|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
3-130 |
9.02e-82 |
|
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and similar proteins; SLMAP, also called sarcolemmal-associated protein (SLAP), is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. It is a cardiac membrane protein that plays an important role in E-C coupling and the adrenergic response of the heart. Overexpression of the SLMAP gene has been associated with diabetes and endothelial dysfunction of macro- and micro-blood vessels. SLMAP contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438731 [Multi-domain] Cd Length: 126 Bit Score: 256.04 E-value: 9.02e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 3 SALAIFTCRPNSHPFQERHVYLDEPIKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINS 82
Cdd:cd22679 1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1799135526 83 QRLSRGSEESPPCEILSGDIIQFGVDVTENTRKVTHGCIVSTIKLFLP 130
Cdd:cd22679 79 QRLSKGSEESEPRELHSGDIVQFGVDVVENSRKVTHGCIVATVTLFLP 126
|
|
| CC1_SLMAP |
cd21911 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal ... |
163-225 |
2.17e-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: 102.38 E-value: 2.17e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799135526 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQ 225
Cdd:cd21911 1 QELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQLS 63
|
|
| FHA_DMA-like |
cd22692 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest ... |
27-108 |
1.64e-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: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 27 PIKIGRSVARCRPAQNNAT-FDCKVLSRNHALVWfdHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQF 105
Cdd:cd22692 38 QIHIGRYTERVRQAIYHPVvFKSKVVSRTHGCIK--VDEGNWYIKDVKSSSGTFLNHQRLSPASRTSKPYPLRDGDILQL 115
|
...
gi 1799135526 106 GVD 108
Cdd:cd22692 116 GMD 118
|
|
| FHA_VPS64-like |
cd22695 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ... |
6-126 |
5.28e-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: 5.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 6 AIFTCRPNSHPFQERHV---YLDEPIKIGRSVARCRPAQN---------------NATFDCKVLSRNHALVWFDHKTGKF 67
Cdd:cd22695 2 HILVLKSLNATFETKFLvvpFKPDGLKLGRPVTNSVNKNNsgskrdlfsqqvrpdNGNFDSRVLSRNHACLSCDPTTGKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135526 68 YLQDTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFGVDVTEntrKVTHGCIVSTIK 126
Cdd:cd22695 82 YIRDLKSSNGTFVNGQKIRQND-----VELKVGDEVDLGTDIDS---KIEHRKISAYVE 132
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
239-702 |
3.21e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.10 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 239 ELIALQEDKHNYETTAKESLRRV--LQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKD 316
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 317 LSDKLKVAEGKQEEIQQKGQAEKK--ELQHKIDEMEEKEQELQAKIEALQ--ADNDFTNERLTALQEKLIVEGHLTKAVE 392
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 393 ETKLSKENQTRAKESDFSDTLSPSKE---------KSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYR-NQVEES 462
Cdd:PTZ00121 1442 EAKKADEAKKKAEEAKKAEEAKKKAEeakkadeakKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEaKKAEEA 1521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 463 TKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSA---------------RDEILLLHQAAAKVASERDTDIASLQ 527
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAeekkkaeeakkaeedKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 528 EELKKVRAE----LERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVL 603
Cdd:PTZ00121 1602 EEEKKMKAEeakkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK 1681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 604 LSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYE---KTQT 680
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEekkKIAH 1761
|
490 500
....*....|....*....|..
gi 1799135526 681 VLSELKLKFEMTEQEKQSITDE 702
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
13-106 |
4.64e-14 |
|
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.
Pssm-ID: 438714 [Multi-domain] Cd Length: 92 Bit Score: 68.07 E-value: 4.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 13 NSHPFQERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINSQRLsrgseeS 92
Cdd:cd00060 6 DGDGGGREFPLTKGVVTIGRS------PDCDIVLDDPSVSRRHARIEVDG--GGVYLEDLGSTNGTFVNGKRI------T 71
|
90
....*....|....
gi 1799135526 93 PPCEILSGDIIQFG 106
Cdd:cd00060 72 PPVPLQDGDVIRLG 85
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-716 |
6.35e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.86 E-value: 6.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 156 NTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQA--CSKNQTE 233
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvAQLELQI 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 234 DSLRKELIAL------QEDKHNYETTAKESLRRVLQE--KIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELAN 305
Cdd:TIGR02168 396 ASLNNEIERLearlerLEDRRERLQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 306 KYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKID---------EMEEKEQELQAKIEA-----LQA------ 365
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlsELISVDEGYEAAIEAalggrLQAvvvenl 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 366 ---------------------------DNDFTNERLTALQEKLIVEGHLTKAVE----------------------ETKL 396
Cdd:TIGR02168 556 naakkaiaflkqnelgrvtflpldsikGTEIQGNDREILKNIEGFLGVAKDLVKfdpklrkalsyllggvlvvddlDNAL 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 397 SKENQTRAKESDFS---DTLSP--------SKEKSSDDTTDAQMDEqdLNEPLAKVSLLKALLEEERKAYRNQVEESTKQ 465
Cdd:TIGR02168 636 ELAKKLRPGYRIVTldgDLVRPggvitggsAKTNSSILERRREIEE--LEEKIEELEEKIAELEKALAELRKELEELEEE 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 466 IQVLQAQLQRLHIDTENLREEKD----------SEITSTRDELLSARDEILLLHQAAAKV---ASERDTDIASLQEELKK 532
Cdd:TIGR02168 714 LEQLRKELEELSRQISALRKDLArleaeveqleERIAQLSKELTELEAEIEELEERLEEAeeeLAEAEAEIEELEAQIEQ 793
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 533 VRAELERWRKAASEYEKEITSLQNSF---QLRCQQCEDQQREEATRLQ----------GELEKLRKEWNALETECHSLKR 599
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATERRLEdleeqieelsEDIESLAAEIEELEELIEELES 873
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 600 ENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHlrdsADLKTLLSKAENQAKDVQkeyektQ 679
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL----AQLELRLEGLEVRIDNLQ------E 943
|
650 660 670
....*....|....*....|....*....|....*..
gi 1799135526 680 TVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 716
Cdd:TIGR02168 944 RLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
163-705 |
6.46e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.86 E-value: 6.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSknqteDSLRKELIA 242
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL-----ESLEAELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 243 LQEDKHNYETTAKEsLRRVLQEKIEVVRKLSEVERSLSNT----EDECTHLKEMNERTQEELRELA--------NKYNGA 310
Cdd:TIGR02168 363 LEAELEELESRLEE-LEEQLETLRSKVAQLELQIASLNNEierlEARLERLEDRRERLQQEIEELLkkleeaelKELQAE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 311 VNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQAD----NDFTNERLTALQEKLIVEGH 386
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLqenlEGFSEGVKALLKNQSGLSGI 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 387 L-------------TKAVEET------KLSKENQTRAKesdfsDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKAL 447
Cdd:TIGR02168 522 LgvlselisvdegyEAAIEAAlggrlqAVVVENLNAAK-----KAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKN 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 448 LEEERKAYRNQVEESTKQIQVLQAQLQRLHIdTENLREEKDSEITSTRDELL-SARDEILLLHQAAAKVASERDTDIASL 526
Cdd:TIGR02168 597 IEGFLGVAKDLVKFDPKLRKALSYLLGGVLV-VDDLDNALELAKKLRPGYRIvTLDGDLVRPGGVITGGSAKTNSSILER 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 527 QEELKKVRAELERWRKAASEYEKEITSLQNSFQlrcqqcedQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSS 606
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELE--------ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 607 ELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTL---LSKAENQAKDVQKEYEKTQTVLS 683
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALreaLDELRAELTLLNEEAANLRERLE 827
|
570 580
....*....|....*....|..
gi 1799135526 684 ELKLKFEMTEQEKQSITDELKQ 705
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEE 849
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
28-105 |
1.36e-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: 1.36e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135526 28 IKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRLSRgseesPPCEILSGDIIQF 105
Cdd:pfam00498 1 VTIGRS------PDCDIVLDDPSVSRRHAEIRYD-GGGRFYLEDLGSTNGTFVNGQRLGP-----EPVRLKDGDVIRL 66
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
161-686 |
7.29e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 7.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 161 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKEL 240
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 241 IALQEDkhnyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDK 320
Cdd:COG1196 298 ARLEQD-----------IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 321 LKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKEN 400
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 401 QTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQ--DLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHI 478
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAAlaELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAV 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 479 DTENLREEKDSEITSTR----------DELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVR------------AE 536
Cdd:COG1196 527 AVLIGVEAAYEAALEAAlaaalqnivvEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALargaigaavdlvAS 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 537 LERWRKAASEYEKEITSLQNSFQLRCQQCEDQQRE----------EATRLQGELEKLRKEWNALETECHSLKRENVLLSS 606
Cdd:COG1196 607 DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTlagrlrevtlEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 607 ELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELK 686
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
217-711 |
8.78e-13 |
|
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: 72.07 E-value: 8.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 217 LEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTakeslrrvlqekieVVRKLSEVERSLSNTEDECTHLKEMNERT 296
Cdd:pfam15921 278 VEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSM--------------YMRQLSDLESTVSQLRSELREAKRMYEDK 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 297 QEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEiqqkgqaekkELQHKIDEMEEKEQELQAKIEalqadndftnerlta 376
Cdd:pfam15921 344 IEELEKQLVLANSELTEARTERDQFSQESGNLDD----------QLQKLLADLHKREKELSLEKE--------------- 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 377 lQEKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDE-QDLNEPLAKVSLLKALLEEERKAY 455
Cdd:pfam15921 399 -QNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAiQGKNESLEKVSSLTAQLESTKEML 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 456 RNQVEESTKQIQVLQAQlQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDtdiaslqeELKKVRA 535
Cdd:pfam15921 478 RKVVEELTAKKMTLESS-ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGD--------HLRNVQT 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 536 ELERWRKAASEYEKEITSLQNSFQlRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLK----------RENVLLS 605
Cdd:pfam15921 549 ECEALKLQMAEKDKVIEILRQQIE-NMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKilkdkkdakiRELEARV 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 606 SELQRQEKELHNSQKQSLELTSDlsiLQMSRKELENQVGSLKEqhlrdsaDLKTLLSKAENQAKDVQKEYEKTQTVLSEL 685
Cdd:pfam15921 628 SDLELEKVKLVNAGSERLRAVKD---IKQERDQLLNEVKTSRN-------ELNSLSEDYEVLKRNFRNKSEEMETTTNKL 697
|
490 500
....*....|....*....|....*.
