|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
3-130 |
1.29e-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: 256.04 E-value: 1.29e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 3 SALAIFTCRPNSHPFQERHVYLDEPIKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINS 82
Cdd:cd22679 1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1799135562 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 |
2.94e-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: 101.99 E-value: 2.94e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799135562 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 |
1.69e-18 |
|
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: 82.62 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 27 PIKIGRSVARCRPAQNNAT-FDCKVLSRNHALVWfdHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQF 105
Cdd:cd22692 38 QIHIGRYTERVRQAIYHPVvFKSKVVSRTHGCIK--VDEGNWYIKDVKSSSGTFLNHQRLSPASRTSKPYPLRDGDILQL 115
|
...
gi 1799135562 106 GVD 108
Cdd:cd22692 116 GMD 118
|
|
| FHA_VPS64-like |
cd22695 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ... |
6-126 |
5.37e-16 |
|
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: 75.03 E-value: 5.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 6 AIFTCRPNSHPFQERHV---YLDEPIKIGRSVARCRPAQN---------------NATFDCKVLSRNHALVWFDHKTGKF 67
Cdd:cd22695 2 HILVLKSLNATFETKFLvvpFKPDGLKLGRPVTNSVNKNNsgskrdlfsqqvrpdNGNFDSRVLSRNHACLSCDPTTGKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135562 68 YLQDTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFGVDVTEntrKVTHGCIVSTIK 126
Cdd:cd22695 82 YIRDLKSSNGTFVNGQKIRQND-----VELKVGDEVDLGTDIDS---KIEHRKISAYVE 132
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-733 |
9.58e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 78.56 E-value: 9.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 156 NTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQA--CSKNQTE 233
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvAQLELQI 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 234 DSLRKELIAL------QEDKHNYETTAKESLRRVLQE--KIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELAN 305
Cdd:TIGR02168 396 ASLNNEIERLearlerLEDRRERLQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 306 KYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKidemEEKEQELQAKIEALQADNDFTNERLTALQVRLEHL- 384
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ----SGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVv 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 385 ---QEKTLKECSSLEK------------LIVEGHLTKAVEETKLSKE--------------------------------- 416
Cdd:TIGR02168 552 venLNAAKKAIAFLKQnelgrvtflpldSIKGTEIQGNDREILKNIEgflgvakdlvkfdpklrkalsyllggvlvvddl 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 417 -------NQTRAKESDFS---DTLSP--------SKEKSSDDTTDAQMDEqdLNEPLAKVSLLKALLEEERKAYRNQVEE 478
Cdd:TIGR02168 632 dnalelaKKLRPGYRIVTldgDLVRPggvitggsAKTNSSILERRREIEE--LEEKIEELEEKIAELEKALAELRKELEE 709
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 479 STKQIQVLQAQLQRLHIDTENLREEKD----------SEITSTRDELLSARDEILLLHQAAAKV---ASERDTDIASLQE 545
Cdd:TIGR02168 710 LEEELEQLRKELEELSRQISALRKDLArleaeveqleERIAQLSKELTELEAEIEELEERLEEAeeeLAEAEAEIEELEA 789
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 546 ELKKVRAELERWRKAASEYEKEITSLQNSF---QLRCQQCEDQQREEATRL----------QGELEKLRKEWNALETECH 612
Cdd:TIGR02168 790 QIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATERRLedleeqieelSEDIESLAAEIEELEELIE 869
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 613 SLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHlrdsADLKTLLSKAENQAKDVQkey 692
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL----AQLELRLEGLEVRIDNLQ--- 942
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1799135562 693 ektQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 733
Cdd:TIGR02168 943 ---ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
13-106 |
4.75e-14 |
|
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: 68.07 E-value: 4.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 13 NSHPFQERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINSQRLsrgseeS 92
Cdd:cd00060 6 DGDGGGREFPLTKGVVTIGRS------PDCDIVLDDPSVSRRHARIEVDG--GGVYLEDLGSTNGTFVNGKRI------T 71
|
90
....*....|....
gi 1799135562 93 PPCEILSGDIIQFG 106
Cdd:cd00060 72 PPVPLQDGDVIRLG 85
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
172-722 |
6.78e-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: 75.86 E-value: 6.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 172 LQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRllsrlevmgnqlqacSKNQTEDSLRKELIALQEDKHNYE 251
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS---------------ELEEEIEELQKELYALANEISRLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 252 ttakeslrrvlQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEI 331
Cdd:TIGR02168 302 -----------QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 332 QQKGQAEKKELQH---KIDEMEEKEQELQAKIEALQAdndftneRLTALQVRLEHLQEKTLKECSSLEKLIVEGHLTKAV 408
Cdd:TIGR02168 371 ESRLEELEEQLETlrsKVAQLELQIASLNNEIERLEA-------RLERLEDRRERLQQEIEELLKKLEEAELKELQAELE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 409 EETKLskENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQ---- 484
Cdd:TIGR02168 444 ELEEE--LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgi 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 485 --------------------VLQAQLQRLHIDTEN---------------------LREEKDSEITSTRDELLSARDEIL 523
Cdd:TIGR02168 522 lgvlselisvdegyeaaieaALGGRLQAVVVENLNaakkaiaflkqnelgrvtflpLDSIKGTEIQGNDREILKNIEGFL 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 524 LLHQAAAKVASERD-------------TDIASLQEELKKVRA---------ELERWRKAAS-----------EYEKEITS 570
Cdd:TIGR02168 602 GVAKDLVKFDPKLRkalsyllggvlvvDDLDNALELAKKLRPgyrivtldgDLVRPGGVITggsaktnssilERRREIEE 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 571 LQNSFQLRCQQCEDQQ------REEATRLQGELEKLRKEWNALETECHSLK-------RENVLLSSELQRQEKELHNSQK 637
Cdd:TIGR02168 682 LEEKIEELEEKIAELEkalaelRKELEELEEELEQLRKELEELSRQISALRkdlarleAEVEQLEERIAQLSKELTELEA 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 638 QSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTL---LSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQ 714
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
....*...
gi 1799135562 715 SITDELKQ 722
Cdd:TIGR02168 842 DLEEQIEE 849
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
239-719 |
9.04e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.56 E-value: 9.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 239 ELIALQEDKHNYETTAKESLRRV--LQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKD 316
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 317 LSDKLKVAEGKQEEIQQKGQAEKK--ELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLKECSS 394
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 395 LEKLIVEghLTKAVEETKLSKENQTRAKESDFSDTLspskEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYR- 473
Cdd:PTZ00121 1442 EAKKADE--AKKKAEEAKKAEEAKKKAEEAKKADEA----KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEa 1515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 474 NQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSA---------------RDEILLLHQAAAKVASERDT 538
Cdd:PTZ00121 1516 KKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAeekkkaeeakkaeedKNMALRKAEEAKKAEEARIE 1595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 539 DIASLQEELKKVRAE----LERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSL 614
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEeakkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK 1675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 615 KRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYE- 693
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEe 1755
|
490 500
....*....|....*....|....*...
gi 1799135562 694 --KTQTVLSELKLKFEMTEQEKQSITDE 719
Cdd:PTZ00121 1756 kkKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
28-105 |
1.39e-13 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 66.06 E-value: 1.39e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135562 28 IKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRLSRgseesPPCEILSGDIIQF 105
Cdd:pfam00498 1 VTIGRS------PDCDIVLDDPSVSRRHAEIRYD-GGGRFYLEDLGSTNGTFVNGQRLGP-----EPVRLKDGDVIRL 66
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
298-733 |
2.43e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.92 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 298 EELRELANKYNGAVNEIkdLSDKLKVAEGKQEEIQQKgqaEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTAL 377
Cdd:PRK02224 165 EEYRERASDARLGVERV--LSDQRGSLDQLKAQIEEK---EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 378 QVRLEHlQEKTLKECSSLEKLIVEghLTKAVEETKLSKEnqtrakesDFSDTLSPSKEKSSD--DTTDAQMDEQDLNEPL 455
Cdd:PRK02224 240 DEVLEE-HEERREELETLEAEIED--LRETIAETERERE--------ELAEEVRDLRERLEEleEERDDLLAEAGLDDAD 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 456 AK-VSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEK----------DSEITSTRDELLSARDEILL 524
Cdd:PRK02224 309 AEaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAeelreeaaelESELEEAREAVEDRREEIEE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 525 LhQAAAKVASER----DTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSF----QLR----CQQCE--------- 583
Cdd:PRK02224 389 L-EEEIEELRERfgdaPVDLGNAEDFLEELREERDELREREAELEATLRTARERVeeaeALLeagkCPECGqpvegsphv 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 584 ---DQQREEATRLQGELEKLRKEWNALETECHSLKrenvllssELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQV 660
Cdd:PRK02224 468 etiEEDRERVEELEAELEDLEEEVEEVEERLERAE--------DLVEAEDRIERLEERREDLEELIAERRETIEEKRERA 539
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135562 661 GSLKEQhlrdSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS------ITDELKQCKNNLKLLREK 733
Cdd:PRK02224 540 EELRER----AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESlerirtLLAAIADAEDEIERLREK 614
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
294-607 |
3.42e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 3.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 294 ERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQkgqaEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNER 373
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRL----ELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 374 LTALQVRLEHLQEktlkecsSLEKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNE 453
Cdd:COG1196 311 RRELEERLEELEE-------ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 454 plakvsllkalLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKdSEITSTRDELLSARDEILLLHQAAAKVA 533
Cdd:COG1196 384 -----------LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL-EELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799135562 534 SERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRcqqcEDQQREEATRLQGELEKLRKEWNAL 607
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL----LEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
161-703 |
3.82e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 161 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKEL 240
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 241 IALQEDkhnyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDK 320
Cdd:COG1196 298 ARLEQD-----------IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 321 LKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKT-------LKECS 393
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEeeeeeeeEALEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 394 SLEKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLA-KVSLLKALLEEERKAY 472
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvKAALLLAGLRGLAGAV 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 473 RNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVrA 552
Cdd:COG1196 527 AVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLV-A 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 553 ELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQRE----------EATRLQGELEKLRKEWNALETECHSLKRENVLLS 622
Cdd:COG1196 606 SDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTlagrlrevtlEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 623 SELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSEL 702
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL 765
|
.
gi 1799135562 703 K 703
Cdd:COG1196 766 E 766
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
312-638 |
1.08e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.01 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 312 NEIKDLSDKLKVAEGKQEEIQQkgqaEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNE---RLTALQVRLEHLQEKT 388
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEK----ALAELRKELEELEEELEQLRKELEELSRQISALRKdlaRLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 389 LKECSSLEKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEE 468
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 469 RKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDsEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELK 548
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE-ELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 549 KVRAELERWRKAASEYEKEITSLQNsfqlrcqqcedqqreeatRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQ 628
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGLEV------------------RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR 973
|
330
....*....|
gi 1799135562 629 EKELHNSQKQ 638
Cdd:TIGR02168 974 LKRLENKIKE 983
|
|
| CC1_SLMAP-like |
cd21868 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ... |
167-204 |
1.23e-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: 1.23e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1799135562 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21868 1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
460-733 |
2.38e-12 |
|
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: 70.87 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 460 LLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLhidtENLREEKDSEITSTRDELLSARDeilLLHQAAAKVASERDTD 539
Cdd:TIGR02169 216 LLKEKREYEGYELLKEKEALERQKEAIERQLASL----EEELEKLTEEISELEKRLEEIEQ---LLEELNKKIKDLGEEE 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 540 IASLQEELKKVRAELERWRKAASEYEKEITSLQNsfQLRCQQCE-DQQREEATRLQGELEKLRKEWNALETECHSLKREN 618
Cdd:TIGR02169 289 QLRVKEKIGELEAEIASLERSIAEKERELEDAEE--RLAKLEAEiDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 619 VLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADlktlLSKAENQAKDVQKEYEKTQTV 698
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEE----LADLNAAIAGIEAKINELEEE 442
|
250 260 270
....*....|....*....|....*....|....*
gi 1799135562 699 LSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 733
Cdd:TIGR02169 443 KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
163-666 |
2.80e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDtswQALIDEDRLLSRLEVMGNQLQAcsKNQTEDSLRKELIA 242
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRR---ELEERLEELEEELAELEEELEE--LEEELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 243 LQEDkhnyETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLK 322
Cdd:COG1196 349 AEEE----LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 323 VAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLKEcsSLEKLIVEG 402
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL--LLLLEAEAD 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 403 HLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYR------NQV 476
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRatflplDKI 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 477 EESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELER 556
Cdd:COG1196 583 RARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSL 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 557 WRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVL---LSSELQRQEKELH 633
Cdd:COG1196 663 TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALeeqLEAEREELLEELL 742
|
490 500 510
....*....|....*....|....*....|...
gi 1799135562 634 NSQKQSLELTSDLSILQMSRKELENQVGSLKEQ 666
Cdd:COG1196 743 EEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
212-732 |
4.23e-12 |
|
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: 70.08 E-value: 4.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 212 RLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTAKESLRRVLQEKIEvvrkLSEVERSlSNTEDECTHLKE 291
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE----LDGFERG-PFSERQIKNFHT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 292 MNERTQEELRELANKyngavnEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFT- 370
Cdd:TIGR00606 398 LVIERQEDEAKTAAQ------LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSd 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 371 -----NERLTALQVRLEHLQEKTLKECSSLEKLIVEGHltKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTT-DA 444
Cdd:TIGR00606 472 rilelDQELRKAERELSKAEKNSLTETLKKEVKSLQNE--KADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDkDE 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 445 QMDEQDLNEPLAKVSLL-----KALLEEERKAYRNQVEESTKQIQVLQAQLQRLhidtENLREEKDSEITSTRDELLSAR 519
Cdd:TIGR00606 550 QIRKIKSRHSDELTSLLgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASL----EQNKNHINNELESKEEQLSSYE 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 520 DEILllhqaAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQC------EDQQREEATRL 593
Cdd:TIGR00606 626 DKLF-----DVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCqrvfqtEAELQEFISDL 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 594 QGELEKLRKEWNALETECHSLKRENVLL-------SSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSL--K 664
Cdd:TIGR00606 701 QSKLRLAPDKLKSTESELKKKEKRRDEMlglapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTImpE 780
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 665 EQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVL--SELKLKFEMTEQEKQSITDELKQCKNNLKLLRE 732
Cdd:TIGR00606 781 EESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLqgSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
14-106 |
1.09e-11 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 61.51 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 14 SHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716 8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
|
90
....*....|....
