|
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 157819677 3 SALAIFTCRPNSHPFQERHVYLDEPIKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHktSKFYLQDTKSSNGTFINS 82
Cdd:cd22679 1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 157819677 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 |
4.23e-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: 4.23e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157819677 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 157819677 27 PIKIGRSVARCRPAQNNAT-FDCKVLSRNHALVWfdHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQF 105
Cdd:cd22692 38 QIHIGRYTERVRQAIYHPVvFKSKVVSRTHGCIK--VDEGNWYIKDVKSSSGTFLNHQRLSPASRTSKPYPLRDGDILQL 115
|
...
gi 157819677 106 GVD 108
Cdd:cd22692 116 GMD 118
|
|
| FHA_VPS64-like |
cd22695 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ... |
6-126 |
4.33e-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: 4.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 6 AIFTCRPNSHPFQERHV---YLDEPIKIGRSVARCRPAQN---------------NATFDCKVLSRNHALVWFDHKTSKF 67
Cdd:cd22695 2 HILVLKSLNATFETKFLvvpFKPDGLKLGRPVTNSVNKNNsgskrdlfsqqvrpdNGNFDSRVLSRNHACLSCDPTTGKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 157819677 68 YLQDTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFGVDVTEntrKVTHGCIVSTIK 126
Cdd:cd22695 82 YIRDLKSSNGTFVNGQKIRQND-----VELKVGDEVDLGTDIDS---KIEHRKISAYVE 132
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
239-749 |
5.07e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.80 E-value: 5.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 239 ELVALQEDKHSYETTAKESLRRV--LQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKD 316
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 317 LSDKLKAAEGKQEEIQQKGQAEKK--ELQAKIDDMEEKEQELQAKIEALQ--ADNDFTNERLTALQEKLMVQGHLTKVVE 392
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 393 ESKLSKENQAKAKESDLSDTLSPSKE--KSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQDTQHLRK---- 466
Cdd:PTZ00121 1442 EAKKADEAKKKAEEAKKAEEAKKKAEeaKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKaeea 1521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 467 ----ELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSA 542
Cdd:PTZ00121 1522 kkadEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 543 QDEILLLHQAAAKAVSERDTdfmslQEELKKVRAELEGWRKAASEYEEEIRSLQstfQLRCQQCEVQQREEATRLQGELE 622
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIK-----AEELKKAEEEKKKVEQLKKKEAEEKKKAE---ELKKAEEENKIKAAEEAKKAEED 1673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 623 KLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLsilqmtRKELENQMGSLKEQHLRDEADLKtll 702
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL------KKAEEENKIKAEEAKKEAEEDKK--- 1744
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 157819677 703 skaenQAKDVQKEYE---KTQTVLSELKLKFEMTEQEKQSITDELKQCKD 749
Cdd:PTZ00121 1745 -----KAEEAKKDEEekkKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-757 |
1.42e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 78.17 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 156 NTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQA--CSKNQTE 233
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvAQLELQI 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 234 DSLRKELVALQEDKHSYE------TTAKESLRRVLQE--KIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELAN 305
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEdrrerlQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 306 KYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKiddmEEKEQELQAKIEALQADNDFTNERLTALQEKLmvQG 385
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ----SGLSGILGVLSELISVDEGYEAAIEAALGGRL--QA 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 386 HLTKVVEESKLSKENQAKAKESDLS----DTLSPSKEKSSDDTTDAQMDEQ-----DLNEPLAKVSLLKDDLQG------ 450
Cdd:TIGR02168 550 VVVENLNAAKKAIAFLKQNELGRVTflplDSIKGTEIQGNDREILKNIEGFlgvakDLVKFDPKLRKALSYLLGgvlvvd 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 451 --------------------------------TQAETEAKQDTQHLRKELVEAQELARASKQKCFDLQALL---EEERKA 495
Cdd:TIGR02168 630 dldnalelakklrpgyrivtldgdlvrpggviTGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALaelRKELEE 709
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 496 YRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDT---EISSTRDKLLSAQDEILLLHQAAAKA---VSERDTDFMSLQE 569
Cdd:TIGR02168 710 LEEELEQLRKELEELSRQISALRKDLARLEAEVEQleeRIAQLSKELTELEAEIEELEERLEEAeeeLAEAEAEIEELEA 789
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 570 ELKKVRAELEGWRKAASEYEEEIRSLQSTF---QLRCQQCE----------VQQREEATRLQGELEKLKKEWDVLENECR 636
Cdd:TIGR02168 790 QIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLErriaaterrlEDLEEQIEELSEDIESLAAEIEELEELIE 869
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 637 SLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHlrdeADLKTLLSKAENQAKDVQkey 716
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL----AQLELRLEGLEVRIDNLQ--- 942
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 157819677 717 ektQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 757
Cdd:TIGR02168 943 ---ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| 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 157819677 13 NSHPFQERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKtsKFYLQDTKSSNGTFINSQRLsrgseeS 92
Cdd:cd00060 6 DGDGGGREFPLTKGVVTIGRS------PDCDIVLDDPSVSRRHARIEVDGG--GVYLEDLGSTNGTFVNGKRI------T 71
|
90
....*....|....
gi 157819677 93 PPCEILSGDIIQFG 106
Cdd:cd00060 72 PPVPLQDGDVIRLG 85
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
161-727 |
4.53e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 4.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 161 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKEL 240
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 241 VALQEDkhsyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDK 320
Cdd:COG1196 298 ARLEQD-----------IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 321 LKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQEKLMVQGHLTKVVEESKLSKEN 400
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 401 QAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQ--DLNEPLAKVSLLKDDLQGTQAETEAKQDTQHLRKELVEAQELARA- 477
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAAlaELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAv 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 478 ----SKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLS-AQDEILLLHQA 552
Cdd:COG1196 527 avliGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARgAIGAAVDLVAS 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 553 AAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLqstfqlrcqqcevqqREEATRLQGELEKLKKEWDVLE 632
Cdd:COG1196 607 DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV---------------TLEGEGGSAGGSLTGGSRRELL 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 633 NECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTLLSKAENQAKDV 712
Cdd:COG1196 672 AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
570
....*....|....*
gi 157819677 713 QKEYEKTQTVLSELK 727
Cdd:COG1196 752 ALEELPEPPDLEELE 766
|
|
| 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 157819677 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 |
1.36e-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: 1.36e-12
10 20 30
....*....|....*....|....*....|....*...
gi 157819677 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21868 1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
204-738 |
2.46e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 204 WQALIDEDRLLSRLEVMGNQLQAcsKNQTEDSLRKELVALQEDKhsyeTTAKESLRRVLQEKIEVVRKLSEVERSLSNTE 283
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEE--LEAELEELEAELAELEAEL----EELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 284 DECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEAL 363
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 364 QADNDFTNERLTALQEKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSL 443
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 444 LKDDLQGTQAETEAKQDTQHLRKELVEAQELARASKQKCFDLQALLEEERKAYRN--------------QVEESAKQIQV 509
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLaglrglagavavliGVEAAYEAALE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 510 LQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAqdEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEgWRKAASEYE 589
Cdd:COG1196 542 AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRA--TFLPLDKIRARAALAAALARGAIGAAVDLVASDLR-EADARYYVL 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 590 EEIRSLQSTFQLRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSD 669
Cdd:COG1196 619 GDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEA 698
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 670 LSILQMTRKELENQMGSLKEQHLRDEADLKTLLSKAENQAKDVQKEYEKT-QTVLSELKLKFEMTEQEKQ 738
Cdd:COG1196 699 LLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLeEEALEELPEPPDLEELERE 768
|
|
| 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 157819677 52 SRNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQFG 106
Cdd:cd22686 48 SKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPYPLTHGDELKIG 102
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
190-756 |
2.73e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 190 QRLLAITQEASDTSWQALIDE--------DRLLSRLEVMGNQLQACSKNQTE-----DSLRKELVALQEDKHSYETT--- 253
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLRleelreelEELQEELKEAEEELEELTAELQEleeklEELRLEVSELEEEIEELQKElya 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 254 AKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQ 333
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 334 KGQAEKKELQ---AKIDDMEEKEQELQAKIEALQA---DNDFTNERLTALQEKLMVQGHLTKVVE-ESKLSKENQAKAKE 406
Cdd:TIGR02168 373 RLEELEEQLEtlrSKVAQLELQIASLNNEIERLEArleRLEDRRERLQQEIEELLKKLEEAELKElQAELEELEEELEEL 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 407 SDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQDT--QHLRKELVEAQELARASKQKCFD 484
Cdd:TIGR02168 453 QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGvkALLKNQSGLSGILGVLSELISVD 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 485 --------------LQALLEEERKAYRNQVEESAKQI--------------------QVLQVQLQRLHMDMENLQEEKDT 530
Cdd:TIGR02168 533 egyeaaieaalggrLQAVVVENLNAAKKAIAFLKQNElgrvtflpldsikgteiqgnDREILKNIEGFLGVAKDLVKFDP 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 531 EISSTRDKLLS--------------------------AQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKA 584
Cdd:TIGR02168 613 KLRKALSYLLGgvlvvddldnalelakklrpgyrivtLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEK 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 585 ASEYEEEIRSLQSTFQLRcQQCEVQQREEATRLQGELEKLKKEWDVLENECRSlkkenvlLSSELQRQEKELHNSQKQSL 664
Cdd:TIGR02168 693 IAELEKALAELRKELEEL-EEELEQLRKELEELSRQISALRKDLARLEAEVEQ-------LEERIAQLSKELTELEAEIE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 665 ELTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTL---LSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSIT 741
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
650
....*....|....*
gi 157819677 742 DELKQCKDNLKLLRE 756
Cdd:TIGR02168 845 EQIEELSEDIESLAA 859
|
|
| 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 157819677 14 SHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktSKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716 8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
|
90
....*....|....
gi 157819677 93 pPCEILSGDIIQFG 106
Cdd:COG1716 75 -PAPLRDGDVIRLG 87
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
235-749 |
4.11e-10 |
|
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: 63.50 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 235 SLRKELVALQEDKHSYETTAKE--SLRRVLQEKIEVVRKLSEVERSLsntEDECTHLREMNERTQEELRELANKYNGAVN 312
Cdd:TIGR04523 170 ELENELNLLEKEKLNIQKNIDKikNKLLKLELLLSNLKKKIQKNKSL---ESQISELKKQNNQLKDNIEKKQQEINEKTT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 313 EIKDLSDKLKAAEGKQEEIQQKGQAEKKELQ---AKIDDMEEKEQELQAKIEAL--QADNDFTNERLTALQEKlmvqgHL 387
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQNKIKKQLSEKQKELEqnnKKIKELEKQLNQLKSEISDLnnQKEQDWNKELKSELKNQ-----EK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 388 TKVVEESKLSKENQakaKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEA-KQDTQHLRK 466
Cdd:TIGR04523 322 KLEEIQNQISQNNK---IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNlESQINDLES 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 467 ELVEAQELARASKQKCFDLQA---LLEEERKAYRNQVEESAKQIQvlqvqlqrlhmDMENLQEEKDTEISSTRDKLLSAQ 543
Cdd:TIGR04523 399 KIQNQEKLNQQKDEQIKKLQQekeLLEKEIERLKETIIKNNSEIK-----------DLTNQDSVKELIIKNLDNTRESLE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 544 DEILLLhqaaAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLqstfqlrcqqceVQQREEATRLQGELEK 623
Cdd:TIGR04523 468 TQLKVL----SRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL------------TKKISSLKEKIEKLES 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 624 LKKEwdvLENECRSLKKENVLLSSELQRQ--EKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQ--HLRDEADLK 699
Cdd:TIGR04523 532 EKKE---KESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEkkDLIKEIEEK 608
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 157819677 700 T-LLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKD 749
Cdd:TIGR04523 609 EkKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
250-739 |
5.15e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 250 YETTAKES--LRRVLQEKIEVVRKL----SEVERSLSNTEDECTH-LREMNErTQEELRELANKYNGAVNEIKDLsDKLK 322
Cdd:PRK03918 160 YENAYKNLgeVIKEIKRRIERLEKFikrtENIEELIKEKEKELEEvLREINE-ISSELPELREELEKLEKEVKEL-EELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 323 AAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQAdndfTNERLTALQEKLMVQGHLTKVVEESKlSKENQA 402
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE----KVKELKELKEKAEEYIKLSEFYEEYL-DELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 403 KAKESDLSDTLSPSKEKSSddttDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQDTQHLRKELVE-AQELARASKQK 481
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlKKRLTGLTPEK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 482 CFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERD 561
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKEL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 562 TDFMSLQEELKKVRAELEGWRKAASEY------EEEIRSLQSTFQLRCQQCEVQQREEATRLQGELEKLKKEWDVLENEC 635
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKKESELiklkelAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 636 RS---LKKENVLLSSELQRQEKELHNSQKQSLELT-SDLSILQMTRKELE---NQMGSLK--EQHLRDE----ADLKTLL 702
Cdd:PRK03918 549 EKleeLKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEpfyNEYLELKdaEKELEREekelKKLEEEL 628
|
490 500 510
....*....|....*....|....*....|....*..
