|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
3-130 |
1.82e-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: 256.43 E-value: 1.82e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 3 SALAIFTCRPNSHPFQERHVYLDEPIKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINS 82
Cdd:cd22679 1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1799135528 83 QRLSRGSEESPPCEILSGDIIQFGVDVTENTRKVTHGCIVSTIKLFLP 130
Cdd:cd22679 79 QRLSKGSEESEPRELHSGDIVQFGVDVVENSRKVTHGCIVATVTLFLP 126
|
|
| CC1_SLMAP |
cd21911 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal ... |
163-225 |
3.65e-26 |
|
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal membrane-associated protein (SLMAP), also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. SLMAP contains an N-terminal FHA domain followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409287 [Multi-domain] Cd Length: 63 Bit Score: 101.61 E-value: 3.65e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799135528 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQ 225
Cdd:cd21911 1 QELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQLS 63
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-778 |
9.63e-22 |
|
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: 101.29 E-value: 9.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 156 NTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQA--CSKNQTE 233
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvAQLELQI 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 234 DSLRKELIAL------QEDKHNYETTAKESLRRVLQE--KIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELAN 305
Cdd:TIGR02168 396 ASLNNEIERLearlerLEDRRERLQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 306 KYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKID---------EMEEKEQELQAKIEA-----LQADNDFTN 371
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlsELISVDEGYEAAIEAalggrLQAVVVENL 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 372 ERLTALQEHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSP--SKEKSSDDTTDAQ 449
Cdd:TIGR02168 556 NAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllGGVLVVDDLDNAL 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 450 MDEQDLNEPLAKVSL-----------LKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFEL---QALLEEERK 515
Cdd:TIGR02168 636 ELAKKLRPGYRIVTLdgdlvrpggviTGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELrkeLEELEEELE 715
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 516 AYRNQVEESTKQIQVLQAQLQRLHIDTENLREEkdseITSTRDELLSARDEILLLHQAAAKV---ASERDTDIASLQEEL 592
Cdd:TIGR02168 716 QLRKELEELSRQISALRKDLARLEAEVEQLEER----IAQLSKELTELEAEIEELEERLEEAeeeLAEAEAEIEELEAQI 791
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 593 KKVRAELERWRKAASEYEKEITSLQNSF---QLRCQQCEDQQREEATRLQ----------GELEKLRKEWNALETECHSL 659
Cdd:TIGR02168 792 EQLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATERRLEdleeqieelsEDIESLAAEIEELEELIEEL 871
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 660 KRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHlrdsADLKTLLSKAENQAKDVQkeyek 739
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL----AQLELRLEGLEVRIDNLQ----- 942
|
650 660 670
....*....|....*....|....*....|....*....
gi 1799135528 740 tQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 778
Cdd:TIGR02168 943 -ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| FHA_DMA-like |
cd22692 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest ... |
27-108 |
1.80e-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: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 27 PIKIGRSVARCRPAQNNAT-FDCKVLSRNHALVWfdHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQF 105
Cdd:cd22692 38 QIHIGRYTERVRQAIYHPVvFKSKVVSRTHGCIK--VDEGNWYIKDVKSSSGTFLNHQRLSPASRTSKPYPLRDGDILQL 115
|
...
gi 1799135528 106 GVD 108
Cdd:cd22692 116 GMD 118
|
|
| FHA_VPS64-like |
cd22695 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ... |
6-126 |
5.61e-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: 5.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 6 AIFTCRPNSHPFQERHV---YLDEPIKIGRSVARCRPAQN---------------NATFDCKVLSRNHALVWFDHKTGKF 67
Cdd:cd22695 2 HILVLKSLNATFETKFLvvpFKPDGLKLGRPVTNSVNKNNsgskrdlfsqqvrpdNGNFDSRVLSRNHACLSCDPTTGKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135528 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 ... |
172-778 |
9.00e-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: 78.95 E-value: 9.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 172 LQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRllsrlevmgnqlqacSKNQTEDSLRKELIALQEDKHNYE 251
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS---------------ELEEEIEELQKELYALANEISRLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 252 ttakeslrrvlQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEI 331
Cdd:TIGR02168 302 -----------QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 332 QQKGQAEKKELQH---KIDEMEEKEQELQAKIEALQADNDFTNERLTALQ----EHLLSKSGGDCTFIHQFIECQKKLIV 404
Cdd:TIGR02168 371 ESRLEELEEQLETlrsKVAQLELQIASLNNEIERLEARLERLEDRRERLQqeieELLKKLEEAELKELQAELEELEEELE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 405 EGHLTKAVEETKLSK-ENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLK-----DDLQGAQSEI-- 476
Cdd:TIGR02168 451 ELQEELERLEEALEElREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKnqsglSGILGVLSELis 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 477 --------------------------EAKQEIQHLRKE----------------LIEAQELARTSKQKCFELQAL-LEEE 513
Cdd:TIGR02168 531 vdegyeaaieaalggrlqavvvenlnAAKKAIAFLKQNelgrvtflpldsikgtEIQGNDREILKNIEGFLGVAKdLVKF 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 514 RKAYRNQVE--------------------------------------------ESTKQIQVLQAQLQRLHIDTENLR--E 547
Cdd:TIGR02168 611 DPKLRKALSyllggvlvvddldnalelakklrpgyrivtldgdlvrpggvitgGSAKTNSSILERRREIEELEEKIEelE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 548 EKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQC 627
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 628 EdQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGS 707
Cdd:TIGR02168 771 E-EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799135528 708 LKEQHLRDSA---DLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 778
Cdd:TIGR02168 850 LSEDIESLAAeieELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
239-764 |
2.83e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.49 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 239 ELIALQEDKHNYETTAKESLRRV--LQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKD 316
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 317 LSDKLKVAEGKQEEIQQKGQAEKK--ELQHKIDEMEEKEQELQAKIEALQadndfTNERLTALQEHLLSKSggdctfihq 394
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELK-----KAAAAKKKADEAKKKA--------- 1427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 395 fiECQKKlivEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKE--KSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGA 472
Cdd:PTZ00121 1428 --EEKKK---ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEeaKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA 1502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 473 QSEIEAKQEIQHLRK--ELIEAQELARTSKQKCFELQALLEEERKAYR-NQVEESTKQIQVLQAQLQRlhidtenlREEK 549
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKaeEAKKADEAKKAEEAKKADEAKKAEEKKKADElKKAEELKKAEEKKKAEEAK--------KAEE 1574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 550 DSEITSTRDELLSardeilllhqaaaKVASERDTDIASLQEELKKVRAE----LERWRKAASEYEKEITSLQNSFQLRCQ 625
Cdd:PTZ00121 1575 DKNMALRKAEEAK-------------KAEEARIEEVMKLYEEEKKMKAEeakkAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 626 QCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQV 705
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799135528 706 GSLKEQHLRDSADLKTLLSKAENQAKDVQKEYE---KTQTVLSELKLKFEMTEQEKQSITDE 764
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEekkKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
13-106 |
5.05e-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: 5.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 13 NSHPFQERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINSQRLsrgseeS 92
Cdd:cd00060 6 DGDGGGREFPLTKGVVTIGRS------PDCDIVLDDPSVSRRHARIEVDG--GGVYLEDLGSTNGTFVNGKRI------T 71
|
90
....*....|....
gi 1799135528 93 PPCEILSGDIIQFG 106
Cdd:cd00060 72 PPVPLQDGDVIRLG 85
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
28-105 |
1.48e-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: 1.48e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135528 28 IKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRLSRgseesPPCEILSGDIIQF 105
Cdd:pfam00498 1 VTIGRS------PDCDIVLDDPSVSRRHAEIRYD-GGGRFYLEDLGSTNGTFVNGQRLGP-----EPVRLKDGDVIRL 66
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
481-778 |
2.20e-13 |
|
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: 74.33 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 481 EIQHLRKELIEAQELARTSKQKCFELQALLEEERKA----YRNQVEESTKQIQVLQAQLQRLhidtENLREEKDSEITST 556
Cdd:TIGR02169 188 RLDLIIDEKRQQLERLRREREKAERYQALLKEKREYegyeLLKEKEALERQKEAIERQLASL----EEELEKLTEEISEL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 557 RDELLSARDeilLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNsfQLRCQQCE-DQQREEA 635
Cdd:TIGR02169 264 EKRLEEIEQ---LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE--RLAKLEAEiDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 636 TRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRD 715
Cdd:TIGR02169 339 EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL 418
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799135528 716 SADlktlLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 778
Cdd:TIGR02169 419 SEE----LADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
460-757 |
2.39e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 460 AKVSLLKDDLQGAQSEiEAKQEIQHLRKELIEAQELartskqkcfelQALLEEERKAYRNQVEESTKQIQVLQAQLQRLH 539
Cdd:COG1196 227 AELLLLKLRELEAELE-ELEAELEELEAELEELEAE-----------LAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 540 IDTENLREEKDSEitstRDELLSARDEILLLHQAAAKVASErdtdIASLQEELKKVRAELERWRKAASEYEKEITSLQNS 619
Cdd:COG1196 295 AELARLEQDIARL----EERRRELEERLEELEEELAELEEE----LEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 620 FQLRCQQCEDQQREEATRLQGELEKLRKEwNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRK 699
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAA-AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135528 700 ELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQE 757
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| CC1_SLMAP-like |
cd21868 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ... |
167-204 |
1.35e-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: 1.35e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1799135528 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21868 1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
267-778 |
1.64e-12 |
|
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: 71.20 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 267 EVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKI 346
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 347 DEMEEKEQE---LQAKIEALQADNDFTNERLTALQEHLLSKSGGDCTFIHQFIECQKKLivegHLTKAVEETKLSKENQT 423
Cdd:TIGR04523 117 EQKNKLEVElnkLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENEL----NLLEKEKLNIQKNIDKI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 424 RAKESDFSDTLSPSKEKSSDDTTDaqmdEQDLNEPLAKVSLLKDDLQgaqseiEAKQEIQHLRKELIEAQELARTSKQKC 503
Cdd:TIGR04523 193 KNKLLKLELLLSNLKKKIQKNKSL----ESQISELKKQNNQLKDNIE------KKQQEINEKTTEISNTQTQLNQLKDEQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 504 FELQALLEEERKayrnQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILllhQAAAKVASERDT 583
Cdd:TIGR04523 263 NKIKKQLSEKQK----ELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKL---EEIQNQISQNNK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 584 DIASLQEELKKVRAELERWRKAASEYEKEITSLQNsfqlrcqQCEDQQREEATRLQgELEKLRKEWNALETECHSLKREN 663
Cdd:TIGR04523 336 IISQLNEQISQLKKELTNSESENSEKQRELEEKQN-------EIEKLKKENQSYKQ-EIKNLESQINDLESKIQNQEKLN 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 664 VLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHlrdsADLKTLLSKAENQAKDVQKEYEKTQTV 743
Cdd:TIGR04523 408 QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELII----KNLDNTRESLETQLKVLSRSINKIKQN 483
|
490 500 510
....*....|....*....|....*....|....*
gi 1799135528 744 LSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 778
Cdd:TIGR04523 484 LEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK 518
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
233-778 |
3.41e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.47 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 233 EDSLRKELIALQ-EDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAV 311
Cdd:TIGR02168 222 LRELELALLVLRlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 312 NEIKDLSDKLKVAEGKQEEIQ---QKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNE-------RLTALQEHL 381
Cdd:TIGR02168 302 QQKQILRERLANLERQLEELEaqlEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAeleelesRLEELEEQL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 382 LSKSGGdctfIHQfIECQKKLIvEGHLTKAVEETKLSKENQTRAKEsdfsDTLSPSKEKSSDDTTDAQMDEQDLNEPLAK 461
Cdd:TIGR02168 382 ETLRSK----VAQ-LELQIASL-NNEIERLEARLERLEDRRERLQQ----EIEELLKKLEEAELKELQAELEELEEELEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 462 VSLLKDDLQgaQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQ------------ 529
Cdd:TIGR02168 452 LQEELERLE--EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlseli 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 530 ------------VLQAQLQRLHIDTEN---------------------LREEKDSEITSTRDELLSARDEILLLHQAAAK 576
Cdd:TIGR02168 530 svdegyeaaieaALGGRLQAVVVENLNaakkaiaflkqnelgrvtflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVK 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 577 VASERD-------------TDIASLQEELKKVRAEL-------ERWRKAASEY---EKEITSLQNSFQ--LRCQQCEDQQ 631
Cdd:TIGR02168 610 FDPKLRkalsyllggvlvvDDLDNALELAKKLRPGYrivtldgDLVRPGGVITggsAKTNSSILERRReiEELEEKIEEL 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 632 REEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQ 711
Cdd:TIGR02168 690 EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEER 769
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135528 712 ----------HLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 778
Cdd:TIGR02168 770 leeaeeelaeAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
167-601 |
5.17e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 5.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQAcsKNQTEDSLRKELIALQED 246
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE--LEEAEEALLERLERLEEE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 247 KhnyeTTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEG 326
Cdd:COG1196 423 L----EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 327 KQEEIQQKGQAEKKELQHK--------IDEMEEKEQELQAKIEA-----LQADNDFTNERLTALQEHLLSKSGGDCTFIH 393
Cdd:COG1196 499 AEADYEGFLEGVKAALLLAglrglagaVAVLIGVEAAYEAALEAalaaaLQNIVVEDDEVAAAAIEYLKAAKAGRATFLP 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 394 QFIECQKKLIVEGHLTKAVEETKLSKENQTR---AKESDFSDTLSpskekssDDTTDAQMDEQDLNEPLAKVSLLKDDLQ 470
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLReadARYYVLGDTLL-------GRTLVAARLEAALRRAVTLAGRLREVTL 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 471 GAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKD 550
Cdd:COG1196 652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1799135528 551 SEitstRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELER 601
Cdd:COG1196 732 AE----REELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-773 |
8.45e-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: 69.33 E-value: 8.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 197 QEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTE-----DSLRKELIALQEDKHNYETTAKESLRRV--LQEKIE-V 268
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKlteeyAELKEELEDLRAELEEVDKEFAETRDELkdYREKLEkL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 269 VRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKE---LQHK 345
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQElydLKEE 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 346 IDEMEEKEQELQAKIEALQADNDFTNERLT---ALQEHLLSKSGGDCTFIHQFIECQKK---------------LIVEGH 407
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEAQARASEERVRggrAVEEVLKASIQGVHGTVAQLGSVGERyataievaagnrlnnVVVEDD 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 408 LTkAVEETKLSKE-----------NQTRAKESDfsdtLSPSKEK------------------------------SSDDTT 446
Cdd:TIGR02169 558 AV-AKEAIELLKRrkagratflplNKMRDERRD----LSILSEDgvigfavdlvefdpkyepafkyvfgdtlvvEDIEAA 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 447 DAQMD-------EQDLNEP--------LAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLE 511
Cdd:TIGR02169 633 RRLMGkyrmvtlEGELFEKsgamtggsRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELS 712
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 512 EERKayrnQVEESTKQIQVLQAQLQRLHIDTENLRE---EKDSEITSTRDELLSARDEILLLHQAAAKV--------ASE 580
Cdd:TIGR02169 713 DASR----KIGEIEKEIEQLEQEEEKLKERLEELEEdlsSLEQEIENVKSELKELEARIEELEEDLHKLeealndleARL 788
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 581 RDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQ----------NSFQLRCQQCEDQQREEATR----------LQG 640
Cdd:TIGR02169 789 SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTlekeylekeiQELQEQRIDLKEQIKSIEKEienlngkkeeLEE 868
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 641 ELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLK 720
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE 948
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135528 721 TLLS----KAENQAKDVQ------------KEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCkNNLK 773
Cdd:TIGR02169 949 EELSledvQAELQRVEEEiralepvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY-EKKK 1016
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
14-106 |
1.16e-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: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 14 SHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716 8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
|
90
....*....|....
