRDAADLKTLLSKA 705
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEallEELRSLQERlnaSERKVEGLGEELSSM 263
|
250 260
....*....|....*....|....
gi 1907106148 706 ENQAKDVQKEYEKTQTVLSELKLK 729
Cdd:pfam07888 264 AAQRDRTQAELHQARLQAAQLTLQ 287
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
451-690 |
1.16e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 451 TQSETEAKQDIQHLRKELVEAQELARTSKQKcfelQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEekdt 530
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 531 EISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQssfqlrcqqcedQQ 610
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR------------AD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 611 REEATRLQGELEKLKKEWDVLETEchsLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQ 690
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAE---LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
27-106 |
1.35e-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: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 27 PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTSkfYLQDTKSSNGTFINSQRLsrgseeSPPCEILSGDIIQFG 106
Cdd:cd22668 19 SNIIGRG------SDADFRLPDTGVSRRHAEIRWDGQVA--HLTDLGSTNGTTVNNAPV------TPEWRLADGDVITLG 84
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
613-736 |
1.70e-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: 41.23 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 613 EATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNsQKQSFELTSDLSilqmtrkELEKQVGSLKeqhl 692
Cdd:pfam15294 134 EIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGA-KKDVKSNLKEIS-------DLEEKMAALK---- 201
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1907106148 693 rdaADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQE 736
Cdd:pfam15294 202 ---SDLEKTLNASTALQKSLEEDLASTKHELLKVQEQLEMAEKE 242
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
49-112 |
1.78e-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: 1.78e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907106148 49 KVLSRNHALVWFDHKTS--KFYLQDTKSSNGTFINsqrlsrgSEESPPC---EILSGDIIQFGVDVTEN 112
Cdd:cd22681 64 ETCSKQHCVIQFRNVKGilKPYIMDLDSSNGTCLN-------DNVIPSSryvELRSGDVITFSKSNDYE 125
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
1-106 |
2.55e-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: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 1 MPSALAIFTCRPNSHPFQERHVYLDEPIKIGRSvARC-----RPAQnnatfdckVLSRNHALVWFDHktSKFYLQDTkSS 75
Cdd:COG3456 1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRS-ADCdwvlpDPDR--------SVSRRHAEIRFRD--GAFCLTDL-ST 68
|
90 100 110
....*....|....*....|....*....|...
gi 1907106148 76 NGTFIN--SQRLSRGSEEsppcEILSGDIIQFG 106
Cdd:COG3456 69 NGTFLNgsDHPLGPGRPV----RLRDGDRLRIG 97
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
208-381 |
2.58e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.36 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 208 IDEDRLLSRLEVMGNQLQACSKNQTE---DSLRKELIALQED-KHSYETTAKEslrrvLQEKIEVVRKLSEVERSLsnte 283
Cdd:PRK04778 249 LDHLDIEKEIQDLKEQIDENLALLEEldlDEAEEKNEEIQERiDQLYDILERE-----VKARKYVEKNSDTLPDFL---- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 284 decTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKG----------QAEKKELQTKIDEME 350
Cdd:PRK04778 320 ---EHAKEQNKELKEEIDRVKQSYtlnESELESVRQLEKQLESLEKQYDEITERIaeqeiayselQEELEEILKQLEEIE 396
|
170 180 190
....*....|....*....|....*....|.
gi 1907106148 351 EKEQELQAKIEALQADNDFTNERLTALQEKL 381
Cdd:PRK04778 397 KEQEKLSEMLQGLRKDELEAREKLERYRNKL 427
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
163-348 |
2.77e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWqALIDEDRLLSRLEVMGNQLQACSKNQTE-DSLRKELI 241
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-DEIDVASAEREIAELEAELERLDASSDDlAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 242 ALQEDkhsyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLK----EMNERTQEELRELANKYNGAVNEIKDL 317
Cdd:COG4913 696 ELEAE-----------LEELEEELDELKGEIGRLEKELEQAEEELDELQdrleAAEDLARLELRALLEERFAAALGDAVE 764
|
170 180 190
....*....|....*....|....*....|.