gi 157819677 703 SKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 739
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR 665
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
431-757 |
6.59e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 6.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 431 EQDLNEPLAKVSLLKDDLQGTQAETEAKQDTQHLRKELVEAQELARASKQKCfdlqalLEEERKAYRNQVEEsakqiqvl 510
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEA------LERQKEAIERQLAS-------- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 511 qvqlqrlhmdMENLQEEKDTEISSTRDKLLSAQDeilLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEE 590
Cdd:TIGR02169 249 ----------LEEELEKLTEEISELEKRLEEIEQ---LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 591 EIRSLQStfqlRCQQCEVQ---QREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKEL------HNSQK 661
Cdd:TIGR02169 316 ELEDAEE----RLAKLEAEidkLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFaetrdeLKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 662 QSLE-LTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTLLSK---AENQAKDVQKEYEKTQTVLSELKLKFEMTEQEK 737
Cdd:TIGR02169 392 EKLEkLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKineLEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL 471
|
330 340
....*....|....*....|
gi 157819677 738 QSITDELKQCKDNLKLLREK 757
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQRE 491
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
238-752 |
1.31e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.08 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 238 KELVALQEDKHSYETTAKESLRRVLQ-EKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELR--ELANKYNGAVNEI 314
Cdd:PTZ00121 1191 EELRKAEDARKAEAARKAEEERKAEEaRKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRkfEEARMAHFARRQA 1270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 315 KDLSDKLKAAE--GKQEEIQQKGQAEKKELQAKIDDMEEKEQElQAKIEALQADNDFTNERLTALQEKlmvqghltkvvE 392
Cdd:PTZ00121 1271 AIKAEEARKADelKKAEEKKKADEAKKAEEKKKADEAKKKAEE-AKKADEAKKKAEEAKKKADAAKKK-----------A 1338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 393 ESKLSKENQAKAKESDLSDTLSPSKEKssddttdAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQDTQHLRKELVEAQ 472
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEK-------AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELK 1411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 473 ElARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQeeKDTEISSTRDKLLSAQDEILLLHQA 552
Cdd:PTZ00121 1412 K-AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAK--KKAEEAKKADEAKKKAEEAKKADEA 1488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 553 AAKA-VSERDTDFMSLQEELKKVRAELegwRKA--ASEYEEEIRSLQSTFQLRCQQCEVQQREEATRLQGELEKLKKEWD 629
Cdd:PTZ00121 1489 KKKAeEAKKKADEAKKAAEAKKKADEA---KKAeeAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK 1565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 630 VLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLK----EQHLRDEADLKTLLSKA 705
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkaEEEKKKVEQLKKKEAEE 1645
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 157819677 706 ENQAKDVQKEYEKTQTVLSELKLKfemtEQEKQSITDELKQCKDNLK 752
Cdd:PTZ00121 1646 KKKAEELKKAEEENKIKAAEEAKK----AEEDKKKAEEAKKAEEDEK 1688
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
255-756 |
5.50e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 5.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 255 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNgavnEIKDLSDKLKAAEGKQEEIQQk 334
Cdd:PRK03918 178 IERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELESLEG- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 335 gqaEKKELQAKIDDMEEKEQELQAKIEALQAdndfTNERLTALQEKLMVQGHLTKVVEESKlSKENQAKAKESDLSDTLS 414
Cdd:PRK03918 253 ---SKRKLEEKIRELEERIEELKKEIEELEE----KVKELKELKEKAEEYIKLSEFYEEYL-DELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 415 PSKEKSSDdttdAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQDTQHLRKELVE-AQELARASKQKCFDLQALLEEER 493
Cdd:PRK03918 325 GIEERIKE----LEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlKKRLTGLTPEKLEKELEELEKAK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 494 KAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKK 573
Cdd:PRK03918 401 EEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRK 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 574 VRAELEGWRKAASEY------EEEIRSLQSTFQLRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRS---LKKENVL 644
Cdd:PRK03918 481 ELRELEKVLKKESELiklkelAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKleeLKKKLAE 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 645 LSSELQRQEKELHNSQKQSLELT-SDLSILQMTRKELE---NQMGSLK--EQHLRDE----ADLKTLLSKAENQAKDVQK 714
Cdd:PRK03918 561 LEKKLDELEEELAELLKELEELGfESVEELEERLKELEpfyNEYLELKdaEKELEREekelKKLEEELDKAFEELAETEK 640
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157819677 715 EYEKTQTVLSELKLKFEMTEQEK-------------------QSITDELKQCKDNLKLLRE 756
Cdd:PRK03918 641 RLEELRKELEELEKKYSEEEYEElreeylelsrelaglraelEELEKRREEIKKTLEKLKE 701
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
212-756 |
8.53e-09 |
|
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: 59.29 E-value: 8.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 212 RLLSRLEVMGNQLQACSKNQTEDSLRKELVALQEDKHSYETTAKESLRRVLQEKIEvvrkLSEVERSlSNTEDECTHLRE 291
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE----LDGFERG-PFSERQIKNFHT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 292 MNERTQEELRELANKyngavnEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQadndftn 371
Cdd:TIGR00606 398 LVIERQEDEAKTAAQ------LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ------- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 372 eRLTALQEKLMvqghltKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGT 451
Cdd:TIGR00606 465 -QLEGSSDRIL------ELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQM 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 452 QAETEAKQDTQHLRKELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLhmdmENLQEEKDTE 531
Cdd:TIGR00606 538 EMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASL----EQNKNHINNE 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 532 ISSTRDKLLSAQDEILllhqaAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQC----- 606
Cdd:TIGR00606 614 LESKEEQLSSYEDKLF-----DVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCqrvfq 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 607 -EVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLL-------SSELQRQEKELHNSQKQSLELTSDLSILQMTRK 678
Cdd:TIGR00606 689 tEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIE 768
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 679 ELENQMGSL--KEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVL--SELKLKFEMTEQEKQSITDELKQCKDNLKLL 754
Cdd:TIGR00606 769 EQETLLGTImpEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLqgSDLDRTVQQVNQEKQEKQHELDTVVSKIELN 848
|
..
gi 157819677 755 RE 756
Cdd:TIGR00606 849 RK 850
|
|
| CC1_T3JAM |
cd21912 |
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ... |
164-204 |
1.16e-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: 51.58 E-value: 1.16e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 157819677 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 157819677 14 SHPFQERHV---YLDEPIKIGRSvARCRPAQNNATfdckvLSRNHALVW---FDHKT-SKFYLQDTkSSNGTFINSQRLS 86
Cdd:cd22670 7 SSPGSTDIVlpiYKNQVITIGRS-PSCDIVINDPF-----VSRTHCRIYsvqFDESSaPLVYVEDL-SSNGTYLNGKLIG 79
|
90 100
....*....|....*....|....*
gi 157819677 87 RGseespPCEILS-GDIIQFGVDVT 110
Cdd:cd22670 80 RN-----NTVLLSdGDVIEIAHSAT 99
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-757 |
2.14e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 197 QEASDTSWQALIDEDRLLSRLEVMGNQLQacsknqtedSLRKELVALQEDKHSYETTAKESLRRVLQEKI---EVVRKLS 273
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIE---------EERKRRDKLTEEYAELKEELEDLRAELEEVDKefaETRDELK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 274 EVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKE 353
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 354 QElqakIEALQADNDFTNERLTALQEKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQD 433
Cdd:TIGR02169 469 QE----LYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVA 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 434 LNEPLAKVsLLKDDLQGTQAETEAKQDTQH------LRKELVEAQELARASKQKCFDLQALLEEERKAYRNQVE------ 501
Cdd:TIGR02169 545 AGNRLNNV-VVEDDAVAKEAIELLKRRKAGratflpLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKyvfgdt 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 502 ------ESAKQ----------------------------------IQVLQVQLQRLHMDMENLQEEKDTeISSTRDKLLS 541
Cdd:TIGR02169 624 lvvediEAARRlmgkyrmvtlegelfeksgamtggsraprggilfSRSEPAELQRLRERLEGLKRELSS-LQSELRRIEN 702
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 542 AQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEvQQREEATRLQGEL 621
Cdd:TIGR02169 703 RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE-ELEEDLHKLEEAL 781
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 622 EKLKKE-----WDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEA 696
Cdd:TIGR02169 782 NDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157819677 697 ---DLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 757
Cdd:TIGR02169 862 kkeELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
245-731 |
3.28e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 57.49 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 245 EDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTH-LREMNERTQEE---LRELANKYNGAVNEIKDLSDK 320
Cdd:pfam01576 32 EKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEiLHELESRLEEEeerSQQLQNEKKKMQQHIQDLEEQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 321 LKAAEGKQeeiqQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQEKLMVQGHLTKVV------EES 394
Cdd:pfam01576 112 LDEEEAAR----QKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLsklknkHEA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 395 KLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLA--KVSLLK--DDLQGTQA--ETEAKQDTQHLRK-- 466
Cdd:pfam01576 188 MISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAelRAQLAKkeEELQAALArlEEETAQKNNALKKir 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 467 -------ELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQ----EEK---DTEI 532
Cdd:pfam01576 268 eleaqisELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKkaleEETrshEAQL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 533 SSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQST---FQLRCQQCEVQ 609
Cdd:pfam01576 348 QEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQlqeLQARLSESERQ 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 610 QREEA---TRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLsilqmtrKELENQMGS 686
Cdd:pfam01576 428 RAELAeklSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRL-------RQLEDERNS 500
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 157819677 687 LKEQhlrdeadlktlLSKAENQAKDVQKEYEKTQTVLSELKLKFE 731
Cdd:pfam01576 501 LQEQ-----------LEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
298-757 |
3.63e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.97 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 298 EELRELANKYNGAVNEIkdLSDKLKAAEGKQEEIQQKgqaEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTAL 377
Cdd:PRK02224 165 EEYRERASDARLGVERV--LSDQRGSLDQLKAQIEEK---EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 378 QEklmvqghltkVVEESKLSKENqakakesdlSDTLSPSKEKSSDDTTDAQMDEQDLNEPL----AKVSLLKDDLQGTQA 453
Cdd:PRK02224 240 DE----------VLEEHEERREE---------LETLEAEIEDLRETIAETEREREELAEEVrdlrERLEELEEERDDLLA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 454 ETE---AKQDTQHLRKELVEAQELAraskqkcfdLQALLEEER---KAYRNQVEESAKQIQVLQVQLQRLHMDMENLqee 527
Cdd:PRK02224 301 EAGlddADAEAVEARREELEDRDEE---------LRDRLEECRvaaQAHNEEAESLREDADDLEERAEELREEAAEL--- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 528 kDTEISSTRDKLLSAQDEILLLH---QAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTF----Q 600
Cdd:PRK02224 369 -ESELEEAREAVEDRREEIEELEeeiEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVeeaeA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 601 LR----CQQCE------------VQQREEATRLQGELEKLKKEWDVLENECRSLKkenvllssELQRQEKELHNSQKQSL 664
Cdd:PRK02224 448 LLeagkCPECGqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAE--------DLVEAEDRIERLEERRE 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 665 ELTSDLSILQMTRKELENQMGSLKEQhlrdEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS----- 739
Cdd:PRK02224 520 DLEELIAERRETIEEKRERAEELRER----AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESlerir 595
|
490
....*....|....*....