gi 1799135526 686 KLKFemteqekQSITDELKQCKNNLK 711
Cdd:pfam15921 698 KMQL-------KSAQSELEQTRNTLK 716
|
|
| CC1_SLMAP-like |
cd21868 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ... |
167-204 |
1.01e-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: 1.01e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1799135526 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21868 1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
443-716 |
2.14e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.87 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 443 LLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLhidtENLREEKDSEITSTRDELLSARDeilLLHQAAAKVASERDTD 522
Cdd:TIGR02169 216 LLKEKREYEGYELLKEKEALERQKEAIERQLASL----EEELEKLTEEISELEKRLEEIEQ---LLEELNKKIKDLGEEE 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 523 IASLQEELKKVRAELERWRKAASEYEKEITSLQNsfQLRCQQCE-DQQREEATRLQGELEKLRKEWNALETECHSLKREN 601
Cdd:TIGR02169 289 QLRVKEKIGELEAEIASLERSIAEKERELEDAEE--RLAKLEAEiDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 602 VLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADlktlLSKAENQAKDVQKEYEKTQTV 681
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEE----LADLNAAIAGIEAKINELEEE 442
|
250 260 270
....*....|....*....|....*....|....*
gi 1799135526 682 LSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 716
Cdd:TIGR02169 443 KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
172-716 |
3.80e-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: 70.09 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 172 LQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRllsrlevmgnqlqacSKNQTEDSLRKELIALQEDKHNYE 251
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS---------------ELEEEIEELQKELYALANEISRLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 252 ttakeslrrvlQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEI 331
Cdd:TIGR02168 302 -----------QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 332 QQKGQAEKKELQH---KIDEMEEKEQELQAKIEALQAD--------NDFTNERLTALQEKLIVEGHLTKAVEETKLSKEN 400
Cdd:TIGR02168 371 ESRLEELEEQLETlrsKVAQLELQIASLNNEIERLEARlerledrrERLQQEIEELLKKLEEAELKELQAELEELEEELE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 401 QTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQ------------- 467
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlselis 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 468 -----------VLQAQLQRLHIDTEN---------------------LREEKDSEITSTRDELLSARDEILLLHQAAAKV 515
Cdd:TIGR02168 531 vdegyeaaieaALGGRLQAVVVENLNaakkaiaflkqnelgrvtflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKF 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 516 ASERD-------------TDIASLQEELKKVRAEL-------ERWRKAASEY---EKEITSLQNSFQ--LRCQQCEDQQR 570
Cdd:TIGR02168 611 DPKLRkalsyllggvlvvDDLDNALELAKKLRPGYrivtldgDLVRPGGVITggsAKTNSSILERRReiEELEEKIEELE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 571 EEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQ- 649
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERl 770
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799135526 650 ---------HLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 716
Cdd:TIGR02168 771 eeaeeelaeAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
211-539 |
5.04e-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: 69.70 E-value: 5.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 211 DRLLSRLEVMGNQLQACSKNQTEdsLRKELIALQEDkhnyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLK 290
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAE--LRKELEELEEE-----------LEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 291 EMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEgkqeeiqqkgqAEKKELQHKIDEMEEKEQELQAKIEALQADNDFT 370
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAE-----------AEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 371 NERLTALQEKLivEGHLTKAVEETKLSKENQTRAKEsdfsdtLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEE 450
Cdd:TIGR02168 816 NEEAANLRERL--ESLERRIAATERRLEDLEEQIEE------LSEDIESLAAEIEELEELIEELESELEALLNERASLEE 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 451 ERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREE------KDSEITSTRDELLSA-RDEILLLHQAAAKVASERDTDI 523
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELRRELEELREKlaqlelRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDE 967
|
330
....*....|....*.
gi 1799135526 524 ASLQEELKKVRAELER 539
Cdd:TIGR02168 968 EEARRRLKRLENKIKE 983
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
298-716 |
8.88e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.91 E-value: 8.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 298 EELRELANKYNGAVNEIkdLSDKLKVAEGKQEEIQQKgqaEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTAL 377
Cdd:PRK02224 165 EEYRERASDARLGVERV--LSDQRGSLDQLKAQIEEK---EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 378 QEklIVEGH---------LTKAVEETKLSKENQTRAKEsDFSDTLSPSKEKSSD--DTTDAQMDEQDLNEPLAK-VSLLK 445
Cdd:PRK02224 240 DE--VLEEHeerreeletLEAEIEDLRETIAETERERE-ELAEEVRDLRERLEEleEERDDLLAEAGLDDADAEaVEARR 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 446 ALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEK----------DSEITSTRDELLSARDEILLLhQAAAKV 515
Cdd:PRK02224 317 EELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAeelreeaaelESELEEAREAVEDRREEIEEL-EEEIEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 516 ASER----DTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSF----QLR----CQQCE------------DQQRE 571
Cdd:PRK02224 396 LRERfgdaPVDLGNAEDFLEELREERDELREREAELEATLRTARERVeeaeALLeagkCPECGqpvegsphvetiEEDRE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 572 EATRLQGELEKLRKEWNALETECHSLKrenvllssELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQhl 651
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAE--------DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER-- 545
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799135526 652 rdSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS------ITDELKQCKNNLKLLREK 716
Cdd:PRK02224 546 --AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESlerirtLLAAIADAEDEIERLREK 614
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
212-715 |
1.06e-11 |
|
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: 68.53 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 212 RLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTAKESLRRVLQEKIEvvrkLSEVERSlSNTEDECTHLKE 291
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE----LDGFERG-PFSERQIKNFHT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 292 MNERTQEELRELANKyngavnEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTN 371
Cdd:TIGR00606 398 LVIERQEDEAKTAAQ------LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 372 ERLTALQEKLIVEGHLTKAVE----ETKLSKENQTRAKESDFSDTL----SPSKEKSSDDTTDAQM-----DEQDLNEPL 438
Cdd:TIGR00606 472 RILELDQELRKAERELSKAEKnsltETLKKEVKSLQNEKADLDRKLrkldQEMEQLNHHTTTRTQMemltkDKMDKDEQI 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 439 AK---------VSLL-----KALLEEERKAYRNQVEESTKQIQVLQAQLQRLhidtENLREEKDSEITSTRDELLSARDE 504
Cdd:TIGR00606 552 RKiksrhsdelTSLLgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASL----EQNKNHINNELESKEEQLSSYEDK 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 505 ILllhqaAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQC------EDQQREEATRLQG 578
Cdd:TIGR00606 628 LF-----DVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCqrvfqtEAELQEFISDLQS 702
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 579 ELEKLRKEWNALETECHSLKRENVLL-------SSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSL--KEQ 649
Cdd:TIGR00606 703 KLRLAPDKLKSTESELKKKEKRRDEMlglapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTImpEEE 782
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135526 650 HLRDSADLKTLLSKAENQAKDVQKEYEKTQTVL--SELKLKFEMTEQEKQSITDELKQCKNNLKLLRE 715
Cdd:TIGR00606 783 SAKVCLTDVTIMERFQMELKDVERKIAQQAAKLqgSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
14-106 |
1.06e-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: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 14 SHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716 8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
|
90
....*....|....
gi 1799135526 93 pPCEILSGDIIQFG 106
Cdd:COG1716 75 -PAPLRDGDVIRLG 87
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
190-719 |
1.28e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.54 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 190 QRLLAITQEASDTSWQALIDedrllsRLEVMGNQLQAcsKNQTEDSLRKELIALQEDKHNYET--TAKESLRRVLQEKIE 267
Cdd:TIGR02168 213 ERYKELKAELRELELALLVL------RLEELREELEE--LQEELKEAEEELEELTAELQELEEklEELRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 268 --------VVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEK 339
Cdd:TIGR02168 285 elqkelyaLANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 340 KELQhkidEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEG----HLTKAVEETKLSKENQTRAKESDFSDTLSP 415
Cdd:TIGR02168 365 AELE----ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEarleRLEDRRERLQQEIEELLKKLEEAELKELQA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 416 SKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKD------- 488
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKnqsglsg 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 489 -----SEITSTR--------------------DELLSARDEILLLHQAAAKVA------SERDTDIASLQEELKK----V 533
Cdd:TIGR02168 521 ilgvlSELISVDegyeaaieaalggrlqavvvENLNAAKKAIAFLKQNELGRVtflpldSIKGTEIQGNDREILKniegF 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 534 RAELERWRKAASEYEKEI----------TSLQNSFQLRCQQCEDQQ--------------------REEATRL--QGELE 581
Cdd:TIGR02168 601 LGVAKDLVKFDPKLRKALsyllggvlvvDDLDNALELAKKLRPGYRivtldgdlvrpggvitggsaKTNSSILerRREIE 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 582 KLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLL 661
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799135526 662 SKAENQAKDVQKEYEKTQTVLSE---LKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNN 719
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEieeLEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
52-106 |
1.30e-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: 1.30e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1799135526 52 SRNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQFG 106
Cdd:cd22686 48 SKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPYPLTHGDELKIG 102
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
161-625 |
3.87e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 3.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 161 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQeasdtswqalidedRLLSRLEVMGNQLQACSKNQTEdsLRKEL 240
Cdd:PRK03918 291 KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIE--------------ERIKELEEKEERLEELKKKLKE--LEKRL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 241 IALQEDKHNYETTakeslrRVLQEKIEVVRKlSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSD- 319
Cdd:PRK03918 355 EELEERHELYEEA------KAKKEELERLKK-RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKa 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 320 --KLKVAEGK------------QEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALqadndftnERLTALQEKLIVEG 385
Cdd:PRK03918 428 ieELKKAKGKcpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL--------EKVLKKESELIKLK 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 386 HLTKAVEET--KLSKENqtrakesdfsdtlspsKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEErKAYRNQVEEST 463
Cdd:PRK03918 500 ELAEQLKELeeKLKKYN----------------LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL-EELKKKLAELE 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 464 KQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDtDIASLQEELKKVRAELERWRKA 543
Cdd:PRK03918 563 KKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEK-ELKKLEEELDKAFEELAETEKR 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 544 ASEYEKEITSLQNSFqlrcqqcedqQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSL 623
Cdd:PRK03918 642 LEELRKELEELEKKY----------SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
..
gi 1799135526 624 EL 625
Cdd:PRK03918 712 EL 713
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
163-649 |
4.14e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 4.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDtswQALIDEDRLLSRLEVMGNQLQAcsKNQTEDSLRKELIA 242
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRR---ELEERLEELEEELAELEEELEE--LEEELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 243 LQEDkhnyETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLK 322
Cdd:COG1196 349 AEEE----LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 323 VAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADndftnERLTALQEKLIVEGHLTKAVEETKLSKENQT 402
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL-----LEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 403 RAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQ----RLHI 478
Cdd:COG1196 500 EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratFLPL 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 479 DTENLREEKDSEITST---------------RDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKA 543
Cdd:COG1196 580 DKIRARAALAAALARGaigaavdlvasdlreADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 544 ASEYE-KEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQS 622
Cdd:COG1196 660 GSLTGgSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
490 500 510
....*....|....*....|....*....|....*.