gi 1799135528 93 pPCEILSGDIIQFG 106
Cdd:COG1716 75 -PAPLRDGDVIRLG 87
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
161-711 |
1.17e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 161 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKEL 240
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 241 IALQEDKHNYETT---AKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDL 317
Cdd:COG1196 298 ARLEQDIARLEERrreLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 318 SDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEHLLsksggdctfihQFIE 397
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE-----------ALEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 398 CQKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLA-KVSLLKDDLQGAQSEI 476
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvKAALLLAGLRGLAGAV 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 477 EAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEEST----KQIQVLQAQLQRLHIDTENLREEKDSE 552
Cdd:COG1196 527 AVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflplDKIRARAALAAALARGAIGAAVDLVAS 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 553 ITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYE-KEITSLQNSFQLRCQQCEDQQ 631
Cdd:COG1196 607 DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGgSRRELLAALLEAEAELEELAE 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 632 REEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQ---------MSRKELE 702
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEealeelpepPDLEELE 766
|
....*....
gi 1799135528 703 NQVGSLKEQ 711
Cdd:COG1196 767 RELERLERE 775
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
52-106 |
1.42e-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: 1.42e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1799135528 52 SRNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQFG 106
Cdd:cd22686 48 SKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPYPLTHGDELKIG 102
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
452-777 |
6.76e-11 |
|
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: 66.24 E-value: 6.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 452 EQDLNEPLAKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCfelqalLEEERKAYRNQVEESTKQIQVL 531
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEA------LERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 532 QAQLQ-----------RLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASER---DTDIASLQEELKKVRA 597
Cdd:TIGR02169 257 TEEISelekrleeieqLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELedaEERLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 598 ELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQRE------EATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQ 671
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEleevdkEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 672 RQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADlktlLSKAENQAKDVQKEYEKTQTVLSELKLKF 751
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD----LSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
330 340
....*....|....*....|....*.
gi 1799135528 752 EMTEQEKQSITDELKQCKNNLKLLRE 777
Cdd:TIGR02169 493 AEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
233-767 |
8.95e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 8.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 233 EDSLRKELIALQEDKhnyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVN 312
Cdd:COG1196 222 LKELEAELLLLKLRE------LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 313 EIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQAdndfTNERLTALQEHLLSksggdctfi 392
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE----AEEELEEAEAELAE--------- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 393 hqfiecqkkliveghLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGA 472
Cdd:COG1196 363 ---------------AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 473 QSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLRE-EKDS 551
Cdd:COG1196 428 EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADyEGFL 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 552 EITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKE------------------- 612
Cdd:COG1196 508 EGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAakagratflpldkiraraa 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 613 ----ITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELT 688
Cdd:COG1196 588 laaaLARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSR 667
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135528 689 SDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 767
Cdd:COG1196 668 RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
505-778 |
1.77e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 505 ELQALLEEERKAYRNQVEE-----STKQIQVLQAQLQRLHIDTENLREEKDsEITSTRDELLSARDEILLLHQAAAKVAS 579
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRElelalLVLRLEELREELEELQEELKEAEEELE-ELTAELQELEEKLEELRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 580 ERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQlRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSL 659
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE-ELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 660 KRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKA-ENQAKDVQKEYE 738
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELE 443
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1799135528 739 KTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 778
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
163-703 |
3.45e-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: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDtswQALIDEDRLLSRLEVMGNQLQACSKNQTE-----DSLR 237
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRR---ELEERLEELEEELAELEEELEELEEELEEleeelEEAE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 238 KELIALQEDKHNYETTAKESLRRVL---QEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEI 314
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAeaeEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 315 KDLSDKLKVAEGKQEEIQQK---GQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEHLLSKSGGDctf 391
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEeaeLEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL--- 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 392 ihQFIECQKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKssDDTTDAQMDEQDLNEPLAKVSLLKDDLQG 471
Cdd:COG1196 508 --EGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE--DDEVAAAAIEYLKAAKAGRATFLPLDKIR 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 472 AQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQvEESTKQIQVLQAQLQRLHIDTENLREEKDS 551
Cdd:COG1196 584 ARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARL-EAALRRAVTLAGRLREVTLEGEGGSAGGSL 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 552 EITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQ 631
Cdd:COG1196 663 TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL 742
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 632 REEATRLQGELEKLRKE--WNALETECHSLKRE-------NVLLSSELQRQEKELHnsqkqslELTSDLSILQMSRKELE 702
Cdd:COG1196 743 EEEELLEEEALEELPEPpdLEELERELERLEREiealgpvNLLAIEEYEELEERYD-------FLSEQREDLEEARETLE 815
|
.
gi 1799135528 703 N 703
Cdd:COG1196 816 E 816
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
529-767 |
5.56e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 5.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 529 QVLQAQLQRLHIdteNLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASE 608
Cdd:COG1196 216 RELKEELKELEA---ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 609 YEKEITSLQNSFQLRCQQCEDQQREEAtRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELT 688
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLE-ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135528 689 SDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 767
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
255-778 |
6.36e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 6.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 255 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNgAVNEIKDLSDKLKVAEGKQEEIQQK 334
Cdd:PRK03918 178 IERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 335 GQAEKKELQHKIDEMEEKEQELQAKI-------------EALQADNDFTNERLTALQEHLLSKSGGDCTFIHQFIECQKK 401
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVkelkelkekaeeyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 402 LIVEGHLTKAVEETKlSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQ- 480
Cdd:PRK03918 337 EERLEELKKKLKELE-KRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIg 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 481 EIQHLRKELIEAQELARTSKQKCFELQALLEEERKAyrNQVEESTKQIQVLQAQLQRLHIDTENLREEKdseitSTRDEL 560
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRK--ELLEEYTAELKRIEKELKEIEEKERKLRKEL-----RELEKV 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 561 LSARDEILLLHQAAAKvaserdtdIASLQEELKKVraELERWRKAASEYEKeitslqnsfqlrcqqcedqQREEATRLQG 640
Cdd:PRK03918 489 LKKESELIKLKELAEQ--------LKELEEKLKKY--NLEELEKKAEEYEK-------------------LKEKLIKLKG 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 641 ELEKLRKEWNALEtechSLKRENVLLSSELQRQEKELHNSQKQSLELT-SDLSILQMSRKELE---NQVGSLK------E 710
Cdd:PRK03918 540 EIKSLKKELEKLE----ELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEpfyNEYLELKdaekelE 615
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135528 711 QHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFemTEQEKQSITDELKQCKNNLKLLREK 778
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY--SEEEYEELREEYLELSRELAGLRAE 681
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
212-777 |
6.85e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 63.14 E-value: 6.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 212 RLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTAKESLRRVLQEKIEvvrkLSEVERSlSNTEDECTHLKE 291
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE----LDGFERG-PFSERQIKNFHT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 292 MNERTQEELRELANKyngavnEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQadndftn 371
Cdd:TIGR00606 398 LVIERQEDEAKTAAQ------LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ------- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 372 eRLTALQEHLLSKsggdctfihqfiecqkklivEGHLTKAveETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMD 451
Cdd:TIGR00606 465 -QLEGSSDRILEL--------------------DQELRKA--ERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLD 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 452 EQDLNEPLAKVSlLKDDLQGAQSEIEAKQEIQHLRKEliEAQELarTSKQKCFELQALLEEERKAYRNQVEESTKQIQVL 531
Cdd:TIGR00606 522 QEMEQLNHHTTT-RTQMEMLTKDKMDKDEQIRKIKSR--HSDEL--TSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKL 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 532 QAQLQRLhidtENLREEKDSEITSTRDELLSARDEILllhqaAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEK 611
Cdd:TIGR00606 597 NKELASL----EQNKNHINNELESKEEQLSSYEDKLF-----DVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQ 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 612 EITSLQNSFQLRCQQC------EDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLL-------SSELQRQEKELH 678
Cdd:TIGR00606 668 FITQLTDENQSCCPVCqrvfqtEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglapgrQSIIDLKEKEIP 747
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 679 NSQKQSLELTSDLSILQMSRKELENQVGSL--KEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVL--SELKLKFEMT 754
Cdd:TIGR00606 748 ELRNKLQKVNRDIQRLKNDIEEQETLLGTImpEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLqgSDLDRTVQQV 827
|
570 580
....*....|....*....|...
gi 1799135528 755 EQEKQSITDELKQCKNNLKLLRE 777
Cdd:TIGR00606 828 NQEKQEKQHELDTVVSKIELNRK 850
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
336-683 |
1.02e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 336 QAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEHLLSKSggdctfihqfiecqkkliVEGHLTKAVEET 415
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS------------------RQISALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 416 KLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEA-KQEIQHLRKELIEAQE 494
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlREALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 495 LARTSKQKCFELQALLEEERKayrnQVEESTKQIQVLQAQLQRLHIDTENLREEKDsEITSTRDELLSARDEILLLHQAA 574
Cdd:TIGR02168 818 EAANLRERLESLERRIAATER----RLEDLEEQIEELSEDIESLAAEIEELEELIE-ELESELEALLNERASLEEALALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 575 AKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNsfqlrcqqcedqqreeatRLQGELEKLRKEWNALET 654
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV------------------RIDNLQERLSEEYSLTLE 954
|
330 340
....*....|....*....|....*....
gi 1799135528 655 ECHSLKRENVLLSSELQRQEKELHNSQKQ 683
Cdd:TIGR02168 955 EAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
467-686 |
1.13e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 467 DDLQGAQSEIE-AKQEIQHLRkELIEAQELARTSKQKCFELQALLEeerkayRNQVEESTKQIQVLQAQLQRLhidtENL 545
Cdd:COG4913 235 DDLERAHEALEdAREQIELLE-PIRELAERYAAARERLAELEYLRA------ALRLWFAQRRLELLEAELEEL----RAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 546 REEKDSEITSTRDELLSARDEILLLHQAAAKVASERdtdIASLQEELKKVRAELERWRKAASEYEKEITSLQNSfqlrcq 625
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRGNGGDR---LEQLEREIERLERELEERERRRARLEALLAALGLP------ 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799135528 626 qcEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNsQKQSLE 686
Cdd:COG4913 375 --LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA-EIASLE 432
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
161-748 |
1.68e-09 |
|
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: 61.67 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 161 YSQELFQLSQYLQEA--LHREQ--MLEQKLATLQRLLAITQEASDtswqALIDedrlLSRLEvmgNQLQACSKNQTEDSL 236
Cdd:pfam15921 83 YSHQVKDLQRRLNESneLHEKQkfYLRQSVIDLQTKLQEMQMERD----AMAD----IRRRE---SQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 237 RKELIA--LQEDKHNYETTAKESLRR-------VLQEKIEVVRKLSEVERSLSNTEDECT--HLKEMNERTQEELRELAN 305
Cdd:pfam15921 152 HELEAAkcLKEDMLEDSNTQIEQLRKmmlshegVLQEIRSILVDFEEASGKKIYEHDSMStmHFRSLGSAISKILRELDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 306 KYNGAVNEIKDLSDKLKVAEGK-QEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEHLLSK 384
Cdd:pfam15921 232 EISYLKGRIFPVEDQLEALKSEsQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 385 sggDCTFIHQFIECQKKLiveGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQmDEQDLNEPLAKvsl 464
Cdd:pfam15921 312 ---NSMYMRQLSDLESTV---SQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQ-ESGNLDDQLQK--- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 465 LKDDLQGAQSEIEAKQE---------------IQHLRKEL----IEAQEL------------------------ARTSKQ 501
Cdd:pfam15921 382 LLADLHKREKELSLEKEqnkrlwdrdtgnsitIDHLRRELddrnMEVQRLeallkamksecqgqmerqmaaiqgKNESLE 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 502 KCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLrEEKDSEITSTRDELLSARDEILLLHQAAAKVASER 581
Cdd:pfam15921 462 KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASL-QEKERAIEATNAEITKLRSRVDLKLQELQHLKNEG 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 582 DtdiaslqeELKKVRAELERWRKAASEYEKEITSLQNSFQlRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLK- 660
Cdd:pfam15921 541 D--------HLRNVQTECEALKLQMAEKDKVIEILRQQIE-NMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKi 611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 661 ---------RENVLLSSELQRQEKELHNSQKQSLELTSD--------LSILQMSRKELEN---QVGSLKEQHLRDSADLK 720
Cdd:pfam15921 612 lkdkkdakiRELEARVSDLELEKVKLVNAGSERLRAVKDikqerdqlLNEVKTSRNELNSlseDYEVLKRNFRNKSEEME 691
|
650 660
....*....|....*....|....*...
gi 1799135528 721 TLLSKAENQAKDVQKEYEKTQTVLSELK 748
Cdd:pfam15921 692 TTTNKLKMQLKSAQSELEQTRNTLKSME 719
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
255-770 |
1.85e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.19 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 255 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNE-------IKDLSDKLKVAEGK 327
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEklniqknIDKIKNKLLKLELL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 328 QEEIQQKGQaEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEHLLSKSGGDCTFIHQFIECQKKLIVEGH 407
Cdd:TIGR04523 203 LSNLKKKIQ-KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 408 LTKAVE------ETKLSKENQTRAKE--SDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAK 479
Cdd:TIGR04523 282 KIKELEkqlnqlKSEISDLNNQKEQDwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 480 QEiqHLRKELIEAQELARTSKQKCFELQAlLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKD---SEITST 556
Cdd:TIGR04523 362 QR--ELEEKQNEIEKLKKENQSYKQEIKN-LESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIErlkETIIKN 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 557 RDELLSARDEILLLHQAAAKVASERD---TDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQRE 633
Cdd:TIGR04523 439 NSEIKDLTNQDSVKELIIKNLDNTREsleTQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 634 EATRLQGElEKLRKEWNALETECHSLKRENVLLSSELQRQ--EKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQ 711
Cdd:TIGR04523 519 ISSLKEKI-EKLESEKKEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE 597
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799135528 712 HL---RDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKN 770
Cdd:TIGR04523 598 KKdliKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
509-778 |
3.88e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 509 LLEEERKAYRNQVEESTKQIQVLQAQLQRLhidtENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERD---TDI 585
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAEL----EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIArleERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 586 ASLQEELKKVRAELERWRKAASEYEKEItslqnsfqlrcqqceDQQREEATRLQGELEKLRKEWNALETECHSLKREnvl 665
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEEL---------------EELEEELEEAEEELEEAEAELAEAEEALLEAEAE--- 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 666 lSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLS 745
Cdd:COG1196 374 -LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270
....*....|....*....|....*....|...