gi 157819677 740 -ITDELKQCKDNLKLLREK 757
Cdd:PRK02224 596 tLLAAIADAEDEIERLREK 614
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
229-718 |
4.59e-08 |
|
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: 56.98 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 229 KNQTEDSLRK---ELVALQEDKHSYettakeslRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELA- 304
Cdd:TIGR00606 586 INQTRDRLAKlnkELASLEQNKNHI--------NNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAm 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 305 -----NKYNGAVNEIKD-------LSDKLKAAEGKQEEIQQKGQA-------EKKELQAKIDDMEEKEQELQAKIEALQA 365
Cdd:TIGR00606 658 lagatAVYSQFITQLTDenqsccpVCQRVFQTEAELQEFISDLQSklrlapdKLKSTESELKKKEKRRDEMLGLAPGRQS 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 366 DNDFTNERLTALQEKLMvqgHLTKVVEESKLSKENQAKakesdLSDTLSPSKEKSSDDTTDAQMDEQ---DLNEPLAKVS 442
Cdd:TIGR00606 738 IIDLKEKEIPELRNKLQ---KVNRDIQRLKNDIEEQET-----LLGTIMPEEESAKVCLTDVTIMERfqmELKDVERKIA 809
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 443 LLKDDLQGTqaetEAKQDTQHLRKELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHM--D 520
Cdd:TIGR00606 810 QQAAKLQGS----DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRrqQ 885
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 521 MENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQ 600
Cdd:TIGR00606 886 FEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQ 965
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 601 LRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKenvllSSELQRQEKELHNSQKQSLELTSDLSILQMTRKEL 680
Cdd:TIGR00606 966 DGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQ-----DIDTQKIQERWLQDNLTLRKRENELKEVEEELKQH 1040
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 157819677 681 ENQMG-----SLKEQHLRDEADLKtLLSKAENQAKDVQKEYEK 718
Cdd:TIGR00606 1041 LKEMGqmqvlQMKQEHQKLEENID-LIKRNHVLALGRQKGYEK 1082
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
135-699 |
4.70e-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: 57.05 E-value: 4.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 135 ARLRSDVIHAPLpSPVDKVAANTPSMYSQELFQL----SQYLQEALHREQMLEQKLATLQRLLAItqeASDTSWQALIDE 210
Cdd:pfam15921 290 ARSQANSIQSQL-EIIQEQARNQNSMYMRQLSDLestvSQLRSELREAKRMYEDKIEELEKQLVL---ANSELTEARTER 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 211 DRLLSRLEVMGNQLQAC----SKNQTEDSLRKELVALQEDKHSYETTAKESLRRVLQEKIEVVRKLS------------E 274
Cdd:pfam15921 366 DQFSQESGNLDDQLQKLladlHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEallkamksecqgQ 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 275 VERSLSNTEDECTHLREMN------ERTQEELR----ELANKYNGAVNEIKDLSDkLKAAEGKQEEIQQKGQAEKKELQA 344
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSsltaqlESTKEMLRkvveELTAKKMTLESSERTVSD-LTASLQEKERAIEATNAEITKLRS 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 345 KIDdmeEKEQELQAkieaLQADNDFTNERLTALQEKLMVQGHLTKVVEESKLSKEN--QAKAKESDLSDTLSPSKEKSSD 422
Cdd:pfam15921 525 RVD---LKLQELQH----LKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENmtQLVGQHGRTAGAMQVEKAQLEK 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 423 DTTDAQMDEQDLNeplakvsLLKDDLQGTQAETEAKQDTQHLRK-ELVEA-QELARASKQkcfdlqalLEEERKAYRNQV 500
Cdd:pfam15921 598 EINDRRLELQEFK-------ILKDKKDAKIRELEARVSDLELEKvKLVNAgSERLRAVKD--------IKQERDQLLNEV 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 501 EESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDEillLHQAAAKAVSERDTDFMSLQEELkkvraeleG 580
Cdd:pfam15921 663 KTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSE---LEQTRNTLKSMEGSDGHAMKVAM--------G 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 581 WRKAASEYEEEIRSLQSTFQLrCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQ 660
Cdd:pfam15921 732 MQKQITAKRGQIDALQSKIQF-LEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME 810
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 157819677 661 ----KQSLELTSDLSILQmtRKELENQmgSLKEQHLRDEADLK 699
Cdd:pfam15921 811 valdKASLQFAECQDIIQ--RQEQESV--RLKLQHTLDVKELQ 849
|
|
| 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 157819677 28 IKIGRSvarcrPAQNNATFDCKVLSRNHALVWFDhKTSKFYLQDTKSSNGTFINSQRL 85
Cdd:smart00240 1 VTIGRS-----SEDCDIQLDGPSISRRHAVIVYD-GGGRFYLIDLGSTNGTFVNGKRI 52
|
|
| FHA_TCF19 |
cd22685 |
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ... |
29-119 |
5.74e-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 157819677 29 KIGRSVARCRPAQNNATFDcKVLSRNHALVWFDHKTS---KFYLQDTkSSNGTFINSQRLSRGSEEsppcEILSGDIIQF 105
Cdd:cd22685 31 RIGRNPEVCDVFLCSSQHP-NLISREHAEIHAERDGNgnwKVLIEDR-STNGTYVNDVRLQDGQRR----ELSDGDTITF 104
|
90
....*....|....*.
gi 157819677 106 G--VDVTENTRKVTHG 119
Cdd:cd22685 105 GhkNGRRVKQWPYQKS 120
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
255-641 |
6.37e-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: 6.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 255 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQK 334
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 335 GQA---EKKELQAKIDDMEEKEQELQAKIEALQADndftnERLTALQEklmVQGHLTKVVEESKlskenqakakesdlsd 411
Cdd:TIGR02169 753 IENvksELKELEARIEELEEDLHKLEEALNDLEAR-----LSHSRIPE---IQAELSKLEEEVS---------------- 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 412 tlspSKEKSSDDTtdaqmdEQDLNEPLAKVSLLKDDLQGTQAETEakqDTQHLRKELVEAQELARASKQKcfdlqalLEE 491
Cdd:TIGR02169 809 ----RIEARLREI------EQKLNRLTLEKEYLEKEIQELQEQRI---DLKEQIKSIEKEIENLNGKKEE-------LEE 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 492 ERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDtEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEE- 570
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE-ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIp 947
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 571 -----LKKVRAELEgwrkaasEYEEEIRSLQSTFQLRCQQCEvqqrEEATR---LQGELEKLKKEWDVLE---NECRSLK 639
Cdd:TIGR02169 948 eeelsLEDVQAELQ-------RVEEEIRALEPVNMLAIQEYE----EVLKRldeLKEKRAKLEEERKAILeriEEYEKKK 1016
|
..
gi 157819677 640 KE 641
Cdd:TIGR02169 1017 RE 1018
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
167-595 |
6.68e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQAcsKNQTEDSLRKELVALQED 246
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE--LEEAEEALLERLERLEEE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 247 KHSYETTAKESLRRVLQEKievvRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEG 326
Cdd:COG1196 423 LEELEEALAELEEEEEEEE----EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 327 KQEEIQQKGQAEKKelQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQEKLMVQ--GHLTKVVEESKLSKENQAKA 404
Cdd:COG1196 499 AEADYEGFLEGVKA--ALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEddEVAAAAIEYLKAAKAGRATF 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 405 KESDLSDTLSPSKEKSSDDTTDAQMD--EQDLNEPLAKVSLLKDDLQGTQAETEAKQDTQHLRKELVEAQELARASKQKC 482
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGAAVDlvASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 483 FDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDT 562
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 157819677 563 DFMSLQEELKKVRAE----------LEGWRKAASEYEEEIRSL 595
Cdd:COG1196 737 LLEELLEEEELLEEEaleelpeppdLEELERELERLEREIEAL 779
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
310-559 |
7.09e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.61 E-value: 7.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 310 AVNEIKDLSDKLKAAEGKQEEIQqkgqAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQEKLmvqghltk 389
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQ----AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 390 vveesklskenqaKAKESDLSDTLSPSKEKSSD-DTTDAQMDEQDLNEPLAKVSLLKddlQGTQAETEAKQDTQHLRKEL 468
Cdd:COG3883 82 -------------EERREELGERARALYRSGGSvSYLDVLLGSESFSDFLDRLSALS---KIADADADLLEELKADKAEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 469 VEAQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDEILL 548
Cdd:COG3883 146 EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
250
....*....|.
gi 157819677 549 LHQAAAKAVSE 559
Cdd:COG3883 226 AAAAAAAAAAA 236
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
525-757 |
7.15e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 7.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 525 QEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDtdfmSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQL--- 601
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELE----ELEAELAELEAELEELRLELEELELELEEAQAEEYElla 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 602 ---RCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRK 678
Cdd:COG1196 296 elaRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 679 ELENQMGSLKEQHL---RDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLR 755
Cdd:COG1196 376 EAEEELEELAEELLealRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
..
gi 157819677 756 EK 757
Cdd:COG1196 456 EE 457
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
161-756 |
1.43e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.12 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 161 YSQELFQLSQYLQEA--LHREQ--MLEQKLATLQRLLAITQEASDtswqALIDedrlLSRLEvmgNQLQACSKNQTEDSL 236
Cdd:pfam15921 83 YSHQVKDLQRRLNESneLHEKQkfYLRQSVIDLQTKLQEMQMERD----AMAD----IRRRE---SQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 237 RKELVA--LQEDKHSYETTAKESLRR-------VLQEKIEVVRKLSEVERSLSNTEDECT--HLREMNERTQEELRELAN 305
Cdd:pfam15921 152 HELEAAkcLKEDMLEDSNTQIEQLRKmmlshegVLQEIRSILVDFEEASGKKIYEHDSMStmHFRSLGSAISKILRELDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 306 KYNGAVNEIKDLSDKLKAAegkqeeiqqkgqaeKKELQAKIDDMEEKEQElqaKIEALQADND-----FTNERLTALQEK 380
Cdd:pfam15921 232 EISYLKGRIFPVEDQLEAL--------------KSESQNKIELLLQQHQD---RIEQLISEHEveitgLTEKASSARSQA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 381 LMVQGHLTKVVEESKlskeNQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLqgTQAETEAKQD 460
Cdd:pfam15921 295 NSIQSQLEIIQEQAR----NQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEL--TEARTERDQF 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 461 TQHLRKELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRlHMDMENLQEEKDTEISSTRDKLL 540
Cdd:pfam15921 369 SQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDR-NMEVQRLEALLKAMKSECQGQME 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 541 SAQDEILLLHQAAAKaVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQQrEEATRLQG- 619
Cdd:pfam15921 448 RQMAAIQGKNESLEK-VSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATN-AEITKLRSr 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 620 ------ELEKLKKEWDVLEN---ECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMG----S 686
Cdd:pfam15921 526 vdlklqELQHLKNEGDHLRNvqtECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINdrrlE 605
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157819677 687 LKE-QHLRDEADLKtlLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 756
Cdd:pfam15921 606 LQEfKILKDKKDAK--IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSE 674
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
464-746 |
1.95e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 464 LRKELVEAQELARASKQKcfdlqaLLEEERKAYRNQVEESAKQIQVLQVQLQRLhmdmENLQEEKDTEISSTRDKLLSAQ 543
Cdd:COG1196 218 LKEELKELEAELLLLKLR------ELEAELEELEAELEELEAELEELEAELAEL----EAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 544 DEILLLHQAAAKAVSERD---TDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQstfqlrcqqcevqqrEEATRLQGE 620
Cdd:COG1196 288 AEEYELLAELARLEQDIArleERRRELEERLEELEEELAELEEELEELEEELEELE---------------EELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 621 LEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLKT 700
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 157819677 701 LLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 746
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
267-757 |
2.30e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.64 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 267 EVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKI 346
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 347 DDMEEKEQE---LQAKIEALQADNDFTNERLTALQEKLMVQGH----LTKVVEESKLSK---ENQAKAKESDLSDT---- 412
Cdd:TIGR04523 117 EQKNKLEVElnkLEKQKKENKKNIDKFLTEIKKKEKELEKLNNkyndLKKQKEELENELnllEKEKLNIQKNIDKIknkl 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 413 ------LSPSKEKSSDDTTdaqmDEQDLNEPLAKVSLLKDDLQgtqaetEAKQDTQHLRKELVEAQELARASKQKCFDLQ 486
Cdd:TIGR04523 197 lklellLSNLKKKIQKNKS----LESQISELKKQNNQLKDNIE------KKQQEINEKTTEISNTQTQLNQLKDEQNKIK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 487 ALLEEERKayrnQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDEILllhQAAAKAVSERDTDFMS 566
Cdd:TIGR04523 267 KQLSEKQK----ELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKL---EEIQNQISQNNKIISQ 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 567 LQEELKKVRAELEGWRKAASEYEEEIRSLQstfqlrcQQCEVQQREEATRLQgELEKLKKEWDVLENECRSLKKENVLLS 646
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELEEKQ-------NEIEKLKKENQSYKQ-EIKNLESQINDLESKIQNQEKLNQQKD 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 647 SELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHlrdeADLKTLLSKAENQAKDVQKEYEKTQTVLSEL 726
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELII----KNLDNTRESLETQLKVLSRSINKIKQNLEQK 487
|
490 500 510
....*....|....*....|....*....|.