gi 1799135526 623 LELTSDLSILQ---------MSRKELENQVGSLKEQ 649
Cdd:COG1196 740 ELLEEEELLEEealeelpepPDLEELERELERLERE 775
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
235-716 |
8.16e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.43 E-value: 8.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 235 SLRKELIALQEDKHNYETTAKE--SLRRVLQEKIEVVRKLSEVERSLsntEDECTHLKEMNERTQEELRELANKYNGAVN 312
Cdd:TIGR04523 170 ELENELNLLEKEKLNIQKNIDKikNKLLKLELLLSNLKKKIQKNKSL---ESQISELKKQNNQLKDNIEKKQQEINEKTT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 313 EIKDLSDKLKVAEGKQEEIQQKGQAEKKELQH---KIDEMEEKEQELQAKIEAL--QADNDFTNERLTALQEKlivEGHL 387
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLnnQKEQDWNKELKSELKNQ---EKKL 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 388 TKAveETKLSKENQtraKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKalleEERKAYRNQVEESTKQIQ 467
Cdd:TIGR04523 324 EEI--QNQISQNNK---IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK----KENQSYKQEIKNLESQIN 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 468 VLQAQLQrlhiDTENLREEKDSEITSTRDELLSardeilllhqaaakvaserdtdiasLQEELKKVRAELERWRKAASEY 547
Cdd:TIGR04523 395 DLESKIQ----NQEKLNQQKDEQIKKLQQEKEL-------------------------LEKEIERLKETIIKNNSEIKDL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 548 EKEITSLQNSFQlrcqqcedqqreeatrlqgELEKLRKEwnaLETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTS 627
Cdd:TIGR04523 446 TNQDSVKELIIK-------------------NLDNTRES---LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 628 DLSILQMSRKELENQVGSLKEQhlrdSADLKTLLSKAENQAKDVQKEYEKTQTVLselklKFEMTEQEKQSITDELKQCK 707
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEK----IEKLESEKKEKESKISDLEDELNKDDFEL-----KKENLEKEIDEKNKEIEELK 574
|
....*....
gi 1799135526 708 NNLKLLREK 716
Cdd:TIGR04523 575 QTQKSLKKK 583
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
226-716 |
2.01e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 64.27 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 226 ACSKNQTEDSLRKELIALQEDKHNYETTAKeSLRRVLQEKIEVVR----KLSEVERSLSNTEDECTHLKEMNERTQEELR 301
Cdd:TIGR04523 28 ANKQDTEEKQLEKKLKTIKNELKNKEKELK-NLDKNLNKDEEKINnsnnKIKILEQQIKDLNDKLKKNKDKINKLNSDLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 302 ELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQ 378
Cdd:TIGR04523 107 KINSEIkndKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 379 EKlIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSL----LKALLEEERKA 454
Cdd:TIGR04523 187 KN-IDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNtqtqLNQLKDEQNKI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 455 YR------NQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILllhQAAAKVASERDTDIASLQE 528
Cdd:TIGR04523 266 KKqlsekqKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKL---EEIQNQISQNNKIISQLNE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 529 ELKKVRAELERWRKAASEYEKEITSLQNsfqlrcqQCEDQQREEATRLQgELEKLRKEWNALETECHSLKRENVLLSSEL 608
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQRELEEKQN-------EIEKLKKENQSYKQ-EIKNLESQINDLESKIQNQEKLNQQKDEQI 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 609 QRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHlrdsADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLK 688
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELII----KNLDNTRESLETQLKVLSRSINKIKQNLEQKQKE 490
|
490 500
....*....|....*....|....*...
gi 1799135526 689 FEMTEQEKQSITDELKQCKNNLKLLREK 716
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLTKK 518
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
229-591 |
2.01e-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: 64.31 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 229 KNQTEDSLRKELIALQ--EDKHNYETTAKESLRR---VLQEKIEVVRKLSEVERSLSntedecthLKEMNERtQEELREL 303
Cdd:TIGR02168 174 RKETERKLERTRENLDrlEDILNELERQLKSLERqaeKAERYKELKAELRELELALL--------VLRLEEL-REELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 304 ANKYNGAVNEIKDLSDKLKVAEGKQEEIQqkgqAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLI- 382
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELR----LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEe 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 383 VEGHLTKAVEETKLSKENQTRAKESdfSDTLSPSKEKSSDDTTDAQMDEQDLNEplaKVSLLKALLEEERKAY---RNQV 459
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEK--LEELKEELESLEAELEELEAELEELES---RLEELEEQLETLRSKVaqlELQI 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 460 EESTKQIQVLQAQLQRLhidtENLREEKDSEITSTRDELLSARdeillLHQAAAKVAsERDTDIASLQEELKKVRAELER 539
Cdd:TIGR02168 396 ASLNNEIERLEARLERL----EDRRERLQQEIEELLKKLEEAE-----LKELQAELE-ELEEELEELQEELERLEEALEE 465
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1799135526 540 WRKAASEYEKEITSLQNSF---QLRCQQCEDQQReeatRLQGELEKLRKEWNALE 591
Cdd:TIGR02168 466 LREELEEAEQALDAAERELaqlQARLDSLERLQE----NLEGFSEGVKALLKNQS 516
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-619 |
7.41e-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: 62.77 E-value: 7.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 263 QEKIEVVRKLSEVERSLSNTEDEcthLKEMNERTQ--EELRELANKYNGAVNEIKDLS-----DKLKVAEGKQEEIQQkg 335
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDI---LNELERQLKslERQAEKAERYKELKAELRELElallvLRLEELREELEELQE-- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 336 qaEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKENQTRAkesdfsdtLSP 415
Cdd:TIGR02168 247 --ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN--------LER 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 416 SKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQrlhiDTENLREEKDSEITSTR 495
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE----ELEEQLETLRSKVAQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 496 DELLSARDEILLLhqaaakvaserDTDIASLQEELKKVRAELERWRKAASEYEKEitslqnsfqlrcqqcedQQREEATR 575
Cdd:TIGR02168 393 LQIASLNNEIERL-----------EARLERLEDRRERLQQEIEELLKKLEEAELK-----------------ELQAELEE 444
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1799135526 576 LQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQ 619
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
152-592 |
2.80e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 152 KVAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDtswqaliDEDRLLSRLEVMGNQLQACSKNQ 231
Cdd:COG4717 60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA-------ELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 232 TEDSLRKELIALQEdkhnyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKE-MNERTQEELRELANKYNGA 310
Cdd:COG4717 133 ELEALEAELAELPE--------RLEELEERLEELRELEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 311 VNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEA----LQADNDFTNERLTALQEKLIVEGH 386
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallaLLGLGGSLLSLILTIAGVLFLVLG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 387 LTkAVEETKLSKENQTRAKESDFSDTLsPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLE-EERKAYRNQVEESTKQ 465
Cdd:COG4717 285 LL-ALLFLLLAREKASLGKEAEELQAL-PALEELEEEELEELLAALGLPPDLSPEELLELLDRiEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 466 IQVLQAQ------LQRLHIDTEN---LREEKDSEITSTRDELLSARDEI-----LLLHQAAAKVASERDTDIASLQEELK 531
Cdd:COG4717 363 LQLEELEqeiaalLAEAGVEDEEelrAALEQAEEYQELKEELEELEEQLeellgELEELLEALDEEELEEELEELEEELE 442
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799135526 532 KVRAELERWRKAASEYEKEITSLQNSFQLrcqqceDQQREEATRLQGELEKLRKEWNALET 592
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLEEDGEL------AELLQELEELKAELRELAEEWAALKL 497
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
333-715 |
3.49e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 333 QKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDfTNERLTALQEKLI-VEGH-LTKAVEETKLSKEnQTRAKESDFS 410
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLERLRRERE-KAERYQALLKEKReYEGYeLLKEKEALERQKE-AIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 411 DTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVsllKALLEEERKAYRNQVEESTKQIQVLQAQLQrlhidtENLREEKDSE 490
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKI---KDLGEEEQLRVKEKIGELEAEIASLERSIA------EKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 491 itSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLqnsfqlrcqqcedqqR 570
Cdd:TIGR02169 322 --ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET---------------R 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 571 EEATRLQGELEKLRKEWNaletechSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQH 650
Cdd:TIGR02169 385 DELKDYREKLEKLKREIN-------ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799135526 651 LRDSADlktlLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLRE 715
Cdd:TIGR02169 458 EQLAAD----LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
228-716 |
3.97e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 228 SKNQTEDSLRKELIALQEDKHNYETTA------KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEmNERTQEELR 301
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKELEELKeeieelEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE-KVKELKELK 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 302 ELANKYNgavnEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKE---QELQAKIEALQADNDFTNERLTALQ 378
Cdd:PRK03918 290 EKAEEYI----KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELYE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 379 EKLIVEGHLTK--------AVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDE--QDLNEPLAKVSLLKALL 448
Cdd:PRK03918 366 EAKAKKEELERlkkrltglTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKaiEELKKAKGKCPVCGREL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 449 EEERKAyrNQVEESTKQIQVLQAQLQRLHIDTENLREEKdseitSTRDELLSARDEILLLHQAAAKVASERDTDIASLQE 528
Cdd:PRK03918 446 TEEHRK--ELLEEYTAELKRIEKELKEIEEKERKLRKEL-----RELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 529 ELKKVRAELERWRKAASEYEKEITSLQNSFqlrcqqcedqqrEEATRLQGELEKLRKEWNALETECHSLKRENVLLS--- 605
Cdd:PRK03918 519 ELEKKAEEYEKLKEKLIKLKGEIKSLKKEL------------EKLEELKKKLAELEKKLDELEEELAELLKELEELGfes 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 606 -SELQRQEKELHNSQKQSLELT---SDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSK--------AENQAKDVQK 673
Cdd:PRK03918 587 vEELEERLKELEPFYNEYLELKdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEleelekkySEEEYEELRE 666
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1799135526 674 EYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 716
Cdd:PRK03918 667 EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
271-690 |
4.21e-09 |
|
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: 60.19 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 271 KLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAvneIKDLSDKLKvaegKQEEIQQKGQAEKKELQHKIDEME 350
Cdd:pfam01576 149 KLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAM---ISDLEERLK----KEEKGRQELEKAKRKLEGESTDLQ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 351 EKEQELQAKIEALQADNDFTNERLTALQEKLI---------------VEGHLTKAVEETKLSKENQTRAKES--DFSDTL 413
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAKKEEELQAALARLEeetaqknnalkkireLEAQISELQEDLESERAARNKAEKQrrDLGEEL 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 414 SPSKEKSSD--DTTDAQMDEQDLNEplAKVSLLKALLEEERKAYRNQVEEstkqiqvlqaqlqrlhidtenLREEKDSEI 491
Cdd:pfam01576 302 EALKTELEDtlDTTAAQQELRSKRE--QEVTELKKALEEETRSHEAQLQE---------------------MRQKHTQAL 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 492 TSTRDELLSARDEILLLHQAAAKVASERdtdiASLQEELKKVRAelerwRKAASEYEKEITSLQ-NSFQLRCQQCEDQQR 570
Cdd:pfam01576 359 EELTEQLEQAKRNKANLEKAKQALESEN----AELQAELRTLQQ-----AKQDSEHKRKKLEGQlQELQARLSESERQRA 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 571 EEA---TRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLsilqmsrKELENQVGSLK 647
Cdd:pfam01576 430 ELAeklSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRL-------RQLEDERNSLQ 502
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1799135526 648 EQhlrdsadlktlLSKAENQAKDVQKEYEKTQTVLSELKLKFE 690
Cdd:pfam01576 503 EQ-----------LEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
167-465 |
6.73e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.70 E-value: 6.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTE-----DSLRKELI 241
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvkselKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 242 ALQEDKHNYETTAKESLRRVLQEKI-EVVRKLSEVERSLSNTEDECTHL-KEMNERTQE------ELRELANKYNGAVNE 313
Cdd:TIGR02169 769 ELEEDLHKLEEALNDLEARLSHSRIpEIQAELSKLEEEVSRIEARLREIeQKLNRLTLEkeylekEIQELQEQRIDLKEQ 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 314 IKDLSDKLKVAEGKQEEIQQKGQ----------AEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKL-I 382
Cdd:TIGR02169 849 IKSIEKEIENLNGKKEELEEELEeleaalrdleSRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLeA 928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 383 VEGHLTKAVEETKLSKE------------NQTRAKESDFSDtLSPSKEKSSDDTTDAQMDEQDLNEPLAKvsllkalLEE 450
Cdd:TIGR02169 929 LEEELSEIEDPKGEDEEipeeelsledvqAELQRVEEEIRA-LEPVNMLAIQEYEEVLKRLDELKEKRAK-------LEE 1000
|
330
....*....|....*
gi 1799135526 451 ERKAYRNQVEESTKQ 465
Cdd:TIGR02169 1001 ERKAILERIEEYEKK 1015
|
|
| CC1_T3JAM |
cd21912 |
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ... |
164-204 |
7.27e-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: 51.96 E-value: 7.27e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1799135526 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21912 5 EILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
|
|
| FHA_TCF19 |
cd22685 |
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ... |
29-119 |
1.03e-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: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 29 KIGRSVARCRPAQNNATFDcKVLSRNHALVW---FDHKTGKFYLQDTkSSNGTFINSQRLSRGSEEsppcEILSGDIIQF 105
Cdd:cd22685 31 RIGRNPEVCDVFLCSSQHP-NLISREHAEIHaerDGNGNWKVLIEDR-STNGTYVNDVRLQDGQRR----ELSDGDTITF 104
|
90
....*....|....*.