gi 1799135528 746 ELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 778
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
217-720 |
4.86e-09 |
|
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: 60.13 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 217 LEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTakeslrrvlqekieVVRKLSEVERSLSNTEDECTHLKEMNERT 296
Cdd:pfam15921 278 VEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSM--------------YMRQLSDLESTVSQLRSELREAKRMYEDK 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 297 QEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAK-------IEALQADNDF 369
Cdd:pfam15921 344 IEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDD 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 370 TN---ERLTALQEHLLSKSGGDCTFIHQFIECQKKLIVE-GHLTKAVEETK--LSK--ENQTRAKEsdfsdTLSPSKEKS 441
Cdd:pfam15921 424 RNmevQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKvSSLTAQLESTKemLRKvvEELTAKKM-----TLESSERTV 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 442 SDDTTDAQMDEQDLNEPLAKVSLLKddlqgaqSEIEAK-QEIQHLRKE---------LIEAQELARTSKQKCFEL----- 506
Cdd:pfam15921 499 SDLTASLQEKERAIEATNAEITKLR-------SRVDLKlQELQHLKNEgdhlrnvqtECEALKLQMAEKDKVIEIlrqqi 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 507 --------------------QALLEEERKAYRNQVEE-------STKQIQVLQAQLQRLHID--------TENLREEKD- 550
Cdd:pfam15921 572 enmtqlvgqhgrtagamqveKAQLEKEINDRRLELQEfkilkdkKDAKIRELEARVSDLELEkvklvnagSERLRAVKDi 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 551 --------SEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWR--------------KAASE 608
Cdd:pfam15921 652 kqerdqllNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRntlksmegsdghamKVAMG 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 609 YEKEITSLQNsfQLRCQQCEDQQREEATR--------LQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNS 680
Cdd:pfam15921 732 MQKQITAKRG--QIDALQSKIQFLEEAMTnankekhfLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANM 809
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1799135528 681 Q----KQSLELTSDLSILQmsRKELENQvgSLKEQHLRDSADLK 720
Cdd:pfam15921 810 EvaldKASLQFAECQDIIQ--RQEQESV--RLKLQHTLDVKELQ 849
|
|
| CC1_T3JAM |
cd21912 |
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ... |
164-204 |
9.68e-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: 9.68e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1799135528 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21912 5 EILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
237-687 |
1.01e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 237 RKELIALQEDKHNYETTaKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTqEELRELANKYNGAVNEIKD 316
Cdd:PRK03918 282 VKELKELKEKAEEYIKL-SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL-EELKKKLKELEKRLEELEE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 317 LSDKLKVAEGKQEEIQQ----KGQAEKKELQHKIDEMEEKEQELQAKIEALQAD----NDFTNERLTALQEhlLSKSGGD 388
Cdd:PRK03918 360 RHELYEEAKAKKEELERlkkrLTGLTPEKLEKELEELEKAKEEIEEEISKITARigelKKEIKELKKAIEE--LKKAKGK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 389 CTFIHQFI--ECQKKLIVEGHLT-KAVEETKL---SKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEqdLNEPLAKV 462
Cdd:PRK03918 438 CPVCGRELteEHRKELLEEYTAElKRIEKELKeieEKERKLRKELRELEKVLKKESELIKLKELAEQLKE--LEEKLKKY 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 463 SLlkddlqgaqSEIEAK-QEIQHLRKELIEAQELARTSKQKCFELQALlEEERKAYRNQVEESTKQIQVLQAQLQRLHID 541
Cdd:PRK03918 516 NL---------EELEKKaEEYEKLKEKLIKLKGEIKSLKKELEKLEEL-KKKLAELEKKLDELEEELAELLKELEELGFE 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 542 TENLREEKDSEITSTRDELLSARDeilllhqaAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQ 621
Cdd:PRK03918 586 SVEELEERLKELEPFYNEYLELKD--------AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS 657
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799135528 622 lrcqqcedqqREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLEL 687
Cdd:PRK03918 658 ----------EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL 713
|
|
| FHA_TCF19 |
cd22685 |
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ... |
29-119 |
1.12e-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: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 29 KIGRSVARCRPAQNNATFDcKVLSRNHALVW---FDHKTGKFYLQDTkSSNGTFINSQRLSRGSEEsppcEILSGDIIQF 105
Cdd:cd22685 31 RIGRNPEVCDVFLCSSQHP-NLISREHAEIHaerDGNGNWKVLIEDR-STNGTYVNDVRLQDGQRR----ELSDGDTITF 104
|
90
....*....|....*.
gi 1799135528 106 G--VDVTENTRKVTHG 119
Cdd:cd22685 105 GhkNGRRVKQWPYQKS 120
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
14-110 |
2.70e-08 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine/threonine-protein kinase MEK1 and similar proteins; MEK1 (EC 2.7.11.1), also known as MRE4, is a meiosis-specific protein kinase required for chromosome synapsis and meiotic recombination. The recruitment and activation of MEK1 require the phosphorylation of the chromosome axis protein Hop1 at Thr318 (pT318), which is necessary for recognition by the MEK1 FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438722 [Multi-domain] Cd Length: 105 Bit Score: 52.23 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 14 SHPFQERHV---YLDEPIKIGRSvARCRPAQNNATfdckvLSRNHALVW---FDHKTG-KFYLQDTkSSNGTFINSQRLS 86
Cdd:cd22670 7 SSPGSTDIVlpiYKNQVITIGRS-PSCDIVINDPF-----VSRTHCRIYsvqFDESSApLVYVEDL-SSNGTYLNGKLIG 79
|
90 100
....*....|....*....|....*
gi 1799135528 87 RGseespPCEILS-GDIIQFGVDVT 110
Cdd:cd22670 80 RN-----NTVLLSdGDVIEIAHSAT 99
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
472-711 |
3.32e-08 |
|
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: 56.31 E-value: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 472 AQSEIEAKQEIQHLRKELIEAQELARTSKQKcfelQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREekds 551
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 552 EITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQnsfqlrcqqcedQQ 631
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR------------AD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 632 REEATRLQGELEKLRKEWNALETEchsLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQ 711
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAE---LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
28-85 |
4.43e-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: 4.43e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135528 28 IKIGRSvarcrPAQNNATFDCKVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRL 85
Cdd:smart00240 1 VTIGRS-----SEDCDIQLDGPSISRRHAVIVYD-GGGRFYLIDLGSTNGTFVNGKRI 52
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
301-655 |
6.31e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 6.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 301 RELANKYNGAVNEIKDLSDKLKVAEGKQEeiqqkgQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEH 380
Cdd:COG1196 209 AEKAERYRELKEELKELEAELLLLKLREL------EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 381 LlsksggdctfihqfiecqkkliveghltkaveETKLSKENQTRAKESDFSDTLSPSKEKSSDdttdaqmdeqdlnepla 460
Cdd:COG1196 283 L--------------------------------EEAQAEEYELLAELARLEQDIARLEERRRE----------------- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 461 kvslLKDDLQGAQSEI-EAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLh 539
Cdd:COG1196 314 ----LEERLEELEEELaELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 540 idtENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNS 619
Cdd:COG1196 389 ---LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
330 340 350
....*....|....*....|....*....|....*.
gi 1799135528 620 FQLRcQQCEDQQREEATRLQGELEKLRKEWNALETE 655
Cdd:COG1196 466 AELL-EEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
276-752 |
7.09e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 56.34 E-value: 7.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 276 ERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAE---GKQEEIQQKGQAEKKELQHKIDEMEEK 352
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETelcAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 353 EQELQAKIEALQADNDFTNERLTALQEHLLSKSGGDCTFIHQFIECQKKL--IVEGHLTKAVEETKLSKE-NQTRAKESD 429
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIkkLEEDILLLEDQNSKLSKErKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 430 FSDTLSPSKEKSSDDTTDAQMDE---QDLNEPLAKVSLLKDDLQGAQSEIEAkqEIQHLRKELIEAQ----ELARTSKQK 502
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEamiSDLEERLKKEEKGRQELEKAKRKLEG--ESTDLQEQIAELQaqiaELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 503 CFELQALLE--EERKAYRNQVEestKQIQVLQAQLQRLHIDTENLRE-----------------------EKDSEITSTR 557
Cdd:pfam01576 242 EEELQAALArlEEETAQKNNAL---KKIRELEAQISELQEDLESERAarnkaekqrrdlgeelealktelEDTLDTTAAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 558 DELLSARD-EILLLHQAAAKVASERDTDIASLQ--------------EELKKVRAELERWRKA----ASEYEKEITSLQ- 617
Cdd:pfam01576 319 QELRSKREqEVTELKKALEEETRSHEAQLQEMRqkhtqaleelteqlEQAKRNKANLEKAKQAleseNAELQAELRTLQq 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 618 ----------------NSFQLRCQQCEDQQREEA---TRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELH 678
Cdd:pfam01576 399 akqdsehkrkklegqlQELQARLSESERQRAELAeklSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799135528 679 NSQKQSLELTSDLsilqmsrKELENQVGSLKEQhlrdsadlktlLSKAENQAKDVQKEYEKTQTVLSELKLKFE 752
Cdd:pfam01576 479 EETRQKLNLSTRL-------RQLEDERNSLQEQ-----------LEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
167-381 |
7.77e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 7.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTE-----DSLRKELI 241
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvkselKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 242 ALQEDKHNYETTAKESLRRVLQEKI-EVVRKLSEVERSLSNTEDECTHL-KEMNERTQE------ELRELANKYNGAVNE 313
Cdd:TIGR02169 769 ELEEDLHKLEEALNDLEARLSHSRIpEIQAELSKLEEEVSRIEARLREIeQKLNRLTLEkeylekEIQELQEQRIDLKEQ 848
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135528 314 IKDLSDKLKVAEGKQEEIQQKGQ----------AEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEHL 381
Cdd:TIGR02169 849 IKSIEKEIENLNGKKEELEEELEeleaalrdleSRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
231-601 |
8.70e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 8.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 231 QTEDSLRKELIALQEDKHNYEttakESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGA 310
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELE----EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 311 vneikdlsdklkvaegkqeeiqqkgQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEHLLSKSggdct 390
Cdd:TIGR02168 767 -------------------------EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN----- 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 391 fihqfIECQKKLIVEGHLTKAVEETKLSKENQTRAKEsdfsdtlspskekssddttdaqmdeqDLNEPLAKVSLLKDDLQ 470
Cdd:TIGR02168 817 -----EEAANLRERLESLERRIAATERRLEDLEEQIE--------------------------ELSEDIESLAAEIEELE 865
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 471 GAQSEIEAK-QEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEk 549
Cdd:TIGR02168 866 ELIEELESElEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER- 944
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1799135528 550 dseitstrdelLSARDEILLlhQAAAKVASERDTDIASLQEELKKVRAELER 601
Cdd:TIGR02168 945 -----------LSEEYSLTL--EEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
229-712 |
1.11e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 55.82 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 229 KNQTEDSLRK---ELIALQEDKHNYettakeslRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELAn 305
Cdd:TIGR00606 586 INQTRDRLAKlnkELASLEQNKNHI--------NNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRA- 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 306 KYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNdftnERLTALQEHLLSKS 385
Cdd:TIGR00606 657 MLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESEL----KKKEKRRDEMLGLA 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 386 GGDctfiHQFIECQKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQdLNEPLAKVSLL 465
Cdd:TIGR00606 733 PGR----QSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMER-FQMELKDVERK 807
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 466 KDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRN----QVEESTKQIQVLQAQLQRLHID 541
Cdd:TIGR00606 808 IAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHlkskTNELKSEKLQIGTNLQRRQQFE 887
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 542 TENlrEEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQ 621
Cdd:TIGR00606 888 EQL--VELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQ 965
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 622 LRCQQCEDQQREEATRLQGEL-------EKLRKEWNALETECHSLKRENVLLSSELQRQE-----KELHNSQKQSLELTS 689
Cdd:TIGR00606 966 DGKDDYLKQKETELNTVNAQLeecekhqEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKrenelKEVEEELKQHLKEMG 1045
|
490 500
....*....|....*....|....*
gi 1799135528 690 DLSILQMSR--KELENQVGSLKEQH 712
Cdd:TIGR00606 1046 QMQVLQMKQehQKLEENIDLIKRNH 1070
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
178-655 |
1.19e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 178 REQML--EQKLATLQRLLAITQEAsDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKhnyetTAK 255
Cdd:COG4913 241 HEALEdaREQIELLEPIRELAERY-AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAEL-----ERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 256 ESLRRVLQEKIEVVR---------KLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEG 326
Cdd:COG4913 315 EARLDALREELDELEaqirgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 327 KQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEHL---LSKSGGDCTFIHQFIECQKK-- 401
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALaeaLGLDEAELPFVGELIEVRPEee 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 402 ----------------LIVEGH----LTKAVEETKL-------------SKENQTRA-----------KESDFSDTLSPS 437
Cdd:COG4913 475 rwrgaiervlggfaltLLVPPEhyaaALRWVNRLHLrgrlvyervrtglPDPERPRLdpdslagkldfKPHPFRAWLEAE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 438 KEKSSD----DTTDA------------------QMDEQDLNEPLAKVSLLKDDlqgAQSEIEAK-QEIQHLRKELIEAQE 494
Cdd:COG4913 555 LGRRFDyvcvDSPEElrrhpraitragqvkgngTRHEKDDRRRIRSRYVLGFD---NRAKLAALeAELAELEEELAEAEE 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 495 LARTSKQKcfelQALLEEERKAYRNQVEESTKQIQVLQAQLQRlhidtENLREEKDsEITSTRDELLSARDEILLLHQAA 574
Cdd:COG4913 632 RLEALEAE----LDALQERREALQRLAEYSWDEIDVASAEREI-----AELEAELE-RLDASSDDLAALEEQLEELEAEL 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 575 AKVASERD---TDIASLQEELKKVRAELERWRKAASEYEKEITSLQNS-FQLRCQQ--CEDQQREEATRLQGELEKLRKE 648
Cdd:COG4913 702 EELEEELDelkGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAalGDAVERELRENLEERIDALRAR 781
|
....*..
gi 1799135528 649 WNALETE 655
Cdd:COG4913 782 LNRAEEE 788
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
289-760 |
1.27e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 289 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKgQAEKKELQHKIDEMEEKEQELQAKIEALQADND 368
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 369 F--TNERLTALQEHLLSksggdctFIHQFIECQKKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTT 446
Cdd:COG4717 127 LlpLYQELEALEAELAE-------LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 447 DAQMDEQDLNEplakvslLKDDLQGAQSEIE-AKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEEST 525
Cdd:COG4717 200 ELEELQQRLAE-------LEEELEEAQEELEeLEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 526 KQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKA 605
Cdd:COG4717 273 LTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 606 ASEYEKEITSLQ--------NSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQ--EK 675
Cdd:COG4717 353 LREAEELEEELQleeleqeiAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 676 ELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHlrDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTE 755
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQLEEDG--ELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
|
....*
gi 1799135528 756 QEKQS 760
Cdd:COG4717 511 EERLP 515
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
27-106 |
3.59e-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: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 27 PIKIGRSVARcRPAQNNATFDC-----KVLSRNHALVWFDHKTGKFYLQdTKSSNGTFINSQRLSRGseeSPPCEILSGD 101
Cdd:cd22701 18 EVVLGRNSKN-SSSTAADSVDIdlgpsKKISRRHARIFYDFTTQCFELS-VLGRNGVKVDGILVKPG---SPPVPLRSGS 92
|
....*
gi 1799135528 102 IIQFG 106
Cdd:cd22701 93 LIQIG 97
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
506-760 |
6.44e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 6.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 506 LQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDseITSTRDELLSARDEIlllhqaaakvaSERDTDI 585
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG--LVDLSEEAKLLLQQL-----------SELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 586 ASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRcqqcedQQREEATRLQGELEKLRKEWnaleTECHSLKREnvl 665
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQ------QLRAQLAELEAELAELSARY----TPNHPDVIA--- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 666 LSSELQRQEKELHNSQKQSL-ELTSDLSILQMSRKELENQVGSLKEQHLRdsadlktlLSKAENQAKDVQKEYEKTQTVL 744
Cdd:COG3206 296 LRAQIAALRAQLQQEAQRILaSLEAELEALQAREASLQAQLAQLEARLAE--------LPELEAELRRLEREVEVARELY 367
|
250
....*....|....*.