gi 157819677 727 KLKFEMTEQEKQSITDELKQCKDNLKLLREK 757
Cdd:TIGR04523 488 QKELKSKEKELKKLNEEKKELEEKVKDLTKK 518
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
235-681 |
5.76e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 5.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 235 SLRKELVALQEDKHSYETTAKEsLRRVLQEKIEVVRKLSEVER---SLSNTEDECTHLREMNERTQEELRELANKYNGAV 311
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRE-LEERIEELKKEIEELEEKVKelkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 312 NEIKDLSDKLKAAEGKQEEIQqKGQAEKKELQAKIDDMEEKEQELQaKIEALQADNDFTNERLTAL------QEKLMVQG 385
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLtpekleKELEELEK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 386 HLTKVVEESK--LSKENQAKAKESDLSDTLSPSKE-KSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQdtQ 462
Cdd:PRK03918 399 AKEEIEEEISkiTARIGELKKEIKELKKAIEELKKaKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKE--R 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 463 HLRKELVEAQ-ELARASK----QKCFDLQALLEEERKAYR-NQVEESAKQIQVLQVQLQRLHMDMENLQEE--KDTEISS 534
Cdd:PRK03918 477 KLRKELRELEkVLKKESEliklKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKEleKLEELKK 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 535 TRDKLLSAQDEIL-----LLHQAAAKAVSERDTDFMSLQEeLKKVRAELEGWRKAASEYEEEIRSLQStfqlrCQQCEVQ 609
Cdd:PRK03918 557 KLAELEKKLDELEeelaeLLKELEELGFESVEELEERLKE-LEPFYNEYLELKDAEKELEREEKELKK-----LEEELDK 630
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157819677 610 QREEATRLQGELEKLKKEWDVL-----ENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELE 681
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELekkysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
449-752 |
7.08e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 449 QGTQAETEAKQDTQHLRKELVEAQELARASKQKCFDLQA---LLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQ 525
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEdlsSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 526 EEKDTEISSTRDKLLSAQDEIlllhqaaakaVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQ 605
Cdd:TIGR02169 786 ARLSHSRIPEIQAELSKLEEE----------VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 606 CEVQQREEAtRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMG 685
Cdd:TIGR02169 856 IENLNGKKE-ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 686 SLKEQHLRDEADLKTLLS----KAENQAKDVQ------------KEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCkD 749
Cdd:TIGR02169 935 EIEDPKGEDEEIPEEELSledvQAELQRVEEEiralepvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY-E 1013
|
...
gi 157819677 750 NLK 752
Cdd:TIGR02169 1014 KKK 1016
|
|
| 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 157819677 27 PIKIGRSVARcRPAQNNATFDC-----KVLSRNHALVWFDHKTSKFYLQdTKSSNGTFINSQRLSRGseeSPPCEILSGD 101
Cdd:cd22701 18 EVVLGRNSKN-SSSTAADSVDIdlgpsKKISRRHARIFYDFTTQCFELS-VLGRNGVKVDGILVKPG---SPPVPLRSGS 92
|
....*
gi 157819677 102 IIQFG 106
Cdd:cd22701 93 LIQIG 97
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
152-601 |
1.47e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 152 KVAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDtswqaliDEDRLLSRLEVMGNQLQACSKNQ 231
Cdd:COG4717 60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA-------ELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 232 TEDSLRKELVALQEdkhsyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDEC-THLREMNERTQEELRELANKYNGA 310
Cdd:COG4717 133 ELEALEAELAELPE--------RLEELEERLEELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 311 VNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEAL------QADNDFTNERLTALQEKLMVQ 384
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAAllallgLGGSLLSLILTIAGVLFLVLG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 385 GHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLnEPLAKVSLLKDDLQGTQAETEAKQDTQHL 464
Cdd:COG4717 285 LLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDL-SPEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 465 RKELVEAQELARASKQKCFDLQALLE--EERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEK-DTEISSTRDKLLS 541
Cdd:COG4717 364 QLEELEQEIAALLAEAGVEDEEELRAalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEElEEELEELEEELEE 443
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 542 AQDEILLLHQAAAKAVSERDTdfMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQL 601
Cdd:COG4717 444 LEEELEELREELAELEAELEQ--LEEDGELAELLQELEELKAELRELAEEWAALKLALEL 501
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
25-114 |
1.77e-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: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 25 DEPIKIGRSVArcrpAQNNATFDC-KVLSRNHALVWFDHKTSKFyLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDII 103
Cdd:cd22663 20 GKEVTVGRGLG----VTYQLVSTCpLMISRNHCVLKKNDEGQWT-IKDNKSLNGVWVNGERI----EPLKPYPLNEGDLI 90
|
90
....*....|.
gi 157819677 104 QFGVDVTENTR 114
Cdd:cd22663 91 QLGVPPENKEP 101
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
26-106 |
1.79e-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: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 26 EPIKIGRSVArcrpaqNNATFDCKVLSRNHALVwfDHKTSKFYLQDTKSSNGTFINSQRLSRGseesppcEILSGDIIQF 105
Cdd:cd22698 21 DEFTIGRSSN------NDIRLNDHSVSRHHARI--VRQGDKCNLTDLGSTNGTFLNGIRVGTH-------ELKHGDRIQL 85
|
.
gi 157819677 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 157819677 27 PIKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLsrgSEESPPCEILSGDIIQFG 106
Cdd:cd22678 24 PLTIGRIQ------RGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESI---SPNGRPVVLSSGDVITLG 94
|
90
....*....|.
gi 157819677 107 vdvTENTRKVT 117
Cdd:cd22678 95 ---SETKILVR 102
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
55-108 |
3.52e-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: 3.52e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 157819677 55 HALVWFDHKTSKFYLQDTKSSNGTFINSQRLSrgseESPPCEILSGDIIQFGVD 108
Cdd:cd22704 39 HAVITYDQIDNEFKIKDLGSLNGTFVNDSRIP----EQTYITLKLGDSIRFGYD 88
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
434-757 |
5.99e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.74 E-value: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 434 LNEPLAKVSLLKDDLQGTQAETEAKQDTQHLRKElveAQELARaskqkcfdlqallEEERkayRNQVEESAKQIQVLQVQ 513
Cdd:pfam17380 271 LNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQE---KEEKAR-------------EVER---RRKLEEAEKARQAEMDR 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 514 LQRLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELK--KVRAELEGWRKAASEYEEE 591
Cdd:pfam17380 332 QAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKneRVRQELEAARKVKILEEER 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 592 IRSLQStfQLRCQQCEVQQREEATrlQGELEKLKKEwdvLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDls 671
Cdd:pfam17380 412 QRKIQQ--QKVEMEQIRAEQEEAR--QREVRRLEEE---RAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE-- 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 672 ilQMTRKELENQMGSLKEQHLRDEadlKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQ-EKQSITDELKQCKDN 750
Cdd:pfam17380 483 --KRDRKRAEEQRRKILEKELEER---KQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEErRKQQEMEERRRIQEQ 557
|
....*..
gi 157819677 751 LKLLREK 757
Cdd:pfam17380 558 MRKATEE 564
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
564-757 |
8.22e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 8.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 564 FMSLQEELKKVRAELegWRKAASEYEEEIRSLQSTFQLRCQQCEVQQREEATrLQGELEKLKKEWDVLENECRSLKKENV 643
Cdd:COG1196 215 YRELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAE-LEAELEELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 644 LLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQhlrdEADLKTLLSKAENQAKDVQKEYEKTQTVL 723
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE----LEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190
....*....|....*....|....*....|....
gi 157819677 724 SELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 757
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
567-757 |
9.51e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 9.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 567 LQEELKKVRAELEGWRKAASEYeeeiRSLQSTFQLRCQQCEVQQREEatrLQGELEKLKKEWDVLENECRSLKKENVLLS 646
Cdd:COG1196 194 ILGELERQLEPLERQAEKAERY----RELKEELKELEAELLLLKLRE---LEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 647 SELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTLlskaENQAKDVQKEYEKTQTVLSEL 726
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL----EEELAELEEELEELEEELEEL 342
|
170 180 190
....*....|....*....|....*....|.
gi 157819677 727 KLKFEMTEQEKQSITDELKQCKDNLKLLREK 757
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
178-365 |
1.09e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 178 REQML--EQKLATLQRLLAITQEAsDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKELVALQEDKhsyetTAK 255
Cdd:COG4913 241 HEALEdaREQIELLEPIRELAERY-AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAEL-----ERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 256 ESLRRVLQEKIEVVR---------KLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEG 326
Cdd:COG4913 315 EARLDALREELDELEaqirgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE 394
|
170 180 190
....*....|....*....|....*....|....*....
gi 157819677 327 KQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQA 365
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
210-502 |
1.27e-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: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 210 EDRLLSRLEVMGNQLQacsKNQTEDSLRKELVALQEDKHSYETTAK--------ESLRRVLQEKIEVVRKLSEVERSLSN 281
Cdd:TIGR02169 186 IERLDLIIDEKRQQLE---RLRREREKAERYQALLKEKREYEGYELlkekealeRQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 282 TEDECTH----LREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQ 357
Cdd:TIGR02169 263 LEKRLEEieqlLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 358 AKIEALQADNDFTNERLTALQEKLMV-QGHLTKVVEESKLSKENQAKAKE--SDLSDTLSPSKEKSSDDTTDAQMDEQDL 434
Cdd:TIGR02169 343 REIEEERKRRDKLTEEYAELKEELEDlRAELEEVDKEFAETRDELKDYREklEKLKREINELKRELDRLQEELQRLSEEL 422
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157819677 435 NEPLAKVSLLKDDLQGTQAETEAKQD-TQHLRKELVEAQELARASKQKCFDLQA---LLEEERKAYRNQVEE 502
Cdd:TIGR02169 423 ADLNAAIAGIEAKINELEEEKEDKALeIKKQEWKLEQLAADLSKYEQELYDLKEeydRVEKELSKLQRELAE 494
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
229-760 |
1.50e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.56 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 229 KNQTEDSLRKELVALQEDKHSYETTAK---------ESLRRVLQEKIEVVRKLSEVERSlsnTEDECTHLREMNERTQEE 299
Cdd:pfam05483 94 KVSIEAELKQKENKLQENRKIIEAQRKaiqelqfenEKVSLKLEEEIQENKDLIKENNA---TRHLCNLLKETCARSAEK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 300 LRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAkiEALQADNDFTNErltalqe 379
Cdd:pfam05483 171 TKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEE--EYKKEINDKEKQ------- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 380 klmVQGHLTKVVEesklsKENQAKakesDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQ 459
Cdd:pfam05483 242 ---VSLLLIQITE-----KENKMK----DLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSM 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 460 DTQHLRKElveaqELARASKQKCfdlqaLLEEERKAyrnQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEisstRDKL 539
Cdd:pfam05483 310 STQKALEE-----DLQIATKTIC-----QLTEEKEA---QMEELNKAKAAHSFVVTEFEATTCSLEELLRTE----QQRL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 540 LSAQDEILLLHQAAAKAVSERD--TDFMSLQE----ELKKVRAELEGWRKAASEYEEEIRSLQSTFQlrcqqcevqqree 613
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSSELEemTKFKNNKEveleELKKILAEDEKLLDEKKQFEKIAEELKGKEQ------------- 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 614 atRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSL------ 687
Cdd:pfam05483 440 --ELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMtlelkk 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 688 --------KEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREKGN 759
Cdd:pfam05483 518 hqediincKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCN 597
|
.
gi 157819677 760 N 760
Cdd:pfam05483 598 N 598
|
|
| 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 157819677 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 157819677 51 LSRNHALVWF----DHKTSKFYLQDTKSSNGTFINSQRLsrgseesPP---CEILSGDIIQFG 106
Cdd:cd22677 41 ISRYHAVLQYrgdaDDHDGGFYLYDLGSTHGTFLNKQRI-------PPkqyYRLRVGHVLKFG 96
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
28-106 |
2.74e-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: 2.74e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157819677 28 IKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDhkTSKFYLQDTKSSNGTFINSQRlsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22680 23 VSIGRDP------ENVIVIPDPFVSRNHARITVD--SNEIYIEDLGSTNGTFVNDFK-----RIKGPAKLHPNDIIKLG 88
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
14-106 |
2.79e-05 |
|
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.