gi 1799135526 106 G--VDVTENTRKVTHG 119
Cdd:cd22685 105 GhkNGRRVKQWPYQKS 120
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
238-716 |
1.48e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 238 KELIALQEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDL 317
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 318 SDKLKVAEGKQEEIQQ-KGQAEK-KELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETK 395
Cdd:PRK03918 272 KKEIEELEEKVKELKElKEKAEEyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 396 lSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQR 475
Cdd:PRK03918 352 -KRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 476 LhidtenlreEKDSEITSTRDELLSARDEILLLHQAAAKVASERDtDIASLQEELKKVRAELERWRKAASEYEKEITSLQ 555
Cdd:PRK03918 431 L---------KKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEK-ELKEIEEKERKLRKELRELEKVLKKESELIKLKE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 556 NSFQLRC--QQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRE---NVLLSSELQRQEKELHNSQKQSLELTSDLS 630
Cdd:PRK03918 501 LAEQLKEleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKElekLEELKKKLAELEKKLDELEEELAELLKELE 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 631 ILQM-SRKELENQVGSLKEQH-----LRDSA----DLKTLLSKAENQAKDVQKEYEKTQTVLSELK-----LKFEMTEQE 695
Cdd:PRK03918 581 ELGFeSVEELEERLKELEPFYneyleLKDAEkeleREEKELKKLEEELDKAFEELAETEKRLEELRkeleeLEKKYSEEE 660
|
490 500
....*....|....*....|.
gi 1799135526 696 KQSITDELKQCKNNLKLLREK 716
Cdd:PRK03918 661 YEELREEYLELSRELAGLRAE 681
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
289-716 |
1.76e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 289 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKgQAEKKELQHKIDEMEEKEQELQAKIEALQADND 368
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 369 F--TNERLTALQEKLIVEGHLTKAVEETKL---SKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSL 443
Cdd:COG4717 127 LlpLYQELEALEAELAELPERLEELEERLEelrELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 444 LKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHiDTENLREEKDS--------EITSTRDELLSARDEILLLHQAAAKV 515
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAA-LEERLKEARLLlliaaallALLGLGGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 516 ASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRcqqcEDQQREEATRLQGELEKLRKEWNALETECH 595
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLP----PDLSPEELLELLDRIEELQELLREAEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 596 SLKRE------NVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQ-HLRDSADLKTLLSKAENQA 668
Cdd:COG4717 362 ELQLEeleqeiAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELlEALDEEELEEELEELEEEL 441
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1799135526 669 KDVQKEYEKTQTVLSELKLKFEMTEQEK--QSITDELKQCKNNLKLLREK 716
Cdd:COG4717 442 EELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRELAEE 491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
459-715 |
1.89e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 459 VEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDtdiaSLQEELKKVRAELE 538
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELE----ELTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 539 RWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEAtRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNS 618
Cdd:TIGR02168 271 ELRLEVSELEEEIEELQKELYALANEISRLEQQKQ-ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 619 QKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQK-EYEKTQTVLSELKLKFEMTEQEKQ 697
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERlEARLERLEDRRERLQQEIEELLKK 429
|
250
....*....|....*...
gi 1799135526 698 SITDELKQCKNNLKLLRE 715
Cdd:TIGR02168 430 LEEAELKELQAELEELEE 447
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
250-716 |
1.96e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 250 YETTAKES--LRRVLQEKIEVVRKL----SEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLsDKLKV 323
Cdd:PRK03918 160 YENAYKNLgeVIKEIKRRIERLEKFikrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-EELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 324 AEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQAdndfTNERLTALQEKLIVEGHLTKAVEETKlSKENQTR 403
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE----KVKELKELKEKAEEYIKLSEFYEEYL-DELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 404 AKESDFSDTLSPSKEKSSD---DTTDAQMDEQDLNEPLAKVSLLK--ALLEEERKAYRNQVEESTKQIQVLQAQ-LQRLH 477
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKEleeKEERLEELKKKLKELEKRLEELEerHELYEEAKAKKEELERLKKRLTGLTPEkLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 478 IDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVAS---------------ERDTDIASLQEELKKVRAELERWRK 542
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteeHRKELLEEYTAELKRIEKELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 543 AASEYEKEITSLQNSFQ-----LRCQQCEDQQREEATRLQG-ELEKLRKEWNALETechsLKRENVLLSSELQRQEKELH 616
Cdd:PRK03918 474 KERKLRKELRELEKVLKkeselIKLKELAEQLKELEEKLKKyNLEELEKKAEEYEK----LKEKLIKLKGEIKSLKKELE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 617 NSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAE------NQAKDVQKEYEKTQTVLSELKLKFE 690
Cdd:PRK03918 550 KLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEpfyneyLELKDAEKELEREEKELKKLEEELD 629
|
490 500
....*....|....*....|....*.
gi 1799135526 691 MTEQEKQSITDELKQCKNNLKLLREK 716
Cdd:PRK03918 630 KAFEELAETEKRLEELRKELEELEKK 655
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
14-110 |
2.48e-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: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 14 SHPFQERHV---YLDEPIKIGRSvARCRPAQNNATfdckvLSRNHALVW---FDHKTG-KFYLQDTkSSNGTFINSQRLS 86
Cdd:cd22670 7 SSPGSTDIVlpiYKNQVITIGRS-PSCDIVINDPF-----VSRTHCRIYsvqFDESSApLVYVEDL-SSNGTYLNGKLIG 79
|
90 100
....*....|....*....|....*
gi 1799135526 87 RGseespPCEILS-GDIIQFGVDVT 110
Cdd:cd22670 80 RN-----NTVLLSdGDVIEIAHSAT 99
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
448-711 |
4.06e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 448 LEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLRE---EKDSEITSTRDELLSARDEI-----------LLLHQAAA 513
Cdd:TIGR02169 700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKErleELEEDLSSLEQEIENVKSELkelearieeleEDLHKLEE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 514 KV----ASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQ----------NSFQLRCQQCEDQQREEATR---- 575
Cdd:TIGR02169 780 ALndleARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTlekeylekeiQELQEQRIDLKEQIKSIEKEienl 859
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 576 ------LQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQ 649
Cdd:TIGR02169 860 ngkkeeLEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDP 939
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135526 650 HLRDSADLKTLLS----KAENQAKDVQ------------KEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCkNNLK 711
Cdd:TIGR02169 940 KGEDEEIPEEELSledvQAELQRVEEEiralepvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY-EKKK 1016
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
28-85 |
4.08e-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: 4.08e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135526 28 IKIGRSvarcrPAQNNATFDCKVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRL 85
Cdd:smart00240 1 VTIGRS-----SEDCDIQLDGPSISRRHAVIVYD-GGGRFYLIDLGSTNGTFVNGKRI 52
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
247-716 |
4.79e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 4.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 247 KHNYETTAKESLRRVLQEKIEVVRKLSEVERSlsntEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAE- 325
Cdd:PTZ00121 1207 KAEEERKAEEARKAEDAKKAEAVKKAEEAKKD----AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADe 1282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 326 -GKQEEIQQKGQAEKKELQHKIDEMEEKEQElQAKIEALQADNDFTNERLTALQEKliveghltkavEETKLSKENQTRA 404
Cdd:PTZ00121 1283 lKKAEEKKKADEAKKAEEKKKADEAKKKAEE-AKKADEAKKKAEEAKKKADAAKKK-----------AEEAKKAAEAAKA 1350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 405 KESDFSDTLSPSKEKssddttdAQMDEQDLNEPLAKVSLLKALLEEERKA--YRNQVEESTKQIQVL------QAQLQRL 476
Cdd:PTZ00121 1351 EAEAAADEAEAAEEK-------AEAAEKKKEEAKKKADAAKKKAEEKKKAdeAKKKAEEDKKKADELkkaaaaKKKADEA 1423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 477 HIDTENLRE----EKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAEL----ERWRKAASEYE 548
Cdd:PTZ00121 1424 KKKAEEKKKadeaKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAkkkaEEAKKKADEAK 1503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 549 KEITSLQNSFQLR----CQQCEDQQREEATRLQGELEKLRKEWNALEtechsLKRENVLLSSELQRQEKELHNSQKQSLE 624
Cdd:PTZ00121 1504 KAAEAKKKADEAKkaeeAKKADEAKKAEEAKKADEAKKAEEKKKADE-----LKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 625 LTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKlkfemTEQEKQSITDELK 704
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK-----KEAEEKKKAEELK 1653
|
490
....*....|..
gi 1799135526 705 QCKNNLKLLREK 716
Cdd:PTZ00121 1654 KAEEENKIKAAE 1665
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
237-681 |
5.27e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.45 E-value: 5.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 237 RKELIALQEDKHNYETTAK--ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERtQEELRELANKYNGAVNEI 314
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQilSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQ-ILELEGYEMDYNSYLKSI 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 315 KDLSDKLKVAEGKQE-------EIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKL-IVEGH 386
Cdd:PRK01156 373 ESLKKKIEEYSKNIErmsafisEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMeMLNGQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 387 LTKAVEETKLSKENQTRAKEsDFSDTLSPSKEkssdDTTDAQMDEQDLNEplaKVSLLKALLEEERKAYRNQVEESTKQI 466
Cdd:PRK01156 453 SVCPVCGTTLGEEKSNHIIN-HYNEKKSRLEE----KIREIEIEVKDIDE---KIVDLKKRKEYLESEEINKSINEYNKI 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 467 QVLQAQLQRLHIDTENLR------EEKDSEITSTRDELLSARDEILLlhqaaaKVASERDT-DIASLQEELKKVRAELER 539
Cdd:PRK01156 525 ESARADLEDIKIKINELKdkhdkyEEIKNRYKSLKLEDLDSKRTSWL------NALAVISLiDIETNRSRSNEIKKQLND 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 540 WRKAASEYEKEITSLQNSFQLRCQQCEDQ------QREEATRLQGELEKLRKewnaletechslKRENvllsseLQRQEK 613
Cdd:PRK01156 599 LESRLQEIEIGFPDDKSYIDKSIREIENEannlnnKYNEIQENKILIEKLRG------------KIDN------YKKQIA 660
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799135526 614 ELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLS---KAENQAKDVQKEYEKTQTV 681
Cdd:PRK01156 661 EIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTrinELSDRINDINETLESMKKI 731
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
310-557 |
6.37e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.61 E-value: 6.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 310 AVNEIKDLSDKLKVAEGKQEEIQqkgqAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLiveghlTK 389
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQ----AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI------EE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 390 AVEETKlskenqTRAKESdfsdtlspSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAyrnqveesTKQIQVL 469
Cdd:COG3883 84 RREELG------ERARAL--------YRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADL--------LEELKAD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 470 QAQLqrlhidtenlrEEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEK 549
Cdd:COG3883 142 KAEL-----------EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
....*...