gi 1799135562 93 pPCEILSGDIIQFG 106
Cdd:COG1716 75 -PAPLRDGDVIRLG 87
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
256-728 |
1.33e-11 |
|
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: 68.22 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 256 ESLRRVLQEKIEVVRKLSE--VERSLSNTEDECTHLKEmnertqeelrelanKYNGAVNEIKDLSDKLKVAEGKQEEIQQ 333
Cdd:pfam15921 248 EALKSESQNKIELLLQQHQdrIEQLISEHEVEITGLTE--------------KASSARSQANSIQSQLEIIQEQARNQNS 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 334 KGQAEKKELQHKID----EMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLKECSSLEKLIVEGHltKAVE 409
Cdd:pfam15921 314 MYMRQLSDLESTVSqlrsELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLH--KREK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 410 ETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTD------------------AQMDEQ-----DLNEPLAKVSLLKALLE 466
Cdd:pfam15921 392 ELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNmevqrleallkamksecqGQMERQmaaiqGKNESLEKVSSLTAQLE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 467 EERKAYRNQVEESTKQIQVLQAQlQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDtdiaslqeE 546
Cdd:pfam15921 472 STKEMLRKVVEELTAKKMTLESS-ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGD--------H 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 547 LKKVRAELERWRKAASEYEKEITSLQNSFQlRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLK----------R 616
Cdd:pfam15921 543 LRNVQTECEALKLQMAEKDKVIEILRQQIE-NMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKilkdkkdakiR 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 617 ENVLLSSELQRQEKELHNSQKQSLELTSDlsiLQMSRKELENQVGSLKEqhlrdsaDLKTLLSKAENQAKDVQKEYEKTQ 696
Cdd:pfam15921 622 ELEARVSDLELEKVKLVNAGSERLRAVKD---IKQERDQLLNEVKTSRN-------ELNSLSEDYEVLKRNFRNKSEEME 691
|
490 500 510
....*....|....*....|....*....|..
gi 1799135562 697 TVLSELKLKFemteqekQSITDELKQCKNNLK 728
Cdd:pfam15921 692 TTTNKLKMQL-------KSAQSELEQTRNTLK 716
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
52-106 |
1.34e-11 |
|
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 (AGGF1) and similar proteins; AGGF1, also called angiogenic factor VG5Q, or G patch domain-containing protein 7 (GPATC7), or vasculogenesis gene on 5q protein, is an angiogenic factor involved in vascular development, angiogenesis, specification of hemangioblasts, and differentiation of veins. It promotes angiogenesis and the proliferation of endothelial cells. It inhibits inflammatory effect and preserve vascular integrity in non-nervous system diseases. Mutated AGGF1 causes susceptibility to Klippel-Trenaunay syndrome, a vascular disorder. Increased AGGF1 expression is associated with tumor angiogenesis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438738 [Multi-domain] Cd Length: 123 Bit Score: 62.30 E-value: 1.34e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1799135562 52 SRNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQFG 106
Cdd:cd22686 48 SKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPYPLTHGDELKIG 102
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
267-733 |
4.88e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 66.20 E-value: 4.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 267 EVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKI 346
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 347 DEMEEKEQE---LQAKIEALQADNDFTNERLTALQVRLEHLQEK-----------------TLKECSSLEKLIVEGHLTK 406
Cdd:TIGR04523 117 EQKNKLEVElnkLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKyndlkkqkeelenelnlLEKEKLNIQKNIDKIKNKL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 407 AVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSL----LKALLEEERKAYR------NQV 476
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNtqtqLNQLKDEQNKIKKqlsekqKEL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 477 EESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILllhQAAAKVASERDTDIASLQEELKKVRAELER 556
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKL---EEIQNQISQNNKIISQLNEQISQLKKELTN 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 557 WRKAASEYEKEITSLQNsfqlrcqQCEDQQREEATRLQgELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQ 636
Cdd:TIGR04523 354 SESENSEKQRELEEKQN-------EIEKLKKENQSYKQ-EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 637 KQSLELTSDLSILQMSRKELENQVGSLKEQHlrdsADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSI 716
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELII----KNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL 501
|
490
....*....|....*..
gi 1799135562 717 TDELKQCKNNLKLLREK 733
Cdd:TIGR04523 502 NEEKKELEEKVKDLTKK 518
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
271-707 |
6.22e-11 |
|
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: 66.35 E-value: 6.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 271 KLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAvneIKDLSDKLKvaegKQEEIQQKGQAEKKELQHKIDEME 350
Cdd:pfam01576 149 KLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAM---ISDLEERLK----KEEKGRQELEKAKRKLEGESTDLQ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 351 EKEQELQAKIEALQADNDFTNERLTALQVRLEhlqEKTLKECSSLEKLI-VEGHLTKAVEETKLSKENQTRAKES--DFS 427
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAKKEEELQAALARLE---EETAQKNNALKKIReLEAQISELQEDLESERAARNKAEKQrrDLG 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 428 DTLSPSKEKSSD--DTTDAQMDEQDLNEplAKVSLLKALLEEERKAYRNQVEEstkqiqvlqaqlqrlhidtenLREEKD 505
Cdd:pfam01576 299 EELEALKTELEDtlDTTAAQQELRSKRE--QEVTELKKALEEETRSHEAQLQE---------------------MRQKHT 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 506 SEITSTRDELLSARDEILLLHQAAAKVASERdtdiASLQEELKKVRAelerwRKAASEYEKEITSLQ-NSFQLRCQQCED 584
Cdd:pfam01576 356 QALEELTEQLEQAKRNKANLEKAKQALESEN----AELQAELRTLQQ-----AKQDSEHKRKKLEGQlQELQARLSESER 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 585 QQREEA---TRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLsilqmsrKELENQVG 661
Cdd:pfam01576 427 QRAELAeklSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRL-------RQLEDERN 499
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1799135562 662 SLKEQhlrdsadlktlLSKAENQAKDVQKEYEKTQTVLSELKLKFE 707
Cdd:pfam01576 500 SLQEQ-----------LEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
271-733 |
1.62e-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: 64.66 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 271 KLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHK----- 345
Cdd:TIGR04523 125 ELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLellls 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 346 -IDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLKECSSLEKLIVEGHLTKAVEETKLSKENQTRAKES 424
Cdd:TIGR04523 205 nLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIK 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 425 DFSDTLSPSKEKSSDDTTDAQMD-EQDLNEPLAKVsllkallEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLR-- 501
Cdd:TIGR04523 285 ELEKQLNQLKSEISDLNNQKEQDwNKELKSELKNQ-------EKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEse 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 502 --------EEKDSEITSTRDELLSARDEILLLH----------QAAAKVASERDTDIASLQEELKKVRAELERWRKAASE 563
Cdd:TIGR04523 358 nsekqrelEEKQNEIEKLKKENQSYKQEIKNLEsqindleskiQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 564 YEKEITSLQNsfqlrcqqcedqqreEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELT 643
Cdd:TIGR04523 438 NNSEIKDLTN---------------QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLN 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 644 SDLSILQMSRKELENQVGSLKEQhlrdSADLKTLLSKAENQAKDVQKEYEKTQTVLselklKFEMTEQEKQSITDELKQC 723
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLKEK----IEKLESEKKEKESKISDLEDELNKDDFEL-----KKENLEKEIDEKNKEIEEL 573
|
490
....*....|
gi 1799135562 724 KNNLKLLREK 733
Cdd:TIGR04523 574 KQTQKSLKKK 583
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
162-658 |
3.63e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 162 SQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgNQLQAcsKNQTEDSLRKELI 241
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE---AELAE--AEEELEELAEELL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 242 ALQEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKL 321
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 322 KVAEGKQEEIQQKGQAE---KKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLKEC-SSLEK 397
Cdd:COG1196 470 EEAALLEAALAELLEELaeaAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAlAAALQ 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 398 LIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQV- 476
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVa 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 477 ---EESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAE 553
Cdd:COG1196 630 arlEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 554 LERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKE--WNALETECHSLKRE-------NVLLSSE 624
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPpdLEELERELERLEREiealgpvNLLAIEE 789
|
490 500 510
....*....|....*....|....*....|....
gi 1799135562 625 LQRQEKELHnsqkqslELTSDLSILQMSRKELEN 658
Cdd:COG1196 790 YEELEERYD-------FLSEQREDLEEARETLEE 816
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
135-675 |
5.40e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.21 E-value: 5.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 135 ARLRSDVIHAPLpSPVDKVAANTPSMYSQELFQL----SQYLQEALHREQMLEQKLATLQRLLAItqeASDTSWQALIDE 210
Cdd:pfam15921 290 ARSQANSIQSQL-EIIQEQARNQNSMYMRQLSDLestvSQLRSELREAKRMYEDKIEELEKQLVL---ANSELTEARTER 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 211 DRLLSRLEVMGNQLQAC----SKNQTEDSLRKELIALQEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNtedec 286
Cdd:pfam15921 366 DQFSQESGNLDDQLQKLladlHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKS----- 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 287 thlkEMNERTQEELRELANKyNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQAD 366
Cdd:pfam15921 441 ----ECQGQMERQMAAIQGK-NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAT 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 367 N----------DFTNERLTALQVRLEHLQEkTLKECSSLEKLIVEGhlTKAVEETKLSKENQTR--AKESDFSDTLSPSK 434
Cdd:pfam15921 516 NaeitklrsrvDLKLQELQHLKNEGDHLRN-VQTECEALKLQMAEK--DKVIEILRQQIENMTQlvGQHGRTAGAMQVEK 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 435 EKSSDDTTDAQMDEQDLNeplakvsllkaLLEEERKAYRNQVEESTKQIQVLQAQLqrLHIDTENLREEKD--------- 505
Cdd:pfam15921 593 AQLEKEINDRRLELQEFK-----------ILKDKKDAKIRELEARVSDLELEKVKL--VNAGSERLRAVKDikqerdqll 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 506 SEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWR--------------KAASEYEKEITSL 571
Cdd:pfam15921 660 NEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRntlksmegsdghamKVAMGMQKQITAK 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 572 QNsfQLRCQQCEDQQREEATR--------LQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQ----KQS 639
Cdd:pfam15921 740 RG--QIDALQSKIQFLEEAMTnankekhfLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEvaldKAS 817
|
570 580 590
....*....|....*....|....*....|....*.
gi 1799135562 640 LELTSDLSILQmsRKELENQvgSLKEQHLRDSADLK 675
Cdd:pfam15921 818 LQFAECQDIIQ--RQEQESV--RLKLQHTLDVKELQ 849
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
161-642 |
5.45e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 5.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 161 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQeasdtswqalidedRLLSRLEVMGNQLQACSKNQTEdsLRKEL 240
Cdd:PRK03918 291 KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIE--------------ERIKELEEKEERLEELKKKLKE--LEKRL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 241 IALQEDKHNYETTakeslrRVLQEKIEVVRKlSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSD- 319
Cdd:PRK03918 355 EELEERHELYEEA------KAKKEELERLKK-RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKa 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 320 --KLKVAEGK------------QEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALqadndftnerltalqvrlehlq 385
Cdd:PRK03918 428 ieELKKAKGKcpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL---------------------- 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 386 EKTLKECSSLEKLIVEGHLTKAVEEtKLSKENqtrakesdfsdtlspsKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALL 465
Cdd:PRK03918 486 EKVLKKESELIKLKELAEQLKELEE-KLKKYN----------------LEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 466 EEErKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDtDIASLQE 545
Cdd:PRK03918 549 EKL-EELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEK-ELKKLEE 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 546 ELKKVRAELERWRKAASEYEKEITSLQNSFQlrcqqcedqqREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSEL 625
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKYS----------EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTL 696
|
490
....*....|....*..
gi 1799135562 626 QRQEKELHNSQKQSLEL 642
Cdd:PRK03918 697 EKLKEELEEREKAKKEL 713
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
228-733 |
5.99e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 5.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 228 SKNQTEDSLRKELIALQEDKHNYETTA------KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEmNERTQEELR 301
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKELEELKeeieelEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE-KVKELKELK 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 302 ELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHK---IDEMEEKEQELQAKIEALQADNDfTNERLT 375
Cdd:PRK03918 290 EKAEEYiklSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKeerLEELKKKLKELEKRLEELEERHE-LYEEAK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 376 ALQVRLEHLQEKtlKECSSLEKLIVEGHLTKAVEETKLSKENQTRAKESdfsdtlspSKEKSSDDTTDAQMDeqdLNEPL 455
Cdd:PRK03918 369 AKKEELERLKKR--LTGLTPEKLEKELEELEKAKEEIEEEISKITARIG--------ELKKEIKELKKAIEE---LKKAK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 456 AKVSLLKALLEEERKAyrNQVEESTKQIQVLQAQLQRLHIDTENLREEKdseitSTRDELLSARDEILLLHQAAAKVASE 535
Cdd:PRK03918 436 GKCPVCGRELTEEHRK--ELLEEYTAELKRIEKELKEIEEKERKLRKEL-----RELEKVLKKESELIKLKELAEQLKEL 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 536 RDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFqlrcqqcedqqrEEATRLQGELEKLRKEWNALETECHSLK 615
Cdd:PRK03918 509 EEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL------------EKLEELKKKLAELEKKLDELEEELAELL 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 616 RENVLLS----SELQRQEKELHNSQKQSLELT---SDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSK-------- 680
Cdd:PRK03918 577 KELEELGfesvEELEERLKELEPFYNEYLELKdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEleelekky 656
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1799135562 681 AENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 733
Cdd:PRK03918 657 SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
238-733 |
2.89e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 238 KELIALQEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTqEELRELANKYNGavnEIKDL 317
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI-EELEKELESLEG---SKRKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 318 SDKLKVAEGKQEEIqqkgQAEKKELQHKIDEMEEKEqELQAKIEALQADNDFTNERLTALQVRLEHLQ------EKTLKE 391
Cdd:PRK03918 258 EEKIRELEERIEEL----KKEIEELEEKVKELKELK-EKAEEYIKLSEFYEEYLDELREIEKRLSRLEeeingiEERIKE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 392 CSSLEKLIVEghLTKAVEETKlSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKA 471
Cdd:PRK03918 333 LEEKEERLEE--LKKKLKELE-KRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISK 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 472 YRNQVEESTKQIQVLQAQLQRLhidtenlreEKDSEITSTRDELLSARDEILLLHQAAAKVASERDtDIASLQEELKKVR 551
Cdd:PRK03918 410 ITARIGELKKEIKELKKAIEEL---------KKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEK-ELKEIEEKERKLR 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 552 AELERWRKAASEYEKEITSLQNSFQLRC--QQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRE---NVLLSSELQ 626
Cdd:PRK03918 480 KELRELEKVLKKESELIKLKELAEQLKEleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKElekLEELKKKLA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 627 RQEKELHNSQKQSLELTSDLSILQM-SRKELENQVGSLKEQHlrdsadlktllsKAENQAKDVQKEYEKTQTVLSELKLK 705
Cdd:PRK03918 560 ELEKKLDELEEELAELLKELEELGFeSVEELEERLKELEPFY------------NEYLELKDAEKELEREEKELKKLEEE 627
|
490 500
....*....|....*....|....*...