Pssm-ID: 438734 [Multi-domain] Cd Length: 96 Bit Score: 43.67 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 14 SHPFQERHvyldepIKIGRSVarcrpaQNNATFDCKVLSRNHALvwFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEesp 93
Cdd:cd22682 14 QFPITEST------IVIGRSV------ESQVQIDDDSVSRYHAK--LAVNPSAVSIIDLGSTNGTIVNGKKIPKLAS--- 76
|
90
....*....|...
gi 157819677 94 pCEILSGDIIQFG 106
Cdd:cd22682 77 -CDLQNGDQIKIG 88
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
153-381 |
2.91e-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: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 153 VAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgNQLQAcsKNQT 232
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE---QELAA--LEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 233 EDSLRKELVALQEDKhsyettakESLRRVLQEKIEVVRKLSEVER--SLSNTEDECTHLR--EMNERTQEELRELANKYN 308
Cdd:COG4942 85 LAELEKEIAELRAEL--------EAQKEELAELLRALYRLGRQPPlaLLLSPEDFLDAVRrlQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157819677 309 GAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQEKL 381
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| 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 157819677 12 PNSHPfqerHVYL-DEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTSKF---YLQDTkSSNGTFINSQRLSR 87
Cdd:cd22690 8 NPSYP----DIELtQNTTFIGRS------KDCDEEITDPRISKHHCIITRKRSGKGLddvYVTDT-STNGTFINNNRLGK 76
|
90
....*....|....*.
gi 157819677 88 GSEesppCEILSGDII 103
Cdd:cd22690 77 GSQ----SLLQDGDEI 88
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
236-502 |
3.30e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 236 LRKELVALQEDKHSYETTAK--ESLRRVLQEKIEVVRKLSEVERSLSNTEDecthLREMNERTQEELRELANkyngAVNE 313
Cdd:COG4913 615 LEAELAELEEELAEAEERLEalEAELDALQERREALQRLAEYSWDEIDVAS----AEREIAELEAELERLDA----SSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 314 IKDLSDKLKAAEGKQEEIQQKGQA---EKKELQAKIDDMEEKEQELQAKIEALQAD-NDFTNERLTALQEKLMVQGHLTK 389
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDElkgEIGRLEKELEQAEEELDELQDRLEAAEDLaRLELRALLEERFAAALGDAVERE 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 390 VVE--ESKLSKENQAKAK-ESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDlqgtqaeteakqdtqhlrk 466
Cdd:COG4913 767 LREnlEERIDALRARLNRaEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEED------------------- 827
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 157819677 467 ELVEAQE-----LARASKQKCFDLQALLEEERKAYRNQVEE 502
Cdd:COG4913 828 GLPEYEErfkelLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
182-684 |
3.63e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 182 LEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgnqlqacSKNQTEDSLRKELVALQEDKHSYETTaKESLRRV 261
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHE---------ERREELETLEAEIEDLRETIAETERE-REELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 262 LQEKIEVVRKLSE------VERSLSNTEDECTHLR-----EMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEGKQEE 330
Cdd:PRK02224 281 VRDLRERLEELEEerddllAEAGLDDADAEAVEARreeleDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 331 IQQKGQAEKKELQA---KIDDMEEKEQELQAKIEALQADNDFTNERLTALQEKLmvqghltkvveESKLSKENQAKAKES 407
Cdd:PRK02224 361 LREEAAELESELEEareAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL-----------EELREERDELREREA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 408 DLSDTLS------------------PSKEKSSDDTTDAQMDEQDlNEPLAKVSLLKDDLQGTQAETEAKQDTQhlrKELV 469
Cdd:PRK02224 430 ELEATLRtarerveeaealleagkcPECGQPVEGSPHVETIEED-RERVEELEAELEDLEEEVEEVEERLERA---EDLV 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 470 EAQELARASKQKCFDLQALLEEErkayRNQVEESAKQIQVLQVQLQRLHMDMENLQE---EKDTEISSTRDKLLSAQDEI 546
Cdd:PRK02224 506 EAEDRIERLEERREDLEELIAER----RETIEEKRERAEELRERAAELEAEAEEKREaaaEAEEEAEEAREEVAELNSKL 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 547 LLLHQA--AAKAVSERDTDFMSLQEELKKVRAELEGW-------RKAASEYEEEIRSLQSTFQLRCQQCEVQQREEAT-- 615
Cdd:PRK02224 582 AELKERieSLERIRTLLAAIADAEDEIERLREKREALaelnderRERLAEKRERKRELEAEFDEARIEEAREDKERAEey 661
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157819677 616 --RLQGELEKLKKEWDVLENECRSLkkENVLLSSELQRQEKELHNSQKQSLE-LTSDLSILQMTRKELENQM 684
Cdd:PRK02224 662 leQVEEKLDELREERDDLQAEIGAV--ENELEELEELRERREALENRVEALEaLYDEAEELESMYGDLRAEL 731
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
245-742 |
3.94e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.41 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 245 EDKHSYETTAKES-LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKA 323
Cdd:pfam05483 228 EEEYKKEINDKEKqVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 324 AEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQEKLMV-QGHLTKVVEESKL-SKENQ 401
Cdd:pfam05483 308 SMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTeQQRLEKNEDQLKIiTMELQ 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 402 AKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQDTQHLRKELVEAQELARASKQK 481
Cdd:pfam05483 388 KKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 482 cfdlqalleeerkAYRNQVEEsakqiqvlqvqlqrLHMDMENlQEEKDTEISSTRDKLLSAQDEILLLHQAAAKAVSERD 561
Cdd:pfam05483 468 -------------HYLKEVED--------------LKTELEK-EKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQ 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 562 TDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQ--CEVQQREEATR-LQGELEKLKKEWDVLENECRSL 638
Cdd:pfam05483 520 EDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEvkCKLDKSEENARsIEYEVLKKEKQMKILENKCNNL 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 639 KKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTLLSKAENQAKDVQKEYEK 718
Cdd:pfam05483 600 KKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEK 679
|
490 500
....*....|....*....|....*
gi 157819677 719 TQTVLSE-LKLKFEMTEQEKQSITD 742
Cdd:pfam05483 680 AKAIADEaVKLQKEIDKRCQHKIAE 704
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
546-757 |
5.84e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 546 ILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQStfQLRCQQCEVQQRE-EATRLQGELEKL 624
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER--RIAALARRIRALEqELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 625 KKEWDVLENECRSLKKE-----------------NVLLSSE-LQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGS 686
Cdd:COG4942 89 EKEIAELRAELEAQKEElaellralyrlgrqpplALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157819677 687 LKEQHlrdeADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 757
Cdd:COG4942 169 LEAER----AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
329-627 |
6.08e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 329 EEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQadndftnERLTALQeKLMVQGHLTKVveesklskenqakakesd 408
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAK-------EGLSALN-RLLPRLNLLAD------------------ 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 409 lsDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEakqDTQHLRKELVEAQELARASKQKCFDLQAL 488
Cdd:PRK04863 890 --ETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPE---QFEQLKQDYQQAQQTQRDAKQQAFALTEV 964
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 489 LeeERKAYRNqVEESAKQIQVLQVQLQRLHMDMENLQEEKDTeissTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQ 568
Cdd:PRK04863 965 V--QRRAHFS-YEDAAEMLAKNSDLNEKLRQRLEQAEQERTR----AREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQ 1037
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157819677 569 E---ELKK--VRAElEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQ---QREEATRLQGELEKLKKE 627
Cdd:PRK04863 1038 ElkqELQDlgVPAD-SGAEERARARRDELHARLSANRSRRNQLEKQltfCEAEMDNLTKKLRKLERD 1103
|
|
| 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 157819677 13 NSHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTskFYLQDTKSSNGTFINSQRLSrgsee 91
Cdd:cd22665 7 SQAHGPEKDFPLYEgENVIGRD------PSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRL----- 73
|
90 100
....*....|....*....|.
gi 157819677 92 SPPC--EILSGDIIQFGvDVT 110
Cdd:cd22665 74 KPNVryELIDGDLLLFG-DVK 93
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
162-735 |
7.00e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.35 E-value: 7.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 162 SQELFQLSQYLQEALHR----EQMLEQKLATLQRLLAITQEASDTSWQALIDEDRllsRLEVMGNQLQACSKNQTEDSLR 237
Cdd:pfam10174 129 AKELFLLRKTLEEMELRietqKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWER---TRRIAEAEMQLGHLEVLLDQKE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 238 KELVALQEDKHS-YETTAKESLRRVLQEKIEVV-RKLSEVERSLSNTEDECTHLREMNERTQEELRELANKyngaVNEIK 315
Cdd:pfam10174 206 KENIHLREELHRrNQLQPDPAKTKALQTVIEMKdTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQ----MEVYK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 316 DLSDKLKAaegKQEEIQQKGQAEKKELQAkiddmeekeqeLQAKIEALQADNDFTNERLTALQEKLMVQGHLTKVVEESK 395
Cdd:pfam10174 282 SHSKFMKN---KIDQLKQELSKKESELLA-----------LQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 396 LSKENQAKAKESDL---SDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKqDTQ--HLRKELVE 470
Cdd:pfam10174 348 DALRLRLEEKESFLnkkTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDK-DKQlaGLKERVKS 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 471 AQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDteiSSTRDKLLSAQDEILLLH 550
Cdd:pfam10174 427 LQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVS---ALQPELTEKESSLIDLKE 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 551 QAAAKAVS--ERDTDFMSLQEELKKVRAE---LEGWRKAASEYEEEIR-SLQSTFQLRCQQCEVQQ-REEATRLQGELEK 623
Cdd:pfam10174 504 HASSLASSglKKDSKLKSLEIAVEQKKEEcskLENQLKKAHNAEEAVRtNPEINDRIRLLEQEVARyKEESGKAQAEVER 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 624 LKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQsleltsdlsiLQMTRKELENQMGSLKEQHLRDEADLKTllS 703
Cdd:pfam10174 584 LLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVAN----------IKHGQQEMKKKGAQLLEEARRREDNLAD--N 651
|
570 580 590
....*....|....*....|....*....|..
gi 157819677 704 KAENQAKDVQKEYEKTQTVLSELKLKFEMTEQ 735
Cdd:pfam10174 652 SQQLQLEELMGALEKTRQELDATKARLSSTQQ 683
|
|
| 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 157819677 52 SRNHALVWFDH---------KTSKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQFGV 107
Cdd:cd22667 40 SRKHATLTVLHpeanlsdpdTRPELTLKDL-SKYGTFVNGEKLKGGSE----VTLKDGDVITFGV 99
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
234-641 |
7.45e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 234 DSLRKELVALQEDKHSYETtAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNER--TQEELRELANKYNGAV 311
Cdd:COG4717 74 KELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELeaLEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 312 NEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQEKLMVQGHLTKVV 391
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 392 EESKLSKENQAKAKESDLS----------DTLSPSKEKSSDDTTDAQMdeqdLNEPLAKVSLLKDDLQGTQAETEAKQDT 461
Cdd:COG4717 233 ENELEAAALEERLKEARLLlliaaallalLGLGGSLLSLILTIAGVLF----LVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 462 QHLRKELVEAQELARASKQKCFDLQALLEEERKAYRNQVEesaKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLS 541
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE---LQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 542 AQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAEL-----EGWRKAASEYEEEIRSLQSTF-QLRCQQCEVQQREEAT 615
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLealdeEELEEELEELEEELEELEEELeELREELAELEAELEQL 465
|
410 420
....*....|....*....|....*.