gi 1799135528 745 SELKLKFEMTEQEKQS 760
Cdd:COG3206 368 ESLLQRLEEARLAEAL 383
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
337-655 |
7.94e-07 |
|
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: 52.76 E-value: 7.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 337 AEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEHLLSksggdctfihqfiECQKKL-------IVEGHLT 409
Cdd:pfam13166 89 EESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLD-------------ECWKKIkrkknsaLSEALNG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 410 KAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTT---DAQMDEQDLNEPLA------KVSLLKDDLQGAQSEIEAKQ 480
Cdd:pfam13166 156 FKYEANFKSRLLREIEKDNFNAGVLLSDEDRKAALATvfsDNKPEIAPLTFNVIdfdaleKAEILIQKVIGKSSAIEELI 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 481 EIQHLRKELIEAQELARTSKQKC--------FELQALLEE---------------------------------------E 513
Cdd:pfam13166 236 KNPDLADWVEQGLELHKAHLDTCpfcgqplpAERKAALEAhfddeftefqnrlqkliekvesaissllaqlpavsdlasL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 514 RKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREE--KDSEITSTRDELLSARDEILLLHQAAAKvASERDTDIASLQEE 591
Cdd:pfam13166 316 LSAFELDVEDIESEAEVLNSQLDGLRRALEAKRKDpfKSIELDSVDAKIESINDLVASINELIAK-HNEITDNFEEEKNK 394
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799135528 592 LKKvraelERWRKAASEYEKEITSLQNSFQLRCQQCEDQQrEEATRLQGELEKLRKEWNALETE 655
Cdd:pfam13166 395 AKK-----KLRLHLVEEFKSEIDEYKDKYAGLEKAINSLE-KEIKNLEAEIKKLREEIKELEAQ 452
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
25-114 |
7.99e-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: 7.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 25 DEPIKIGRSVArcrpAQNNATFDC-KVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDII 103
Cdd:cd22663 20 GKEVTVGRGLG----VTYQLVSTCpLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERI----EPLKPYPLNEGDLI 90
|
90
....*....|.
gi 1799135528 104 QFGVDVTENTR 114
Cdd:cd22663 91 QLGVPPENKEP 101
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
26-106 |
9.97e-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: 47.41 E-value: 9.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 26 EPIKIGRSVArcrpaqNNATFDCKVLSRNHALVwfDHKTGKFYLQDTKSSNGTFINSQRLSRGseesppcEILSGDIIQF 105
Cdd:cd22698 21 DEFTIGRSSN------NDIRLNDHSVSRHHARI--VRQGDKCNLTDLGSTNGTFLNGIRVGTH-------ELKHGDRIQL 85
|
.
gi 1799135528 106 G 106
Cdd:cd22698 86 G 86
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
55-108 |
1.28e-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: 1.28e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1799135528 55 HALVWFDHKTGKFYLQDTKSSNGTFINSQRLSrgseESPPCEILSGDIIQFGVD 108
Cdd:cd22704 39 HAVITYDQIDNEFKIKDLGSLNGTFVNDSRIP----EQTYITLKLGDSIRFGYD 88
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
508-683 |
3.03e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 508 ALLEEERKAYRNQVEESTKQIQVLQAQLQRLhiDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVaSERDTDIAS 587
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDAL--QERREALQRLAEYSWDEIDVASAEREIAELEAELERL-DASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 588 LQEELKKVRAELERWRKAASEYEKEITSLQNSFqlrcQQCEDQQREEATRLQGELEKLRKEWNA-LETECHSLKRENVL- 665
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKEL----EQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALGDAVEr 765
|
170 180
....*....|....*....|...
gi 1799135528 666 -----LSSELQRQEKELHNSQKQ 683
Cdd:COG4913 766 elrenLEERIDALRARLNRAEEE 788
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
251-778 |
3.47e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 251 ETTAKESLRRVLQ-EKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELR-ELANKYNGA--VNEIKDLSDKLKVAE- 325
Cdd:PTZ00121 1114 ARKAEEAKKKAEDaRKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKaEEARKAEDAkkAEAARKAEEVRKAEEl 1193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 326 GKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKI------------EALQADNDFTNERLTALQEHLLSKSGGDCTFIH 393
Cdd:PTZ00121 1194 RKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAvkkaeeakkdaeEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK 1273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 394 QFIECQKKLIVEGHLTKAVEETKLSKEnqtrAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQ 473
Cdd:PTZ00121 1274 AEEARKADELKKAEEKKKADEAKKAEE----KKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAK 1349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 474 SEIEAKQEIQHLRKELIEAQELART-SKQKCFELQALLEEERKA--YRNQVEESTKQIQVL------QAQLQRLHIDTEN 544
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEeAKKKADAAKKKAEEKKKAdeAKKKAEEDKKKADELkkaaaaKKKADEAKKKAEE 1429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 545 LRE----EKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAEL----ERWRKAASEYEKEITSL 616
Cdd:PTZ00121 1430 KKKadeaKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAkkkaEEAKKKADEAKKAAEAK 1509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 617 QNSFQLR----CQQCEDQQREEATRLQGELEKLRKEWNALEtechsLKRENVLLSSELQRQEKELHNSQKQSLELTSDLS 692
Cdd:PTZ00121 1510 KKADEAKkaeeAKKADEAKKAEEAKKADEAKKAEEKKKADE-----LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE 1584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 693 ILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKlkfemTEQEKQSITDELKQCKNNL 772
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK-----KEAEEKKKAEELKKAEEEN 1659
|
....*.
gi 1799135528 773 KLLREK 778
Cdd:PTZ00121 1660 KIKAAE 1665
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
588-777 |
3.51e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 588 LQEELKKVRAEL-----ERWRKAASEYEKEITSLQNSfqlrcqqcEDQQREEATRLQGELEKLRKEWNALETECHSLKRE 662
Cdd:COG1196 218 LKEELKELEAELlllklRELEAELEELEAELEELEAE--------LEELEAELAELEAELEELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 663 NVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTL---LSKAENQAKDVQKEYEK 739
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAeeeLEEAEAELAEAEEALLE 369
|
170 180 190
....*....|....*....|....*....|....*...
gi 1799135528 740 TQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLRE 777
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
452-617 |
4.03e-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: 49.76 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 452 EQDLNEPLAKVSLLKDDLQGAQSEI-EAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQ--- 527
Cdd:COG4942 40 EKELAALKKEEKALLKQLAALERRIaALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLgrq 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 528 -------------------------IQVLQAQLQRLHIDTENLREEKDsEITSTRDELLSARDEILLLHQAAAKVASERD 582
Cdd:COG4942 120 pplalllspedfldavrrlqylkylAPARREQAEELRADLAELAALRA-ELEAERAELEALLAELEEERAALEALKAERQ 198
|
170 180 190
....*....|....*....|....*....|....*
gi 1799135528 583 TDIASLQEELKKVRAELERWRKAASEYEKEITSLQ 617
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
588-778 |
4.06e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 588 LQEELKKVRAELERWRKAASEYeKEITSLQNSFQLRCQQCEDQQREEatrlqgELEKLRKEWNALETECHSLKRENVLLS 667
Cdd:COG1196 194 ILGELERQLEPLERQAEKAERY-RELKEELKELEAELLLLKLRELEA------ELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 668 SELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQhlrdSADLKTLLSKAENQAKDVQKEYEKTQTVLSEL 747
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER----RRELEERLEELEEELAELEEELEELEEELEEL 342
|
170 180 190
....*....|....*....|....*....|.
gi 1799135528 748 KLKFEMTEQEKQSITDELKQCKNNLKLLREK 778
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
289-523 |
4.37e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.01 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 289 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQAD-- 366
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDEll 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 367 -------------NDFTNERL-------TALQEHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKAVEETKLSKENQTRAK 426
Cdd:PHA02562 245 nlvmdiedpsaalNKLNTAAAkikskieQFQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 427 EsdfsdtlspskEKSSDDTTDAQMDEQDLNeplAKVSLLKDDLQGAQSEI-EAKQEIQHLRKE-LIEAQELArtskqkcf 504
Cdd:PHA02562 325 L-----------EEIMDEFNEQSKKLLELK---NKISTNKQSLITLVDKAkKVKAAIEELQAEfVDNAEELA-------- 382
|
250
....*....|....*....
gi 1799135528 505 ELQALLEEERKAYRNQVEE 523
Cdd:PHA02562 383 KLQDELDKIVKTKSELVKE 401
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
264-742 |
4.39e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 264 EKIEVVRKLSEVERSLSNTEDECTHLKEMNER---TQEELRELANKYNGAVNEIKDLSDKLkvaEGKQEEIQQKgQAEKK 340
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQareTRDEADEVLEEHEERREELETLEAEI---EDLRETIAET-ERERE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 341 ELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEHLLSKSGGDCTFIHQFIECqkKLIVEGHLTKAVEETKLSKE 420
Cdd:PRK02224 276 ELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEEC--RVAAQAHNEEAESLREDADD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 421 NQTRAKE-----SDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQE-IQHLRKELIEAQE 494
Cdd:PRK02224 354 LEERAEElreeaAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREeRDELREREAELEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 495 LARTSKQKCFELQALLEE----------ERKAYRNQVEESTKQIQVLQAQLQRLHIDTENL-----REEKDSEITSTRDE 559
Cdd:PRK02224 434 TLRTARERVEEAEALLEAgkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVeerleRAEDLVEAEDRIER 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 560 LLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQN---SFQLRCQQCEDQ------ 630
Cdd:PRK02224 514 LEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREevaELNSKLAELKERiesler 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 631 ------QREEATRLQGELEKLRKEWNALETECH---SLKRENVL-LSSELQRQEKELHNSQKQSLE-----LTSDLSILQ 695
Cdd:PRK02224 594 irtllaAIADAEDEIERLREKREALAELNDERRerlAEKRERKReLEAEFDEARIEEAREDKERAEeyleqVEEKLDELR 673
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1799135528 696 MSRKELENQVGSLKEQhLRDSADLKTLLSKAENQAKDVQKEYEKTQT 742
Cdd:PRK02224 674 EERDDLQAEIGAVENE-LEELEELRERREALENRVEALEALYDEAEE 719
|
|
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
462-599 |
5.16e-06 |
|
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: 48.07 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 462 VSLLKDDLQGAQSEIEAK-QEIQHLRKELIEAQELARTSKQKCFELQAlleeerkayrnQVEESTKQIQVLQAQLQRLHI 540
Cdd:pfam06818 12 ISLLKQQLKDSQAEVTQKlNEIVALRAQLRELRAKLEEKEEQIQELED-----------SLRSKTLELEVCENELQRKKN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799135528 541 DTENLRE---EKDSEITSTRDEL--LSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAEL 599
Cdd:pfam06818 81 EAELLREkvgKLEEEVSGLREALsdVSPSGYESVYESDEAKEQRQEEADLGSLRREVERLRAEL 144
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
27-117 |
5.19e-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: 5.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 27 PIKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLsrgSEESPPCEILSGDIIQFG 106
Cdd:cd22678 24 PLTIGRIQ------RGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESI---SPNGRPVVLSSGDVITLG 94
|
90
....*....|.
gi 1799135528 107 vdvTENTRKVT 117
Cdd:cd22678 95 ---SETKILVR 102
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
437-722 |
6.83e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 437 SKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEakqeiqhlrkELIEAQELARTSKQkcfELQALLEEERKA 516
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIE----------RYEEQREQARETRD---EADEVLEEHEER 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 517 yRNQVEESTKQIQVLQAQLQRLHIDTENLREEKdSEITSTRDELLSARDEILllhqAAAKVASERDTDIASLQEELKK-- 594
Cdd:PRK02224 250 -REELETLEAEIEDLRETIAETEREREELAEEV-RDLRERLEELEEERDDLL----AEAGLDDADAEAVEARREELEDrd 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 595 --VRAELERWRKAASEYEKEITSLqnsfqlrcqqcedqqREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQR 672
Cdd:PRK02224 324 eeLRDRLEECRVAAQAHNEEAESL---------------REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE 388
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1799135528 673 QEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTL 722
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTA 438
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
229-781 |
7.79e-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: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 229 KNQTEDSLRKELIALQEDKHNYETTAK---------ESLRRVLQEKIEVVRKLSEVERSlsnTEDECTHLKEMNERTQEE 299
Cdd:pfam05483 94 KVSIEAELKQKENKLQENRKIIEAQRKaiqelqfenEKVSLKLEEEIQENKDLIKENNA---TRHLCNLLKETCARSAEK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 300 LRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKiealqadndftnerltaLQE 379
Cdd:pfam05483 171 TKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEE-----------------YKK 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 380 HLLSKSGGDCTFIHQFIECQKKLiveGHLTKAVEETKlSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPL 459
Cdd:pfam05483 234 EINDKEKQVSLLLIQITEKENKM---KDLTFLLEESR-DKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSM 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 460 AKVSLLKDDLQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQAL-LEEERKAYRNQVEESTKQIQVLQAQLQRl 538
Cdd:pfam05483 310 STQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCsLEELLRTEQQRLEKNEDQLKIITMELQK- 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 539 hidtenlreeKDSEItstrdellsardeilllhQAAAKVASERDTDIaslqEELKKVRAELERWRKAASEYEKEITSLQN 618
Cdd:pfam05483 389 ----------KSSEL------------------EEMTKFKNNKEVEL----EELKKILAEDEKLLDEKKQFEKIAEELKG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 619 SFQlrcqqcedqqreeatRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSR 698
Cdd:pfam05483 437 KEQ---------------ELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLEN 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 699 KELENQVGSL--------------KEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDE 764
Cdd:pfam05483 502 KELTQEASDMtlelkkhqediincKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYE 581
|
570
....*....|....*..