gi 1799135562 706 FEMTEQEKQSITDELKQCKNNLKLLREK 733
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKK 655
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-733 |
5.12e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.08 E-value: 5.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 197 QEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTE-----DSLRKELIALQEDKHNYETTAKESLRRV--LQEKIE-V 268
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKlteeyAELKEELEDLRAELEEVDKEFAETRDELkdYREKLEkL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 269 VRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKE---LQHK 345
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQElydLKEE 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 346 IDEMEEKEQELQAKIEALQADNDFTNER-----------------LTALQVRLEHLQEKTLKECSS-----LEKLIVEGH 403
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEAQARASEERvrggraveevlkasiqgVHGTVAQLGSVGERYATAIEVaagnrLNNVVVEDD 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 404 LTkAVEETKLSKE-----------NQTRAKESDfsdtLSPSKEKSSDDTTDAQMDEQDLNEPLAK--------------- 457
Cdd:TIGR02169 558 AV-AKEAIELLKRrkagratflplNKMRDERRD----LSILSEDGVIGFAVDLVEFDPKYEPAFKyvfgdtlvvedieaa 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 458 ---------VSLLKALLE----------EERKAYRNQVEESTKqIQVLQAQLQRLHIDTENLREEKDsEITSTRDELLSA 518
Cdd:TIGR02169 633 rrlmgkyrmVTLEGELFEksgamtggsrAPRGGILFSRSEPAE-LQRLRERLEGLKRELSSLQSELR-RIENRLDELSQE 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 519 RDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQlrcqqcedQQREEATRLQGELE 598
Cdd:TIGR02169 711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE--------ELEEDLHKLEEALN 782
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 599 KL-----RKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSL-KEQHL--RD 670
Cdd:TIGR02169 783 DLearlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIeKEIENlnGK 862
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799135562 671 SADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 733
Cdd:TIGR02169 863 KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
465-732 |
8.68e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 8.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 465 LEEERKAYRNQVEESTKQIQVLQAQLQ-----------RLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVA 533
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISelekrleeieqLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 534 SER---DTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQRE------EATRLQGELEKLRKEW 604
Cdd:TIGR02169 315 RELedaEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEleevdkEFAETRDELKDYREKL 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 605 NALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADlktlLSKAENQ 684
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD----LSKYEQE 470
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1799135562 685 AKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLRE 732
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| CC1_T3JAM |
cd21912 |
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ... |
164-204 |
9.23e-09 |
|
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; TRAF3-interacting JNK-activating modulator (T3JAM), also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. The model corresponds to a conserved region that shows high sequence similarity with the first CC (CC1) domain of Sarcolemmal membrane-associated protein (SLMAP), which is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409288 [Multi-domain] Cd Length: 45 Bit Score: 51.58 E-value: 9.23e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1799135562 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21912 5 EILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
|
|
| FHA_TCF19 |
cd22685 |
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ... |
29-119 |
1.05e-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: 54.34 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 29 KIGRSVARCRPAQNNATFDcKVLSRNHALVW---FDHKTGKFYLQDTkSSNGTFINSQRLSRGSEEsppcEILSGDIIQF 105
Cdd:cd22685 31 RIGRNPEVCDVFLCSSQHP-NLISREHAEIHaerDGNGNWKVLIEDR-STNGTYVNDVRLQDGQRR----ELSDGDTITF 104
|
90
....*....|....*.
gi 1799135562 106 G--VDVTENTRKVTHG 119
Cdd:cd22685 105 GhkNGRRVKQWPYQKS 120
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
177-728 |
2.28e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 57.72 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 177 HREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQL--QACSKNQTEDSLRKELIALQEDKHNYetta 254
Cdd:TIGR04523 33 TEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILeqQIKDLNDKLKKNKDKINKLNSDLSKI---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 255 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQK 334
Cdd:TIGR04523 109 NSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 335 GQAEKKELQHK------IDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLKECSSLEKLIVEGHLTKAV 408
Cdd:TIGR04523 189 IDKIKNKLLKLelllsnLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 409 EETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMD-EQDLNEPLAKVsllkallEEERKAYRNQVEESTKQIQVLQ 487
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDwNKELKSELKNQ-------EKKLEEIQNQISQNNKIISQLN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 488 AQLQRLHIDTENLR----------EEKDSEITSTRDELLSARDEILLLH----------QAAAKVASERDTDIASLQEEL 547
Cdd:TIGR04523 342 EQISQLKKELTNSEsensekqrelEEKQNEIEKLKKENQSYKQEIKNLEsqindleskiQNQEKLNQQKDEQIKKLQQEK 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 548 KKVRAELERWRKAASEYEKEITSLQNsfqlrcqqcedqqreEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQR 627
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTN---------------QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQ 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 628 QEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQhlrdSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFE 707
Cdd:TIGR04523 487 KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK----IEKLESEKKEKESKISDLEDELNKDDFELKKENLEKE 562
|
570 580
....*....|....*....|.
gi 1799135562 708 MteQEKQSITDELKQCKNNLK 728
Cdd:TIGR04523 563 I--DEKNKEIEELKQTQKSLK 581
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
289-733 |
2.54e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 289 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKgQAEKKELQHKIDEMEEKEQELQAKIEALQADND 368
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 369 F--TNERLTALQVRLEHLQEKtlkecssLEKLIVEGHLTKAVEETKLSKENQTRAKESDFsdtlspsKEKSSDDTTDAQM 446
Cdd:COG4717 127 LlpLYQELEALEAELAELPER-------LEELEERLEELRELEEELEELEAELAELQEEL-------EELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 447 DEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHiDTENLREEKDS--------EITSTRDELLSA 518
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA-LEERLKEARLLlliaaallALLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 519 RDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRcqqcEDQQREEATRLQGELE 598
Cdd:COG4717 272 ILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLP----PDLSPEELLELLDRIE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 599 KLRKEWNALETECHSLKRE------NVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQ-HLRDS 671
Cdd:COG4717 348 ELQELLREAEELEEELQLEeleqeiAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELlEALDE 427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799135562 672 ADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEK--QSITDELKQCKNNLKLLREK 733
Cdd:COG4717 428 EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRELAEE 491
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
14-110 |
2.54e-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: 52.23 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 14 SHPFQERHV---YLDEPIKIGRSvARCRPAQNNATfdckvLSRNHALVW---FDHKTG-KFYLQDTkSSNGTFINSQRLS 86
Cdd:cd22670 7 SSPGSTDIVlpiYKNQVITIGRS-PSCDIVINDPF-----VSRTHCRIYsvqFDESSApLVYVEDL-SSNGTYLNGKLIG 79
|
90 100
....*....|....*....|....*
gi 1799135562 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 ... |
162-522 |
3.89e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 162 SQELFQLSQY--LQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQL---QACSKNQTEDsL 236
Cdd:TIGR02169 664 GGILFSRSEPaeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLeqeEEKLKERLEE-L 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 237 RKELIALQEDKHNYEttakeslrrvlQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQ-EELRELANKYNGAVNEIK 315
Cdd:TIGR02169 743 EEDLSSLEQEIENVK-----------SELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 316 DLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQV-------RLEHLQEKT 388
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAalrdlesRLGDLKKER 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 389 LKECSSLEKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTD--AQMDEQDLNEPLAKVSLLKALLE 466
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeEELSLEDVQAELQRVEEEIRALE 971
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1799135562 467 EERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEI 522
Cdd:TIGR02169 972 PVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAI 1027
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
28-85 |
4.18e-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: 4.18e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135562 28 IKIGRSvarcrPAQNNATFDCKVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRL 85
Cdd:smart00240 1 VTIGRS-----SEDCDIQLDGPSISRRHAVIVYD-GGGRFYLIDLGSTNGTFVNGKRI 52
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
182-638 |
4.36e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 182 LEQKLATLQRLLAI----TQEASDTSWQALIDEDRllSRLEVMGNQLQACSknQTEDSLRKELIALQEDKHNYETTAKES 257
Cdd:COG4913 267 ARERLAELEYLRAAlrlwFAQRRLELLEAELEELR--AELARLEAELERLE--ARLDALREELDELEAQIRGNGGDRLEQ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 258 LRRVLQEKievVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQA 337
Cdd:COG4913 343 LEREIERL---ERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 338 EKKELQHKIDEMEEK----EQELQAKIEALQADNDFTNERL----TALQVRLEHLQEKTlkecsSLEK--------LIVE 401
Cdd:COG4913 420 ELRELEAEIASLERRksniPARLLALRDALAEALGLDEAELpfvgELIEVRPEEERWRG-----AIERvlggfaltLLVP 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 402 GH----LTKAVEETKL-------------SKENQTRA-----------KESDFSDTLSPSKEKSSD----DTTDA----- 444
Cdd:COG4913 495 PEhyaaALRWVNRLHLrgrlvyervrtglPDPERPRLdpdslagkldfKPHPFRAWLEAELGRRFDyvcvDSPEElrrhp 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 445 -------------QMDEQDLNEPLAKVSLL-------KALLEEERKAYRNQVEESTKQIQVLQAQLQRLhiDTENLREEK 504
Cdd:COG4913 575 raitragqvkgngTRHEKDDRRRIRSRYVLgfdnrakLAALEAELAELEEELAEAEERLEALEAELDAL--QERREALQR 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 505 DSEITSTRDELLSARDEILLLHQAAAKVaSERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFqlrcQQCED 584
Cdd:COG4913 653 LAEYSWDEIDVASAEREIAELEAELERL-DASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL----EQAEE 727
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799135562 585 QQREEATRLQGELEKLRKEWNA-LETECHSLKRENVL------LSSELQRQEKELHNSQKQ 638
Cdd:COG4913 728 ELDELQDRLEAAEDLARLELRAlLEERFAAALGDAVErelrenLEERIDALRARLNRAEEE 788
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
465-728 |
4.41e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 465 LEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLRE---EKDSEITSTRDELLSARDEI-----------LLLHQAAA 530
Cdd:TIGR02169 700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKErleELEEDLSSLEQEIENVKSELkelearieeleEDLHKLEE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 531 KV----ASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQ----------NSFQLRCQQCEDQQREEATR---- 592
Cdd:TIGR02169 780 ALndleARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTlekeylekeiQELQEQRIDLKEQIKSIEKEienl 859
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 593 ------LQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQ 666
Cdd:TIGR02169 860 ngkkeeLEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDP 939
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135562 667 HLRDSADLKTLLS----KAENQAKDVQ------------KEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCkNNLK 728
Cdd:TIGR02169 940 KGEDEEIPEEELSledvQAELQRVEEEiralepvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY-EKKK 1016
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
276-727 |
5.37e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 56.72 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 276 ERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAE---GKQEEIQQKGQAEKKELQHKIDEMEEK 352
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETelcAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 353 EQELQAKIEALQADNDFTNERLTALQVRLEhlQEKTLKECSSLEKLIVEGHLTKAVEET--------KLSKE-NQTRAKE 423
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLD--EEEAARQKLQLEKVTTEAKIKKLEEDIllledqnsKLSKErKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 424 SDFSDTLSPSKEKSSDDTTDAQMDE---QDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTenl 500
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEamiSDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQL--- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 501 rEEKDSEITSTRDELlsarDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQ 580
Cdd:pfam01576 239 -AKKEEELQAALARL----EEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 581 QCEDQQREEATRLQgELEKLRKewnALETECHslkrenvllSSELQRQEKELHNSQkQSLELTSDLSILQMSRKELENQV 660
Cdd:pfam01576 314 TTAAQQELRSKREQ-EVTELKK---ALEEETR---------SHEAQLQEMRQKHTQ-ALEELTEQLEQAKRNKANLEKAK 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135562 661 GSLKEQHLRDSADLKTLlskaeNQAK-DVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNL 727
Cdd:pfam01576 380 QALESENAELQAELRTL-----QQAKqDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSEL 442
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
182-558 |
6.58e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.20 E-value: 6.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 182 LEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgnqlqacSKNQTEDSLRKELIALQEDKHNYETTaKESLRRV 261
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHE---------ERREELETLEAEIEDLRETIAETERE-REELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 262 LQEKIEVVRKLSEVERSL-----------SNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEE 330
Cdd:PRK02224 281 VRDLRERLEELEEERDDLlaeaglddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 331 IQQKGQAEKKELQH---KIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQE---------KTLK-ECSSLEK 397
Cdd:PRK02224 361 LREEAAELESELEEareAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREerdelrereAELEaTLRTARE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 398 LIVEGHltKAVEETKLSKENQTrAKESDFSDTLSPSKEKSSD---DTTDAQMDEQDLNEPLAKVSLLKAL------LEEE 468
Cdd:PRK02224 441 RVEEAE--ALLEAGKCPECGQP-VEGSPHVETIEEDRERVEEleaELEDLEEEVEEVEERLERAEDLVEAedrierLEER 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 469 RKAYRNQVEESTKQIQVLQAQLQRLHIDTENLR---EEKDSEITSTRDELLSARDEILLLHQAAAKVASERDT--DIASL 543
Cdd:PRK02224 518 REDLEELIAERRETIEEKRERAEELRERAAELEaeaEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESleRIRTL 597
|
410
....*....|....*
gi 1799135562 544 QEELKKVRAELERWR 558
Cdd:PRK02224 598 LAAIADAEDEIERLR 612
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
152-609 |
1.23e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 152 KVAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDtswqaliDEDRLLSRLEVMGNQLQACSKNQ 231
Cdd:COG4717 60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA-------ELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 232 TEDSLRKELIALQEdkhnyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKE-MNERTQEELRELANKYNGA 310
Cdd:COG4717 133 ELEALEAELAELPE--------RLEELEERLEELRELEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 311 VNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQektlk 390
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVL----- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 391 ecsslekLIVEGHLtkAVEETKLSKENQTRAKESDFSDTLsPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLE-EER 469
Cdd:COG4717 280 -------FLVLGLL--ALLFLLLAREKASLGKEAEELQAL-PALEELEEEELEELLAALGLPPDLSPEELLELLDRiEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 470 KAYRNQVEESTKQIQVLQAQ------LQRLHIDTEN---LREEKDSEITSTRDELLSARDEI-----LLLHQAAAKVASE 535
Cdd:COG4717 350 QELLREAEELEEELQLEELEqeiaalLAEAGVEDEEelrAALEQAEEYQELKEELEELEEQLeellgELEELLEALDEEE 429
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799135562 536 RDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLrcqqceDQQREEATRLQGELEKLRKEWNALET 609
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL------AELLQELEELKAELRELAEEWAALKL 497
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
310-572 |
2.00e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 310 AVNEIKDLSDKLKVAEGKQEEIQqkgqAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKtl 389
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQ----AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 390 kecssLEKLIveghltkaveetklsKENQTRAKESDFSDTLSpskekSSDDTTDAqmdeqdlnepLAKVSLLKALLEEER 469
Cdd:COG3883 88 -----LGERA---------------RALYRSGGSVSYLDVLL-----GSESFSDF----------LDRLSALSKIADADA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 470 KAyrnqveesTKQIQVLQAQLqrlhidtenlrEEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKK 549
Cdd:COG3883 133 DL--------LEELKADKAEL-----------EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193
|
250 260
....*....|....*....|...
gi 1799135562 550 VRAELERWRKAASEYEKEITSLQ 572
Cdd:COG3883 194 AEAQLAELEAELAAAEAAAAAAA 216
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
322-715 |
2.69e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 53.98 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 322 KVAEGKQEEIQQKGQAEKKELQHKidemeEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLKECSSLEKLIVE 401
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHK-----RARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 402 GHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRN---QVEE 478
Cdd:pfam05557 78 NRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEaeqLRQN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 479 STKQIQVLQAQLQRLH-IDTENLREEKDSEITST-RDELLS---------------------ARDEILL---LHQAAAKV 532
Cdd:pfam05557 158 LEKQQSSLAEAEQRIKeLEFEIQSQEQDSEIVKNsKSELARipelekelerlrehnkhlnenIENKLLLkeeVEDLKRKL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 533 ASERDT--DIASLQEELKKVRAELERWRKAASEYEKEITS--LQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALE 608
Cdd:pfam05557 238 EREEKYreEAATLELEKEKLEQELQSWVKLAQDTGLNLRSpeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 609 TECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDL----SILQMSRKELENQVGSlkEQHLRDSADLKTLLSKAENQ 684
Cdd:pfam05557 318 QELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgyrAILESYDKELTMSNYS--PQLLERIEEAEDMTQKMQAH 395
|
410 420 430
....*....|....*....|....*....|.