gi 1799135526 550 EITSLQNS 557
Cdd:COG3883 211 AAAAAAAA 218
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
162-591 |
6.57e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 6.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 162 SQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgNQLQAcsKNQTEDSLRKELI 241
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE---AELAE--AEEELEELAEELL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 242 ALQEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKL 321
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 322 KVAEGKQEEIQQ-KGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKE- 399
Cdd:COG1196 470 EEAALLEAALAElLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALq 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 400 NQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAK----------VSLLKALLEEERKAYRNQVEES------T 463
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAalargaigaaVDLVASDLREADARYYVLGDTLlgrtlvA 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 464 KQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKA 543
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799135526 544 ASEYEKEITSLQNSFQLRCQQCEDQQREEATR-----------------------LQGELEKLRKEWNALE 591
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELleeeelleeealeelpeppdleeLERELERLEREIEALG 780
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
135-658 |
8.05e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.89 E-value: 8.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 135 ARLRSDVIHAPLpSPVDKVAANTPSMYSQELFQL----SQYLQEALHREQMLEQKLATLQRLLAItqeASDTSWQALIDE 210
Cdd:pfam15921 290 ARSQANSIQSQL-EIIQEQARNQNSMYMRQLSDLestvSQLRSELREAKRMYEDKIEELEKQLVL---ANSELTEARTER 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 211 DRLLSRLEVMGNQLQAC----SKNQTEDSLRKELIALQEDKHNYETTAKESLRRVLQEKIEVVRKLS------------E 274
Cdd:pfam15921 366 DQFSQESGNLDDQLQKLladlHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEallkamksecqgQ 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 275 VERSLSNTEDECTHL-------------KEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQE-------EIQQK 334
Cdd:pfam15921 446 MERQMAAIQGKNESLekvssltaqlestKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEatnaeitKLRSR 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 335 GQAEKKELQHKIDEmEEKEQELQAKIEALQADNDFTNERLTALQEKL-----IVEGHLTKA----VEETKLSKE-NQTRA 404
Cdd:pfam15921 526 VDLKLQELQHLKNE-GDHLRNVQTECEALKLQMAEKDKVIEILRQQIenmtqLVGQHGRTAgamqVEKAQLEKEiNDRRL 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 405 KESDFsdtlspskeKSSDDTTDAQMDEQDlneplAKVSLLKalleeerkayrnqveesTKQIQVLQAQLQRLHIdTENLR 484
Cdd:pfam15921 605 ELQEF---------KILKDKKDAKIRELE-----ARVSDLE-----------------LEKVKLVNAGSERLRA-VKDIK 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 485 EEKD---SEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWR--------------KAASEY 547
Cdd:pfam15921 653 QERDqllNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRntlksmegsdghamKVAMGM 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 548 EKEITSLQNsfQLRCQQCEDQQREEATR--------LQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQ 619
Cdd:pfam15921 733 QKQITAKRG--QIDALQSKIQFLEEAMTnankekhfLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME 810
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1799135526 620 ----KQSLELTSDLSILQmsRKELENQvgSLKEQHLRDSADLK 658
Cdd:pfam15921 811 valdKASLQFAECQDIIQ--RQEQESV--RLKLQHTLDVKELQ 849
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
255-600 |
8.59e-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: 55.84 E-value: 8.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 255 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQK 334
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 335 GQAEKKELQHKIDEMEEKEQ---ELQAKIEALQADNDftNERLTALQEKLiveghltKAVEETKLSKENQTRAKESDFSD 411
Cdd:TIGR02169 753 IENVKSELKELEARIEELEEdlhKLEEALNDLEARLS--HSRIPEIQAEL-------SKLEEEVSRIEARLREIEQKLNR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 412 tLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKdSEI 491
Cdd:TIGR02169 824 -LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL-REL 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 492 TSTRDELLSARDEilllhqaAAKVASERDTDIASLQEELKkvraELERWRKAASEYEKEITSLQNsFQLRCQQCED---- 567
Cdd:TIGR02169 902 ERKIEELEAQIEK-------KRKRLSELKAKLEALEEELS----EIEDPKGEDEEIPEEELSLED-VQAELQRVEEeira 969
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1799135526 568 ---------QQREEATR----LQGELEKLRKEWNALE---TECHSLKRE 600
Cdd:TIGR02169 970 lepvnmlaiQEYEEVLKrldeLKEKRAKLEEERKAILeriEEYEKKKRE 1018
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
223-650 |
1.51e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 55.05 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 223 QLQACSKNQTEDSLRKELIALQEDKHNYE--------TTAKESLRRVLQEKIEVVRK-----------LSEVERSLSNTE 283
Cdd:TIGR00606 597 NKELASLEQNKNHINNELESKEEQLSSYEdklfdvcgSQDEESDLERLKEEIEKSSKqramlagatavYSQFITQLTDEN 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 284 DECTHLKEMNERTQEELRE----LANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAK 359
Cdd:TIGR00606 677 QSCCPVCQRVFQTEAELQEfisdLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKV 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 360 IEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLA 439
Cdd:TIGR00606 757 NRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQH 836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 440 KVSLLKALLEEERKAyrnqVEESTKQIQVLQAQL-----QRLHIDT--------ENLREEKDSEITSTRDELLSARDEIL 506
Cdd:TIGR00606 837 ELDTVVSKIELNRKL----IQDQQEQIQHLKSKTnelksEKLQIGTnlqrrqqfEEQLVELSTEVQSLIREIKDAKEQDS 912
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 507 LLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGEL------ 580
Cdd:TIGR00606 913 PLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLeecekh 992
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135526 581 -EKLRKEWNALETECHSLKRENVLLSSELQRQE-----KELHNSQKQSLELTSDLSILQMSR--KELENQVGSLKEQH 650
Cdd:TIGR00606 993 qEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKrenelKEVEEELKQHLKEMGQMQVLQMKQehQKLEENIDLIKRNH 1070
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
210-555 |
1.56e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 210 EDRLLSRLEVMGNQLQacsKNQTEDSLRKELIALQEDKHNYETTAK--------ESLRRVLQEKIEVVRKLSEVERSLSN 281
Cdd:TIGR02169 186 IERLDLIIDEKRQQLE---RLRREREKAERYQALLKEKREYEGYELlkekealeRQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 282 TEDECTH----LKEMNERtqeelrelankyngavneIKDLSdklkvaEGKQEEIQQK---GQAEKKELQHKIDEMEEKEQ 354
Cdd:TIGR02169 263 LEKRLEEieqlLEELNKK------------------IKDLG------EEEQLRVKEKigeLEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 355 ELQAKIEALQADNDFTNERLTALQEKLiveghLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQdl 434
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREI-----EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR-- 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 435 neplakvsllkalleEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREE---KDSEITSTRDELLSARDEIlllhqa 511
Cdd:TIGR02169 392 ---------------EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAiagIEAKINELEEEKEDKALEI------ 450
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1799135526 512 aakvaSERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQ 555
Cdd:TIGR02169 451 -----KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
263-710 |
2.14e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.80 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 263 QEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGA----------VNEIKDLSDKLKVAEGKQEEIQ 332
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAeemrarlaarKQELEEILHELESRLEEEEERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 333 QKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEK-LIVEGHLTKAVEETKLSKEnqtraKESDFSD 411
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDiLLLEDQNSKLSKERKLLEE-----RISEFTS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 412 TLSPSKEKSSDDTTDAQMDE---QDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTenlrEEKD 488
Cdd:pfam01576 167 NLAEEEEKAKSLSKLKNKHEamiSDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQL----AKKE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 489 SEITSTRDELlsarDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQ 568
Cdd:pfam01576 243 EELQAALARL----EEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 569 QREEATRLQgELEKLRKewnALETECHslkrenvllSSELQRQEKELHNSQkQSLELTSDLSILQMSRKELENQVGSLKE 648
Cdd:pfam01576 319 QELRSKREQ-EVTELKK---ALEEETR---------SHEAQLQEMRQKHTQ-ALEELTEQLEQAKRNKANLEKAKQALES 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799135526 649 QHLRDSADLKTLlskaeNQAK-DVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNL 710
Cdd:pfam01576 385 ENAELQAELRTL-----QQAKqDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSEL 442
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-705 |
2.39e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 197 QEASDTSWQALIDEDRLLSRLEVMGNQLQacsknqtedSLRKELIALQEDKHNYETTAKESLRRVLQEKI---EVVRKLS 273
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIE---------EERKRRDKLTEEYAELKEELEDLRAELEEVDKefaETRDELK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 274 EVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIqqkgQAEKKELQHKIDEMEEKE 353
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK----ALEIKKQEWKLEQLAADL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 354 QELQAKIEALQADNDFTNERLTALQEKLIV----------EGHLTKAVEETK---------------------------- 395
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELSKLQRELAEaeaqaraseeRVRGGRAVEEVLkasiqgvhgtvaqlgsvgeryataieva 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 396 ----------------------LSKENQTRA------KESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAK------- 440
Cdd:TIGR02169 545 agnrlnnvvveddavakeaielLKRRKAGRAtflplnKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKyvfgdtl 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 441 -----------------VSLLKALLE----------EERKAYRNQVEESTKqIQVLQAQLQRLHIDTENLREEKDsEITS 493
Cdd:TIGR02169 625 vvedieaarrlmgkyrmVTLEGELFEksgamtggsrAPRGGILFSRSEPAE-LQRLRERLEGLKRELSSLQSELR-RIEN 702
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 494 TRDELLSARD-----------EILLLHQAAAKVA----------SERDTDIASLQEELKKVRAELERWRKAASEYEKEIT 552
Cdd:TIGR02169 703 RLDELSQELSdasrkigeiekEIEQLEQEEEKLKerleeleedlSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN 782
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 553 SLQNSF----------QLRCQQCEDQQREEATR-LQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQ 621
Cdd:TIGR02169 783 DLEARLshsripeiqaELSKLEEEVSRIEARLReIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK 862
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 622 SLELTSDLSILQMSRKELENQVGSLKeqhlRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITD 701
Cdd:TIGR02169 863 KEELEEELEELEAALRDLESRLGDLK----KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED 938
|
....