gi 1907106148 318 SDKLKVAEGKQEEIQQKGQAEKKELQTKIDE 348
Cdd:COG4913 765 RELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
484-715 |
2.79e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 484 ELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLqeekDTEISSTRDKLLSAQDEILLLRQAAAEavserdtd 563
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAELAE-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 564 fvsLQEELKKVRAELEGWRKaasEYENEIRSLQSS-------FQLRCQQCEDQQREeATRLQGELEKLKKEWDVLETECH 636
Cdd:COG4942 88 ---LEKEIAELRAELEAQKE---ELAELLRALYRLgrqpplaLLLSPEDFLDAVRR-LQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 637 SLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQ---HLRDAADLKTLLSKAENQAKDVQ 713
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAElaeLQQEAEELEALIARLEAEAAAAA 240
|
..
gi 1907106148 714 KE 715
Cdd:COG4942 241 ER 242
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
253-574 |
2.86e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 253 TAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQ 332
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 333 ---QKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLMVQGHLTKVVEESKLSKENQAKAKESDL 409
Cdd:COG4372 115 eelEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 410 SDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEAKQDIQHLRKELVEAQELARTSKQKCFELQALL 489
Cdd:COG4372 195 NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 490 EEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQE 569
Cdd:COG4372 275 EEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDND 354
|
....*
gi 1907106148 570 ELKKV 574
Cdd:COG4372 355 VLELL 359
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
255-621 |
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 1907106148 255 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQE-----------ELRELANKYNGAVNEIKDLSDKLKV 323
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEyyqlkekleleEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 324 AEGKQEEIQQKGQ---AEKKELQTKIDEMEEKEQELQaKIEALQADNDFTNERLTALQEKLMVQgHLTKVVEESKLSKEN 400
Cdd:pfam02463 248 DEQEEIESSKQEIekeEEKLAQVLKENKEEEKEKKLQ-EEELKLLAKEEEELKSELLKLERRKV-DDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 401 QAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEAKQDIQHLRKELVEAQELARTSKQ 480
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 481 KCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISstrdKLLSAQDEILLLRQAAAEAVSER 560
Cdd:pfam02463 406 EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQEL----KLLKDELELKKSEDLLKETQLVK 481
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907106148 561 DTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQREEATRLQGEL 621
Cdd:pfam02463 482 LQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYK 542
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
457-750 |
3.40e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 457 AKQDIQHLRKELVEAQELARTSKQKCFELQAL---LEEERKAYRNQVEESAKQIqvlqvqlqklhmDMENLQEEKDtEIS 533
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAEldaLQERREALQRLAEYSWDEI------------DVASAEREIA-ELE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 534 STRDKLLSAQDEILLLRQAAAEAVSERDTdfvsLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQREE 613
Cdd:COG4913 675 AELERLDASSDDLAALEEQLEELEAELEE----LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 614 ATRLQGELEKLKKEWDVLEtechSLKKENVLLSSELQRQEKELHNSQKQ--------SFELTSDLSILQMTRKELEKQVG 685
Cdd:COG4913 751 LEERFAAALGDAVERELRE----NLEERIDALRARLNRAEEELERAMRAfnrewpaeTADLDADLESLPEYLALLDRLEE 826
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 686 S---LKEQHLRDA------ADLKTLLSKAENQAKDVQKEYEKTQTVLSELK------LKFEMTEQEKQSITD---ELKQC 747
Cdd:COG4913 827 DglpEYEERFKELlnensiEFVADLLSKLRRAIREIKERIDPLNDSLKRIPfgpgryLRLEARPRPDPEVREfrqELRAV 906
|
...