gi 1799135562 685 AKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 715
Cdd:pfam05557 396 NEEMEAQLSVAEEELGGYKQQAQTLERELQA 426
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
257-521 |
2.73e-07 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 54.16 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 257 SLRRVLQEKIEVVRKLSEVERslsnteDECTHLKEmNERTqEELRELANKYNGAVNEIKDLSDKLKVAEGKQ-------- 328
Cdd:PRK05771 13 TLKSYKDEVLEALHELGVVHI------EDLKEELS-NERL-RKLRSLLTKLSEALDKLRSYLPKLNPLREEKkkvsvksl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 329 EEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTnERLTALQVRLEHLQEKTLKEcssleklIVEGHLTKAV 408
Cdd:PRK05771 85 EELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERL-EPWGNFDLDLSLLLGFKYVS-------VFVGTVPEDK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 409 EETKLSKENQTRAKESDFSDTLSP-----SKEkssddttdaqmDEQDLNEPLAKVSLLKALLEEERKAYRnQVEESTKQI 483
Cdd:PRK05771 157 LEELKLESDVENVEYISTDKGYVYvvvvvLKE-----------LSDEVEEELKKLGFERLELEEEGTPSE-LIREIKEEL 224
|
250 260 270
....*....|....*....|....*....|....*...
gi 1799135562 484 QVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDE 521
Cdd:PRK05771 225 EEIEKERESLLEELKELAKKYLEELLALYEYLEIELER 262
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
229-667 |
2.93e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 54.28 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 229 KNQTEDSLRK---ELIALQEDKHNYettakeslRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELA- 304
Cdd:TIGR00606 586 INQTRDRLAKlnkELASLEQNKNHI--------NNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAm 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 305 -----NKYNGAVNEIKD-------LSDKLKVAEGKQEEIQQKGQA-------EKKELQHKIDEMEEKEQELQAKIEALQA 365
Cdd:TIGR00606 658 lagatAVYSQFITQLTDenqsccpVCQRVFQTEAELQEFISDLQSklrlapdKLKSTESELKKKEKRRDEMLGLAPGRQS 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 366 DNDFTNERLTALQVRLEHLQEKTLKECSSLEKliVEGHLTKAVEETKLSKENQT----------RAKESDFSDTLSPSKE 435
Cdd:TIGR00606 738 IIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE--QETLLGTIMPEEESAKVCLTdvtimerfqmELKDVERKIAQQAAKL 815
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 436 KSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAyrnqVEESTKQIQVLQAQL-----QRLHIDT--------ENLRE 502
Cdd:TIGR00606 816 QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKL----IQDQQEQIQHLKSKTnelksEKLQIGTnlqrrqqfEEQLV 891
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 503 EKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQC 582
Cdd:TIGR00606 892 ELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDY 971
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 583 EDQQREEATRLQGEL-------EKLRKEWNALETECHSLKRENVLLSSELQRQE-----KELHNSQKQSLELTSDLSILQ 650
Cdd:TIGR00606 972 LKQKETELNTVNAQLeecekhqEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKrenelKEVEEELKQHLKEMGQMQVLQ 1051
|
490
....*....|....*....
gi 1799135562 651 MSR--KELENQVGSLKEQH 667
Cdd:TIGR00606 1052 MKQehQKLEENIDLIKRNH 1070
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
27-106 |
3.37e-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: 49.16 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 27 PIKIGRSVARcRPAQNNATFDC-----KVLSRNHALVWFDHKTGKFYLQdTKSSNGTFINSQRLSRGseeSPPCEILSGD 101
Cdd:cd22701 18 EVVLGRNSKN-SSSTAADSVDIdlgpsKKISRRHARIFYDFTTQCFELS-VLGRNGVKVDGILVKPG---SPPVPLRSGS 92
|
....*
gi 1799135562 102 IIQFG 106
Cdd:cd22701 93 LIQIG 97
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
460-638 |
3.49e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 460 LLKALLEEERKAYR----------NQVEESTKQIQVLQAQLQRLHIDTENLrEEKDSEITSTRDELLSARDEILLLHQAA 529
Cdd:COG4717 47 LLERLEKEADELFKpqgrkpelnlKELKELEEELKEAEEKEEEYAELQEEL-EELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 530 AKVA-----SERDTDIASLQEELKKVRAELERWRKAASEY---EKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLR 601
Cdd:COG4717 126 QLLPlyqelEALEAELAELPERLEELEERLEELRELEEELeelEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190
....*....|....*....|....*....|....*..
gi 1799135562 602 KEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQ 638
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
26-106 |
8.11e-07 |
|
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: 47.79 E-value: 8.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 26 EPIKIGRSVArcrpaqNNATFDCKVLSRNHALVwfDHKTGKFYLQDTKSSNGTFINSQRLSRGseesppcEILSGDIIQF 105
Cdd:cd22698 21 DEFTIGRSSN------NDIRLNDHSVSRHHARI--VRQGDKCNLTDLGSTNGTFLNGIRVGTH-------ELKHGDRIQL 85
|
.
gi 1799135562 106 G 106
Cdd:cd22698 86 G 86
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
25-114 |
8.78e-07 |
|
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: 48.12 E-value: 8.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 25 DEPIKIGRSVArcrpAQNNATFDC-KVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDII 103
Cdd:cd22663 20 GKEVTVGRGLG----VTYQLVSTCpLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERI----EPLKPYPLNEGDLI 90
|
90
....*....|.
gi 1799135562 104 QFGVDVTENTR 114
Cdd:cd22663 91 QLGVPPENKEP 101
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
234-659 |
9.04e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 9.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 234 DSLRKELIALQEDKHNYETtAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNER--TQEELRELANKYNGAV 311
Cdd:COG4717 74 KELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELeaLEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 312 NEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEK---- 387
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEleql 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 388 -TLKECSSLEKLIVEGHLTKAVEETKLSKENQTRAKESDFSDT----------LSPSKEKSSDDTTDAQMDEQDLNEPLA 456
Cdd:COG4717 233 eNELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIagvlflvlglLALLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 457 KVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHidtENLREEKDSEITSTRDELLSARDEILllhqAAAKVASER 536
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ---ELLREAEELEEELQLEELEQEIAALL----AEAGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 537 D-TDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQL-RCQQCEDQQREEATRLQGELEKLRKEWNALETECHSL 614
Cdd:COG4717 386 ElRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEeELEEELEELEEELEELEEELEELREELAELEAELEQL 465
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1799135562 615 KRENVL--LSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQ 659
Cdd:COG4717 466 EEDGELaeLLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
55-108 |
1.18e-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: 47.31 E-value: 1.18e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1799135562 55 HALVWFDHKTGKFYLQDTKSSNGTFINSQRLSrgseESPPCEILSGDIIQFGVD 108
Cdd:cd22704 39 HAVITYDQIDNEFKIKDLGSLNGTFVNDSRIP----EQTYITLKLGDSIRFGYD 88
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
461-715 |
1.25e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 461 LKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDseITSTRDELLSARDEIlllhqaaakvaSERDTDI 540
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG--LVDLSEEAKLLLQQL-----------SELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 541 ASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRcqqcedQQREEATRLQGELEKLRKEWnaleTECHSLKREnvl 620
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQ------QLRAQLAELEAELAELSARY----TPNHPDVIA--- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 621 LSSELQRQEKELHNSQKQSL-ELTSDLSILQMSRKELENQVGSLKEQHLRdsadlktlLSKAENQAKDVQKEYEKTQTVL 699
Cdd:COG3206 296 LRAQIAALRAQLQQEAQRILaSLEAELEALQAREASLQAQLAQLEARLAE--------LPELEAELRRLEREVEVARELY 367
|
250
....*....|....*.
gi 1799135562 700 SELKLKFEMTEQEKQS 715
Cdd:COG3206 368 ESLLQRLEEARLAEAL 383
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
237-698 |
1.37e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.83 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 237 RKELIALQEDKHNYETTAK--ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERtQEELRELANKYNGAVNEI 314
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQilSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQ-ILELEGYEMDYNSYLKSI 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 315 KDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTlkecss 394
Cdd:PRK01156 373 ESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNM------ 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 395 lekLIVEGHLTKAVEETKLSKENQTRAKEsDFSDTLSPSKEkssdDTTDAQMDEQDLNEplaKVSLLKALLEEERKAYRN 474
Cdd:PRK01156 447 ---EMLNGQSVCPVCGTTLGEEKSNHIIN-HYNEKKSRLEE----KIREIEIEVKDIDE---KIVDLKKRKEYLESEEIN 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 475 QVEESTKQIQVLQAQLQRLHIDTENLR------EEKDSEITSTRDELLSARDEILLlhqaaaKVASERDT-DIASLQEEL 547
Cdd:PRK01156 516 KSINEYNKIESARADLEDIKIKINELKdkhdkyEEIKNRYKSLKLEDLDSKRTSWL------NALAVISLiDIETNRSRS 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 548 KKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQ------QREEATRLQGELEKLRKewnaletechslKRENvll 621
Cdd:PRK01156 590 NEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEannlnnKYNEIQENKILIEKLRG------------KIDN--- 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 622 sseLQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLS---KAENQAKDVQKEYEKTQTV 698
Cdd:PRK01156 655 ---YKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTrinELSDRINDINETLESMKKI 731
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
210-549 |
1.48e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 210 EDRLLSRLEVMGNQLQacsKNQTEDSLRKELIALQEDKHNYETTAK--------ESLRRVLQEKIEVVRKLSEVERSLSN 281
Cdd:TIGR02169 186 IERLDLIIDEKRQQLE---RLRREREKAERYQALLKEKREYEGYELlkekealeRQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 282 TEDECTH----LKEMNER----TQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQ---QKGQAEKKELQHKIDEME 350
Cdd:TIGR02169 263 LEKRLEEieqlLEELNKKikdlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEerlAKLEAEIDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 351 EKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEK---TLKECSSLEKlivegHLTKAVEETKLSKENQTRakesdfs 427
Cdd:TIGR02169 343 REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEfaeTRDELKDYRE-----KLEKLKREINELKRELDR------- 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 428 dtLSPSKEKSSDDTTDAQMDEQDLNEPLAKvsllkalLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREekdsE 507
Cdd:TIGR02169 411 --LQEELQRLSEELADLNAAIAGIEAKINE-------LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKE----E 477
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1799135562 508 ITSTRDELLSARDEILLLhQAAAKVASERDTDIASLQEELKK 549
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEA-EAQARASEERVRGGRAVEEVLKA 518
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
266-561 |
1.55e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 266 IEVVRKLSEVERSLSNTEDECTHLkemnertqEELRELANKYNGAVNEIKDLSDKLKVAEgkqeeiQQKGQAEKKELQHK 345
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELL--------EPIRELAERYAAARERLAELEYLRAALR------LWFAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 346 IDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLKEcssLEKLIveghltkaveETKLSKENQTRAKESD 425
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ---LEREI----------ERLERELEERERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 426 FSDTLSPSKEKSSDdttdaqmDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLReEKD 505
Cdd:COG4913 364 LEALLAALGLPLPA-------SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE-RRK 435
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1799135562 506 SEITStrdELLSARDEIlllhqAAAKVASERDTDIASlqeELKKVRAELERWRKAA 561
Cdd:COG4913 436 SNIPA---RLLALRDAL-----AEALGLDEAELPFVG---ELIEVRPEEERWRGAI 480
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
437-666 |
1.60e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 437 SSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREE---KDSEITSTRD 513
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaeLEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 514 ELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQnsfqlrcqqcedQQREEATRL 593
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR------------ADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799135562 594 QGELEKLRKEWNALETEchsLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQ 666
Cdd:COG4942 166 RAELEAERAELEALLAE---LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
449-641 |
1.86e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 449 QDLNEPLAKVSLLKALLEEERKAYRnqVEESTKQIQVLQAQLQRLhidtENLREEKDSEITSTRDELLSARDEILLLHQA 528
Cdd:COG4913 258 RELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEEL----RAELARLEAELERLEARLDALREELDELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 529 AAKVASERdtdIASLQEELKKVRAELERWRKAASEYEKEITSLQNSfqlrcqqcEDQQREEATRLQGELEKLRKEWNALE 608
Cdd:COG4913 332 IRGNGGDR---LEQLEREIERLERELEERERRRARLEALLAALGLP--------LPASAEEFAALRAEAAALLEALEEEL 400
|
170 180 190
....*....|....*....|....*....|...
gi 1799135562 609 TECHSLKRENVLLSSELQRQEKELHNsQKQSLE 641
Cdd:COG4913 401 EALEEALAEAEAALRDLRRELRELEA-EIASLE 432
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
27-117 |
4.88e-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: 45.81 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 27 PIKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLsrgSEESPPCEILSGDIIQFG 106
Cdd:cd22678 24 PLTIGRIQ------RGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESI---SPNGRPVVLSSGDVITLG 94
|
90
....*....|.