gi 1799135526 702 ELKQ 705
Cdd:TIGR02169 939 PKGE 942
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
443-621 |
3.02e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 443 LLKALLEEERKAYR----------NQVEESTKQIQVLQAQLQRLHIDTENLrEEKDSEITSTRDELLSARDEILLLHQAA 512
Cdd:COG4717 47 LLERLEKEADELFKpqgrkpelnlKELKELEEELKEAEEKEEEYAELQEEL-EELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 513 AKVA-----SERDTDIASLQEELKKVRAELERWRKAASEY---EKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLR 584
Cdd:COG4717 126 QLLPlyqelEALEAELAELPERLEELEERLEELRELEEELeelEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190
....*....|....*....|....*....|....*..
gi 1799135526 585 KEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQ 621
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
27-106 |
3.29e-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: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 27 PIKIGRSVARcRPAQNNATFDC-----KVLSRNHALVWFDHKTGKFYLQdTKSSNGTFINSQRLSRGseeSPPCEILSGD 101
Cdd:cd22701 18 EVVLGRNSKN-SSSTAADSVDIdlgpsKKISRRHARIFYDFTTQCFELS-VLGRNGVKVDGILVKPG---SPPVPLRSGS 92
|
....*
gi 1799135526 102 IIQFG 106
Cdd:cd22701 93 LIQIG 97
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
266-710 |
4.74e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 266 IEVVRKLSEVERSLSNTEDECTHLKEMNERTQE--ELRELANKYNGAVNEIKDLSDKLKVAEGKQEeiQQKGQAEKKELQ 343
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELLEPIRELAERyaAARERLAELEYLRAALRLWFAQRRLELLEAE--LEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 344 HKIDEMEEKEQELQAKIEALQAD-NDFTNERLTALQEKLiveghltkaveETKLSKENQTRAKESDFSDTLSPSKEKSSD 422
Cdd:COG4913 309 AELERLEARLDALREELDELEAQiRGNGGDRLEQLEREI-----------ERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 423 DttdaqmdEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREeKDSEITStrdELLSAR 502
Cdd:COG4913 378 S-------AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER-RKSNIPA---RLLALR 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 503 DEIlllhqAAAKVASERDTDIASlqeELKKVRAELERWRKAA--------------SEYEKEIT----SLQNSFQLRCQQ 564
Cdd:COG4913 447 DAL-----AEALGLDEAELPFVG---ELIEVRPEEERWRGAIervlggfaltllvpPEHYAAALrwvnRLHLRGRLVYER 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 565 CEDQQREEATR---------------------LQGEL------------EKLRKEWNALETEC--------------HSL 597
Cdd:COG4913 519 VRTGLPDPERPrldpdslagkldfkphpfrawLEAELgrrfdyvcvdspEELRRHPRAITRAGqvkgngtrhekddrRRI 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 598 KRENVL----------LSSELQRQEKELHNSQKQSLELTSDLSILQMSR----------------KELENQVGSLKEQH- 650
Cdd:COG4913 599 RSRYVLgfdnraklaaLEAELAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidvASAEREIAELEAELe 678
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799135526 651 --LRDSADLKTLlskaENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNL 710
Cdd:COG4913 679 rlDASSDDLAAL----EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
182-621 |
5.39e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 182 LEQKLATLQRLLAI----TQEASDTSWQALIDEDRllSRLEVMGNQLQACSknQTEDSLRKELIALQEDKHNYETTAKES 257
Cdd:COG4913 267 ARERLAELEYLRAAlrlwFAQRRLELLEAELEELR--AELARLEAELERLE--ARLDALREELDELEAQIRGNGGDRLEQ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 258 LRRVLQEKievVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQA 337
Cdd:COG4913 343 LEREIERL---ERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 338 EKKELQHKIDEMEEK----EQELQAKIEALQADNDFTNERL-----------------TALqEK--------LIVEGH-- 386
Cdd:COG4913 420 ELRELEAEIASLERRksniPARLLALRDALAEALGLDEAELpfvgelievrpeeerwrGAI-ERvlggfaltLLVPPEhy 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 387 --LTKAVEETKL-------------SKENQTRA-----------KESDFSDTLSPSKEKSSD----DTTDA--------- 427
Cdd:COG4913 499 aaALRWVNRLHLrgrlvyervrtglPDPERPRLdpdslagkldfKPHPFRAWLEAELGRRFDyvcvDSPEElrrhprait 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 428 ---------QMDEQDLNEPLAKVSLL-------KALLEEERKAYRNQVEESTKQIQVLQAQLQRLhiDTENLREEKDSEI 491
Cdd:COG4913 579 ragqvkgngTRHEKDDRRRIRSRYVLgfdnrakLAALEAELAELEEELAEAEERLEALEAELDAL--QERREALQRLAEY 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 492 TSTRDELLSARDEILLLHQAAAKVaSERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFqlrcQQCEDQQRE 571
Cdd:COG4913 657 SWDEIDVASAEREIAELEAELERL-DASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL----EQAEEELDE 731
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135526 572 EATRLQGELEKLRKEWNA-LETECHSLKRENVL------LSSELQRQEKELHNSQKQ 621
Cdd:COG4913 732 LQDRLEAAEDLARLELRAlLEERFAAALGDAVErelrenLEERIDALRARLNRAEEE 788
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
257-504 |
6.20e-07 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 53.01 E-value: 6.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 257 SLRRVLQEKIEVVRKLSEVERslsnteDECTHLKEmNERTqEELRELANKYNGAVNEIKDLSDKLKVAEGKQ-------- 328
Cdd:PRK05771 13 TLKSYKDEVLEALHELGVVHI------EDLKEELS-NERL-RKLRSLLTKLSEALDKLRSYLPKLNPLREEKkkvsvksl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 329 EEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQA---------DNDFTNERLTALQEKLIVEGHLTKAVEETKLSKE 399
Cdd:PRK05771 85 EELIKDVEEELEKIEKEIKELEEEISELENEIKELEQeierlepwgNFDLDLSLLLGFKYVSVFVGTVPEDKLEELKLES 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 400 NQTRAKESDFSDTLSP-----SKEkssddttdaqmDEQDLNEPLAKVSLLKALLEEERKAYRnQVEESTKQIQVLQAQLQ 474
Cdd:PRK05771 165 DVENVEYISTDKGYVYvvvvvLKE-----------LSDEVEEELKKLGFERLELEEEGTPSE-LIREIKEELEEIEKERE 232
|
250 260 270
....*....|....*....|....*....|
gi 1799135526 475 RLHIDTENLREEKDSEITSTRDELLSARDE 504
Cdd:PRK05771 233 SLLEELKELAKKYLEELLALYEYLEIELER 262
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
26-106 |
8.00e-07 |
|
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438750 [Multi-domain] Cd Length: 93 Bit Score: 47.79 E-value: 8.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 26 EPIKIGRSVArcrpaqNNATFDCKVLSRNHALVwfDHKTGKFYLQDTKSSNGTFINSQRLSRGseesppcEILSGDIIQF 105
Cdd:cd22698 21 DEFTIGRSSN------NDIRLNDHSVSRHHARI--VRQGDKCNLTDLGSTNGTFLNGIRVGTH-------ELKHGDRIQL 85
|
.
gi 1799135526 106 G 106
Cdd:cd22698 86 G 86
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
25-114 |
8.16e-07 |
|
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. Specially, RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438715 [Multi-domain] Cd Length: 110 Bit Score: 48.12 E-value: 8.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 25 DEPIKIGRSVArcrpAQNNATFDC-KVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDII 103
Cdd:cd22663 20 GKEVTVGRGLG----VTYQLVSTCpLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERI----EPLKPYPLNEGDLI 90
|
90
....*....|.
gi 1799135526 104 QFGVDVTENTR 114
Cdd:cd22663 91 QLGVPPENKEP 101
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
234-698 |
9.89e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 9.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 234 DSLRKELIALQEDKHNYETtAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNER--TQEELRELANKYNGAV 311
Cdd:COG4717 74 KELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELeaLEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 312 NEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLiveGHLTKAV 391
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL---EELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 392 EETKLSKENQTRAKESDFSDTLSPSkekssddttdaqmdeqdlnepLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQA 471
Cdd:COG4717 230 EQLENELEAAALEERLKEARLLLLI---------------------AAALLALLGLGGSLLSLILTIAGVLFLVLGLLAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 472 QLQRLHIDTENLREEKDSEITSTRDELLSAR--DEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAA--SEY 547
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELEEEelEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqlEEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 548 EKEITSLQNSFQLrcqQCEDQQREEATRLQgELEKLRKEWNALETECHSLKRENVLLSSELQRQ--EKELHNSQKQSLEL 625
Cdd:COG4717 369 EQEIAALLAEAGV---EDEEELRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEEL 444
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799135526 626 TSDLSILQMSRKELENQVGSLKEQHlrDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 698
Cdd:COG4717 445 EEELEELREELAELEAELEQLEEDG--ELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLP 515
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
229-719 |
1.10e-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: 52.03 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 229 KNQTEDSLRKELIALQEDKHNYETTAK---------ESLRRVLQEKIEVVRKLSEVERSlsnTEDECTHLKEMNERTQEE 299
Cdd:pfam05483 94 KVSIEAELKQKENKLQENRKIIEAQRKaiqelqfenEKVSLKLEEEIQENKDLIKENNA---TRHLCNLLKETCARSAEK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 300 LRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAkiEALQADNDFTNE---RLTA 376
Cdd:pfam05483 171 TKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEE--EYKKEINDKEKQvslLLIQ 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 377 LQEKLIVEGHLTKAVEETKlSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYR 456
Cdd:pfam05483 249 ITEKENKMKDLTFLLEESR-DKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTIC 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 457 NQVEESTKQIQVLQAQLQrlhidTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVR-- 534
Cdd:pfam05483 328 QLTEEKEAQMEELNKAKA-----AHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKnn 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 535 --AELERWRKAASEYEKEITSlQNSFQLRCQQCEDQQREeatrLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQE 612
Cdd:pfam05483 403 keVELEELKKILAEDEKLLDE-KKQFEKIAEELKGKEQE----LIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLK 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 613 KELHNSQKQSLELTSDLSILQMSRKELENQVGSL--------------KEQHLRDSADLKTLLSKAENQAKDVQKEYEKT 678
Cdd:pfam05483 478 TELEKEKLKNIELTAHCDKLLLENKELTQEASDMtlelkkhqediincKKQEERMLKQIENLEEKEMNLRDELESVREEF 557
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1799135526 679 QTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNN 719
Cdd:pfam05483 558 IQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN 598
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
55-108 |
1.15e-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: 1.15e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1799135526 55 HALVWFDHKTGKFYLQDTKSSNGTFINSQRLSrgseESPPCEILSGDIIQFGVD 108
Cdd:cd22704 39 HAVITYDQIDNEFKIKDLGSLNGTFVNDSRIP----EQTYITLKLGDSIRFGYD 88
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
444-698 |
1.26e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 444 LKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDseITSTRDELLSARDEIlllhqaaakvaSERDTDI 523
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG--LVDLSEEAKLLLQQL-----------SELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 524 ASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRcqqcedQQREEATRLQGELEKLRKEWnaleTECHSLKREnvl 603
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQ------QLRAQLAELEAELAELSARY----TPNHPDVIA--- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 604 LSSELQRQEKELHNSQKQSL-ELTSDLSILQMSRKELENQVGSLKEQHLRdsadlktlLSKAENQAKDVQKEYEKTQTVL 682
Cdd:COG3206 296 LRAQIAALRAQLQQEAQRILaSLEAELEALQAREASLQAQLAQLEARLAE--------LPELEAELRRLEREVEVARELY 367
|
250
....*....|....*.