gi 1799135528 765 LKQCKNNLKLLREKGNN 781
Cdd:pfam05483 582 VLKKEKQMKILENKCNN 598
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
51-106 |
1.06e-05 |
|
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also called human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP), is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438729 [Multi-domain] Cd Length: 106 Bit Score: 44.85 E-value: 1.06e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799135528 51 LSRNHALVWF----DHKTGKFYLQDTKSSNGTFINSQRLsrgseesPP---CEILSGDIIQFG 106
Cdd:cd22677 41 ISRYHAVLQYrgdaDDHDGGFYLYDLGSTHGTFLNKQRI-------PPkqyYRLRVGHVLKFG 96
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
213-767 |
1.10e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 213 LLSRLEVMGNQLQACSKNQteDSLRKELIALQE--DKHNYETTAKESLRRVLQEKIE---------VVRKLSEVERSLSN 281
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQL--ASLEEELEKLTEeiSELEKRLEEIEQLLEELNKKIKdlgeeeqlrVKEKIGELEAEIAS 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 282 TEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLsdklkvaEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQA--- 358
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEEL-------EREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdk 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 359 --------------KIEALQADNDFTNERLTALQEHLLSKSgGDCTFIHQFIEC--QKKLIVEGHLTKAVEETKLSKEN- 421
Cdd:TIGR02169 379 efaetrdelkdyreKLEKLKREINELKRELDRLQEELQRLS-EELADLNAAIAGieAKINELEEEKEDKALEIKKQEWKl 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 422 ---------------QTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQG--------------- 471
Cdd:TIGR02169 458 eqlaadlskyeqelyDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGvhgtvaqlgsvgery 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 472 ----------------AQSEIEAKQEIQHLRKE----------------------------------------------- 488
Cdd:TIGR02169 538 ataievaagnrlnnvvVEDDAVAKEAIELLKRRkagratflplnkmrderrdlsilsedgvigfavdlvefdpkyepafk 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 489 -------LIEAQELAR---------TSKQKCFELQALL----EEERKAYRNQVEESTKqIQVLQAQLQRLHIDTENLREE 548
Cdd:TIGR02169 618 yvfgdtlVVEDIEAARrlmgkyrmvTLEGELFEKSGAMtggsRAPRGGILFSRSEPAE-LQRLRERLEGLKRELSSLQSE 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 549 KDsEITSTRDELLSARD-----------EILLLHQAAAKVA----------SERDTDIASLQEELKKVRAELERWRKAAS 607
Cdd:TIGR02169 697 LR-RIENRLDELSQELSdasrkigeiekEIEQLEQEEEKLKerleeleedlSSLEQEIENVKSELKELEARIEELEEDLH 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 608 EYEKEITSLQNSF----------QLRCQQCEDQQREEATR-LQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKE 676
Cdd:TIGR02169 776 KLEEALNDLEARLshsripeiqaELSKLEEEVSRIEARLReIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE 855
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 677 LHNSQKQSLELTSDLSILQMSRKELENQVGSLKeqhlRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQ 756
Cdd:TIGR02169 856 IENLNGKKEELEEELEELEAALRDLESRLGDLK----KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
730
....*....|.
gi 1799135528 757 EKQSITDELKQ 767
Cdd:TIGR02169 932 ELSEIEDPKGE 942
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
52-106 |
1.24e-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: 1.24e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135528 52 SRNH-ALVWfdHK-TGKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22674 48 SRVHaALVY--HKhLNRVFLIDLGSTHGTFVGGIRL----EPHKPQQLPIDSTLRFG 98
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
336-738 |
1.26e-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: 48.53 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 336 QAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEHLLSKSGGDctfihqfiecqKKLIvegHLTKAVEET 415
Cdd:pfam05622 6 QEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGG-----------KKYL---LLQKQLEQL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 416 KlskENQTRAKESdfSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKD--DLQGAQSEIEAKQE--IQHLRKELIE 491
Cdd:pfam05622 72 Q---EENFRLETA--RDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDemDILRESSDKVKKLEatVETYKKKLED 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 492 AQELARTSKQ------KCFELQALLEEERKAY---RNQVEESTKQIQVLQAQLQRLHIDTENLR------EEKDSEITST 556
Cdd:pfam05622 147 LGDLRRQVKLleernaEYMQRTLQLEEELKKAnalRGQLETYKRQVQELHGKLSEESKKADKLEfeykklEEKLEALQKE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 557 RDELLSARD------EILLLHQAAAKVASERDTDIASLQEELKKVRAELerwrkAASEYEKEITSLQNSFQ-LRCQQcED 629
Cdd:pfam05622 227 KERLIIERDtlretnEELRCAQLQQAELSQADALLSPSSDPGDNLAAEI-----MPAEIREKLIRLQHENKmLRLGQ-EG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 630 QQREEATRLQGELEKLRKEWNALETEcHSLKRENVLLSS----ELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQV 705
Cdd:pfam05622 301 SYRERLTELQQLLEDANRRKNELETQ-NRLANQRILELQqqveELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSEL 379
|
410 420 430
....*....|....*....|....*....|....*
gi 1799135528 706 GSLKEQ--HLRDSADLKTLLSKAENQAKDVQKEYE 738
Cdd:pfam05622 380 QKKKEQieELEPKQDSNLAQKIDELQEALRKKDED 414
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
310-580 |
1.32e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 310 AVNEIKDLSDKLKVAEGKQEEIQqkgqAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEhllsksggdc 389
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQ----AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA---------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 390 tfihqfiecqkkliveghltkavEETKLSKENQTRAKESdfsdtlspSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDL 469
Cdd:COG3883 80 -----------------------EIEERREELGERARAL--------YRSGGSVSYLDVLLGSESFSDFLDRLSALSKIA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 470 QGAQSEIEakqEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEK 549
Cdd:COG3883 129 DADADLLE---ELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
250 260 270
....*....|....*....|....*....|.
gi 1799135528 550 DSEITSTRDELLSARDEILLLHQAAAKVASE 580
Cdd:COG3883 206 AAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
28-106 |
1.62e-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: 44.25 E-value: 1.62e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135528 28 IKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDhkTGKFYLQDTKSSNGTFINSQRlsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22680 23 VSIGRDP------ENVIVIPDPFVSRNHARITVD--SNEIYIEDLGSTNGTFVNDFK-----RIKGPAKLHPNDIIKLG 88
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
266-772 |
2.33e-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: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 266 IEVVRKLSEVERSLSNTEDECTHLkemnertqEELRELANKYNGAVNEIKDLSDKLKVAEgkqeeiQQKGQAEKKELQHK 345
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELL--------EPIRELAERYAAARERLAELEYLRAALR------LWFAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 346 IDEMEEKEQELQAKIEALQADNDFTNERLTALQEHLLSKSGGDCTFIHQFIECQKKLIVE-----GHLTKAVEETKLS-- 418
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEErerrrARLEALLAALGLPlp 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 419 ------KENQTRAKEsdFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQeiQHLRKELieA 492
Cdd:COG4913 377 asaeefAALRAEAAA--LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL--LALRDAL--A 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 493 QELARTSKQKCF--ELQALLEEER-------KAYRNQ-----VEESTKQiQVLQA--QLQ-RLHIDTENLREEKDSEITS 555
Cdd:COG4913 451 EALGLDEAELPFvgELIEVRPEEErwrgaieRVLGGFaltllVPPEHYA-AALRWvnRLHlRGRLVYERVRTGLPDPERP 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 556 TRDEllsardeilllHQAAAKVASERDTDIASLQEELKKVRA--------ELERWRKAaseyekeITS---LQNSFQLRc 624
Cdd:COG4913 530 RLDP-----------DSLAGKLDFKPHPFRAWLEAELGRRFDyvcvdspeELRRHPRA-------ITRagqVKGNGTRH- 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 625 qQCEDQQREEATRLQGE-----LEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRK 699
Cdd:COG4913 591 -EKDDRRRIRSRYVLGFdnrakLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE 669
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799135528 700 --ELENQVGSLkeqhLRDSADLKTLlskaENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNL 772
Cdd:COG4913 670 iaELEAELERL----DASSDDLAAL----EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
212-654 |
2.43e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 212 RLLSRLEVMGNQLQACSKNQTEdsLRKELIALQEDKHNYETTAK-ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLK 290
Cdd:COG4717 92 ELQEELEELEEELEELEAELEE--LREELEKLEKLLQLLPLYQElEALEAELAELPERLEELEERLEELRELEEELEELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 291 EMNERTQEELRELANKYNGAV-NEIKDLSDKLKVAegkqeeiqqkgQAEKKELQHKIDEMEEKEQELQAKIEALQAD--N 367
Cdd:COG4717 170 AELAELQEELEELLEQLSLATeEELQDLAEELEEL-----------QQRLAELEEELEEAQEELEELEEELEQLENEleA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 368 DFTNERLTALQEHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKAVEETKLSKENQTRAKESdfsdtLSPSKEKSSDDTTD 447
Cdd:COG4717 239 AALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAS-----LGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 448 AQMDEQDLNEPLAKVSLLKDdlQGAQSEIEAKQEIQHLRKELIEAQELARTSKQKCF--ELQALLEEERKAYRNQVEEST 525
Cdd:COG4717 314 EELEEEELEELLAALGLPPD--LSPEELLELLDRIEELQELLREAEELEEELQLEELeqEIAALLAEAGVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 526 KQIQVLQAQLQRLHIDTENLREEKDSeitstrdellsardeilLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKA 605
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGE-----------------LEELLEALDEEELEEELEELEEELEELEEELEELREE 454
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1799135528 606 ASEYEKEITSLQNSFQLrcqqceDQQREEATRLQGELEKLRKEWNALET 654
Cdd:COG4717 455 LAELEAELEQLEEDGEL------AELLQELEELKAELRELAEEWAALKL 497
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
297-551 |
2.52e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 297 QEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQkgqaEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTA 376
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK----QLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 377 LQEHLlsksggdctfihqfiECQKKLIVEghLTKAVEETKLSKENQTRAKESDFSDTLspSKEKSSDDTTDAQMDE-QDL 455
Cdd:COG4942 95 LRAEL---------------EAQKEELAE--LLRALYRLGRQPPLALLLSPEDFLDAV--RRLQYLKYLAPARREQaEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 456 NEPLAKVSLLKDDLQgaqseiEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQL 535
Cdd:COG4942 156 RADLAELAALRAELE------AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250
....*....|....*.
gi 1799135528 536 QRLHIDTENLREEKDS 551
Cdd:COG4942 230 ARLEAEAAAAAERTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
328-551 |
2.66e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 328 QEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEHLlsksggdctfihQFIECQKKLIVEGH 407
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI------------RALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 408 LTKAVEETKLSKENQTRAKEsdFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEakqEIQHLRK 487
Cdd:COG4942 86 AELEKEIAELRAELEAQKEE--LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAE---ELRADLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799135528 488 ELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDS 551
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| FHA_RAD53-like_rpt2 |
cd22690 |
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
12-103 |
3.02e-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: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 12 PNSHPfqerHVYL-DEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFD-HKTGK--FYLQDTkSSNGTFINSQRLSR 87
Cdd:cd22690 8 NPSYP----DIELtQNTTFIGRS------KDCDEEITDPRISKHHCIITRKrSGKGLddVYVTDT-STNGTFINNNRLGK 76
|
90
....*....|....*.
gi 1799135528 88 GSEesppCEILSGDII 103
Cdd:cd22690 77 GSQ----SLLQDGDEI 88
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
237-639 |
3.02e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.59 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 237 RKELIALQEDKHNYETTAK--ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERtQEELRELANKYNGAVNEI 314
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQilSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQ-ILELEGYEMDYNSYLKSI 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 315 KDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEHLLSKSggdctfihq 394
Cdd:PRK01156 373 ESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELS--------- 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 395 fiecQKKLIVEGHLTKAVEETKLSKENQTRAKEsDFSDTLSPSKEkssdDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQS 474
Cdd:PRK01156 444 ----RNMEMLNGQSVCPVCGTTLGEEKSNHIIN-HYNEKKSRLEE----KIREIEIEVKDIDEKIVDLKKRKEYLESEEI 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 475 E--IEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEEstKQIQVLQAQLQRLHIDTENLREEKDsE 552
Cdd:PRK01156 515 NksINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDS--KRTSWLNALAVISLIDIETNRSRSN-E 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 553 ITSTRDELLSARDEILLlhqAAAKVASERDTDIASLQEELKKVR----------AELERWRKAASEYEKEITSL------ 616
Cdd:PRK01156 592 IKKQLNDLESRLQEIEI---GFPDDKSYIDKSIREIENEANNLNnkyneiqenkILIEKLRGKIDNYKKQIAEIdsiipd 668
|
410 420
....*....|....*....|...
gi 1799135528 617 QNSFQLRCQQCEDQQREEATRLQ 639
Cdd:PRK01156 669 LKEITSRINDIEDNLKKSRKALD 691
|
|
| FHA_CHFR |
cd22672 |
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ... |
49-105 |
3.74e-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: 3.74e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135528 49 KVLSRNHALVWFDHKtGKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQF 105
Cdd:cd22672 39 KLVSGDHCKIIRDEK-GQVWLEDT-STNGTLVNKVKVVKGQK----VELKHGDVIYL 89
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
14-106 |
3.81e-05 |
|
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.
Pssm-ID: 438734 [Multi-domain] Cd Length: 96 Bit Score: 43.29 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 14 SHPFQERHvyldepIKIGRSVarcrpaQNNATFDCKVLSRNHALvwFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEesp 93
Cdd:cd22682 14 QFPITEST------IVIGRSV------ESQVQIDDDSVSRYHAK--LAVNPSAVSIIDLGSTNGTIVNGKKIPKLAS--- 76
|
90
....*....|...
gi 1799135528 94 pCEILSGDIIQFG 106
Cdd:cd22682 77 -CDLQNGDQIKIG 88
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
25-108 |
4.24e-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: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 25 DEPIKIGRsvarcRPAQNNAT----FDCKVLSRNHALVWFdhKTGKFYLQDTKSSNGTFINSQRLSR-GSEESPPCEILS 99
Cdd:cd22702 31 KQPCIIGS-----DPHQAISGisvvIPSPQVSELHARITC--KNGAFFLTDLGSEHGTWINDNEGRRyRAPPNFPVRLHP 103
|
....*....
gi 1799135528 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 |
5.10e-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: 5.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135528 18 QERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhkTGKFYLQDTKSSNGTFINSQRLS 86
Cdd:cd22694 8 GELRFDPGSSVRIGRD------PDADVRLDDPRVSRRHALLEFD--GDGWVYTDLGSRNGTYLNGRRVQ 68
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
444-605 |
5.23e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 444 DTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIE-AKQEIQHLRKELIEAQELARTSKQKcfelQALLEEERKAYRNQVE 522
Cdd:COG4913 662 DVASAEREIAELEAELERLDASSDDLAALEEQLEeLEAELEELEEELDELKGEIGRLEKE----LEQAEEELDELQDRLE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 523 ESTKQIQV-----LQAQLQRLHID--TENLREEKDSEITSTRDELLSARDEILLLHQAAAKV----ASERDTDIASL--- 588
Cdd:COG4913 738 AAEDLARLelralLEERFAAALGDavERELRENLEERIDALRARLNRAEEELERAMRAFNREwpaeTADLDADLESLpey 817
|
170 180
....*....|....*....|..