gi 1799135562 107 vdvTENTRKVT 117
Cdd:cd22678 95 ---SETKILVR 102
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
229-736 |
6.04e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.72 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 229 KNQTEDSLRKELIALQEDKHNYETTAK---------ESLRRVLQEKIEVVRKLSEVERSlsnTEDECTHLKEMNERT--- 296
Cdd:pfam05483 94 KVSIEAELKQKENKLQENRKIIEAQRKaiqelqfenEKVSLKLEEEIQENKDLIKENNA---TRHLCNLLKETCARSaek 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 297 -------QEELRELANKYNGAVNEIKDLSDKLKV-AEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADND 368
Cdd:pfam05483 171 tkkyeyeREETRQVYMDLNNNIEKMILAFEELRVqAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQIT 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 369 FTNERLTALQVRLE-------HLQEKTLKECSSLEKLI-VEGHLTKAVEETKLSKENQTRAKESdFSDTLSPSKEKSSDD 440
Cdd:pfam05483 251 EKENKMKDLTFLLEesrdkanQLEEKTKLQDENLKELIeKKDHLTKELEDIKMSLQRSMSTQKA-LEEDLQIATKTICQL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 441 TTDAQMDEQDLNEPLAKVSLL-------KALLEEERKAYRNQVEESTKQIQVLQAQLQRlhidtenlreeKDSEItstrd 513
Cdd:pfam05483 330 TEEKEAQMEELNKAKAAHSFVvtefeatTCSLEELLRTEQQRLEKNEDQLKIITMELQK-----------KSSEL----- 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 514 ellsardeilllhQAAAKVASERDTDIaslqEELKKVRAELERWRKAASEYEKEITSLQNSFQlrcqqcedqqreeatRL 593
Cdd:pfam05483 394 -------------EEMTKFKNNKEVEL----EELKKILAEDEKLLDEKKQFEKIAEELKGKEQ---------------EL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 594 QGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSL---------- 663
Cdd:pfam05483 442 IFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMtlelkkhqed 521
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135562 664 ----KEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNN 736
Cdd:pfam05483 522 iincKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN 598
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
258-401 |
6.20e-06 |
|
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: 48.00 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 258 LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQ----- 332
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkey 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135562 333 QKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLKECSSLEKLIVE 401
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
162-711 |
8.08e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.44 E-value: 8.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 162 SQELFQLSQYLQEALHR----EQMLEQKLATLQRLLAITQEASDTSWQALIDEDRllsRLEVMGNQLQACSKNQTEDSLR 237
Cdd:pfam10174 129 AKELFLLRKTLEEMELRietqKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWER---TRRIAEAEMQLGHLEVLLDQKE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 238 KELIALQEDKH-NYETTAKESLRRVLQEKIEVV-RKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIK 315
Cdd:pfam10174 206 KENIHLREELHrRNQLQPDPAKTKALQTVIEMKdTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSK 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 316 DLsdKLKVAEGKQEeiQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQ-------VRLEHLQEKT 388
Cdd:pfam10174 286 FM--KNKIDQLKQE--LSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQtevdalrLRLEEKESFL 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 389 LKECSSLEKLIVE-GHLTKAVE------ETKLSKENQTRAKESDFSDTLSpSKEKSSDDTTDA--QMDEQDLNEPLAKVS 459
Cdd:pfam10174 362 NKKTKQLQDLTEEkSTLAGEIRdlkdmlDVKERKINVLQKKIENLQEQLR-DKDKQLAGLKERvkSLQTDSSNTDTALTT 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 460 LLKALLEEERKAYRNQvEESTKQIQVLQAQLQRLHIDTENLREEkdseITSTRDELLSARDEILLLHQAAAKVAS---ER 536
Cdd:pfam10174 441 LEEALSEKERIIERLK-EQREREDRERLEELESLKKENKDLKEK----VSALQPELTEKESSLIDLKEHASSLASsglKK 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 537 DTDIASLQEELKKVRAELERW----RKAASEYEKEITSLQNSFQLRCQQCEDQQ-REEATRLQGELEKLRKEWNALETEC 611
Cdd:pfam10174 516 DSKLKSLEIAVEQKKEECSKLenqlKKAHNAEEAVRTNPEINDRIRLLEQEVARyKEESGKAQAEVERLLGILREVENEK 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 612 HSLKRENVLLSSELQRQEKELHNSQKQsleltsdlsiLQMSRKELENQVGSLKEQHLRDSADLKTllSKAENQAKDVQKE 691
Cdd:pfam10174 596 NDKDKKIAELESLTLRQMKEQNKKVAN----------IKHGQQEMKKKGAQLLEEARRREDNLAD--NSQQLQLEELMGA 663
|
570 580
....*....|....*....|
gi 1799135562 692 YEKTQTVLSELKLKFEMTEQ 711
Cdd:pfam10174 664 LEKTRQELDATKARLSSTQQ 683
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
51-106 |
9.94e-06 |
|
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: 44.85 E-value: 9.94e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799135562 51 LSRNHALVWF----DHKTGKFYLQDTKSSNGTFINSQRLsrgseesPP---CEILSGDIIQFG 106
Cdd:cd22677 41 ISRYHAVLQYrgdaDDHDGGFYLYDLGSTHGTFLNKQRI-------PPkqyYRLRVGHVLKFG 96
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
52-106 |
1.16e-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: 44.95 E-value: 1.16e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135562 52 SRNH-ALVWfdHK-TGKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22674 48 SRVHaALVY--HKhLNRVFLIDLGSTHGTFVGGIRL----EPHKPQQLPIDSTLRFG 98
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
213-483 |
1.74e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.51 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 213 LLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTAKEslrrvlqeKIEVVRKLSEVERSlsntedecthlKEM 292
Cdd:TIGR01612 1455 LFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSKGC--------KDEADKNAKAIEKN-----------KEL 1515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 293 NERTQEELRELANKYNGAvnEIKDLSDKLK------VAEGKQEEIQQKGQAEKKElqHKIDEMEEKeqelQAKIEALQAD 366
Cdd:TIGR01612 1516 FEQYKKDVTELLNKYSAL--AIKNKFAKTKkdseiiIKEIKDAHKKFILEAEKSE--QKIKEIKKE----KFRIEDDAAK 1587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 367 NDFTNERLTALQVRLEHLQEKTLK-------------ECSSLEKLIveGHLTKAVEETKLSKENQTRAKESDFSDTLSPS 433
Cdd:TIGR01612 1588 NDKSNKAAIDIQLSLENFENKFLKisdikkkindclkETESIEKKI--SSFSIDSQDTELKENGDNLNSLQEFLESLKDQ 1665
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1799135562 434 KEKSSDDTTdaQMDEQDlneplAKVSLLKALLEEERKAYRNQVEESTKQI 483
Cdd:TIGR01612 1666 KKNIEDKKK--ELDELD-----SEIEKIEIDVDQHKKNYEIGIIEKIKEI 1708
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
28-106 |
1.75e-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: 43.87 E-value: 1.75e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135562 28 IKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDhkTGKFYLQDTKSSNGTFINSQRlsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22680 23 VSIGRDP------ENVIVIPDPFVSRNHARITVD--SNEIYIEDLGSTNGTFVNDFK-----RIKGPAKLHPNDIIKLG 88
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
228-733 |
2.01e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 228 SKNQTEDSLRKELIALQEDKHNYETT--AKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHlKEMNERTQEELR--EL 303
Cdd:PTZ00121 1120 AKKKAEDARKAEEARKAEDARKAEEArkAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAAR-KAEEVRKAEELRkaED 1198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 304 ANKYNGA--VNEIKDLSDKLKVAEGKQ-EEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVR 380
Cdd:PTZ00121 1199 ARKAEAArkAEEERKAEEARKAEDAKKaEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR 1278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 381 ----LEHLQEKTLKE---------------CSSLEKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDT 441
Cdd:PTZ00121 1279 kadeLKKAEEKKKADeakkaeekkkadeakKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE 1358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 442 TD-----AQMDEQDLNEPLAKVSLLKALLEEERKA--YRNQVEESTKQIQVL------QAQLQRLHIDTENLRE----EK 504
Cdd:PTZ00121 1359 AEaaeekAEAAEKKKEEAKKKADAAKKKAEEKKKAdeAKKKAEEDKKKADELkkaaaaKKKADEAKKKAEEKKKadeaKK 1438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 505 DSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAEL----ERWRKAASEYEKEITSLQNSFQLR-- 578
Cdd:PTZ00121 1439 KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAkkkaEEAKKKADEAKKAAEAKKKADEAKka 1518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 579 --CQQCEDQQREEATRLQGELEKLRKEWNALEtechsLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKEL 656
Cdd:PTZ00121 1519 eeAKKADEAKKAEEAKKADEAKKAEEKKKADE-----LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135562 657 ENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKlkfemTEQEKQSITDELKQCKNNLKLLREK 733
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK-----KEAEEKKKAEELKKAEEENKIKAAE 1665
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
258-693 |
2.01e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 47.76 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 258 LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKgQA 337
Cdd:pfam05622 2 LSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRL-ET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 338 EKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVrLEHLQEKTLKECSSLEkliveghltkaveetklsken 417
Cdd:pfam05622 81 ARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDI-LRESSDKVKKLEATVE--------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 418 qtrakesdfsdtlspSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAY---RNQVEESTKQIQVLQAQLQRLH 494
Cdd:pfam05622 139 ---------------TYKKKLEDLGDLRRQVKLLEERNAEYMQRTLQLEEELKKAnalRGQLETYKRQVQELHGKLSEES 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 495 IDTENLR------EEKDSEITSTRDELLSARD------EILLLHQAAAKVASERDTDIASLQEELKKVRAELerwrkAAS 562
Cdd:pfam05622 204 KKADKLEfeykklEEKLEALQKEKERLIIERDtlretnEELRCAQLQQAELSQADALLSPSSDPGDNLAAEI-----MPA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 563 EYEKEITSLQNSFQ-LRCQQcEDQQREEATRLQGELEKLRKEWNALETEcHSLKRENVLLSS----ELQRQEKELHNSQK 637
Cdd:pfam05622 279 EIREKLIRLQHENKmLRLGQ-EGSYRERLTELQQLLEDANRRKNELETQ-NRLANQRILELQqqveELQKALQEQGSKAE 356
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135562 638 QSLELTSDLSILQMSRKELENQVGSLKEQ--HLRDSADLKTLLSKAENQAKDVQKEYE 693
Cdd:pfam05622 357 DSSLLKQKLEEHLEKLHEAQSELQKKKEQieELEPKQDSNLAQKIDELQEALRKKDED 414
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
488-703 |
2.50e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 488 AQLQRLHIDTENLREEKD--SEITSTRDELLSARDEILLLHQAAAKVASERD-TDIASLQEELKKVRAELERWRKAASEY 564
Cdd:COG4913 235 DDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAqRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 565 EKEITSLQNsfqlRCQQCEDQQREEATRlqgELEKLRKEWNALETECHSLKREnvllSSELQRQEKELHnsqkqsLELTS 644
Cdd:COG4913 315 EARLDALRE----ELDELEAQIRGNGGD---RLEQLEREIERLERELEERERR----RARLEALLAALG------LPLPA 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135562 645 DLSILQMSRKELENQVGSLKEQHlrdsADLKTLLSKAENQAKDVQKEYEKTQTVLSELK 703
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEEL----EALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| FHA_RAD53-like_rpt2 |
cd22690 |
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
12-103 |
2.84e-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: 43.82 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 12 PNSHPfqerHVYL-DEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFD-HKTGK--FYLQDTkSSNGTFINSQRLSR 87
Cdd:cd22690 8 NPSYP----DIELtQNTTFIGRS------KDCDEEITDPRISKHHCIITRKrSGKGLddVYVTDT-STNGTFINNNRLGK 76
|
90
....*....|....*.
gi 1799135562 88 GSEesppCEILSGDII 103
Cdd:cd22690 77 GSQ----SLLQDGDEI 88
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
14-106 |
2.98e-05 |
|
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.
Pssm-ID: 438734 [Multi-domain] Cd Length: 96 Bit Score: 43.29 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 14 SHPFQERHvyldepIKIGRSVarcrpaQNNATFDCKVLSRNHALvwFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEesp 93
Cdd:cd22682 14 QFPITEST------IVIGRSV------ESQVQIDDDSVSRYHAK--LAVNPSAVSIIDLGSTNGTIVNGKKIPKLAS--- 76
|
90
....*....|...
gi 1799135562 94 pCEILSGDIIQFG 106
Cdd:cd22682 77 -CDLQNGDQIKIG 88
|
|
| FHA_CHFR |
cd22672 |
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ... |
49-105 |
3.49e-05 |
|
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: 43.43 E-value: 3.49e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135562 49 KVLSRNHALVWFDHKtGKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQF 105
Cdd:cd22672 39 KLVSGDHCKIIRDEK-GQVWLEDT-STNGTLVNKVKVVKGQK----VELKHGDVIYL 89
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
25-108 |
3.98e-05 |
|
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: 43.57 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 25 DEPIKIGRsvarcRPAQNNAT----FDCKVLSRNHALVWFdhKTGKFYLQDTKSSNGTFINSQRLSR-GSEESPPCEILS 99
Cdd:cd22702 31 KQPCIIGS-----DPHQAISGisvvIPSPQVSELHARITC--KNGAFFLTDLGSEHGTWINDNEGRRyRAPPNFPVRLHP 103
|
....*....
gi 1799135562 100 GDIIQFGVD 108
Cdd:cd22702 104 SDVIEFGSD 112
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
18-86 |
4.80e-05 |
|
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: 42.70 E-value: 4.80e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135562 18 QERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhkTGKFYLQDTKSSNGTFINSQRLS 86
Cdd:cd22694 8 GELRFDPGSSVRIGRD------PDADVRLDDPRVSRRHALLEFD--GDGWVYTDLGSRNGTYLNGRRVQ 68
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
271-610 |
5.63e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 5.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 271 KLSEVERSLSNTEDECTHLKEMNERTQEELRElankyngAVNEIKDLsdkLKVAEGKQEEIQQKGQaEKKELQHKIDEME 350
Cdd:TIGR04523 336 IISQLNEQISQLKKELTNSESENSEKQRELEE-------KQNEIEKL---KKENQSYKQEIKNLES-QINDLESKIQNQE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 351 EKEQELQAKIEALQADNDFTNERLTalqvRLEHLQEKTLKECSSLEKLIVEghLTKAVEETKLSKENQtRAKESDFSDTL 430
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIE----RLKETIIKNNSEIKDLTNQDSV--KELIIKNLDNTRESL-ETQLKVLSRSI 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 431 SPSKEKSSDDTTDAQMDEQDLNEplakvsllkalLEEERKAYRNQVEESTKQIQVLQAQLQRLhidtENLREEKDSEITS 510
Cdd:TIGR04523 478 NKIKQNLEQKQKELKSKEKELKK-----------LNEEKKELEEKVKDLTKKISSLKEKIEKL----ESEKKEKESKISD 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 511 TRDELLSARDEilLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQcedqqreeA 590
Cdd:TIGR04523 543 LEDELNKDDFE--LKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKK--------I 612
|
330 340
....*....|....*....|
gi 1799135562 591 TRLQGELEKLRKEWNALETE 610
Cdd:TIGR04523 613 SSLEKELEKAKKENEKLSSI 632
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
13-110 |
6.40e-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: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 13 NSHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTgkFYLQDTKSSNGTFINSQRLSrgsee 91
Cdd:cd22665 7 SQAHGPEKDFPLYEgENVIGRD------PSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRL----- 73
|
90 100
....*....|....*....|.