gi 1799135526 683 SELKLKFEMTEQEKQS 698
Cdd:COG3206 368 ESLLQRLEEARLAEAL 383
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
182-680 |
1.29e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 182 LEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgnqlqacSKNQTEDSLRKELIALQEDKHNYETTaKESLRRV 261
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHE---------ERREELETLEAEIEDLRETIAETERE-REELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 262 LQEKIEVVRKLSEVERSL-----------SNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEE 330
Cdd:PRK02224 281 VRDLRERLEELEEERDDLlaeaglddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 331 IQQKGQAEKKELQH---KIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLiveghltkaveETKLSKENQTRAKES 407
Cdd:PRK02224 361 LREEAAELESELEEareAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL-----------EELREERDELREREA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 408 DFSDTLS------------------PSKEKSSDDTTDAQMDEQDlNEPLAKVSLLKALLEEERKAYRNQVE------EST 463
Cdd:PRK02224 430 ELEATLRtarerveeaealleagkcPECGQPVEGSPHVETIEED-RERVEELEAELEDLEEEVEEVEERLEraedlvEAE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 464 KQIQVLQAQLQRLhidtENLREEKDSEITSTRDELLSARDEilllhqaaakvASERDTDIASLQEELKKVRAELERWRKA 543
Cdd:PRK02224 509 DRIERLEERREDL----EELIAERRETIEEKRERAEELRER-----------AAELEAEAEEKREAAAEAEEEAEEAREE 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 544 ASEYEKEITSLQNSFQ-LRCQQCEDQQREEATRLQGELEKLRKEWNALETECH---SLKRENVL-LSSELQRQEKELHNS 618
Cdd:PRK02224 574 VAELNSKLAELKERIEsLERIRTLLAAIADAEDEIERLREKREALAELNDERRerlAEKRERKReLEAEFDEARIEEARE 653
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135526 619 QKQSLE-----LTSDLSILQMSRKELENQVGSLKEQhLRDSADLKTLLSKAENQAKDVQKEYEKTQT 680
Cdd:PRK02224 654 DKERAEeyleqVEEKLDELREERDDLQAEIGAVENE-LEELEELRERREALENRVEALEALYDEAEE 719
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
420-649 |
1.61e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 420 SSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREE---KDSEITSTRD 496
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaeLEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 497 ELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQnsfqlrcqqcedQQREEATRL 576
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR------------ADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799135526 577 QGELEKLRKEWNALETEchsLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQ 649
Cdd:COG4942 166 RAELEAERAELEALLAE---LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
213-651 |
2.10e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 51.36 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 213 LLSRLEVMGNQLQACskNQTEDSLRKELialqedkhnyetTAKESLRRVLQEKIEVVR-KLSEVERSLSNTedecthlke 291
Cdd:pfam10174 308 LQTKLETLTNQNSDC--KQHIEVLKESL------------TAKEQRAAILQTEVDALRlRLEEKESFLNKK--------- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 292 mnertQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQaekkELQHKIDEMEEKEQELQAKIEALQADNDFTN 371
Cdd:pfam10174 365 -----TKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIE----NLQEQLRDKDKQLAGLKERVKSLQTDSSNTD 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 372 ERLTALQEKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLK---ALL 448
Cdd:pfam10174 436 TALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLAssgLKK 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 449 EEERKAYRNQVEESTKQIQVLQAQLQRLH--IDTENLREEKDSEITSTRDELLSARDEilllhqaaakvASERDTDIASL 526
Cdd:pfam10174 516 DSKLKSLEIAVEQKKEECSKLENQLKKAHnaEEAVRTNPEINDRIRLLEQEVARYKEE-----------SGKAQAEVERL 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 527 QEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSS 606
Cdd:pfam10174 585 LGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGAL 664
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1799135526 607 ELQRQE----KELHNSQKQSL-ELTSDLSILQMSRKELENQVGSLKEQHL 651
Cdd:pfam10174 665 EKTRQEldatKARLSSTQQSLaEKDGHLTNLRAERRKQLEEILEMKQEAL 714
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
258-676 |
2.19e-06 |
|
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: 50.84 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 258 LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELAN----------KYNGAVNEIKDLSDKLKVAEGK 327
Cdd:pfam05622 2 LSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESgddsgtpggkKYLLLQKQLEQLQEENFRLETA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 328 QEEIQQKGQAEKK---ELQHKIDEMEEKEQELQA---KIEALQADNDftnerltalqekliveghltkaveetKLSKENQ 401
Cdd:pfam05622 82 RDDYRIKCEELEKevlELQHRNEELTSLAEEAQAlkdEMDILRESSD--------------------------KVKKLEA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 402 TrakesdfsdtlSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAY---RNQVEESTKQIQVLQAQLQRLHI 478
Cdd:pfam05622 136 T-----------VETYKKKLEDLGDLRRQVKLLEERNAEYMQRTLQLEEELKKAnalRGQLETYKRQVQELHGKLSEESK 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 479 DTENLR------EEKDSEITSTRDELLSARD------EILLLHQAAAKVASERDTDIASLQEELKKVRAELerwrkAASE 546
Cdd:pfam05622 205 KADKLEfeykklEEKLEALQKEKERLIIERDtlretnEELRCAQLQQAELSQADALLSPSSDPGDNLAAEI-----MPAE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 547 YEKEITSLQNSFQ-LRCQQcEDQQREEATRLQGELEKLRKEWNALETEcHSLKRENVLLSS----ELQRQEKELHNSQKQ 621
Cdd:pfam05622 280 IREKLIRLQHENKmLRLGQ-EGSYRERLTELQQLLEDANRRKNELETQ-NRLANQRILELQqqveELQKALQEQGSKAED 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135526 622 SLELTSDLSILQMSRKELENQVGSLKEQ--HLRDSADLKTLLSKAENQAKDVQKEYE 676
Cdd:pfam05622 358 SSLLKQKLEEHLEKLHEAQSELQKKKEQieELEPKQDSNLAQKIDELQEALRKKDED 414
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
289-551 |
3.51e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 289 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALqadnd 368
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEEL----- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 369 ftNERLTALQEKLI-VEGHLTK-AVEETKLSKENQTRAKESDF----------SDTLSPSKEKSSDDTTDAQMDEQDLNE 436
Cdd:PHA02562 240 --TDELLNLVMDIEdPSAALNKlNTAAAKIKSKIEQFQKVIKMyekggvcptcTQQISEGPDRITKIKDKLKELQHSLEK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 437 plakvsLLKALLEEERKAyrNQVEESTKQIQVLQAQLqrlhidtenlrEEKDSEITSTRDELLSARDEIlllHQAAAKVA 516
Cdd:PHA02562 318 ------LDTAIDELEEIM--DEFNEQSKKLLELKNKI-----------STNKQSLITLVDKAKKVKAAI---EELQAEFV 375
|
250 260 270
....*....|....*....|....*....|....*
gi 1799135526 517 SErdtdiaslQEELKKVRAELERWRKAASEYEKEI 551
Cdd:PHA02562 376 DN--------AEELAKLQDELDKIVKTKSELVKEK 402
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
322-648 |
4.55e-06 |
|
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: 50.14 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 322 KVAEGKQEEIQQKGQAeKKELQHKIDEMEEKEQELQAKIEALQADNDFT-NERLTALQEKLIVE-GHLTKAVEETKLSKE 399
Cdd:pfam09731 78 ESKEPKEEKKQVKIPR-QSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEkEKALEEVLKEAISKaESATAVAKEAKDDAI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 400 NQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRN---------------QVEESTK 464
Cdd:pfam09731 157 QAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLdaapetppklpehldNVEEKVE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 465 QIQVLQAQLQRLHIDTENLREEKDSEITSTRDEL----------LSARDEILLLH------QAAAKVASERDTDIASLQE 528
Cdd:pfam09731 237 KAQSLAKLVDQYKELVASERIVFQQELVSIFPDIipvlkednllSNDDLNSLIAHahreidQLSKKLAELKKREEKHIER 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 529 ELKKVRAELERWRkaaseyEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSEL 608
Cdd:pfam09731 317 ALEKQKEELDKLA------EELSARLEEVRAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEI 390
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1799135526 609 QRQEKELHNSQKQSLE----LTSDLSILQMSRKELENQVGSLKE 648
Cdd:pfam09731 391 ELQREFLQDIKEKVEEeragRLLKLNELLANLKGLEKATSSHSE 434
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
27-117 |
4.77e-06 |
|
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 (AtPP2C70) and similar proteins; AtPP2C70, also called kinase-associated protein phosphatase, or protein ROOT ATTENUATED GROWTH 1, dephosphorylates the serine/threonine receptor-like kinase RLK5. It may function as a signaling component in a pathway involving RLK5. It acts as a negative regulator of the CLAVATA1 signaling in plant development by binding and dephosphorylating CLAVATA1. It is also a component of a signaling pathway which mediates adaptation to NaCl stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438730 [Multi-domain] Cd Length: 102 Bit Score: 45.81 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 27 PIKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLsrgSEESPPCEILSGDIIQFG 106
Cdd:cd22678 24 PLTIGRIQ------RGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESI---SPNGRPVVLSSGDVITLG 94
|
90
....*....|.
gi 1799135526 107 vdvTENTRKVT 117
Cdd:cd22678 95 ---SETKILVR 102
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
162-694 |
6.22e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.82 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 162 SQELFQLSQYLQEALHR----EQMLEQKLATLQRLLAITQEASDTSWQALIDEDRllsRLEVMGNQLQACSKNQTEDSLR 237
Cdd:pfam10174 129 AKELFLLRKTLEEMELRietqKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWER---TRRIAEAEMQLGHLEVLLDQKE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 238 KELIALQEDKH-NYETTAKESLRRVLQEKIEVV-RKLSEVERSLSNTEDECTHLKEMNERTQEELRElankyngavnEIK 315
Cdd:pfam10174 206 KENIHLREELHrRNQLQPDPAKTKALQTVIEMKdTKISSLERNIRDLEDEVQMLKTNGLLHTEDREE----------EIK 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 316 dlsdKLKVAEGKQEEIQQKGQAEKKELQHKIDEMeekeQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETK 395
Cdd:pfam10174 276 ----QMEVYKSHSKFMKNKIDQLKQELSKKESEL----LALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 396 LSKENQTRAKES---DFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEerkaYRNQVEESTKQIQVLQAQ 472
Cdd:pfam10174 348 DALRLRLEEKESflnKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIEN----LQEQLRDKDKQLAGLKER 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 473 LQRLHIDT---------------------ENLREEKDSEITSTRDELLSARDEILLLHQ---AAAKVASERDTDIASLQE 528
Cdd:pfam10174 424 VKSLQTDSsntdtalttleealsekeriiERLKEQREREDRERLEELESLKKENKDLKEkvsALQPELTEKESSLIDLKE 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 529 E--------------LKKVRAELERWRKAASEYEKEITSLQNS---------FQLRCQQCEDQ---QREEATRLQGELEK 582
Cdd:pfam10174 504 HasslassglkkdskLKSLEIAVEQKKEECSKLENQLKKAHNAeeavrtnpeINDRIRLLEQEvarYKEESGKAQAEVER 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 583 LRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQsleltsdlsiLQMSRKELENQVGSLKEQHLRDSADLKTllS 662
Cdd:pfam10174 584 LLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVAN----------IKHGQQEMKKKGAQLLEEARRREDNLAD--N 651
|
570 580 590
....*....|....*....|....*....|..