gi 157819677 616 RLQGELEKLKKEWDVLENECRSLKKE 641
Cdd:COG4717 466 EEDGELAELLQELEELKAELRELAEE 491
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
520-759 |
7.63e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 7.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 520 DMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKaVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQStf 599
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEK-LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE-- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 600 QLRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRK- 678
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKk 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 679 --ELENQMGSLKEQHLRDEaDLKTLLSKAENQAKdvqkeyEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 756
Cdd:PRK03918 347 lkELEKRLEELEERHELYE-EAKAKKEELERLKK------RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
...
gi 157819677 757 KGN 759
Cdd:PRK03918 420 EIK 422
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
297-527 |
8.88e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 297 QEELRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQkgqaEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTA 376
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK----QLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 377 LQEKLMVQGHltkvvEESKLSKENQAKAKESDLSDTLSPskekssDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETE 456
Cdd:COG4942 95 LRAELEAQKE-----ELAELLRALYRLGRQPPLALLLSP------EDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157819677 457 AkqdtqhLRKELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEE 527
Cdd:COG4942 164 A------LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
534-730 |
1.01e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 534 STRDKLLSAQDEILLLHQAAAKAVSERDTdfmsLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQcevQQREE 613
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEA----LEAELDALQERREALQRLAEYSWDEIDVASAEREIAELE---AELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 614 ATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLR 693
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
|
170 180 190
....*....|....*....|....*....|....*..
gi 157819677 694 DEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKF 730
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRAEEELERAMRAF 796
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
232-754 |
1.09e-04 |
|
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: 45.88 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 232 TEDSLRKELVALQEDKHSYETTAKE--SLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLR-EMNERTQ---------EE 299
Cdd:pfam15921 494 SERTVSDLTASLQEKERAIEATNAEitKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKlQMAEKDKvieilrqqiEN 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 300 LRELANKYNGAVNEIKDLSDKL-KAAEGKQEEIQQ------KGQAEKKELQAKIDDME-EKEQELQAKIEALQADNDFTN 371
Cdd:pfam15921 574 MTQLVGQHGRTAGAMQVEKAQLeKEINDRRLELQEfkilkdKKDAKIRELEARVSDLElEKVKLVNAGSERLRAVKDIKQ 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 372 ERLTALQEKLMVQGHLTKVVEESKLSKEN-----------------QAKAKESDLSDTLSPSKEKSSDDTTDAQMD---E 431
Cdd:pfam15921 654 ERDQLLNEVKTSRNELNSLSEDYEVLKRNfrnkseemetttnklkmQLKSAQSELEQTRNTLKSMEGSDGHAMKVAmgmQ 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 432 QDLNEPLAKVSLLKDDLQG-TQAETEAKQDTQHLRKELVE-AQELARASKQK---CFDLQALLEEERKAYRN-------- 498
Cdd:pfam15921 734 KQITAKRGQIDALQSKIQFlEEAMTNANKEKHFLKEEKNKlSQELSTVATEKnkmAGELEVLRSQERRLKEKvanmeval 813
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 499 -----QVEESAKQIQVLQVQLQRLHM----DMENLQEEKDTEISSTRDKLL-------------SAQDEILLL--HQAAA 554
Cdd:pfam15921 814 dkaslQFAECQDIIQRQEQESVRLKLqhtlDVKELQGPGYTSNSSMKPRLLqpasftrthsnvpSSQSTASFLshHSRKT 893
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 555 KAVSERDT-DFMSLQEELKKV----------RAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQQREEATRLQGELEK 623
Cdd:pfam15921 894 NALKEDPTrDLKQLLQELRSVineeptvqlsKAEDKGRAPSLGALDDRVRDCIIESSLRSDICHSSSNSLQTEGSKSSET 973
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 624 LKKE-----WDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSlELTSDLSILQMTRKELENQMGSLKEQHLRDEA-D 697
Cdd:pfam15921 974 CSREpvllhAGELEDPSSCFTFPSTASPSVKNSASRSFHSSPKKS-PVHSLLTSSAEGSIGSSSQYRSAKTIHSPDSVkD 1052
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 157819677 698 LKTL-LSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLL 754
Cdd:pfam15921 1053 SQSLpIETTGKTCRKLQNRLESLQTLVEDLQLKNQAMSSMIRNQEKRIQKVKDQEKML 1110
|
|
| 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 157819677 18 QERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhkTSKFYLQDTKSSNGTFINSQRLS 86
Cdd:cd22694 8 GELRFDPGSSVRIGRD------PDADVRLDDPRVSRRHALLEFD--GDGWVYTDLGSRNGTYLNGRRVQ 68
|
|
| FHA_CHFR |
cd22672 |
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ... |
49-105 |
1.47e-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: 41.89 E-value: 1.47e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 157819677 49 KVLSRNHALVWFDHKTsKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQF 105
Cdd:cd22672 39 KLVSGDHCKIIRDEKG-QVWLEDT-STNGTLVNKVKVVKGQK----VELKHGDVIYL 89
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
552-746 |
1.74e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 552 AAAKAVSERDTDFMSLQEELKKVRAE---LEGWRKAASEYEE------EIRSLQSTFQL--------RCQQCEVQQREEA 614
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQielLEPIRELAERYAAarerlaELEYLRAALRLwfaqrrleLLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 615 TRLQGELEKLKKEWDVLENECRSLKKE------NVL--LSSELQRQEKELHNsqkqsleltsdlsiLQMTRKELENQMGS 686
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQirgnggDRLeqLEREIERLERELEE--------------RERRRARLEALLAA 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 687 LKEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 746
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
166-746 |
1.77e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.34 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 166 FQLSQYLQEALHREQMLEQKLATLQRLLAitQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTED--SLRKELVAL 243
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVK--QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQqhTLTQHIHTL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 244 QEDKhsyeTTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLsdklKA 323
Cdd:TIGR00618 385 QQQK----TTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCE----KL 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 324 AEGKQEEIQQKGQAEKKELQAK--IDDMEEKEQELQAKIEALQADNDFTNERLTALQEKLMVQGHLTKVVEESKLSKENQ 401
Cdd:TIGR00618 457 EKIHLQESAQSLKEREQQLQTKeqIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQT 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 402 AKAKESDLSDT---LSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQD-----TQHLRKELVEAQE 473
Cdd:TIGR00618 537 YAQLETSEEDVyhqLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDlteklSEAEDMLACEQHA 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 474 LARASKQKCFDLQALLEEERKAYRNQVEESAkqiqvlqvqlqrLHMDMENLQEEKDTEISstrdkLLSAQDEILLLHQAA 553
Cdd:TIGR00618 617 LLRKLQPEQDLQDVRLHLQQCSQELALKLTA------------LHALQLTLTQERVREHA-----LSIRVLPKELLASRQ 679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 554 AKAVSERdtdfmSLQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQQREeatrLQGELEKLKKEWDVLEN 633
Cdd:TIGR00618 680 LALQKMQ-----SEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSD----LAAREDALNQSLKELMH 750
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 634 ECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHlrdEADLKTLLSKAENQAKDVQ 713
Cdd:TIGR00618 751 QARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEI---GQEIPSDEDILNLQCETLV 827
|
570 580 590
....*....|....*....|....*....|...
gi 157819677 714 KEYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 746
Cdd:TIGR00618 828 QEEEQFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
316-739 |
1.92e-04 |
|
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: 45.12 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 316 DLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDdmeeKEQELQAKIEALQADNdftNERLTALQEKLMVQGHLTKVvEESK 395
Cdd:pfam05557 17 EKKQMELEHKRARIELEKKASALKRQLDRESD----RNQELQKRIRLLEKRE---AEAEEALREQAELNRLKKKY-LEAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 396 LSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETeakQDTQHLRKELVEAQELA 475
Cdd:pfam05557 89 NKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKA---SEAEQLRQNLEKQQSSL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 476 RASKQKCFDLQalleeerkaYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISstrdKLLSAQDEILLLHQAAA- 554
Cdd:pfam05557 166 AEAEQRIKELE---------FEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNK----HLNENIENKLLLKEEVEd 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 555 -KAVSERDTDFM----SLQEELKKVRAELEGWRKAASEYEEEIRS--LQSTFQLRCQQCEVQQREEATRLQGELEKLKKE 627
Cdd:pfam05557 233 lKRKLEREEKYReeaaTLELEKEKLEQELQSWVKLAQDTGLNLRSpeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 628 WDVLENECRSLKKENVLLSSELQRQEKELHNSQKQSLELTSDL----SILQMTRKELENQMGSlkEQHLRDEADLKTLLS 703
Cdd:pfam05557 313 RRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgyrAILESYDKELTMSNYS--PQLLERIEEAEDMTQ 390
|
410 420 430
....*....|....*....|....*....|....*.
gi 157819677 704 KAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 739
Cdd:pfam05557 391 KMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQA 426
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
546-756 |
2.50e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 546 ILLLHQAAAKAVSERDtdfmSLQEELKKVRAELEGWRKAASEYEEEIRSLQStfQLRcqqcevQQREEATRLQGELEKLK 625
Cdd:COG4942 8 ALLLALAAAAQADAAA----EAEAELEQLQQEIAELEKELAALKKEEKALLK--QLA------ALERRIAALARRIRALE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 626 KEWDVLENECRSLKKENVLLSSELQRQEKELHN------------------SQKQSLELTSDLSILQMTRKELENQMGSL 687
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEELAEllralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157819677 688 KEQhLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMT----EQEKQSITDELKQCKDNLKLLRE 756
Cdd:COG4942 156 RAD-LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLlarlEKELAELAAELAELQQEAEELEA 227
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
300-428 |
3.07e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 300 LRELANKYNGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQE 379
Cdd:COG3883 124 LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 157819677 380 KLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQ 428
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
451-690 |
3.11e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 451 TQAETEAKQDTQHLRKELVEAQELARASKQKcfdlQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEekdt 530
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 531 EISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQstfqlrcqqcevQQ 610
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR------------AD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 611 REEATRLQGELEKLKKEWDVLENEcrsLKKENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQ 690
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAE---LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
231-754 |
3.30e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.44 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 231 QTEDSLRKELVALQEDKHSYETTAKEslRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEEL-RELANKYNG 309
Cdd:pfam12128 353 QSELENLEERLKALTGKHQDVTAKYN--RRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALeSELREQLEA 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 310 AVNEIKDLSDKLKAAEGKQEEIQQKGQAEKKEL------QAKIDDMEEKEQELQAKIEALQAD----------------- 366
Cdd:pfam12128 431 GKLEFNEEEYRLKSRLGELKLRLNQATATPELLlqlenfDERIERAREEQEAANAEVERLQSElrqarkrrdqasealrq 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 367 -NDFTNERLTALQE---------------------------------KLMVQGHLTKVVEESKLSKEN----------QA 402
Cdd:pfam12128 511 aSRRLEERQSALDElelqlfpqagtllhflrkeapdweqsigkvispELLHRTDLDPEVWDGSVGGELnlygvkldlkRI 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 403 KAKES-DLSDTLSPSKEKSSDDTTDAQMDEQDLNEPL--AKVSLLKDDLQGTQAETEAKQDTQHLRKELVEAQELARASK 479
Cdd:pfam12128 591 DVPEWaASEEELRERLDKAEEALQSAREKQAAAEEQLvqANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKN 670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 480 QKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAKA--- 556
Cdd:pfam12128 671 KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAelk 750
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 557 --VSERDTDFMS----------LQEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQQRE---EATRLQGEL 621
Cdd:pfam12128 751 alETWYKRDLASlgvdpdviakLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNierAISELQQQL 830
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 622 EKLKKEwdvlenecrslkkenvllsSELQRQ--EKELHNSQKQSLELTSDLSILqmtrKELENQMGSLKEQHLRDEAD-- 697
Cdd:pfam12128 831 ARLIAD-------------------TKLRRAklEMERKASEKQQVRLSENLRGL----RCEMSKLATLKEDANSEQAQgs 887
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157819677 698 -------LKTLLSKAENQAKDVQKEYEKTQTVL-----SELKLKFEMTEQEKQSITDELKQCKDNLKLL 754
Cdd:pfam12128 888 igerlaqLEDLKLKRDYLSESVKKYVEHFKNVIadhsgSGLAETWESLREEDHYQNDKGIRLLDYRKLV 956
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
229-757 |
4.66e-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: 43.81 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 229 KNQTEDSLRKELVALQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYN 308
Cdd:pfam02463 216 KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEE 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 309 GAVNEIKDLSDKLK-AAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQEL---QAKIEALQADNDFTNERLTAL---QEKL 381
Cdd:pfam02463 296 EELKSELLKLERRKvDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELkelEIKREAEEEEEEELEKLQEKLeqlEEEL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 382 MVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQDT 461
Cdd:pfam02463 376 LAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 462 QHLRK------------ELVEAQELARASKQKCFDLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEK- 528
Cdd:pfam02463 456 QELKLlkdelelkksedLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLg 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 529 ------DTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAEL----EGWRKAASEYEEEIRSLQST 598
Cdd:pfam02463 536 vavenyKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLksiaVLEIDPILNLAQLDKATLEA 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 599 FQLRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVllSSELQRQEKELHNSQKQSLELTSDLSILQMTRK 678
Cdd:pfam02463 616 DEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAE--KSEVKASLSELTKELLEIQELQEKAESELAKEE 693
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157819677 679 ELENQMGSLKEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 757
Cdd:pfam02463 694 ILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLK 772
|
|
| 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 157819677 53 RNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPceilsGDIIQFG 106
Cdd:cd22700 36 EQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAP-----GDVLRFG 84
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
553-769 |
4.79e-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: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 553 AAKAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQStfQLRCQQCEVQQ-REEATRLQGELEKLKKEwdvL 631
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA--ELEALQAEIDKlQAEIAEAEAEIEERREE---L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 632 ENECRSLKKE-------NVLLSSE-----LQRQE--KELHNSQKQSLELTSDLsilqmtRKELENQMGSLKEQhlrdEAD 697
Cdd:COG3883 89 GERARALYRSggsvsylDVLLGSEsfsdfLDRLSalSKIADADADLLEELKAD------KAELEAKKAELEAK----LAE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157819677 698 LKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREKGNNPSILQPVPA 769
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| 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 157819677 25 DEPIKIGRsvarcRPAQNNAT----FDCKVLSRNHALVWFdhKTSKFYLQDTKSSNGTFINSQRLSR-GSEESPPCEILS 99
Cdd:cd22702 31 KQPCIIGS-----DPHQAISGisvvIPSPQVSELHARITC--KNGAFFLTDLGSEHGTWINDNEGRRyRAPPNFPVRLHP 103
|
....*....