gi 1799135528 589 QEELKKVRAE-----LERWRKA 605
Cdd:COG4913 818 LALLDRLEEDglpeyEERFKEL 839
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
322-760 |
5.31e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 46.66 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 322 KVAEGKQEEIQQKGQAEKKELQHKidemeEKEQELQAKIEALQADNDFTNERLTALQEHLLSKSGGDctfiHQFIECQKK 401
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHK-----RARIELEKKASALKRQLDRESDRNQELQKRIRLLEKRE----AEAEEALRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 402 LIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQgaqsEIEAK-Q 480
Cdd:pfam05557 74 QAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLD----LLKAKaS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 481 EIQHLRKELIEAQELARTSKQKCFELqalleEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDEL 560
Cdd:pfam05557 150 EAEQLRQNLEKQQSSLAEAEQRIKEL-----EFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 561 LSARDeillLHQAAAKVASERDT--DIASLQEELKKVRAELERWRKAASEYEKEITS--LQNSFQLRCQQCEDQQREEAT 636
Cdd:pfam05557 225 LLKEE----VEDLKRKLEREEKYreEAATLELEKEKLEQELQSWVKLAQDTGLNLRSpeDLSRRIEQLQQREIVLKEENS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 637 RLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDL----SILQMSRKELENQVGSlkEQH 712
Cdd:pfam05557 301 SLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgyrAILESYDKELTMSNYS--PQL 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1799135528 713 LRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 760
Cdd:pfam05557 379 LERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQA 426
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
255-601 |
6.01e-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: 46.89 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 255 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQE-----------ELRELANKYNGAVNEIKDLSDKLKV 323
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEyyqlkekleleEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 324 AEGKQEEIQQKGQ---AEKKELQHKIDEMEEKEQELQaKIEALQADNDFTNERLTALQEHLLSKSGGDCTFIHQfIECQK 400
Cdd:pfam02463 248 DEQEEIESSKQEIekeEEKLAQVLKENKEEEKEKKLQ-EEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE-KEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 401 KLIVEGHLTKAVEETKLSKENQTRAKESDfsdtlspsKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAKQ 480
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAE--------EEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEEL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 481 EIQHlrKELIEAQELARTSKQKcfELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEiTSTRDEL 560
Cdd:pfam02463 398 ELKS--EEEKEAQLLLELARQL--EDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL-ELKKSED 472
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1799135528 561 LSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELER 601
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLL 513
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
525-737 |
6.15e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 525 TKQIQVLQAQLQRLhidtenlrEEKDSEITSTRDELLSARDEILLLHQAAAKVA--SERDTDIASLQEELKKVRAELERW 602
Cdd:COG4913 609 RAKLAALEAELAEL--------EEELAEAEERLEALEAELDALQERREALQRLAeySWDEIDVASAEREIAELEAELERL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 603 RKAASEYEkeitslqnsfqlrcqqcedqqreeatRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQK 682
Cdd:COG4913 681 DASSDDLA--------------------------ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799135528 683 QSLELTSDLSILQmsRKELENQVGSLKEQHLRDS---------ADLKTLLSKAENQAKDVQKEY 737
Cdd:COG4913 735 RLEAAEDLARLEL--RALLEERFAAALGDAVERElrenleeriDALRARLNRAEEELERAMRAF 796
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
478-700 |
6.40e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 478 AKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAY---RNQVEESTKQIQVLQAQLQRLHIDTENLREE------ 548
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYnelQAELEALQAEIDKLQAEIAEAEAEIEERREElgerar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 549 ---KDSEITSTRDELLSARDEILLLHQAAA-KVASERDTDIAslqEELKKVRAELERWRKAASEYEKEITSLQnsfqlrc 624
Cdd:COG3883 94 alyRSGGSVSYLDVLLGSESFSDFLDRLSAlSKIADADADLL---EELKADKAELEAKKAELEAKLAELEALK------- 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799135528 625 qqceDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKE 700
Cdd:COG3883 164 ----AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
13-110 |
6.80e-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: 6.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 13 NSHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTgkFYLQDTKSSNGTFINSQRLSrgsee 91
Cdd:cd22665 7 SQAHGPEKDFPLYEgENVIGRD------PSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRL----- 73
|
90 100
....*....|....*....|.
gi 1799135528 92 SPPC--EILSGDIIQFGvDVT 110
Cdd:cd22665 74 KPNVryELIDGDLLLFG-DVK 93
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
190-778 |
7.19e-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: 46.50 E-value: 7.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 190 QRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYET----TAKESLRRVLQEK 265
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNeeriDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 266 IEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVA-EGKQEEIQQKGQAEKKELQH 344
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDdEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 345 KIDEMEEKEQELQAKIEALQADNDfTNERLTALQEHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKAVEETKLSKENQTR 424
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEE-EEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 425 AKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLqgAQSEIEAKQEIQHLRKELIEAQELARTSKQKCf 504
Cdd:pfam02463 412 ELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQ--ELKLLKDELELKKSEDLLKETQLVKLQEQLEL- 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 505 ELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARD------EILLLHQAAAKVA 578
Cdd:pfam02463 489 LLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVivevsaTADEVEERQKLVR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 579 SERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHS 658
Cdd:pfam02463 569 ALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGL 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 659 LKRENVLLS----SELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQ 734
Cdd:pfam02463 649 RKGVSLEEGlaekSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQ 728
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1799135528 735 KEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 778
Cdd:pfam02463 729 EAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLK 772
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
216-778 |
9.15e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.05 E-value: 9.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 216 RLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTaKESLRRVLQEKIEVVRKLSEVERSLSNTEDECthlkemnER 295
Cdd:PRK01156 151 RKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYL-EEKLKSSNLELENIKKQIADDEKSHSITLKEI-------ER 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 296 TQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIqQKGQAEKKELQHKIDEMEEKEQELqakiealqadNDFTNERLT 375
Cdd:PRK01156 223 LSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI-KTAESDLSMELEKNNYYKELEERH----------MKIINDPVY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 376 ALQEHllsksggdctfIHQFIECQKKLIVEGHLTKAVeETKLSKENQTRAKESDFsdtlspskEKSSDDTTDAQMDEQDL 455
Cdd:PRK01156 292 KNRNY-----------INDYFKYKNDIENKKQILSNI-DAEINKYHAIIKKLSVL--------QKDYNDYIKKKSRYDDL 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 456 NEPLAKVSLLKDDLQGAQSEIEA-KQEIQHLRKElieaQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIqvlQAQ 534
Cdd:PRK01156 352 NNQILELEGYEMDYNSYLKSIESlKKKIEEYSKN----IERMSAFISEILKIQEIDPDAIKKELNEINVKLQDI---SSK 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 535 LQRLHIDTENLREEKDSeitstrdelLSARDEILLLHQAAAKVASERDTDiaslqeelkKVRAELERWRKAASEYEKEIT 614
Cdd:PRK01156 425 VSSLNQRIRALRENLDE---------LSRNMEMLNGQSVCPVCGTTLGEE---------KSNHIINHYNEKKSRLEEKIR 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 615 SLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRenvLLSSELQRQEKELHNSQKQSLELTSDLSIL 694
Cdd:PRK01156 487 EIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLED---IKIKINELKDKHDKYEEIKNRYKSLKLEDL 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 695 QMSRKELenqvgsLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKL 774
Cdd:PRK01156 564 DSKRTSW------LNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNE 637
|
....
gi 1799135528 775 LREK 778
Cdd:PRK01156 638 IQEN 641
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
162-756 |
1.03e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.97 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 162 SQELFQLSQYLQEALHR----EQMLEQKLATLQRLLAITQEASDTSWQALIDEDRllsRLEVMGNQLQACSKNQTEDSLR 237
Cdd:pfam10174 129 AKELFLLRKTLEEMELRietqKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWER---TRRIAEAEMQLGHLEVLLDQKE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 238 KELIALQEDKH-NYETTAKESLRRVLQEKIEVV-RKLSEVERSLSNTEDECTHLKEMNERTQEELRElankyngavnEIK 315
Cdd:pfam10174 206 KENIHLREELHrRNQLQPDPAKTKALQTVIEMKdTKISSLERNIRDLEDEVQMLKTNGLLHTEDREE----------EIK 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 316 dlsdKLKVAEGKQEEIQQKGQAEKKELQHKIDEMeekeQELQAKIEALQADNDFTNERLTALQEHLLSKSggdctfihqf 395
Cdd:pfam10174 276 ----QMEVYKSHSKFMKNKIDQLKQELSKKESEL----LALQTKLETLTNQNSDCKQHIEVLKESLTAKE---------- 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 396 iecQKKLIVEGHLTKAveETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQmDEQDLNEplAKVSLLKDDLQGAQSE 475
Cdd:pfam10174 338 ---QRAAILQTEVDAL--RLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLK-DMLDVKE--RKINVLQKKIENLQEQ 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 476 IEAK-QEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEkdseIT 554
Cdd:pfam10174 410 LRDKdKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEK----VS 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 555 STRDELLSARDEILLLHQAAAKVAS---ERDTDIASLQEELKKVRAELERW----RKAASEYEKEITSLQNSFQLRCQQC 627
Cdd:pfam10174 486 ALQPELTEKESSLIDLKEHASSLASsglKKDSKLKSLEIAVEQKKEECSKLenqlKKAHNAEEAVRTNPEINDRIRLLEQ 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 628 EDQQ-REEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQsleltsdlsiLQMSRKELENQVG 706
Cdd:pfam10174 566 EVARyKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVAN----------IKHGQQEMKKKGA 635
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1799135528 707 SLKEQHLRDSADLKTllSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQ 756
Cdd:pfam10174 636 QLLEEARRREDNLAD--NSQQLQLEELMGALEKTRQELDATKARLSSTQQ 683
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
294-537 |
1.14e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 294 ERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALqadndftNER 373
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL-------GER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 374 LTALQehllsKSGGDCTFIHQFIECQkkliveghltkaveetklskenqtrakesDFSDTLspSKEKSSDDTTDAQMDEq 453
Cdd:COG3883 92 ARALY-----RSGGSVSYLDVLLGSE-----------------------------SFSDFL--DRLSALSKIADADADL- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 454 dlnepLAKVSLLKDDLQGAQSEIEAKQ-EIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQ 532
Cdd:COG3883 135 -----LEELKADKAELEAKKAELEAKLaELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
....*
gi 1799135528 533 AQLQR 537
Cdd:COG3883 210 AAAAA 214
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
239-526 |
1.28e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.69 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 239 ELIALQEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLsntedecthLKEMNERTQEELRELANKYNGAVNEIkdls 318
Cdd:PRK05771 32 HIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPL---------REEKKKVSVKSLEELIKDVEEELEKI---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 319 dklkvaegkQEEIqqkgqaekKELQHKIDEMEEKEQELQAKIEALQ--ADNDFTNERLtalqehllsksgGDCTFIHQFI 396
Cdd:PRK05771 99 ---------EKEI--------KELEEEISELENEIKELEQEIERLEpwGNFDLDLSLL------------LGFKYVSVFV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 397 ecqkkliveGHLTKAVEETKLSKENQTRAKESDFSDTLSP-----SKEkssddttdaqmDEQDLNEPLAKVSLLKDDLQ- 470
Cdd:PRK05771 150 ---------GTVPEDKLEELKLESDVENVEYISTDKGYVYvvvvvLKE-----------LSDEVEEELKKLGFERLELEe 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135528 471 -GAQSEI--EAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTK 526
Cdd:PRK05771 210 eGTPSELirEIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAEALSK 268
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
234-704 |
1.71e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 234 DSLRKELIALQEDKHNYETtAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNER--TQEELRELANKYNGAV 311
Cdd:COG4717 74 KELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELeaLEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 312 NEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEHLlsksggdctf 391
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL---------- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 392 ihQFIECQKKLIVEGHLTKAVEEtKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMdeQDLNEPLAKVSLLKDDLQG 471
Cdd:COG4717 223 --EELEEELEQLENELEAAALEE-RLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV--LFLVLGLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 472 AQSEIEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQveestKQIQVLQAQLQRLH--IDTENLREEK 549
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRI-----EELQELLREAEELEeeLQLEELEQEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 550 DSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAasEYEKEITSLQnsfqlrcqqced 629
Cdd:COG4717 373 AALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELE------------ 438
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135528 630 qqrEEATRLQGELEKLRKEWNALETECHSLKRENVL--LSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQ 704
Cdd:COG4717 439 ---EELEELEEELEELREELAELEAELEQLEEDGELaeLLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
52-107 |
2.38e-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: 2.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799135528 52 SRNHALVWFDHKTG---------KFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQFGV 107
Cdd:cd22667 40 SRKHATLTVLHPEAnlsdpdtrpELTLKDL-SKYGTFVNGEKLKGGSE----VTLKDGDVITFGV 99
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
451-662 |
2.79e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 451 DEQDLNEPLAKVSLLKDDLQGAQSEIEAKQ-EIQHLRKELIEAQELARTSKQKCFELQALlEEERKAYRNQVEESTKQIQ 529
Cdd:COG4913 645 ERREALQRLAEYSWDEIDVASAEREIAELEaELERLDASSDDLAALEEQLEELEAELEEL-EEELDELKGEIGRLEKELE 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 530 VLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERD---TDIASLQEELKKVRAE-LERWRKA 605
Cdd:COG4913 724 QAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDalrARLNRAEEELERAMRAfNREWPAE 803
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135528 606 ASEYEKEITSLqNSFQlrcQQCEDQQREEATRLQGELEKLRKEW--NALETECHSLKRE 662
Cdd:COG4913 804 TADLDADLESL-PEYL---ALLDRLEEDGLPEYEERFKELLNENsiEFVADLLSKLRRA 858
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
574-790 |
3.01e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 574 AAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQlRCQQCEDQQREEATRLQGELEKLRKEwnaLE 653
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE-ALQAEIDKLQAEIAEAEAEIEERREE---LG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 654 TECHSLKRE-------NVLLSSE-----LQRQE--KELHNSQKQSLELTSDLsilqmsRKELENQVGSLKEQhlrdSADL 719
Cdd:COG3883 90 ERARALYRSggsvsylDVLLGSEsfsdfLDRLSalSKIADADADLLEELKAD------KAELEAKKAELEAK----LAEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799135528 720 KTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNNPSILQPVPA 790
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
1-106 |
3.62e-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: 43.60 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 1 MPSALAIFTCRPNSHPFQERHVYLDEPIKIGRSvARC-----RPAQnnatfdckVLSRNHALVWFDHktGKFYLQDTkSS 75
Cdd:COG3456 1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRS-ADCdwvlpDPDR--------SVSRRHAEIRFRD--GAFCLTDL-ST 68
|
90 100 110
....*....|....*....|....*....|...
gi 1799135528 76 NGTFIN--SQRLSRGSEEsppcEILSGDIIQFG 106
Cdd:COG3456 69 NGTFLNgsDHPLGPGRPV----RLRDGDRLRIG 97
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
444-619 |
3.65e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 444 DTTDAQMDE--QDLNEPLAKVSLLKDDLQGAQSEI-EAKQEIQHLRKELIE-AQELARTSKQKCFeLQALLEEE------ 513
Cdd:COG3883 40 DALQAELEElnEEYNELQAELEALQAEIDKLQAEIaEAEAEIEERREELGErARALYRSGGSVSY-LDVLLGSEsfsdfl 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 514 -RKAYRNQVEESTKQ-IQVLQAQLQRLhidtenlrEEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEE 591
Cdd:COG3883 119 dRLSALSKIADADADlLEELKADKAEL--------EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
|
170 180
....*....|....*....|....*...