gi 1907106148 748 KDN 750
Cdd:COG4913 907 TSG 909
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
256-359 |
4.08e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 256 ESLRRVLQEKI-EVVRKLSEVERSLSNTEDEcthLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQK 334
Cdd:PRK00409 526 EELERELEQKAeEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYA 602
|
90 100
....*....|....*....|....*
gi 1907106148 335 GQAEkKELQTKIDEMEEKEQELQAK 359
Cdd:PRK00409 603 SVKA-HELIEARKRLNKANEKKEKK 626
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
247-752 |
4.24e-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: 40.80 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 247 KHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNT---EDECTHLKEMNERTQEELRELANK----YNGAVNEIKDLSD 319
Cdd:TIGR00606 229 KEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKImklDNEIKALKSRKKQMEKDNSELELKmekvFQGTDEQLNDLYH 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 320 KLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTA---LQEKLMVQGHLTKVVEESKL 396
Cdd:TIGR00606 309 NHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRArdsLIQSLATRLELDGFERGPFS 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 397 SKE--NQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEAKQD-IQHLRKELVEAQE 473
Cdd:TIGR00606 389 ERQikNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEeLKFVIKELQQLEG 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 474 LARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQ------KLHMDMENlqEEKDTEISSTRDKLLSAQDEIL 547
Cdd:TIGR00606 469 SSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKadldrkLRKLDQEM--EQLNHHTTTRTQMEMLTKDKMD 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 548 LLRQaaAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQREEATRLQGELEKLKKE 627
Cdd:TIGR00606 547 KDEQ--IRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSY 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 628 WDVLETECHSLKKEnvllsSELQRQEKELHNSQKQSFELTS-----DLSILQMTRKE-----LEKQVGSLKEQHLRDAAD 697
Cdd:TIGR00606 625 EDKLFDVCGSQDEE-----SDLERLKEEIEKSSKQRAMLAGatavySQFITQLTDENqsccpVCQRVFQTEAELQEFISD 699
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1907106148 698 LKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLK 752
Cdd:TIGR00606 700 LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQ 754
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
538-715 |
4.55e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 538 KLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIrslqssfqlrcqqceDQQREEATRL 617
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI---------------EEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 618 QGELEKLK--KEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQmtrKELEKQVGSLKEQHLRDA 695
Cdd:COG1579 79 EEQLGNVRnnKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE---AELEEKKAELDEELAELE 155
|
170 180
....*....|....*....|
gi 1907106148 696 ADLKTLLSKAENQAKDVQKE 715
Cdd:COG1579 156 AELEELEAEREELAAKIPPE 175
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
236-366 |
5.55e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 236 LRKELIALQEDKHSYETTAKESLRRV--LQEKIEVVRKlsevERSLSNTEDECTHLKEMNERTQEELRELankyngaVNE 313
Cdd:COG1579 50 AKTELEDLEKEIKRLELEIEEVEARIkkYEEQLGNVRN----NKEYEALQKEIESLKRRISDLEDEILEL-------MER 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1907106148 314 IKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQAD 366
Cdd:COG1579 119 IEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
172-361 |
7.16e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 38.35 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 172 LQEALHREQMLEQKLATLQRLLaitqeasdtswQALIDEDRLLSRLEVmgNQLQACSKNQTEDSLRKELIAlqedKHSYE 251
Cdd:pfam15619 6 LSARLHKIKELQNELAELQSKL-----------EELRKENRLLKRLQK--RQEKALGKYEGTESELPQLIA----RHNEE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 252 T-TAKESLRRvLQEKIEVV-RKLSEVERSLSNTEDECTHL------KEMNERT--QEELRELANKYNGAVNEIKDLSDKL 321
Cdd:pfam15619 69 VrVLRERLRR-LQEKERDLeRKLKEKEAELLRLRDQLKRLeklsedKNLAEREelQKKLEQLEAKLEDKDEKIQDLERKL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907106148 322 KVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIE 361