gi 157819677 100 GDIIQFGVD 108
Cdd:cd22702 104 SDVIEFGSD 112
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
327-662 |
5.94e-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: 43.51 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 327 KQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTalqeKLMVQGHLTKVV--------EESKLSK 398
Cdd:pfam13166 90 ESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDECW----KKIKRKKNSALSealngfkyEANFKSR 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 399 ENQAKAKESDLSDTLSPSKEKSSDDTT---DAQMDEQDLNEPLA------KVSLLKDDLQGTQAETEAKQDTQHLRKELV 469
Cdd:pfam13166 166 LLREIEKDNFNAGVLLSDEDRKAALATvfsDNKPEIAPLTFNVIdfdaleKAEILIQKVIGKSSAIEELIKNPDLADWVE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 470 EAQELARASKQKCFDLQALLEEERKA-----YRNQVEEsakqiqvlqvqlqrlhmDMENLQEEKDTEISSTRDKL--LSA 542
Cdd:pfam13166 246 QGLELHKAHLDTCPFCGQPLPAERKAaleahFDDEFTE-----------------FQNRLQKLIEKVESAISSLLaqLPA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 543 QDEILLLHQAAAKAVSERDTDFMSLQEELKKVRAELEGWRK---AASEYE------EEIRSLQST--------------F 599
Cdd:pfam13166 309 VSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRALEAKRKdpfKSIELDsvdakiESINDLVASineliakhneitdnF 388
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157819677 600 QLRCQQCEVQ-QREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNSQKQ 662
Cdd:pfam13166 389 EEEKNKAKKKlRLHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQ 452
|
|
| 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 157819677 16 PFQERHVYLD-EPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFdhKTSKFYLQDTKSSNGTFINSQRLSRgseespP 94
Cdd:cd22693 7 TLQGQTFPIDkSGITIGRA------DDNDLVLSDDFVSSRHARIYL--QGSSWYLEDLGSTNGTFVNGNRVTQ------P 72
|
90
....*....|....*..
gi 157819677 95 CEILSGDIIQFGVDVTE 111
Cdd:cd22693 73 VVVQPGDTIRIGATVFE 89
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
325-689 |
6.58e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 43.21 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 325 EGKQEEIQQKGQA--EKKELQAKIDDMEEKEQELQAKIEalQADNdftnERLTALQEKLMVQ-GHLTKVVEESKLSKENQ 401
Cdd:pfam09731 85 EKKQVKIPRQSGVssEVAEEEKEATKDAAEAKAQLPKSE--QEKE----KALEEVLKEAISKaESATAVAKEAKDDAIQA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 402 AKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLkddlqGTQAETEAKQDtqhlrkELVEAQELARASkqk 481
Cdd:pfam09731 159 VKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINL-----AKQSEEEAAPP------LLDAAPETPPKL--- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 482 cfdLQALLEEERKAYRNQVEESAKQIQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDEILL-------LHQAAA 554
Cdd:pfam09731 225 ---PEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLiahahreIDQLSK 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 555 KAVSERDTDFMSLQEELKKVRAELEGWRKAASEYEEEIRSLQstfqlrcqqcEVQQREEatrLQGELEKLKKEWD-VLEN 633
Cdd:pfam09731 302 KLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAAD----------EAQLRLE---FEREREEIRESYEeKLRT 368
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157819677 634 ECRSLKKENVL-LSSELQRQEKELHNSQKQSLE---------LTSDLSILQMTRKELENQMGSLKE 689
Cdd:pfam09731 369 ELERQAEAHEEhLKDVLVEQEIELQREFLQDIKekveeeragRLLKLNELLANLKGLEKATSSHSE 434
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
570-756 |
7.11e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 570 ELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEvQQREEATRLQGELEKL---KKEWDVLENECRSLKKENVLLS 646
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREIN-EISSELPELREELEKLekeVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 647 SELQRQEKELHNSQKQSLELTSDLSILQMTRKELEN---------QMGSLKEQHLRDEADLKTLLSKAENQAKDVQKEYE 717
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190
....*....|....*....|....*....|....*....
gi 157819677 718 KtqtvLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 756
Cdd:PRK03918 332 E----LEEKEERLEELKKKLKELEKRLEELEERHELYEE 366
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
208-381 |
7.24e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.90 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 208 IDEDRLLSRLEVMGNQLQACSKNQTE---DSLRKELVALQED-KHSYETTAKEslrrvLQEKIEVVRKLSEVERSLsnte 283
Cdd:PRK04778 249 LDHLDIEKEIQDLKEQIDENLALLEEldlDEAEEKNEEIQERiDQLYDILERE-----VKARKYVEKNSDTLPDFL---- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 284 decTHLREMNERTQEELRELANKY---NGAVNEIKDLSDKLKAAEGKQEEIQQKG----------QAEKKELQAKIDDME 350
Cdd:PRK04778 320 ---EHAKEQNKELKEEIDRVKQSYtlnESELESVRQLEKQLESLEKQYDEITERIaeqeiayselQEELEEILKQLEEIE 396
|
170 180 190
....*....|....*....|....*....|.
gi 157819677 351 EKEQELQAKIEALQADNDFTNERLTALQEKL 381
Cdd:PRK04778 397 KEQEKLSEMLQGLRKDELEAREKLERYRNKL 427
|
|
| 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 157819677 52 SRNHALVWFDHKTSKFYLQ-----------DTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFG 106
Cdd:cd22683 28 SRSCDLVLSDPSISRFHAElrleqnginviDNNSANGTFINGKRIKGKT-----YILKNGDIIVFG 88
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
163-348 |
7.49e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWqALIDEDRLLSRLEVMGNQLQACSKNQTE-DSLRKELV 241
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-DEIDVASAEREIAELEAELERLDASSDDlAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 242 ALQEDKhsyeTTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDEcthLREMNERTQEELRELANKYNGAVNEIKDLSDKL 321
Cdd:COG4913 696 ELEAEL----EELEEELDELKGEIGRLEKELEQAEEELDELQDR---LEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
170 180
....*....|....*....|....*..
gi 157819677 322 KAAEGKQEEIQQKGQAEKKELQAKIDD 348
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAMRA 795
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
446-656 |
8.02e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 446 DDLQGTQAETE-AKQDTQHLRkELVEAQELARASKQKCFDLQALLEEeRKAYRNQVEesakqiqvlqvqLQRLHMDMENL 524
Cdd:COG4913 235 DDLERAHEALEdAREQIELLE-PIRELAERYAAARERLAELEYLRAA-LRLWFAQRR------------LELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 525 QEEK---DTEISSTRDKLLSAQDEILLLHQAAAKAVSERDTDfmsLQEELKKVRAELEGWRKAASEYEEEIRSLQST--- 598
Cdd:COG4913 301 RAELarlEAELERLEARLDALREELDELEAQIRGNGGDRLEQ---LEREIERLERELEERERRRARLEALLAALGLPlpa 377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157819677 599 --------------FQLRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKEL 656
Cdd:COG4913 378 saeefaalraeaaaLLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
274-381 |
8.69e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.53 E-value: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 274 EVERSLSNTEDECTHLREMNERTQEELRELANKY---NGAVNEIKDLSDKLKAAEGKQEEIQQKGQAEK----------K 340
Cdd:pfam06160 288 YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEvayselqeelE 367
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 157819677 341 ELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQEKL 381
Cdd:pfam06160 368 EILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLEL 408
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
258-505 |
9.20e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.61 E-value: 9.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 258 LRRVLQEKIEVV---RKLSEVERSLSntEDECTHLREMNERTQ----EELRELANKYNGAVNEIKDLSDKLKAAEGKQ-- 328
Cdd:PRK05771 1 LAPVRMKKVLIVtlkSYKDEVLEALH--ELGVVHIEDLKEELSnerlRKLRSLLTKLSEALDKLRSYLPKLNPLREEKkk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 329 ------EEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTnERLTALQEKLMVQGHLTKV-VEESKLSKEnq 401
Cdd:PRK05771 79 vsvkslEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERL-EPWGNFDLDLSLLLGFKYVsVFVGTVPED-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 402 aKAKESDLSDTLSPSKEKSSDDTTD------AQMDEQDLNEPLAKVSLLKDDLQ--GTQAET--EAKQDTQHLRKELVEA 471
Cdd:PRK05771 156 -KLEELKLESDVENVEYISTDKGYVyvvvvvLKELSDEVEEELKKLGFERLELEeeGTPSELirEIKEELEEIEKERESL 234
|
250 260 270
....*....|....*....|....*....|....
gi 157819677 472 QELARASKQKCFDLQALLEEERKAYRNQVEESAK 505
Cdd:PRK05771 235 LEELKELAKKYLEELLALYEYLEIELERAEALSK 268
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
569-743 |
1.01e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 569 EELKKVRAELEGWRKAASEYEEEIRSLQSTFQlRCQQCEvQQREEATRLQGELEKLKKEWDVLEnECRSLKKENVLLSSE 648
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEE-ELEELE-AELEELREELEKLEKLLQLLPLYQ-ELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 649 LQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGSLKEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKL 728
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170
....*....|....*
gi 157819677 729 KFEMTEQEKQSITDE 743
Cdd:COG4717 228 ELEQLENELEAAALE 242
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
613-736 |
1.05e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 41.61 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 613 EATRLQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNsQKQSLELTSDLSilqmtrkELENQMGSLKeqhl 692
Cdd:pfam15294 134 EIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGA-KKDVKSNLKEIS-------DLEEKMAALK---- 201
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 157819677 693 rdeADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQE 736
Cdd:pfam15294 202 ---SDLEKTLNASTALQKSLEEDLASTKHELLKVQEQLEMAEKE 242
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
587-757 |
1.15e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 587 EYEEEIRSLQSTFQLRCQQCEVQQR--EEATRLQGE-LEKLKKEWDVLENECRSLKKENVLLSSELQRQEKELHNsqkqs 663
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKniEEQRKKNGEnIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIED----- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 664 leLTSDLSILQMTRKELENQMGSL-KEQHLRDEADL-----------KTLLSKAENQAKDVQKEYEKTQTVLSELKLKF- 730
Cdd:PHA02562 253 --PSAALNKLNTAAAKIKSKIEQFqKVIKMYEKGGVcptctqqisegPDRITKIKDKLKELQHSLEKLDTAIDELEEIMd 330
|
170 180
....*....|....*....|....*....