gi 1799135562 92 SPPC--EILSGDIIQFGvDVT 110
Cdd:cd22665 74 KPNVryELIDGDLLLFG-DVK 93
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
256-733 |
7.52e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.58 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 256 ESLRRVLQEKIEVVRK--LSEVERSLSNTEDECTHLKEMN--ERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEI 331
Cdd:TIGR01612 1058 DEIEKEIGKNIELLNKeiLEEAEINITNFNEIKEKLKHYNfdDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEI 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 332 QQKGQAEKKELQHKI----------------DEMEEKEQELQAKIEALQADNDFTNERLTAL------QVRLEHLQEKTL 389
Cdd:TIGR01612 1138 KKKSENYIDEIKAQIndledvadkaisnddpEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIaeiekdKTSLEEVKGINL 1217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 390 KECSSLEKLIVEghltkAVEETKLSKENQTRAKESDFSDtLSPSKEKSSDDTTDAQMdEQDLNEPLAKVSllkaLLEEER 469
Cdd:TIGR01612 1218 SYGKNLGKLFLE-----KIDEEKKKSEHMIKAMEAYIED-LDEIKEKSPEIENEMGI-EMDIKAEMETFN----ISHDDD 1286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 470 KAYRNQVEESTKQIQVLQAqlQRLHIDTENLREEKDSEITST-RDELLSARDEILLLHQAAAKVASERD----TDIASLQ 544
Cdd:TIGR01612 1287 KDHHIISKKHDENISDIRE--KSLKIIEDFSEESDINDIKKElQKNLLDAQKHNSDINLYLNEIANIYNilklNKIKKII 1364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 545 EELKKVRAELERWRKAA----SEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLK----- 615
Cdd:TIGR01612 1365 DEVKEYTKEIEENNKNIkdelDKSEKLIKKIKDDINLEECKSKIESTLDDKDIDECIKKIKELKNHILSEESNIDtyfkn 1444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 616 ----RENVLL--SSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENqvgslKEQHLRDSADLKtllSKAENQAKDVQ 689
Cdd:TIGR01612 1445 adenNENVLLlfKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHID-----KSKGCKDEADKN---AKAIEKNKELF 1516
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1799135562 690 KEYEKTQTVL------SELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 733
Cdd:TIGR01612 1517 EQYKKDVTELlnkysaLAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEK 1566
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
289-568 |
7.53e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.16 E-value: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 289 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALqadnd 368
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEEL----- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 369 ftNERLTALQVRLEhlqektlKECSSLEKLiveghltkAVEETKLSKENQTRAKESDF----------SDTLSPSKEKSS 438
Cdd:PHA02562 240 --TDELLNLVMDIE-------DPSAALNKL--------NTAAAKIKSKIEQFQKVIKMyekggvcptcTQQISEGPDRIT 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 439 DDTTDAQMDEQDLNEplakvsLLKALLEEERKAyrNQVEESTKQIQVLQAQLqrlhidtenlrEEKDSEITSTRDELLSA 518
Cdd:PHA02562 303 KIKDKLKELQHSLEK------LDTAIDELEEIM--DEFNEQSKKLLELKNKI-----------STNKQSLITLVDKAKKV 363
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1799135562 519 RDEIlllHQAAAKVASErdtdiaslQEELKKVRAELERWRKAASEYEKEI 568
Cdd:PHA02562 364 KAAI---EELQAEFVDN--------AEELAKLQDELDKIVKTKSELVKEK 402
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
460-610 |
8.13e-05 |
|
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: 46.21 E-value: 8.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 460 LLKALLEEERK--AYRNQVEESTKQIQVLQAQLQRLHIDTENLREE--KDSEITSTRDELLSARDEILLLHQAAAKvASE 535
Cdd:pfam13166 305 QLPAVSDLASLlsAFELDVEDIESEAEVLNSQLDGLRRALEAKRKDpfKSIELDSVDAKIESINDLVASINELIAK-HNE 383
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799135562 536 RDTDIASLQEELKKvraelERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREeATRLQGELEKLRKEWNALETE 610
Cdd:pfam13166 384 ITDNFEEEKNKAKK-----KLRLHLVEEFKSEIDEYKDKYAGLEKAINSLEKE-IKNLEAEIKKLREEIKELEAQ 452
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
153-388 |
8.54e-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: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 153 VAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQAcSKNQT 232
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA-ELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 233 EDSLRKELIALQEDKHNYETTAKESLRRVLQEKIEVV---RKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKyng 309
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLlspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL--- 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135562 310 aVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKT 388
Cdd:COG4942 166 -RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
251-556 |
8.69e-05 |
|
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: 46.12 E-value: 8.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 251 ETTAKESLRRVLQEKIEVVRKLSEVERSLSNTE----DECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEG 326
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKeqakKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 327 KQEEIQQKGQ---AEKKELQHKIDEMEEKEQELQ--------AKIEALQADNDFTNERLTALQVRLEHLQEKTLKECSSL 395
Cdd:pfam02463 251 EEIESSKQEIekeEEKLAQVLKENKEEEKEKKLQeeelkllaKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 396 EKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKAL-LEEERKAYRN 474
Cdd:pfam02463 331 KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELkSEEEKEAQLL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 475 QVEESTKQIQVLQAQLQRLHIDTEnlrEEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAEL 554
Cdd:pfam02463 411 LELARQLEDLLKEEKKEELEILEE---EEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLE 487
|
..
gi 1799135562 555 ER 556
Cdd:pfam02463 488 LL 489
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
216-733 |
1.15e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.66 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 216 RLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTaKESLRRVLQEKIEVVRKLSEVERSLSNTEDECthlkemnER 295
Cdd:PRK01156 151 RKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYL-EEKLKSSNLELENIKKQIADDEKSHSITLKEI-------ER 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 296 TQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIqQKGQAEKKELQHKIDEMEEKEQELqakiealqadNDFTNERLT 375
Cdd:PRK01156 223 LSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI-KTAESDLSMELEKNNYYKELEERH----------MKIINDPVY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 376 ALQVRL-EHLQEKtlKECSSLEKLI--VEGHLTKAVEETKLSKENQtrakeSDFSDTLSPSKEKSSDDT--TDAQMDEQD 450
Cdd:PRK01156 292 KNRNYInDYFKYK--NDIENKKQILsnIDAEINKYHAIIKKLSVLQ-----KDYNDYIKKKSRYDDLNNqiLELEGYEMD 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 451 LNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLR---EEKDSEITSTRDELLSARDEILLLHQ 527
Cdd:PRK01156 365 YNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINvklQDISSKVSSLNQRIRALRENLDELSR 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 528 AAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNAL 607
Cdd:PRK01156 445 NMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKI 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 608 ETECHSLKRenvLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELenqvgsLKEQHLRDSADLKTLLSKAENQAKD 687
Cdd:PRK01156 525 ESARADLED---IKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSW------LNALAVISLIDIETNRSRSNEIKKQ 595
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1799135562 688 VQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 733
Cdd:PRK01156 596 LNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQEN 641
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
52-107 |
2.24e-04 |
|
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: 41.16 E-value: 2.24e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799135562 52 SRNHALVWFDHKTG---------KFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQFGV 107
Cdd:cd22667 40 SRKHATLTVLHPEAnlsdpdtrpELTLKDL-SKYGTFVNGEKLKGGSE----VTLKDGDVITFGV 99
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
236-732 |
2.44e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.04 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 236 LRKELIALQEDKhNYETTAKESLRRVLQEKIEVVRKLSEveRSLSNTEDECTHLKEMNERTQEELRELankynGAVNEIK 315
Cdd:TIGR01612 1202 IEKDKTSLEEVK-GINLSYGKNLGKLFLEKIDEEKKKSE--HMIKAMEAYIEDLDEIKEKSPEIENEM-----GIEMDIK 1273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 316 DLSDKLKVAEGKQEEIQQKGQAEKKelqhKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQE--KTLKECS 393
Cdd:TIGR01612 1274 AEMETFNISHDDDKDHHIISKKHDE----NISDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQKHNSDinLYLNEIA 1349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 394 SLEKLIVEGHLTKAVEETK-----LSKENQTRAKESDFSDTLSPS-KEKSSDDT----TDAQMDEQDLNEPLAKVSLLKA 463
Cdd:TIGR01612 1350 NIYNILKLNKIKKIIDEVKeytkeIEENNKNIKDELDKSEKLIKKiKDDINLEEckskIESTLDDKDIDECIKKIKELKN 1429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 464 -LLEEERK--AYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEilllHQAAAKvaserdtdi 540
Cdd:TIGR01612 1430 hILSEESNidTYFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDHDFNINELKE----HIDKSK--------- 1496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 541 aSLQEELKKVRAELERWRKAASEYEKEITSLQNSF-QLRCQQCEDQQREEATRLQGELEKLRK----EWNALETECHSLK 615
Cdd:TIGR01612 1497 -GCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYsALAIKNKFAKTKKDSEIIIKEIKDAHKkfilEAEKSEQKIKEIK 1575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 616 RENVLLSSELQRQEKE----------LHNSQKQSLELTSDLSILQMSRKE---LENQVGSL----KEQHLRDSAD----L 674
Cdd:TIGR01612 1576 KEKFRIEDDAAKNDKSnkaaidiqlsLENFENKFLKISDIKKKINDCLKEtesIEKKISSFsidsQDTELKENGDnlnsL 1655
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799135562 675 KTLLSKAENQAKDVQKEYEKTQTVLSELK-LKFEMTEQEK-------QSITDELKQCKNNLKLLRE 732
Cdd:TIGR01612 1656 QEFLESLKDQKKNIEDKKKELDELDSEIEkIEIDVDQHKKnyeigiiEKIKEIAIANKEEIESIKE 1721
|
|
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
53-106 |
3.11e-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: 40.32 E-value: 3.11e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1799135562 53 RNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPceilsGDIIQFG 106
Cdd:cd22700 36 EQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAP-----GDVLRFG 84
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
1-106 |
3.17e-04 |
|
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: 43.98 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 1 MPSALAIFTCRPNSHPFQERHVYLDEPIKIGRSvARC-----RPAQnnatfdckVLSRNHALVWFDHktGKFYLQDTkSS 75
Cdd:COG3456 1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRS-ADCdwvlpDPDR--------SVSRRHAEIRFRD--GAFCLTDL-ST 68
|
90 100 110
....*....|....*....|....*....|...
gi 1799135562 76 NGTFIN--SQRLSRGSEEsppcEILSGDIIQFG 106
Cdd:COG3456 69 NGTFLNgsDHPLGPGRPV----RLRDGDRLRIG 97
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
443-631 |
3.66e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 443 DAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEI--------TSTRDE 514
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLralyrlgrQPPLAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 515 LLSARD-----EILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFqlrcQQCEDQQREE 589
Cdd:COG4942 125 LLSPEDfldavRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL----EALKAERQKL 200
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1799135562 590 ATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKE 631
Cdd:COG4942 201 LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
166-733 |
3.86e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.94 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 166 FQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDslRKELIalqe 245
Cdd:pfam05483 215 FKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDEN--LKELI---- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 246 DKHNYETTAKESLRRVLQEKIEVVRKLsevERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIK----DLSDKL 321
Cdd:pfam05483 289 EKKDHLTKELEDIKMSLQRSMSTQKAL---EEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEattcSLEELL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 322 KVAEGKQEEIQQKGQAEKKELQHKIDEMEE-------KEQELQAKIEALQADNDFTNER---------LTALQVRLEHLQ 385
Cdd:pfam05483 366 RTEQQRLEKNEDQLKIITMELQKKSSELEEmtkfknnKEVELEELKKILAEDEKLLDEKkqfekiaeeLKGKEQELIFLL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 386 EKTLKECSSLEKLIV-----EGHLTKAVEE--TKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMdeqdlneplakv 458
Cdd:pfam05483 446 QAREKEIHDLEIQLTaiktsEEHYLKEVEDlkTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTL------------ 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 459 sllkalleeERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEkdseITSTRDELLSARDEILLLHQAAAKVASERDT 538
Cdd:pfam05483 514 ---------ELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDE----LESVREEFIQKGDEVKCKLDKSEENARSIEY 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 539 DIASLQEELKKVRAELERWRKAASEYEKEITSLqnsfqlrcqqcedQQREEATRLQGELEKlrKEWNALETECHSLKREn 618
Cdd:pfam05483 581 EVLKKEKQMKILENKCNNLKKQIENKNKNIEEL-------------HQENKALKKKGSAEN--KQLNAYEIKVNKLELE- 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 619 vlLSSELQRQEKELHNSQKQ----SLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEK 694
Cdd:pfam05483 645 --LASAKQKFEEIIDNYQKEiedkKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEE 722
|
570 580 590
....*....|....*....|....*....|....*....
gi 1799135562 695 TQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 733
Cdd:pfam05483 723 RDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQ 761
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
322-665 |
4.34e-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: 43.59 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 322 KVAEGKQEEIQQKGQAeKKELQHKIDEMEEKEQELQAKIEALQADndftnerltALQVRLEHLQEKTLKECSSLEklive 401
Cdd:pfam09731 78 ESKEPKEEKKQVKIPR-QSGVSSEVAEEEKEATKDAAEAKAQLPK---------SEQEKEKALEEVLKEAISKAE----- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 402 gHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRN------- 474
Cdd:pfam09731 143 -SATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLdaapetp 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 475 --------QVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDEL----------LSARDEILLLH------QAAA 530
Cdd:pfam09731 222 pklpehldNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIipvlkednllSNDDLNSLIAHahreidQLSK 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 531 KVASERDTDIASLQEELKKVRAELERWRkaaseyEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETE 610
Cdd:pfam09731 302 KLAELKKREEKHIERALEKQKEELDKLA------EELSARLEEVRAADEAQLRLEFEREREEIRESYEEKLRTELERQAE 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135562 611 CHSLKRENVLLSSELQRQEKELHNSQKQSLE----LTSDLSILQMSRKELENQVGSLKE 665
Cdd:pfam09731 376 AHEEHLKDVLVEQEIELQREFLQDIKEKVEEeragRLLKLNELLANLKGLEKATSSHSE 434
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
589-735 |
5.16e-04 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 42.77 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 589 EATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNsQKQSLELTSDLSilqmsrkELENQVGSLKeqhl 668
Cdd:pfam15294 134 EIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGA-KKDVKSNLKEIS-------DLEEKMAALK---- 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135562 669 rdsADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGN 735
Cdd:pfam15294 202 ---SDLEKTLNASTALQKSLEEDLASTKHELLKVQEQLEMAEKELEKKFQQTAAYRNMKEMLTKKNE 265
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
534-733 |
5.43e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 534 SERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQ--LRCQQCEDQQRE-EATRLQGELEKLRKEWNALETE 610
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREkaERYQALLKEKREyEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 611 CHSLKRENVLLSSELQRQEKELHNS----------------------QKQSLELTSDLSILQMSRKELENQVGSLKEQHL 668
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIeqlleelnkkikdlgeeeqlrvKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135562 669 RDSADLKTLLSKAENQAKDV---QKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 733
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIeeeRKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
444-733 |
5.87e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 444 AQMDE------QDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHidTENLREEKD--SEITSTRDEL 515
Cdd:PHA02562 166 SEMDKlnkdkiRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKY--DELVEEAKTikAEIEELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 516 LSARDEIlllhqaaakvaSERDTDIASLQEELKKVRAELERWRKAASEYEKEITslqnsfqlrCQQCEDQQREEATRLQG 595
Cdd:PHA02562 244 LNLVMDI-----------EDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGV---------CPTCTQQISEGPDRITK 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 596 ELEKLrkewnaletechslkrenvllsSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQhlrdsadlk 675
Cdd:PHA02562 304 IKDKL----------------------KELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQS--------- 352
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135562 676 tlLSKAENQAKDVQKEYEKTQTvlselklkfemteqEKQSITDELKQCKNNLKLLREK 733
Cdd:PHA02562 353 --LITLVDKAKKVKAAIEELQA--------------EFVDNAEELAKLQDELDKIVKT 394
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
49-112 |
6.03e-04 |
|
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: 40.50 E-value: 6.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135562 49 KVLSRNHALVWFDHKTG--KFYLQDTKSSNGTFINsqrlsrgSEESPPC---EILSGDIIQFGVDVTEN 112
Cdd:cd22681 64 ETCSKQHCVIQFRNVKGilKPYIMDLDSSNGTCLN-------DNVIPSSryvELRSGDVITFSKSNDYE 125
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
16-111 |
6.51e-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: 39.21 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 16 PFQERHVYLD-EPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFdhKTGKFYLQDTKSSNGTFINSQRLSRgseespP 94
Cdd:cd22693 7 TLQGQTFPIDkSGITIGRA------DDNDLVLSDDFVSSRHARIYL--QGSSWYLEDLGSTNGTFVNGNRVTQ------P 72
|
90
....*....|....*..