Cdd:pfam15619 148 ELENKSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLK 187
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
611-737 |
7.29e-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: 39.23 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 611 REEATRLQGELEKLKKEWDVLETECHSLKK----ENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGS 686
Cdd:smart00787 164 MKELELLNSIKPKLRDRKDALEEELRQLKQledeLEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIED 243
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1907106148 687 LKEQHLrdaaDLKTLLSKAENQAKDVQKeyeKTQTVLSELKLKFEMTEQEK 737
Cdd:smart00787 244 LTNKKS----ELNTEIAEAEKKLEQCRG---FTFKEIEKLKEQLKLLQSLT 287
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
163-670 |
8.54e-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: 39.57 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 163 QELFQLSQYLQEALHREQMLEQKLATLQRL----LAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRK 238
Cdd:TIGR00618 379 QHIHTLQQQKTTLTQKLQSLCKELDILQREqatiDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEK 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 239 elIALQEDKHSY-ETTAKESLRRVLQEKIEVVRKLsEVERSLSNTEDECthlkEMNERTQEELRELANKYNGAVNEIKDL 317
Cdd:TIGR00618 459 --IHLQESAQSLkEREQQLQTKEQIHLQETRKKAV-VLARLLELQEEPC----PLCGSCIHPNPARQDIDNPGPLTRRMQ 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 318 SDKLKVAEGKQEE--IQQKGQAEKKELQTKIDEMEEKEQELQAkieALQADNDFTNERLTALQEKLMVQGHLTKVVEESK 395
Cdd:TIGR00618 532 RGEQTYAQLETSEedVYHQLTSERKQRASLKEQMQEIQQSFSI---LTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAED 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 396 LSKENQAKAKESdlsdtLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQgtQSETEAKQDIQHLRKELVEAQELA 475
Cdd:TIGR00618 609 MLACEQHALLRK-----LQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQ--ERVREHALSIRVLPKELLASRQLA 681
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 476 RTSKQKCFELQA----LLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTeISSTRDKLLSAQDEILLLRQ 551
Cdd:TIGR00618 682 LQKMQSEKEQLTywkeMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDA-LNQSLKELMHQARTVLKART 760
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 552 AAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQREEATRLQGELEKLKKEWDVL 631
Cdd:TIGR00618 761 EAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEK 840
|
490 500 510
....*....|....*....|....*....|....*....
gi 1907106148 632 ETECHSLKKENVLLSSELQRQEkELHNSQKQSFELTSDL 670
Cdd:TIGR00618 841 SATLGEITHQLLKYEECSKQLA-QLTQEQAKIIQLSDKL 878
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
180-427 |
9.42e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 180 QMLEQKLATLQRLLAITQEASDTSWQALideDRLLSRLEVMGNQLQAcsKNQTEDSLRKELIALQEDKHSYETTAKESLR 259
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAEL---EELNEEYNELQAELEA--LQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 260 rVLQEKIEVVRKLSEVERSLSNTE--DECTHLKEMNERTQEELRELANkyngAVNEIKDLSDKLKVAEGKQEEIQQKGQA 337
Cdd:COG3883 94 -ALYRSGGSVSYLDVLLGSESFSDflDRLSALSKIADADADLLEELKA----DKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 338 EKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSK 417
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
250
....*....|
gi 1907106148 418 EKSSDDTTDA 427
Cdd:COG3883 249 AGAAGAAGAA 258
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
554-716 |
9.47e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.46 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 554 AEAVSERDTDfvSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQlrcqqcedQQREEATRLQGELEKLKKEWDVLET 633
Cdd:COG2433 379 EEALEELIEK--ELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVE--------RLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106148 634 ECHSLKKE---NVLLSSELQRQEKELHNsqkqsfeLTSDLSILQMTRKELEKQVGSLKE----QHLRDAADLKTLLSKAE 706
Cdd:COG2433 449 ELSEARSEerrEIRKDREISRLDREIER-------LERELEEERERIEELKRKLERLKElwklEHSGELVPVKVVEKFTK 521
|
170
....*....|
gi 1907106148 707 NQAKDVQKEY 716
Cdd:COG2433 522 EAIRRLEEEY 531
|
|
| |