gi 1799135528 592 LKKVRAELERWRKAASEYEKEITSLQNS 619
Cdd:COG3883 191 EAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
480-776 |
3.73e-04 |
|
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: 43.73 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 480 QEIQHLRKELIEAQELARTSKQKCFELQallEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLrEEKDSEITSTRDE 559
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKEKERY---KRDREQWERQRRELESRVAELKEELRQSREKHEEL-EEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 560 LLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWR---KAASEYEKEITSLQNSFQLRCQQCEDQQREEAT 636
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKeraKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 637 RLQG----------------------------------ELEKLRKEWNALETECHSLKRENVLLSSELQ-------RQEK 675
Cdd:pfam07888 193 EFQElrnslaqrdtqvlqlqdtittltqklttahrkeaENEALLEELRSLQERLNASERKVEGLGEELSsmaaqrdRTQA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 676 ELHNSQKQSLELTSDLSILQMSRKELENQvGSLKEQHLRDSADLKTllSKAENQAKDVQKEYEKTQTVLSE-LKLKFEMT 754
Cdd:pfam07888 273 ELHQARLQAAQLTLQLADASLALREGRAR-WAQERETLQQSAEADK--DRIEKLSAELQRLEERLQEERMErEKLEVELG 349
|
330 340
....*....|....*....|..
gi 1799135528 755 eQEKQSITDELKQCKNNLKLLR 776
Cdd:pfam07888 350 -REKDCNRVQLSESRRELQELK 370
|
|
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
53-106 |
3.82e-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: 3.82e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1799135528 53 RNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPceilsGDIIQFG 106
Cdd:cd22700 36 EQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAP-----GDVLRFG 84
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
153-365 |
4.25e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 153 VAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQAcSKNQT 232
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA-ELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 233 EDSLRKELIALQEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEdectHLKEMNERTQEELRELANKyngaVN 312
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ----YLKYLAPARREQAEELRAD----LA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1799135528 313 EIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQA 365
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
634-780 |
4.67e-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: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 634 EATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNsQKQSLELTSDLSilqmsrkELENQVGSLKeqhl 713
Cdd:pfam15294 134 EIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGA-KKDVKSNLKEIS-------DLEEKMAALK---- 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135528 714 rdsADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGN 780
Cdd:pfam15294 202 ---SDLEKTLNASTALQKSLEEDLASTKHELLKVQEQLEMAEKELEKKFQQTAAYRNMKEMLTKKNE 265
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
16-111 |
6.91e-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: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 16 PFQERHVYLD-EPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFdhKTGKFYLQDTKSSNGTFINSQRLSRgseespP 94
Cdd:cd22693 7 TLQGQTFPIDkSGITIGRA------DDNDLVLSDDFVSSRHARIYL--QGSSWYLEDLGSTNGTFVNGNRVTQ------P 72
|
90
....*....|....*..
gi 1799135528 95 CEILSGDIIQFGVDVTE 111
Cdd:cd22693 73 VVVQPGDTIRIGATVFE 89
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
507-747 |
7.34e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 507 QALLEEERKAYRNQVEESTKQIQVLQAQLQrlhiDTENLREEkdseITSTRDELLSARDEILLLHQAAAKVASER--DTD 584
Cdd:PRK11281 51 QKLLEAEDKLVQQDLEQTLALLDKIDRQKE----ETEQLKQQ----LAQAPAKLRQAQAELEALKDDNDEETRETlsTLS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 585 IASLQEELKKVRAELERWRKAASEYEKEITSLQN----------SFQLRCQQCEDQ----QREEATRLQGELEKLRKEWN 650
Cdd:PRK11281 123 LRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTqperaqaalyANSQRLQQIRNLlkggKVGGKALRPSQRVLLQAEQA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 651 ALEtechslkrenvlLSSELQRQEKElHNSQKQSL-ELTSDLSILQMSRKELENQvgslkeqhlrdsaDLKTL-----LS 724
Cdd:PRK11281 203 LLN------------AQNDLQRKSLE-GNTQLQDLlQKQRDYLTARIQRLEHQLQ-------------LLQEAinskrLT 256
|
250 260
....*....|....*....|...
gi 1799135528 725 KAENQAKDVQKEYEKTQTVLSEL 747
Cdd:PRK11281 257 LSEKTVQEAQSQDEAARIQANPL 279
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
49-112 |
7.35e-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: 7.35e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135528 49 KVLSRNHALVWFDHKTG--KFYLQDTKSSNGTFINsqrlsrgSEESPPC---EILSGDIIQFGVDVTEN 112
Cdd:cd22681 64 ETCSKQHCVIQFRNVKGilKPYIMDLDSSNGTCLN-------DNVIPSSryvELRSGDVITFSKSNDYE 125
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
239-778 |
8.64e-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: 42.79 E-value: 8.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 239 ELIALQEDKHNYETTAKES-LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDL 317
Cdd:pfam05483 222 EKIQHLEEEYKKEINDKEKqVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDI 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 318 SDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQEL-QAKIEALQADNDF-----TNERLTALQEHLLSKSGGDCTF 391
Cdd:pfam05483 302 KMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELnKAKAAHSFVVTEFeattcSLEELLRTEQQRLEKNEDQLKI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 392 IHqfIECQKKLIVEGHLTK-------AVEETK--LSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKV 462
Cdd:pfam05483 382 IT--MELQKKSSELEEMTKfknnkevELEELKkiLAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQL 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 463 SLLKDDLQGAQSEIEAKQeiQHLRKELIEAQELARTSKQKCFELQALLEE------ERKAYRNQVEESTKQIQVLQAQLQ 536
Cdd:pfam05483 460 TAIKTSEEHYLKEVEDLK--TELEKEKLKNIELTAHCDKLLLENKELTQEasdmtlELKKHQEDIINCKKQEERMLKQIE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 537 RLHIDTENLREEkdseITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSL 616
Cdd:pfam05483 538 NLEEKEMNLRDE----LESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEEL 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 617 qnsfqlrcqqcedQQREEATRLQGELEKlrKEWNALETECHSLKREnvlLSSELQRQEKELHNSQKQ----SLELTSDLS 692
Cdd:pfam05483 614 -------------HQENKALKKKGSAEN--KQLNAYEIKVNKLELE---LASAKQKFEEIIDNYQKEiedkKISEEKLLE 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 693 ILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNL 772
Cdd:pfam05483 676 EVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAEL 755
|
....*.
gi 1799135528 773 KLLREK 778
Cdd:pfam05483 756 LSLKKQ 761
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
507-736 |
9.97e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 9.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 507 QALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASErdtdIA 586
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE----IA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 587 SLQEELKKVRAELER-----WRKAASEYEKEITSLQNSFQL-----RCQQCEDQQREEATRLQGELEKLRKewnaletec 656
Cdd:COG4942 94 ELRAELEAQKEELAEllralYRLGRQPPLALLLSPEDFLDAvrrlqYLKYLAPARREQAEELRADLAELAA--------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 657 hslkrenvlLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQH-------LRDSADLKTLLSKAENQ 729
Cdd:COG4942 165 ---------LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELaaelaelQQEAEELEALIARLEAE 235
|
....*..
gi 1799135528 730 AKDVQKE 736
Cdd:COG4942 236 AAAAAER 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
229-644 |
1.06e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 229 KNQTEDSLRKELIALQEDKHNYETTAKESLRRV--LQEKIEVVRKLSEVERSLSNTEDECTHLKEMNE--RTQEELRELA 304
Cdd:PTZ00121 1348 AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAdaAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAakKKADEAKKKA 1427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 305 NKYNGAvNEIKDLSDKLKVAEGKQEEIQQKGQAE----KKELQHKIDEMEEKEQElQAKIEALQADNDFTNERLTALQEH 380
Cdd:PTZ00121 1428 EEKKKA-DEAKKKAEEAKKADEAKKKAEEAKKAEeakkKAEEAKKADEAKKKAEE-AKKADEAKKKAEEAKKKADEAKKA 1505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 381 LLSKSGGDctfihQFIECQKKLIVEgHLTKAVEETKLSK----ENQTRAKESDFSDTLSPSKEKSSDDttDAQMDEQDLN 456
Cdd:PTZ00121 1506 AEAKKKAD-----EAKKAEEAKKAD-EAKKAEEAKKADEakkaEEKKKADELKKAEELKKAEEKKKAE--EAKKAEEDKN 1577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 457 EPLAKVSLLKD------DLQGAQSEIEAKQEIQHLRKE---LIEAQELARTSK-QKCFELQALLEEERKAYRNQVEESTK 526
Cdd:PTZ00121 1578 MALRKAEEAKKaeeariEEVMKLYEEEKKMKAEEAKKAeeaKIKAEELKKAEEeKKKVEQLKKKEAEEKKKAEELKKAEE 1657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 527 QIQVLQAQLQRLHIDTENLREE--KDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQ----------EELKK 594
Cdd:PTZ00121 1658 ENKIKAAEEAKKAEEDKKKAEEakKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKkaeeenkikaEEAKK 1737
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1799135528 595 VRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEK 644
Cdd:PTZ00121 1738 EAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
163-362 |
1.13e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALID--------EDRLLSRLEVMGNQLQACSKNQTED 234
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekeiaelRAELEAQKEELAELLRALYRLGRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 235 SLrkELIALQEDKHNYETTAK--ESLRRVLQEKIEVVRK-LSEVERSLSNTEDECTHLKEMNERTQEELRELANkyngAV 311
Cdd:COG4942 121 PL--ALLLSPEDFLDAVRRLQylKYLAPARREQAEELRAdLAELAALRAELEAERAELEALLAELEEERAALEA----LK 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1799135528 312 NEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEA 362
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
477-683 |
1.15e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 477 EAKQEIQHLRKELIEAQELARTSKQKCFELQALLEE----------ERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLR 546
Cdd:COG1340 19 ELREEIEELKEKRDELNEELKELAEKRDELNAQVKElreeaqelreKRDELNEKVKELKEERDELNEKLNELREELDELR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 547 EEKDSEITSTRD-----------------ELLSARDEILLLHQAAAKVAS-ERDTDIASLQEELKKVRAELERWRKAASE 608
Cdd:COG1340 99 KELAELNKAGGSidklrkeierlewrqqtEVLSPEEEKELVEKIKELEKElEKAKKALEKNEKLKELRAELKELRKEAEE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 609 YEKEITSLQNSFQ------LRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQK 682
Cdd:COG1340 179 IHKKIKELAEEAQelheemIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKR 258
|
.
gi 1799135528 683 Q 683
Cdd:COG1340 259 E 259
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
510-669 |
1.67e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 510 LEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDseitstrdELlsaRDEILllhqaaakvasERDTDIASLQ 589
Cdd:COG2433 390 LPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE--------EL---EAELE-----------EKDERIERLE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 590 EELKKVRAElerwRKAASEYEKEITSLQNsfqlrcqqcedqqreEATRLQGELEKLRKEWNALETECHSLKRENVLLSSE 669
Cdd:COG2433 448 RELSEARSE----ERREIRKDREISRLDR---------------EIERLERELEEERERIEELKRKLERLKELWKLEHSG 508
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
327-761 |
1.67e-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: 42.26 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 327 KQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQ---ADNDFTNERLT--------ALQEHLLSKSGGDCTFIHQF 395
Cdd:TIGR00618 236 QQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRaqeAVLEETQERINrarkaaplAAHIKAVTQIEQQAQRIHTE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 396 IECQK-KLIVEGHLTKAVEETKLSKENQTRAKESDFSD----TLSPSKEKSSDDTTDAQM-DEQDLNEPLAKVSLLKDDL 469
Cdd:TIGR00618 316 LQSKMrSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQeihiRDAHEVATSIREISCQQHtLTQHIHTLQQQKTTLTQKL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 470 QGAQSEIEAKQEIQH-----LRKELIEAQELARTSKQKCFElQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTEN 544
Cdd:TIGR00618 396 QSLCKELDILQREQAtidtrTSAFRDLQGQLAHAKKQQELQ-QRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQ 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 545 L--------REEKDSEITSTRDELLSARDEIL---LLHQAAAKVASER-----------DTDIASLQEELKKVRAELERW 602
Cdd:TIGR00618 475 LqtkeqihlQETRKKAVVLARLLELQEEPCPLcgsCIHPNPARQDIDNpgpltrrmqrgEQTYAQLETSEEDVYHQLTSE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 603 RKAASEYEKEITSLQNSFQlRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQ----RQEKELH 678
Cdd:TIGR00618 555 RKQRASLKEQMQEIQQSFS-ILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQpeqdLQDVRLH 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 679 NSQKQSLEltsDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEK 758
Cdd:TIGR00618 634 LQQCSQEL---ALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELE 710
|
...
gi 1799135528 759 QSI 761
Cdd:TIGR00618 711 THI 713
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
27-106 |
1.86e-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: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 27 PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTGkfYLQDTKSSNGTFINSQRLsrgseeSPPCEILSGDIIQFG 106
Cdd:cd22668 19 SNIIGRG------SDADFRLPDTGVSRRHAEIRWDGQVA--HLTDLGSTNGTTVNNAPV------TPEWRLADGDVITLG 84
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
580-781 |
2.16e-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: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 580 ERDT--DIASLQEELKkvraELERWRKAASEYEKEITSLQnsfQLRcqqcedQQREEATRLQGELEKLRKEWNALETECH 657
Cdd:COG4913 220 EPDTfeAADALVEHFD----DLERAHEALEDAREQIELLE---PIR------ELAERYAAARERLAELEYLRAALRLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 658 SLKREnvLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQvgsLKEQHLRDSADLKTLLSKAENQAKDVQKEY 737
Cdd:COG4913 287 QRRLE--LLEAELEELRAELARLEAELERLEARLDALREELDELEAQ---IRGNGGDRLEQLEREIERLERELEERERRR 361
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1799135528 738 EKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNN 781
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
163-691 |
2.30e-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: 41.49 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 163 QELFQLSQYLQEALHREQMLEQKLATLQRL----LAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRK 238
Cdd:TIGR00618 379 QHIHTLQQQKTTLTQKLQSLCKELDILQREqatiDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEK 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 239 elIALQEdkhnyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLS 318
Cdd:TIGR00618 459 --IHLQE------------SAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPG 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 319 DKLKVAEGKQEEIQQKGQAEKKeLQHKIDEMEEKEQELQAKIEALQADNDFTNE---RLTALQEHLLSKSGGDCTFIHQF 395
Cdd:TIGR00618 525 PLTRRMQRGEQTYAQLETSEED-VYHQLTSERKQRASLKEQMQEIQQSFSILTQcdnRSKEDIPNLQNITVRLQDLTEKL 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 396 IECQKKLIVEGHLTKAVEETKLSKEnQTRAKESDFSDTLSpsKEKSSDDTTDAQMDEQDLNEPLAKVSLLKddLQGAQSE 475
Cdd:TIGR00618 604 SEAEDMLACEQHALLRKLQPEQDLQ-DVRLHLQQCSQELA--LKLTALHALQLTLTQERVREHALSIRVLP--KELLASR 678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 476 IEAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEkdseits 555
Cdd:TIGR00618 679 QLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQ------- 751
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 556 tRDELLSARDEILLLHQAAAKVASERDTdiaslqeELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEA 635
Cdd:TIGR00618 752 -ARTVLKARTEAHFNNNEEVTAALQTGA-------ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQC 823
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1799135528 636 TRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEkELHNSQKQSLELTSDL 691
Cdd:TIGR00618 824 ETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA-QLTQEQAKIIQLSDKL 878
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
216-549 |
2.44e-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: 41.42 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 216 RLEVMGNQLQACSKNQTEdsLRKELIALQEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNER 295
Cdd:pfam07888 28 RAELLQNRLEECLQERAE--LLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 296 TQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQ-----------HKIDEMEEKEQeLQAKIEALQ 364
Cdd:pfam07888 106 LSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELErmkerakkagaQRKEEEAERKQ-LQAKLQQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 365 ADNDFTNERLTALQEHLLSKSGGDCTFIHQFIECQKKL------IVEGHLTKA----VEETKLSKENQTRAKESDFSDTL 434
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLttahrkEAENEALLEelrsLQERLNASERKVEGLGEELSSMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 435 SpSKEKSSDDTTDAQMDEQDLNEPLAKVSL--------LKDDLQGAQSEIEAKQE-IQHLRKELIEAQELARTSKQKCFE 505
Cdd:pfam07888 265 A-QRDRTQAELHQARLQAAQLTLQLADASLalregrarWAQERETLQQSAEADKDrIEKLSAELQRLEERLQEERMEREK 343
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1799135528 506 LQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEK 549
Cdd:pfam07888 344 LEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEK 387
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
511-742 |
2.96e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 511 EEERKAYRNQVEESTKQIQVLQAQLQRLhidtenlreekDSEITSTRDELLSARDEILLLHQAAAKVASErdtdIASLQE 590
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDAL-----------QAELEELNEEYNELQAELEALQAEIDKLQAE----IAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 591 ELKKVRAELERWRKAASEYEKEITSLQ-----NSFQ------LRCQQCEDQQREE---ATRLQGELEKLRKEWNALETEC 656
Cdd:COG3883 80 EIEERREELGERARALYRSGGSVSYLDvllgsESFSdfldrlSALSKIADADADLleeLKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 657 HSLKRENVLLSSELQRQEKELhnsQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKE 736
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQ---EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
....*.