gi 157819677 731 EMTEQEK--QSITDELKQCKDNLKLLREK 757
Cdd:PHA02562 331 EFNEQSKklLELKNKISTNKQSLITLVDK 359
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
569-760 |
1.19e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 569 EELKKVRAELEGWRKAASEYEEEIRSLQstfQLRCQQcevQQREEATRLQGELEKLKKEWDVLENEcrslkKENVLLSSE 648
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLE---PIRELA---ERYAAARERLAELEYLRAALRLWFAQ-----RRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 649 LQRQEKELHNSQKQSLELTSDLSILQMTRKELENQmgsLKEQHLRDEADLKTLLSKAENQAKDVQKEYEKTQTVLSELKL 728
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQ---IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
170 180 190
....*....|....*....|....*....|..
gi 157819677 729 KFEMTEQEKQSITDELKQCKDNLKLLREKGNN 760
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
256-661 |
1.28e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 256 ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERtQEELRELANKYNGAVNEIKDLSDKLKAAEGKQE------ 329
Cdd:PRK01156 315 SNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQ-ILELEGYEMDYNSYLKSIESLKKKIEEYSKNIErmsafi 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 330 -EIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQEKL-MVQGHLTKVVEESKLSKEnqakaKES 407
Cdd:PRK01156 394 sEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMeMLNGQSVCPVCGTTLGEE-----KSN 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 408 DLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQDTQ--HLRKELVEAQELARASKQKCFDL 485
Cdd:PRK01156 469 HIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKieSARADLEDIKIKINELKDKHDKY 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 486 QALLEEERKAYRNQVEesAKQIQVLQVQLQRLHMDMENLQEEKDtEISSTRDKLLSAQDEILL----LHQAAAKAVSERD 561
Cdd:PRK01156 549 EEIKNRYKSLKLEDLD--SKRTSWLNALAVISLIDIETNRSRSN-EIKKQLNDLESRLQEIEIgfpdDKSYIDKSIREIE 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 562 TDFMSLQ---EELKKVRAELEGWRKAASEYEEEIRSLQStFQLRCQQCEVQQREEATRL---QGELEKLKKEWDVLENEC 635
Cdd:PRK01156 626 NEANNLNnkyNEIQENKILIEKLRGKIDNYKKQIAEIDS-IIPDLKEITSRINDIEDNLkksRKALDDAKANRARLESTI 704
|
410 420
....*....|....*....|....*.
gi 157819677 636 RSLKKENVLLSSELQRQEKELHNSQK 661
Cdd:PRK01156 705 EILRTRINELSDRINDINETLESMKK 730
|
|
| 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 157819677 27 PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTSkfYLQDTKSSNGTFINSQRLsrgseeSPPCEILSGDIIQFG 106
Cdd:cd22668 19 SNIIGRG------SDADFRLPDTGVSRRHAEIRWDGQVA--HLTDLGSTNGTTVNNAPV------TPEWRLADGDVITLG 84
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
256-365 |
1.36e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 256 ESLRRVLQEKI-EVVRKLSEVERSLSNTEDEcthLREMNERTQEELRELANKYNGAVNEIKdlsdklKAAEGKQEEIQQK 334
Cdd:PRK00409 526 EELERELEQKAeEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLEEAEKEAQQAIKEAK------KEADEIIKELRQL 596
|
90 100 110
....*....|....*....|....*....|.
gi 157819677 335 GQAEKKELQAKidDMEEKEQELQAKIEALQA 365
Cdd:PRK00409 597 QKGGYASVKAH--ELIEARKRLNKANEKKEK 625
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
234-381 |
1.49e-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: 41.06 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 234 DSLRKELVALQEDKhsyeTTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLRE--MNERTQEELRELANKYNGAV 311
Cdd:COG1579 27 KELPAELAELEDEL----AALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNNKEYEALQKEIESLK 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 312 NEIKDLSDKLKAAEGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQEKL 381
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
49-112 |
1.51e-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: 1.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157819677 49 KVLSRNHALVWFDHKTS--KFYLQDTKSSNGTFINsqrlsrgSEESPPC---EILSGDIIQFGVDVTEN 112
Cdd:cd22681 64 ETCSKQHCVIQFRNVKGilKPYIMDLDSSNGTCLN-------DNVIPSSryvELRSGDVITFSKSNDYE 125
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
611-737 |
2.31e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 611 REEATRLQGELEKLKKEWDVLENECRSLKK----ENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMTRKELENQMGS 686
Cdd:smart00787 164 MKELELLNSIKPKLRDRKDALEEELRQLKQledeLEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIED 243
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 157819677 687 LKEQhlrdEADLKTLLSKAENQAKDVQKeyeKTQTVLSELKLKFEMTEQEK 737
Cdd:smart00787 244 LTNK----KSELNTEIAEAEKKLEQCRG---FTFKEIEKLKEQLKLLQSLT 287
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
276-464 |
2.35e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 41.39 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 276 ERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLSDKLKAAEgKQEEIQQKGQAEKKELQA----------- 344
Cdd:PRK00106 34 ELTLLNAEQEAVNLRGKAERDAEHIKKTAKRESKALKKELLLEAKEEARK-YREEIEQEFKSERQELKQiesrlterats 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 345 ---KIDDMEEKEQELQAKIEALQADNDFTNERltalqEKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSS 421
Cdd:PRK00106 113 ldrKDENLSSKEKTLESKEQSLTDKSKHIDER-----EEQVEKLEEQKKAELERVAALSQAEAREIILAETENKLTHEIA 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 157819677 422 DDTTDAQMDEQDLNEPLAKvSLLKDDLQGTQAE--TEAKQDTQHL 464
Cdd:PRK00106 188 TRIREAEREVKDRSDKMAK-DLLAQAMQRLAGEyvTEQTITTVHL 231
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
318-586 |
2.81e-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: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 318 SDKLKAAEGKQEEIQQKGQAEKKEL---QAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQEKLmvqghltKVVEES 394
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELaalKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-------AELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 395 KLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQDTQhlrkelveaQEL 474
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL---------AEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 475 ARaskqkcfdLQALLEEERKAYRNQVEESAKQIQvlqvqlqrlhmDMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAA 554
Cdd:COG4942 163 AA--------LRAELEAERAELEALLAELEEERA-----------ALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
250 260 270
....*....|....*....|....*....|..
gi 157819677 555 kavserdtdfmSLQEELKKVRAELEGWRKAAS 586
Cdd:COG4942 224 -----------ELEALIARLEAEAAAAAERTP 244
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
489-662 |
2.91e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 489 LEEERKAYRNQVEESAKQIQVLQVQLQRLhmdmenlqEEKDTEISSTRDKLLSAQDEILLLHQAAA-KAVSERDTDFMSL 567
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEEL--------EELEAELEELREELEKLEKLLQLLPLYQElEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 568 QEELKKVRAELEGWRKAASEYEEEIRSLQSTFQLRCQQCEVQQREEATRLQGELEKLKKEWDVLENECRSLKKENVLLSS 647
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170
....*....|....*
gi 157819677 648 ELQRQEKELHNSQKQ 662
Cdd:COG4717 228 ELEQLENELEAAALE 242
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
609-757 |
3.01e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 609 QQREEATR----LQGELEKLKKEWDVLENECRSLKKENVLLSSELQRQ--EKELHNSQKQSLELTSDLSILQMTRKELEN 682
Cdd:COG3206 168 LRREEARKalefLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKllLQQLSELESQLAEARAELAEAEARLAALRA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 683 QMGS----------------LKEQHLRDEADLKTLLSK----------AENQAKDVQKEYEK-TQTVLSELKLKFEMTEQ 735
Cdd:COG3206 248 QLGSgpdalpellqspviqqLRAQLAELEAELAELSARytpnhpdviaLRAQIAALRAQLQQeAQRILASLEAELEALQA 327
|
170 180
....*....|....*....|..
gi 157819677 736 EKQSITDELKQCKDNLKLLREK 757
Cdd:COG3206 328 REASLQAQLAQLEARLAELPEL 349
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
180-427 |
3.16e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 180 QMLEQKLATLQRLLAITQEASDTSWQALideDRLLSRLEVMGNQLQAcsKNQTEDSLRKELVALQEDKHSYETTAKESLR 259
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAEL---EELNEEYNELQAELEA--LQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 260 rVLQEKIEVVRKLSEVERSLSNTE--DECTHLREMNERTQEELRELANkyngAVNEIKDLSDKLKAAEGKQEEIQQKGQA 337
Cdd:COG3883 94 -ALYRSGGSVSYLDVLLGSESFSDflDRLSALSKIADADADLLEELKA----DKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 338 EKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQEKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSK 417
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
250
....*....|
gi 157819677 418 EKSSDDTTDA 427
Cdd:COG3883 249 AGAAGAAGAA 258
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
1-106 |
3.49e-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: 40.52 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 1 MPSALAIFTCRPNSHPFQERHVYLDEPIKIGRSvARC-----RPAQnnatfdckVLSRNHALVWFDHktSKFYLQDTkSS 75
Cdd:COG3456 1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRS-ADCdwvlpDPDR--------SVSRRHAEIRFRD--GAFCLTDL-ST 68
|
90 100 110
....*....|....*....|....*....|...
gi 157819677 76 NGTFIN--SQRLSRGSEEsppcEILSGDIIQFG 106
Cdd:COG3456 69 NGTFLNgsDHPLGPGRPV----RLRDGDRLRIG 97
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
343-602 |
3.90e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 343 QAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQEKLMVQGHLTKVVEESK--LSKENQAKAKESDLSDTlspskEKS 420
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERL-----DAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 421 SDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQAETEAKQDTqhLRKELVEAQE-LARASKQKCFDLQALLEEERKAyrnq 499
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ--AEEELDELQDrLEAAEDLARLELRALLEERFAA---- 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 500 veesakqiQVLQVQLQRLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLHQAAAkavSERDTDFMSL---QEELKKVRA 576
Cdd:COG4913 758 --------ALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAET---ADLDADLESLpeyLALLDRLEE 826
|
250 260
....*....|....*....|....*..
gi 157819677 577 E-LEgwrkaasEYEEEIRSLQSTFQLR 602
Cdd:COG4913 827 DgLP-------EYEERFKELLNENSIE 846
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
163-365 |
4.01e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.44 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEasdtsWQALIDEDRLLSR----LEVMGNQLQACSKNQT--EDSL 236
Cdd:COG0497 172 KELEELRADEAERARELDLLRFQLEELEAAALQPGE-----EEELEEERRRLSNaeklREALQEALEALSGGEGgaLDLL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 237 ---RKELVALQEDKHSYETTAkESLRRVLQEKIEVVRklsEVERSLSNTEDECTHLREMNERtQEELRELANKYNGAVNE 313
Cdd:COG0497 247 gqaLRALERLAEYDPSLAELA-ERLESALIELEEAAS---ELRRYLDSLEFDPERLEEVEER-LALLRRLARKYGVTVEE 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 157819677 314 IKDLSDKLkaaegkqeeiqqkgQAEKKELQAKIDDMEEKEQELQAKIEALQA 365
Cdd:COG0497 322 LLAYAEEL--------------RAELAELENSDERLEELEAELAEAEAELLE 359
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
302-393 |
8.96e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 37.17 E-value: 8.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819677 302 ELANKYNGAVNEIKDLSDKLKAA-EGKQEEIQQKGQAEKKELQAKIDDMEEKEQELQAKIEALQADNDFTNERLTALQEK 380
Cdd:pfam03938 12 EESPEGKAAQAQLEKKFKKRQAElEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQE 91
|
90
....*....|....*
gi 157819677 381 LM--VQGHLTKVVEE 393
Cdd:pfam03938 92 LLqpIQDKINKAIKE 106
|
|
| |