gi 1799135562 95 CEILSGDIIQFGVDVTE 111
Cdd:cd22693 73 VVVQPGDTIRIGATVFE 89
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
436-702 |
8.30e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 8.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 436 KSSDDTTDAQMDEQDLNEPLAKVSLLKALlEEERKAYRNQVEESTKQIQVLQAQLQRLhidtenlreeKDSEITSTRDEL 515
Cdd:PRK11281 50 KQKLLEAEDKLVQQDLEQTLALLDKIDRQ-KEETEQLKQQLAQAPAKLRQAQAELEAL----------KDDNDEETRETL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 516 lsardeilllhqaaakvaseRDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQN----------SFQLRCQQCEDQ 585
Cdd:PRK11281 119 --------------------STLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTqperaqaalyANSQRLQQIRNL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 586 ----QREEATRLQGELEKLRKEWNALEtechslkrenvlLSSELQRQEKElHNSQKQSL-ELTSDLSILQMSRKELENQv 660
Cdd:PRK11281 179 lkggKVGGKALRPSQRVLLQAEQALLN------------AQNDLQRKSLE-GNTQLQDLlQKQRDYLTARIQRLEHQLQ- 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1799135562 661 gslkeqhlrdsaDLKTL-----LSKAENQAKDVQKEYEKTQTVLSEL 702
Cdd:PRK11281 245 ------------LLQEAinskrLTLSEKTVQEAQSQDEAARIQANPL 279
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
302-638 |
8.46e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 302 ELANKYNG-AVNEIKDLSDKLKVAEGKQ--EEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADndftnerlTALQ 378
Cdd:pfam17380 255 EYTVRYNGqTMTENEFLNQLLHIVQHQKavSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAE--------KARQ 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 379 VRLehlqEKTLKECSSLEKLIVEghltKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSdDTTDAQMDEQDLNEPLAK- 457
Cdd:pfam17380 327 AEM----DRQAAIYAEQERMAME----RERELERIRQEERKRELERIRQEEIAMEISRMR-ELERLQMERQQKNERVRQe 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 458 --VSLLKALLEEERKayRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAA----- 530
Cdd:pfam17380 398 leAARKVKILEEERQ--RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEerkrk 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 531 KVASERDTDIASLQEELKK--VRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQR----EEATRLQGELEKLRKEW 604
Cdd:pfam17380 476 KLELEKEKRDRKRAEEQRRkiLEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERrreaEEERRKQQEMEERRRIQ 555
|
330 340 350
....*....|....*....|....*....|....*
gi 1799135562 605 NALETECHSLKR-ENVLLSSELQRQEKELHNSQKQ 638
Cdd:pfam17380 556 EQMRKATEERSRlEAMEREREMMRQIVESEKARAE 590
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
164-733 |
9.58e-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: 42.90 E-value: 9.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLlsRLEVMGNQLQACsknqtedslRKELIAL 243
Cdd:pfam12128 259 RLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNG--ELSAADAAVAKD---------RSELEAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 244 QEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERtQEELRELANKYNGAVNE-----IKDLS 318
Cdd:pfam12128 328 EDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNR-RRSKIKEQNNRDIAGIKdklakIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 319 DKLKVAEgkQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEAL---QADNDFTNERLTAL---QVRLEHLQEKTLKEC 392
Cdd:pfam12128 407 DRQLAVA--EDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELklrLNQATATPELLLQLenfDERIERAREEQEAAN 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 393 SSLEKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDT--------TDAQMDEQDLNEPLAKVSLLKAL 464
Cdd:pfam12128 485 AEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAgtllhflrKEAPDWEQSIGKVISPELLHRTD 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 465 LEEErkayrnQVEESTKQIQVLQAQlqRLHIDTENLREEKDSEitstrDELLSARDEILLLHQAAAKVASERDTDIASLQ 544
Cdd:pfam12128 565 LDPE------VWDGSVGGELNLYGV--KLDLKRIDVPEWAASE-----EELRERLDKAEEALQSAREKQAAAEEQLVQAN 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 545 EELKKVRAELERWRKAaseyekeitsLQNSfQLRCQQCEDQQREEATRLQGELE----KLRKEWNALETECHSLKRENVL 620
Cdd:pfam12128 632 GELEKASREETFARTA----------LKNA-RLDLRRLFDEKQSEKDKKNKALAerkdSANERLNSLEAQLKQLDKKHQA 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 621 LSSELQRQEKEL---HNSQKQSLELTSDLSILQMS------RKELENQVGSLKEQHLRD--------------SADLKTL 677
Cdd:pfam12128 701 WLEEQKEQKREArteKQAYWQVVEGALDAQLALLKaaiaarRSGAKAELKALETWYKRDlaslgvdpdviaklKREIRTL 780
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799135562 678 LSKAENQAKDVQK--EYEKTQ--TVLSE---LKLKFEMTEQEKQSITDELKQCKNNLKLLREK 733
Cdd:pfam12128 781 ERKIERIAVRRQEvlRYFDWYqeTWLQRrprLATQLSNIERAISELQQQLARLIADTKLRRAK 843
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
236-399 |
1.07e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 236 LRKELIALQEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIK 315
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFE 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 316 DLSDKLKVAEGKQEEIQQKGQA-EKKELQHKIDEMEEKEQE---LQAKIEALQADNDFTNERLTALQVRLEHLQEKTlKE 391
Cdd:PRK03918 634 ELAETEKRLEELRKELEELEKKySEEEYEELREEYLELSRElagLRAELEELEKRREEIKKTLEKLKEELEEREKAK-KE 712
|
....*...
gi 1799135562 392 CSSLEKLI 399
Cdd:PRK03918 713 LEKLEKAL 720
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
263-673 |
1.11e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.58 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 263 QEKIEVVRKLSEVERS----LSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGkqEEIQQKGQAE 338
Cdd:PLN02939 45 QQKKKRGKNIAPKQRSsnskLQSNTDENGQLENTSLRTVMELPQKSTSSDDDHNRASMQRDEAIAAID--NEQQTNSKDG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 339 KKELQHKIDEMEEKEQELQAKIEAL-QAdndftneRLTALqvrlEHLqEKTLKECSSLEKLIveghltkAVEETKLSkEN 417
Cdd:PLN02939 123 EQLSDFQLEDLVGMIQNAEKNILLLnQA-------RLQAL----EDL-EKILTEKEALQGKI-------NILEMRLS-ET 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 418 QTRAKESdfsdtlspSKEKSSDDTTDAQMDEqdlneplakvslLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDT 497
Cdd:PLN02939 183 DARIKLA--------AQEKIHVEILEEQLEK------------LRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 498 ENLREEKdSEITSTRDELlsardeilllhqaaAKVASERDTDIASLQE-ELKKVRAELERWRKAASEYE---KEITSLQN 573
Cdd:PLN02939 243 QFLKAEL-IEVAETEERV--------------FKLEKERSLLDASLRElESKFIVAQEDVSKLSPLQYDcwwEKVENLQD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 574 SFQlrcqqCEDQQREEATRLQGELEKLRKEWNALETechSLKRENVL-LSSE----LQRQEKELHNS-QKQSLELTSDLS 647
Cdd:PLN02939 308 LLD-----RATNQVEKAALVLDQNQDLRDKVDKLEA---SLKEANVSkFSSYkvelLQQKLKLLEERlQASDHEIHSYIQ 379
|
410 420
....*....|....*....|....*.
gi 1799135562 648 ILQMSRKELENQVGSLKEQHLRDSAD 673
Cdd:PLN02939 380 LYQESIKEFQDTLSKLKEESKKRSLE 405
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
466-697 |
1.74e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 466 EEERKAYRNQVEESTKQIQVLQAQLQRLhidtenlreekDSEITSTRDELLSARDEILLLHQAAAKVASErdtdIASLQE 545
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDAL-----------QAELEELNEEYNELQAELEALQAEIDKLQAE----IAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 546 ELKKVRAELERWRKAASEYEKEITSLQ-----NSFQ------LRCQQCEDQQREE---ATRLQGELEKLRKEWNALETEC 611
Cdd:COG3883 80 EIEERREELGERARALYRSGGSVSYLDvllgsESFSdfldrlSALSKIADADADLleeLKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 612 HSLKRENVLLSSELQRQEKELhnsQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKE 691
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQ---EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
....*.
gi 1799135562 692 YEKTQT 697
Cdd:COG3883 237 AAAAAA 242
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
27-106 |
1.75e-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: 38.22 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 27 PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTGkfYLQDTKSSNGTFINSQRLsrgseeSPPCEILSGDIIQFG 106
Cdd:cd22668 19 SNIIGRG------SDADFRLPDTGVSRRHAEIRWDGQVA--HLTDLGSTNGTTVNNAPV------TPEWRLADGDVITLG 84
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
262-599 |
1.77e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 262 LQEKIEVVRKLSEVERSLSNTE--DECTHLKEMNERTQEELRELANKYNGAvNEIKDLSDKLKVAEGKQ-EEIQQKGQAE 338
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKkaDEAKKKAEEAKKKADEAKKAAEAKKKA-DEAKKAEEAKKADEAKKaEEAKKADEAK 1540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 339 KKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLKECSSLEKLIVEGHLTKAvEETKLSKENQ 418
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA-EEAKKAEEAK 1619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 419 TRA----KESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKayrnQVEESTKQIQVLQAQLQRLH 494
Cdd:PTZ00121 1620 IKAeelkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK----KAEEAKKAEEDEKKAAEALK 1695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 495 IDTENLReeKDSEITSTRDELLSARDEIlllhqaaAKVASERDTDIaslqEELKKVRAELERWRKAASEYEKEITSLQNS 574
Cdd:PTZ00121 1696 KEAEEAK--KAEELKKKEAEEKKKAEEL-------KKAEEENKIKA----EEAKKEAEEDKKKAEEAKKDEEEKKKIAHL 1762
|
330 340
....*....|....*....|....*
gi 1799135562 575 FQLRCQQCEDQQREEATRLQGELEK 599
Cdd:PTZ00121 1763 KKEEEKKAEEIRKEKEAVIEEELDE 1787
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
535-736 |
1.98e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 535 ERDT--DIASLQEELKkvraELERWRKAASEYEKEITSLQnsfQLRcqqcedQQREEATRLQGELEKLRKEWNALETECH 612
Cdd:COG4913 220 EPDTfeAADALVEHFD----DLERAHEALEDAREQIELLE---PIR------ELAERYAAARERLAELEYLRAALRLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 613 SLKREnvLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQvgsLKEQHLRDSADLKTLLSKAENQAKDVQKEY 692
Cdd:COG4913 287 QRRLE--LLEAELEELRAELARLEAELERLEARLDALREELDELEAQ---IRGNGGDRLEQLEREIERLERELEERERRR 361
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1799135562 693 EKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNN 736
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
455-691 |
2.18e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 455 LAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVAS 534
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 535 ErdtdIASLQEELKKVRAELER-----WRKAASEYEKEITSLQNSFQL-----RCQQCEDQQREEATRLQGELEKLRKew 604
Cdd:COG4942 91 E----IAELRAELEAQKEELAEllralYRLGRQPPLALLLSPEDFLDAvrrlqYLKYLAPARREQAEELRADLAELAA-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 605 naletechslkrenvlLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQH-------LRDSADLKTL 677
Cdd:COG4942 165 ----------------LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELaaelaelQQEAEELEAL 228
|
250
....*....|....
gi 1799135562 678 LSKAENQAKDVQKE 691
Cdd:COG4942 229 IARLEAEAAAAAER 242
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
465-624 |
2.18e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 465 LEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDseitstrdELlsaRDEILllhqaaakvasERDTDIASLQ 544
Cdd:COG2433 390 LPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE--------EL---EAELE-----------EKDERIERLE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 545 EELKKVRAElerwRKAASEYEKEITSLQNsfqlrcqqcedqqreEATRLQGELEKLRKEWNALETECHSLKRENVLLSSE 624
Cdd:COG2433 448 RELSEARSE----ERREIRKDREISRLDR---------------EIERLERELEEERERIEELKRKLERLKELWKLEHSG 508
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
260-712 |
2.32e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 260 RVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEK 339
Cdd:COG5022 954 PELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASK 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 340 KELQhkIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEhLQEKTLKECSSLEklIVEGhltkaveetklsKENQT 419
Cdd:COG5022 1034 IISS--ESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRE-NSLLDDKQLYQLE--STEN------------LLKTI 1096
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 420 RAKESDFSDTLSpSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTEN 499
Cdd:COG5022 1097 NVKDLEVTNRNL-VKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFA 1175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 500 LREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAElERWRKAASEYEKEITSLQNSFQLRC 579
Cdd:COG5022 1176 ALSEKRLYQSALYDEKSKLSSSEVNDLKNELIALFSKIFSGWPRGDKLKKLISE-GWVPTEYSTSLKGFNNLNKKFDTPA 1254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 580 QQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRE-NVLLSSELQRQEKELhnSQKQSLELTSDLSILQMSRKELEN 658
Cdd:COG5022 1255 SMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYiNVGLFNALRTKASSL--RWKSATEVNYNSEELDDWCREFEI 1332
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1799135562 659 QVGSLKEQHLRDSADLKTLLSKAENQAKDV-QKEYEKTQTVLSELKLKFEMTEQE 712
Cdd:COG5022 1333 SDVDEELEELIQAVKVLQLLKDDLNKLDELlDACYSLNPAEIQNLKSRYDPADKE 1387
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
586-733 |
2.64e-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: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 586 QREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKE 665
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 666 QHLRDSADLKTLLSKAE-------------------------------NQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQ 714
Cdd:COG4942 98 ELEAQKEELAELLRALYrlgrqpplalllspedfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAELE 177
|
170
....*....|....*....