gi 1799135528 737 YEKTQT 742
Cdd:COG3883 237 AAAAAA 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
631-778 |
3.06e-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: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 631 QREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKE 710
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 711 QHLRDSADLKTLLSKAE-------------------------------NQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQ 759
Cdd:COG4942 98 ELEAQKEELAELLRALYrlgrqpplalllspedfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAELE 177
|
170
....*....|....*....
gi 1799135528 760 SITDELKQCKNNLKLLREK 778
Cdd:COG4942 178 ALLAELEEERAALEALKAE 196
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
487-780 |
3.32e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 487 KELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDsEITSTRDELLSARDE 566
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 567 ILLLHQAAAKVaserDTDIASLQEELKKVRAELERWRkaasEYEKEITSLQnsfqlrcqqcedQQREEATRLQGELEKLR 646
Cdd:PRK03918 247 LESLEGSKRKL----EEKIRELEERIEELKKEIEELE----EKVKELKELK------------EKAEEYIKLSEFYEEYL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 647 KEWNALETECHSLKREnvllSSELQRQEKELHNSQKQSLELTSDLsilqmsrKELENQVGSLKEQHlRDSADLKTLLSKA 726
Cdd:PRK03918 307 DELREIEKRLSRLEEE----INGIEERIKELEEKEERLEELKKKL-------KELEKRLEELEERH-ELYEEAKAKKEEL 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1799135528 727 ENQAKdvqkeyEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGN 780
Cdd:PRK03918 375 ERLKK------RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIK 422
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
256-365 |
3.68e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 256 ESLRRVLQEKI-EVVRKLSEVERSLSNTEDEcthLKEMNERTQEELRELANKYNGAVNE--------IKDLSD--KLKVA 324
Cdd:PRK00409 526 EELERELEQKAeEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLEEAEKEAQQAIKEakkeadeiIKELRQlqKGGYA 602
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1799135528 325 EGKQEEIQQKgqaeKKELQHKIDEMEEKEQELQAKIEALQA 365
Cdd:PRK00409 603 SVKAHELIEA----RKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
172-361 |
4.21e-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: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 172 LQEALHREQMLEQKLATLQRLLaitqeasdtswQALIDEDRLLSRLEVmgNQLQACSKNQTEDSLRKELIAlqedKHNYE 251
Cdd:pfam15619 6 LSARLHKIKELQNELAELQSKL-----------EELRKENRLLKRLQK--RQEKALGKYEGTESELPQLIA----RHNEE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 252 T-TAKESLRRvLQEKIEVV-RKLSEVERSLSNTEDECTHL------KEMNERT--QEELRELANKYNGAVNEIKDLSDKL 321
Cdd:pfam15619 69 VrVLRERLRR-LQEKERDLeRKLKEKEAELLRLRDQLKRLeklsedKNLAEREelQKKLEQLEAKLEDKDEKIQDLERKL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1799135528 322 KVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIE 361
Cdd:pfam15619 148 ELENKSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLK 187
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
236-362 |
4.57e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 236 LRKELIALQEDKHNYETTAKESLRRV--LQEKIEVVRKlsevERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNE 313
Cdd:COG1579 50 AKTELEDLEKEIKRLELEIEEVEARIkkYEEQLGNVRN----NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEE 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1799135528 314 IKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEA 362
Cdd:COG1579 126 LAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
174-677 |
4.70e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 174 EALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDR-------LLSRLEVMGNQLQACSKNQTEDSLRKELIALQED 246
Cdd:TIGR00618 369 EISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQReqatidtRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAIT 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 247 KHNYETTAKE----SLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLK 322
Cdd:TIGR00618 449 CTAQCEKLEKihlqESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTR 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 323 VAEGKQEEIQQKGQAEKKeLQHKIDEMEEKEQELQAKIEALQADNDFTNE---RLTALQEHLLSKSGGDCTFIHQFIECQ 399
Cdd:TIGR00618 529 RMQRGEQTYAQLETSEED-VYHQLTSERKQRASLKEQMQEIQQSFSILTQcdnRSKEDIPNLQNITVRLQDLTEKLSEAE 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 400 KKLIVEGHLTKAVEETKLSKEnQTRAKESDFSDTLspSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKddLQGAQSEIEAK 479
Cdd:TIGR00618 608 DMLACEQHALLRKLQPEQDLQ-DVRLHLQQCSQEL--ALKLTALHALQLTLTQERVREHALSIRVLP--KELLASRQLAL 682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 480 QEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDE 559
Cdd:TIGR00618 683 QKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEA 762
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 560 LLSARDEILLLHQAAAKVA------SERDTDIASLQEELKKVRAELERWRKaasEYEKEITSLQNSFQLRCQQCeDQQRE 633
Cdd:TIGR00618 763 HFNNNEEVTAALQTGAELShlaaeiQFFNRLREEDTHLLKTLEAEIGQEIP---SDEDILNLQCETLVQEEEQF-LSRLE 838
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1799135528 634 EATRLQGELEKLRKEWNaletECHSLKRENVLLSSELQRQEKEL 677
Cdd:TIGR00618 839 EKSATLGEITHQLLKYE----ECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
572-764 |
5.37e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 572 QAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRcqqcedQQREEATRLQGELEKLRKEWNa 651
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL------PLYQELEALEAELAELPERLE- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 652 letechslkrenvllssELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDsadLKTLLSKAENQAK 731
Cdd:COG4717 150 -----------------ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD---LAEELEELQQRLA 209
|
170 180 190
....*....|....*....|....*....|...
gi 1799135528 732 DVQKEYEKTQTVLSELKLKFEMTEQEKQSITDE 764
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
494-704 |
5.43e-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: 40.26 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 494 ELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQA 573
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 574 AAKVASERDTDIASLQEELKKVRaELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEatrlQGELEKLRKEWNALE 653
Cdd:pfam07888 110 SEELSEEKDALLAQRAAHEARIR-ELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEE----EAERKQLQAKLQQTE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1799135528 654 TECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQmsRKELENQ 704
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH--RKEAENE 233
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
477-715 |
6.01e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 477 EAKQEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITST 556
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 557 RDellsardeillLHQAAAKVASErdtdIASLQEELKKVR--AELERWRKAASEYEKEITSLQNS---FQLRCQQCEDQQ 631
Cdd:PHA02562 258 NK-----------LNTAAAKIKSK----IEQFQKVIKMYEkgGVCPTCTQQISEGPDRITKIKDKlkeLQHSLEKLDTAI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 632 REEATRLQgELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSL-KE 710
Cdd:PHA02562 323 DELEEIMD-EFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELvKE 401
|
....*
gi 1799135528 711 QHLRD 715
Cdd:PHA02562 402 KYHRG 406
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
52-106 |
6.17e-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: 6.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799135528 52 SRNHALVWFDHKTGKFYLQ-----------DTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFG 106
Cdd:cd22683 28 SRSCDLVLSDPSISRFHAElrleqnginviDNNSANGTFINGKRIKGKT-----YILKNGDIIVFG 88
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
255-589 |
6.22e-03 |
|
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: 40.19 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 255 KESLRRVLQEKIEvvrKLSEVERslsnteDECTHLKEMNERTQEeLRELANKYNGAVNEIKD-LSDKLKVAEGKQEEIQQ 333
Cdd:pfam10174 392 KERKINVLQKKIE---NLQEQLR------DKDKQLAGLKERVKS-LQTDSSNTDTALTTLEEaLSEKERIIERLKEQRER 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 334 kgqaEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEH---LLSKSGGDCTFIHQF-IECQKK----LIVE 405
Cdd:pfam10174 462 ----EDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHassLASSGLKKDSKLKSLeIAVEQKkeecSKLE 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 406 GHLTKAVEetklsKENQTRAKEsDFSDTLSPSKEKSS---DDTTDAQMDEQDLNEPLAKVSLLKDDLQGAQSEIEAK--- 479
Cdd:pfam10174 538 NQLKKAHN-----AEEAVRTNP-EINDRIRLLEQEVArykEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLtlr 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 480 ----QEIQHLRKELIEAQELARTSKQKCFELQALLEEERKAYRNQVEES----TKQIQVLQAQLQRLHiDTENLREEKDS 551
Cdd:pfam10174 612 qmkeQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELmgalEKTRQELDATKARLS-STQQSLAEKDG 690
|
330 340 350
....*....|....*....|....*....|....*....
gi 1799135528 552 EITSTRDELLSARDEILLLHQAAAKVA-SERDTDIASLQ 589
Cdd:pfam10174 691 HLTNLRAERRKQLEEILEMKQEALLAAiSEKDANIALLE 729
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
163-342 |
6.42e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWqALIDEDRLLSRLEVMGNQLQACSKNQTE-DSLRKELI 241
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-DEIDVASAEREIAELEAELERLDASSDDlAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 242 ALQEDkhnyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLK----EMNERTQEELRELANKYNGAVNEIKDL 317
Cdd:COG4913 696 ELEAE-----------LEELEEELDELKGEIGRLEKELEQAEEELDELQdrleAAEDLARLELRALLEERFAAALGDAVE 764
|
170 180
....*....|....*....|....*
gi 1799135528 318 SDKLKVAEGKQEEIQQKGQAEKKEL 342
Cdd:COG4913 765 RELRENLEERIDALRARLNRAEEEL 789
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
208-366 |
6.66e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 39.82 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 208 IDEDRLLSRLEVMGNQLQACSKNQTE---DSLRKELIALQED-KHNYETTAKEslrrvLQEKIEVVRKLSEVERSLsnte 283
Cdd:PRK04778 249 LDHLDIEKEIQDLKEQIDENLALLEEldlDEAEEKNEEIQERiDQLYDILERE-----VKARKYVEKNSDTLPDFL---- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 284 decTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKK---ELQHKIDEMEEKEQELQ 357
Cdd:PRK04778 320 ---EHAKEQNKELKEEIDRVKQSYtlnESELESVRQLEKQLESLEKQYDEITERIAEQEIaysELQEELEEILKQLEEIE 396
|
....*....
gi 1799135528 358 AKIEALQAD 366
Cdd:PRK04778 397 KEQEKLSEM 405
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
163-365 |
6.70e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.06 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEasdtsWQALIDEDRLLSR----LEVMGNQLQACSKNQT--EDSL 236
Cdd:COG0497 172 KELEELRADEAERARELDLLRFQLEELEAAALQPGE-----EEELEEERRRLSNaeklREALQEALEALSGGEGgaLDLL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 237 RKELIALQEDKHnYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERtQEELRELANKYNGAVNEIKD 316
Cdd:COG0497 247 GQALRALERLAE-YDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEER-LALLRRLARKYGVTVEELLA 324
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1799135528 317 LSDKLkvaegkqeeiqqkgQAEKKELQHKIDEMEEKEQELQAKIEALQA 365
Cdd:COG0497 325 YAEEL--------------RAELAELENSDERLEELEAELAEAEAELLE 359
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
274-382 |
6.74e-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: 39.84 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 274 EVERSLSNTEDECTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEK----------K 340
Cdd:pfam06160 288 YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEvayselqeelE 367
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1799135528 341 ELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEHLL 382
Cdd:pfam06160 368 EILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELR 409
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
322-710 |
7.34e-03 |
|
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: 39.74 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 322 KVAEGKQEEIQQKGQAeKKELQHKIDEMEEKEQELQAKIEALQADNDFT-NERLTALQEHLLSKSGgdctfihqfiecqk 400
Cdd:pfam09731 78 ESKEPKEEKKQVKIPR-QSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEkEKALEEVLKEAISKAE-------------- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 401 klivegHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLkddlqGAQSEIEAKq 480
Cdd:pfam09731 143 ------SATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINL-----AKQSEEEAA- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 481 eiqhlrKELIEAQELArtskqkcfeLQALLEEErkayrNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDEL 560
Cdd:pfam09731 211 ------PPLLDAAPET---------PPKLPEHL-----DNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDI 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 561 ----------LSARDEILLLH------QAAAKVASERDTDIASLQEELKKVRAELERWRkaaseyEKEITSLQNSFQLRC 624
Cdd:pfam09731 271 ipvlkednllSNDDLNSLIAHahreidQLSKKLAELKKREEKHIERALEKQKEELDKLA------EELSARLEEVRAADE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135528 625 QQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLE----LTSDLSILQMSRKE 700
Cdd:pfam09731 345 AQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFLQDIKEKVEEeragRLLKLNELLANLKG 424
|
410
....*....|
gi 1799135528 701 LENQVGSLKE 710
Cdd:pfam09731 425 LEKATSSHSE 434
|
|
| VI_FHA |
TIGR03354 |
type VI secretion system FHA domain protein; Members of this protein family are FHA ... |
49-106 |
8.68e-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: 8.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799135528 49 KVLSRNHALV-WFDhktGKFYLQDTkSSNGTFINS--QRLSRGSEesppcEILS-GDIIQFG 106
Cdd:TIGR03354 43 RHVSGRHARIrYRD---GAYLLTDL-STNGVFLNGsgSPLGRGNP-----VRLEqGDRLRLG 95
|
|
| |