gi 1799135562 715 SITDELKQCKNNLKLLREK 733
Cdd:COG4942 178 ALLAELEEERAALEALKAE 196
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
310-493 |
2.97e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 310 AVNEIKDLSDKLKVAEGKQEEIQ------QKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDF-TNERLTALQVR-L 381
Cdd:PRK11281 47 ALNKQKLLEAEDKLVQQDLEQTLalldkiDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEeTRETLSTLSLRqL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 382 EHLQEKTLKECSSLEKLIVEGHLTKAVEETKLSK------ENQTRAKE-SDFSDTLSPSKEKSSDDTTDAQMDEQDLNEp 454
Cdd:PRK11281 127 ESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERaqaalyANSQRLQQiRNLLKGGKVGGKALRPSQRVLLQAEQALLN- 205
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1799135562 455 lAKVSLLKALLEEERK---AYRNQVEESTKQIQVLQAQLQRL 493
Cdd:PRK11281 206 -AQNDLQRKSLEGNTQlqdLLQKQRDYLTARIQRLEHQLQLL 246
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
303-637 |
3.15e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.65 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 303 LANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADndftNERLTALQVRLE 382
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREK----HEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 383 HLQEKTLKECSSLEKLIVEG-HLTKAVEETKLSKENQTRAKESDFsDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLL 461
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHeARIRELEEDIKTLTQRVLERETEL-ERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 462 KALLEEERKAYRNQVEESTKQIQVLQAQLQRLHiDTENLREEKDSEITSTRDELLSARDEILLLHQAA-------AKVAS 534
Cdd:pfam07888 187 LRSLSKEFQELRNSLAQRDTQVLQLQDTITTLT-QKLTTAHRKEAENEALLEELRSLQERLNASERKVeglgeelSSMAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 535 ERDTDIASL-QEELKKVRAELE------RWRKAASEYEKEITSLQNSFQLRCQQCEdQQREEATRLQGELEKLRKEWNAL 607
Cdd:pfam07888 266 QRDRTQAELhQARLQAAQLTLQladaslALREGRARWAQERETLQQSAEADKDRIE-KLSAELQRLEERLQEERMEREKL 344
|
330 340 350
....*....|....*....|....*....|
gi 1799135562 608 ETECHSLKRENVLLSSELQRQEKELHNSQK 637
Cdd:pfam07888 345 EVELGREKDCNRVQLSESRRELQELKASLR 374
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
256-365 |
3.17e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 256 ESLRRVLQEKI-EVVRKLSEVERSLSNTEDEcthLKEMNERTQEELRELANKYNGAVNE--------IKDLSD--KLKVA 324
Cdd:PRK00409 526 EELERELEQKAeEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLEEAEKEAQQAIKEakkeadeiIKELRQlqKGGYA 602
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1799135562 325 EGKQEEIQQKgqaeKKELQHKIDEMEEKEQELQAKIEALQA 365
Cdd:PRK00409 603 SVKAHELIEA----RKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
163-386 |
3.78e-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: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWqALIDEDRLLSRLEVMGNQLQACSKNQTE-DSLRKELI 241
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-DEIDVASAEREIAELEAELERLDASSDDlAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 242 ALQEDkhnyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLK----EMNERTQEELRELANKYNGAVNEIkdl 317
Cdd:COG4913 696 ELEAE-----------LEELEEELDELKGEIGRLEKELEQAEEELDELQdrleAAEDLARLELRALLEERFAAALGD--- 761
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135562 318 sdklKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQE 386
Cdd:COG4913 762 ----AVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEE 826
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
172-361 |
3.97e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 39.12 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 172 LQEALHREQMLEQKLATLQRLLaitqeasdtswQALIDEDRLLSRLEVmgNQLQACSKNQTEDSLRKELIAlqedKHNYE 251
Cdd:pfam15619 6 LSARLHKIKELQNELAELQSKL-----------EELRKENRLLKRLQK--RQEKALGKYEGTESELPQLIA----RHNEE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 252 T-TAKESLRRvLQEKIEVV-RKLSEVERSLSNTEDECTHL------KEMNERT--QEELRELANKYNGAVNEIKDLSDKL 321
Cdd:pfam15619 69 VrVLRERLRR-LQEKERDLeRKLKEKEAELLRLRDQLKRLeklsedKNLAEREelQKKLEQLEAKLEDKDEKIQDLERKL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1799135562 322 KVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIE 361
Cdd:pfam15619 148 ELENKSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLK 187
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
253-557 |
4.25e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 253 TAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQ 332
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 333 QkgqaEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLKECSSLEKLIVEG------HLTK 406
Cdd:COG4372 115 E----ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeqaldELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 407 AVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVL 486
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799135562 487 QAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERW 557
Cdd:COG4372 271 KDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELAD 341
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
253-733 |
4.84e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 40.59 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 253 TAKESLRRVLQEKIEVVRKLSEVERSLSN--------TEDECTHLKEMNERTQEELRE-LANKYNGAVNEIKDLSDKLKV 323
Cdd:PTZ00440 894 SNKQLVEHLLNNKIDLKNKLEQHMKIINTdniiqkneKLNLLNNLNKEKEKIEKQLSDtKINNLKMQIEKTLEYYDKSKE 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 324 A-EGKQEEIQQKGQAEKKELQH---KIDEMEEKEQELQAKIEAL--QADNDFTNERLTALQVRLEHLQEKTLKECSSLEK 397
Cdd:PTZ00440 974 NiNGNDGTHLEKLDKEKDEWEHfksEIDKLNVNYNILNKKIDDLikKQHDDIIELIDKLIKEKGKEIEEKVDQYISLLEK 1053
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 398 LiveghltkaveETKLSKENQTRAKESDFSDTlspSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVE 477
Cdd:PTZ00440 1054 M-----------KTKLSSFHFNIDIKKYKNPK---IKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSHEHVVNADKEKN 1119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 478 ESTKQIQVLQAQLQRLHIDTENLREEKDS----EITSTRDELLSARDEILLLHQAAAKVASERdTDIASLQEELKKVRAE 553
Cdd:PTZ00440 1120 KQTEHYNKKKKSLEKIYKQMEKTLKELENmnleDITLNEVNEIEIEYERILIDHIVEQINNEA-KKSKTIMEEIESYKKD 1198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 554 LERWRKAASEYEKEITSLQNSfqlrcqqceDQQREEATRLQGELEKLRKEWNALETECHSLKRENvllssELQRQEKELH 633
Cdd:PTZ00440 1199 IDQVKKNMSKERNDHLTTFEY---------NAYYDKATASYENIEELTTEAKGLKGEANRSTNVD-----ELKEIKLQVF 1264
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 634 NSQKQSLELTSDLsilQMSRKELENQVGSLKEQHLRD-SADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQE 712
Cdd:PTZ00440 1265 SYLQQVIKENNKM---ENALHEIKNMYEFLISIDSEKiLKEILNSTKKAEEFSNDAKKELEKTDNLIKQVEAKIEQAKEH 1341
|
490 500
....*....|....*....|...
gi 1799135562 713 KQ--SITDELKQCKNNLKLLREK 733
Cdd:PTZ00440 1342 KNkiYGSLEDKQIDDEIKKIEQI 1364
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
300-387 |
4.95e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 300 LRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQV 379
Cdd:COG3883 124 LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
....*...
gi 1799135562 380 RLEHLQEK 387
Cdd:COG3883 204 ELAAAEAA 211
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
274-381 |
5.29e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 40.22 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 274 EVERSLSNTEDECTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEK----------K 340
Cdd:pfam06160 288 YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEvayselqeelE 367
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1799135562 341 ELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRL 381
Cdd:pfam06160 368 EILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLEL 408
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
174-722 |
5.42e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.34 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 174 EALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLlsrlevmgnQLQACSKNQTEDSLRKELIALqedkhnyETT 253
Cdd:TIGR00618 369 EISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQRE---------QATIDTRTSAFRDLQGQLAHA-------KKQ 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 254 AKESLRRVLQEKIEVVRKLSEVERslsntedECTHLKEMNERTQEELRELANKYNGAvneikdlsdkLKVAEGKQEEiqq 333
Cdd:TIGR00618 433 QELQQRYAELCAAAITCTAQCEKL-------EKIHLQESAQSLKEREQQLQTKEQIH----------LQETRKKAVV--- 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 334 kgqaEKKELQHKIDEMEEKEQELQAKIEALQADNdftnerLTALQVRLEHLQEKTLKECSSLEKliVEGHLTKAVEETKL 413
Cdd:TIGR00618 493 ----LARLLELQEEPCPLCGSCIHPNPARQDIDN------PGPLTRRMQRGEQTYAQLETSEED--VYHQLTSERKQRAS 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 414 SKENQTRAKESDFSDTLSPSKEKSS-DDTTDAQMDEQDLNEPLAKVSLLKA------LLEEERKAYRNQVEESTKQI-QV 485
Cdd:TIGR00618 561 LKEQMQEIQQSFSILTQCDNRSKEDiPNLQNITVRLQDLTEKLSEAEDMLAceqhalLRKLQPEQDLQDVRLHLQQCsQE 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 486 LQAQLQRLHIDTENLREEKDSE--ITSTRDELLSardeiLLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASE 563
Cdd:TIGR00618 641 LALKLTALHALQLTLTQERVREhaLSIRVLPKEL-----LASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEE 715
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 564 YEKEITSLQNSFQLRCQQCEdQQREEATRLQGELEKLRKEWNALETECHSLKRENVL----LSSELQRQEKELHNSQKQS 639
Cdd:TIGR00618 716 YDREFNEIENASSSLGSDLA-AREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTaalqTGAELSHLAAEIQFFNRLR 794
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 640 LELTSDLsilqmsrKELENQVgslkEQHLRDSADLKTL----LSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 715
Cdd:TIGR00618 795 EEDTHLL-------KTLEAEI----GQEIPSDEDILNLqcetLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQ 863
|
....*..
gi 1799135562 716 ITDELKQ 722
Cdd:TIGR00618 864 LTQEQAK 870
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
52-106 |
5.80e-03 |
|
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: 36.70 E-value: 5.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799135562 52 SRNHALVWFDHKTGKFYLQ-----------DTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFG 106
Cdd:cd22683 28 SRSCDLVLSDPSISRFHAElrleqnginviDNNSANGTFINGKRIKGKT-----YILKNGDIIVFG 88
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
163-365 |
5.83e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.06 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEasdtsWQALIDEDRLLSR----LEVMGNQLQACSKNQT--EDSL 236
Cdd:COG0497 172 KELEELRADEAERARELDLLRFQLEELEAAALQPGE-----EEELEEERRRLSNaeklREALQEALEALSGGEGgaLDLL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 237 RKELIALQEDKHnYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERtQEELRELANKYNGAVNEIKD 316
Cdd:COG0497 247 GQALRALERLAE-YDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEER-LALLRRLARKYGVTVEELLA 324
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1799135562 317 LSDKLkvaegkqeeiqqkgQAEKKELQHKIDEMEEKEQELQAKIEALQA 365
Cdd:COG0497 325 YAEEL--------------RAELAELENSDERLEELEAELAEAEAELLE 359
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
496-735 |
5.95e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 496 DTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVaSERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNsf 575
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKL-EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE-- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 576 QLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSD---LSILQMS 652
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKeerLEELKKK 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 653 RKELENQVGSLKEQHlRDSADLKTLLSKAENQAKdvqkeyEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLRE 732
Cdd:PRK03918 347 LKELEKRLEELEERH-ELYEEAKAKKEELERLKK------RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
...
gi 1799135562 733 KGN 735
Cdd:PRK03918 420 EIK 422
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
208-366 |
6.00e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 39.82 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 208 IDEDRLLSRLEVMGNQLQACSKNQTE---DSLRKELIALQED-KHNYETTAKEslrrvLQEKIEVVRKLSEVERSLsnte 283
Cdd:PRK04778 249 LDHLDIEKEIQDLKEQIDENLALLEEldlDEAEEKNEEIQERiDQLYDILERE-----VKARKYVEKNSDTLPDFL---- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 284 decTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKK---ELQHKIDEMEEKEQELQ 357
Cdd:PRK04778 320 ---EHAKEQNKELKEEIDRVKQSYtlnESELESVRQLEKQLESLEKQYDEITERIAEQEIaysELQEELEEILKQLEEIE 396
|
....*....
gi 1799135562 358 AKIEALQAD 366
Cdd:PRK04778 397 KEQEKLSEM 405
|
|
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
465-554 |
6.07e-03 |
|
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.
Pssm-ID: 462015 [Multi-domain] Cd Length: 198 Bit Score: 38.83 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 465 LEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLRE---EKDSEITSTRDEL--LSARDEILLLHQAAAKVASERDTD 539
Cdd:pfam06818 50 KEEQIQELEDSLRSKTLELEVCENELQRKKNEAELLREkvgKLEEEVSGLREALsdVSPSGYESVYESDEAKEQRQEEAD 129
|
90
....*....|....*
gi 1799135562 540 IASLQEELKKVRAEL 554
Cdd:pfam06818 130 LGSLRREVERLRAEL 144
|
|
| VI_FHA |
TIGR03354 |
type VI secretion system FHA domain protein; Members of this protein family are FHA ... |
49-106 |
8.10e-03 |
|
type VI secretion system FHA domain protein; Members of this protein family are FHA (forkhead-associated) domain-containing proteins that are part of type VI secretion loci in a considerable number of bacteria, most of which are known pathogens. Species include Pseudomonas aeruginosa PAO1, Aeromonas hydrophila, Yersinia pestis, Burkholderia mallei, etc. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274537 [Multi-domain] Cd Length: 396 Bit Score: 39.28 E-value: 8.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799135562 49 KVLSRNHALV-WFDhktGKFYLQDTkSSNGTFINS--QRLSRGSEesppcEILS-GDIIQFG 106
Cdd:TIGR03354 43 RHVSGRHARIrYRD---GAYLLTDL-STNGVFLNGsgSPLGRGNP-----VRLEqGDRLRLG 95
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
444-655 |
8.85e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 444 AQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREE---KDSEITSTRDEL----- 515
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeAEAEIEERREELgerar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 516 --------LSARDEIL-------LLHQAAA-KVASERDTDIAslqEELKKVRAELERWRKAASEYEKEITSLQnsfqlrc 579
Cdd:COG3883 94 alyrsggsVSYLDVLLgsesfsdFLDRLSAlSKIADADADLL---EELKADKAELEAKKAELEAKLAELEALK------- 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799135562 580 qqceDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKE 655
Cdd:COG3883 164 ----AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
236-366 |
8.86e-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: 38.37 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 236 LRKELIALQEDKHNYETTAKESLRRV--LQEKIEVVRKlsevERSLSNTEDECTHLKEMNERTQEELRELankyngaVNE 313
Cdd:COG1579 50 AKTELEDLEKEIKRLELEIEEVEARIkkYEEQLGNVRN----NKEYEALQKEIESLKRRISDLEDEILEL-------MER 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1799135562 314 IKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQAD 366
Cdd:COG1579 119 IEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
247-728 |
9.53e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.64 E-value: 9.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 247 KHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNT---EDECTHLKEMNERTQEELRELANKyngavneikdlsdKLKV 323
Cdd:TIGR00606 229 KEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKImklDNEIKALKSRKKQMEKDNSELELK-------------MEKV 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 324 AEGKQEEIQQKGQAEKKELQHKidemEEKEQELQAKIEALQADNDFTNERLTALQVRL-------EHLQEKTLKECSSLE 396
Cdd:TIGR00606 296 FQGTDEQLNDLYHNHQRTVREK----ERELVDCQRELEKLNKERRLLNQEKTELLVEQgrlqlqaDRHQEHIRARDSLIQ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 397 KLIVEGHLTKAVEETKLSKE--NQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRN 474
Cdd:TIGR00606 372 SLATRLELDGFERGPFSERQikNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEK 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 475 QVEE---STKQIQVLQAQLQRLHIDTENLRE--------EKDSEITSTRDELLSARDEILLLHQAAAKVASE-----RDT 538
Cdd:TIGR00606 452 KQEElkfVIKELQQLEGSSDRILELDQELRKaerelskaEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEmeqlnHHT 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 539 DIASLQEELKKVRAEL-ERWRKAASEYEKEITSLQNSFQLRCQQCE---------DQQREEATRLQGELEKLRKEWNALE 608
Cdd:TIGR00606 532 TTRTQMEMLTKDKMDKdEQIRKIKSRHSDELTSLLGYFPNKKQLEDwlhskskeiNQTRDRLAKLNKELASLEQNKNHIN 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 609 TECHSLKRENVLLS-------------SELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRD----- 670
Cdd:TIGR00606 612 NELESKEEQLSSYEdklfdvcgsqdeeSDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVfqtea 691
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799135562 671 -----SADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLK 728
Cdd:TIGR00606 692 elqefISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQ 754
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
353-598 |
9.67e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.23 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 353 EQELQAKIEALQADNDFTNERLTALQVRLEHLQEKtlkecssLEKLiveghltkaveetklskenQTRAKESDFSDTLSP 432
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAA-------LEEF-------------------RQKNGLVDLSEEAKL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 433 SKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEEStkQIQVLQAQLQRLHIDTENLRE---EKDSEIT 509
Cdd:COG3206 217 LLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP--VIQQLRAQLAELEAELAELSArytPNHPDVI 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135562 510 STRDELLSARDEILllhQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEY---EKEITSLQNSFQLRCQQCED-Q 585
Cdd:COG3206 295 ALRAQIAALRAQLQ---QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELYESlL 371
|
250
....*....|...
gi 1799135562 586 QREEATRLQGELE 598
Cdd:COG3206 372 QRLEEARLAEALT 384
|
|
| |