gi 1799135526 663 KAENQAKDVQKEYEKTQTVLSELKLKFEMTEQ 694
Cdd:pfam10174 652 SQQLQLEELMGALEKTRQELDATKARLSSTQQ 683
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
51-106 |
9.71e-06 |
|
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also called human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP), is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438729 [Multi-domain] Cd Length: 106 Bit Score: 44.85 E-value: 9.71e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799135526 51 LSRNHALVWF----DHKTGKFYLQDTKSSNGTFINSQRLsrgseesPP---CEILSGDIIQFG 106
Cdd:cd22677 41 ISRYHAVLQYrgdaDDHDGGFYLYDLGSTHGTFLNKQRI-------PPkqyYRLRVGHVLKFG 96
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
52-106 |
1.13e-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: 1.13e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135526 52 SRNH-ALVWfdHK-TGKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22674 48 SRVHaALVY--HKhLNRVFLIDLGSTHGTFVGGIRL----EPHKPQQLPIDSTLRFG 98
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
294-518 |
1.25e-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: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 294 ERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQqkgqAEKKELQHKIDEMEEKEQELQAKIEALQADndfTNER 373
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQ----AELEALQAEIDKLQAEIAEAEAEIEERREE---LGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 374 LTALQEklivEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQM----DEQDLNEPLAKVSLLKALLE 449
Cdd:COG3883 92 ARALYR----SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAeleaKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135526 450 EERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASE 518
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
28-106 |
1.67e-05 |
|
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438732 [Multi-domain] Cd Length: 96 Bit Score: 43.87 E-value: 1.67e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135526 28 IKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDhkTGKFYLQDTKSSNGTFINSQRlsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22680 23 VSIGRDP------ENVIVIPDPFVSRNHARITVD--SNEIYIEDLGSTNGTFVNDFK-----RIKGPAKLHPNDIIKLG 88
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
255-631 |
2.22e-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: 48.04 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 255 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDlsDKLKVAEGKQEEIQQK 334
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYL--DYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 335 GQAEKKELQHKIDEMEekeqelqaKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLS 414
Cdd:pfam02463 246 LRDEQEEIESSKQEIE--------KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 415 PSKEKSsddttdAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEES-TKQIQVLQAQLQRLHIDTENLREEKDSEITS 493
Cdd:pfam02463 318 ESEKEK------KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEeLEKLQEKLEQLEEELLAKKKLESERLSSAAK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 494 TRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELerwrkaaseyEKEITSLQNSFQLRCQQCEDQqreEA 573
Cdd:pfam02463 392 LKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE----------EESIELKQGKLTEEKEELEKQ---EL 458
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135526 574 TRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSI 631
Cdd:pfam02463 459 KLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALI 516
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
216-716 |
2.50e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.97 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 216 RLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTaKESLRRVLQEKIEVVRKLSEVERSLSNTEDECthlkemnER 295
Cdd:PRK01156 151 RKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYL-EEKLKSSNLELENIKKQIADDEKSHSITLKEI-------ER 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 296 TQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIqQKGQAEKKELQHKIDEMEEKEQELQAKI-EALQADNDFTNERL 374
Cdd:PRK01156 223 LSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI-KTAESDLSMELEKNNYYKELEERHMKIInDPVYKNRNYINDYF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 375 TALQEKLIVEGHLTKAVEETKLSKENQTRAK--ESDFSDTLSPSKEKSSDDT--TDAQMDEQDLNEPLAKVSLLKALLEE 450
Cdd:PRK01156 302 KYKNDIENKKQILSNIDAEINKYHAIIKKLSvlQKDYNDYIKKKSRYDDLNNqiLELEGYEMDYNSYLKSIESLKKKIEE 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 451 ERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLR---EEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQ 527
Cdd:PRK01156 382 YSKNIERMSAFISEILKIQEIDPDAIKKELNEINvklQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTT 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 528 EELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRenvLLSSE 607
Cdd:PRK01156 462 LGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLED---IKIKI 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 608 LQRQEKELHNSQKQSLELTSDLSILQMSRKELenqvgsLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKL 687
Cdd:PRK01156 539 NELKDKHDKYEEIKNRYKSLKLEDLDSKRTSW------LNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPD 612
|
490 500
....*....|....*....|....*....
gi 1799135526 688 KFEMTEQEKQSITDELKQCKNNLKLLREK 716
Cdd:PRK01156 613 DKSYIDKSIREIENEANNLNNKYNEIQEN 641
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
271-719 |
2.57e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.71 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 271 KLSEVERSLSNTEDECTHLKEMNERTQEELRElankyngAVNEIKDLsdkLKVAEGKQEEIQQKGQaEKKELQHKIDEME 350
Cdd:TIGR04523 336 IISQLNEQISQLKKELTNSESENSEKQRELEE-------KQNEIEKL---KKENQSYKQEIKNLES-QINDLESKIQNQE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 351 EKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKENQTrakesdfsdtlspskeKSSDDTTDAQmd 430
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELII----------------KNLDNTRESL-- 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 431 EQDLNEPLAKVSLLKALLEEERKayrnQVEESTKQIQVLQAQLQRLhidtenlrEEKDSEITSTRDELLSARDEIlllhq 510
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQK----ELKSKEKELKKLNEEKKEL--------EEKVKDLTKKISSLKEKIEKL----- 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 511 aaAKVASERDTDIASLQEELKKVRAELERwrkaaSEYEKEITSLQNSFqlrcqqceDQQREEATRLQGELEKLRKEWNAL 590
Cdd:TIGR04523 530 --ESEKKEKESKISDLEDELNKDDFELKK-----ENLEKEIDEKNKEI--------EELKQTQKSLKKKQEEKQELIDQK 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 591 ETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKD 670
Cdd:TIGR04523 595 EKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTK 674
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1799135526 671 VQKEYEKTQTVLSEL------KLKFEMTEQEKQSITDELKQCKNNLKLLREKGNN 719
Cdd:TIGR04523 675 IDDIIELMKDWLKELslhykkYITRMIRIKDLPKLEEKYKEIEKELKKLDEFSKE 729
|
|
| FHA_RAD53-like_rpt2 |
cd22690 |
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
12-103 |
2.77e-05 |
|
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine/threonine-protein kinase RAD53 and similar proteins; RAD53, also called CHEK2 homolog, or serine-protein kinase 1 (Spk1), is a nuclear protein kinase that phosphorylates proteins on serine, threonine, and tyrosine. It controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints and prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. It may be involved in the phosphorylation of RPH1. RAD53 contains two FHA domains. This model corresponds to the second one. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438742 [Multi-domain] Cd Length: 105 Bit Score: 43.82 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 12 PNSHPfqerHVYL-DEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFD-HKTGK--FYLQDTkSSNGTFINSQRLSR 87
Cdd:cd22690 8 NPSYP----DIELtQNTTFIGRS------KDCDEEITDPRISKHHCIITRKrSGKGLddVYVTDT-STNGTFINNNRLGK 76
|
90
....*....|....*.
gi 1799135526 88 GSEesppCEILSGDII 103
Cdd:cd22690 77 GSQ----SLLQDGDEI 88
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
14-106 |
2.88e-05 |
|
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.
Pssm-ID: 438734 [Multi-domain] Cd Length: 96 Bit Score: 43.29 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 14 SHPFQERHvyldepIKIGRSVarcrpaQNNATFDCKVLSRNHALvwFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEesp 93
Cdd:cd22682 14 QFPITEST------IVIGRSV------ESQVQIDDDSVSRYHAK--LAVNPSAVSIIDLGSTNGTIVNGKKIPKLAS--- 76
|
90
....*....|...
gi 1799135526 94 pCEILSGDIIQFG 106
Cdd:cd22682 77 -CDLQNGDQIKIG 88
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
302-621 |
3.03e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.43 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 302 ELANKYNG-AVNEIKDLSDKLKVAEGKQ--EEIQQKGQAEKKELQHKIDEMEEKEQELQAKIE------ALQADNDfTNE 372
Cdd:pfam17380 255 EYTVRYNGqTMTENEFLNQLLHIVQHQKavSERQQQEKFEKMEQERLRQEKEEKAREVERRRKleeaekARQAEMD-RQA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 373 RLTALQEKLIVEghltKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSdDTTDAQMDEQDLNEPLAK---VSLLKALLE 449
Cdd:pfam17380 334 AIYAEQERMAME----RERELERIRQEERKRELERIRQEEIAMEISRMR-ELERLQMERQQKNERVRQeleAARKVKILE 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 450 EERKayRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAA-----KVASERDTDIA 524
Cdd:pfam17380 409 EERQ--RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEerkrkKLELEKEKRDR 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 525 SLQEELKK--VRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQR----EEATRLQGELEKLRKEWNALETECHSLK 598
Cdd:pfam17380 487 KRAEEQRRkiLEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERrreaEEERRKQQEMEERRRIQEQMRKATEERS 566
|
330 340
....*....|....*....|....
gi 1799135526 599 R-ENVLLSSELQRQEKELHNSQKQ 621
Cdd:pfam17380 567 RlEAMEREREMMRQIVESEKARAE 590
|
|
| FHA_CHFR |
cd22672 |
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ... |
49-105 |
3.09e-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: 3.09e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135526 49 KVLSRNHALVWFDHKtGKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQF 105
Cdd:cd22672 39 KLVSGDHCKIIRDEK-GQVWLEDT-STNGTLVNKVKVVKGQK----VELKHGDVIYL 89
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
313-717 |
3.30e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 313 EIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHK---IDEMEEKEQELQAKIEALQA---DNDFTNERLTALQ-EKLIVEG 385
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVlreINEISSELPELREELEKLEKevkELEELKEEIEELEkELESLEG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 386 HLTKAVEETKLSKE--NQTRAKESDFSDTLSPSKEKSSDDTTDAQMDE--QDLNEPLAKVSLLKALLEEERKAYRNQ--- 458
Cdd:PRK03918 253 SKRKLEEKIRELEEriEELKKEIEELEEKVKELKELKEKAEEYIKLSEfyEEYLDELREIEKRLSRLEEEINGIEERike 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 459 -------VEESTKQIQVLQAQLQRLHIDTENLREEKDSEitsTRDELLSARDEILLLHQAAAKV--ASERDTDIaslQEE 529
Cdd:PRK03918 333 leekeerLEELKKKLKELEKRLEELEERHELYEEAKAKK---EELERLKKRLTGLTPEKLEKELeeLEKAKEEI---EEE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 530 LKKVRAELERWRKAASEYEKEITSLQnSFQLRCQQC-----EDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLL 604
Cdd:PRK03918 407 ISKITARIGELKKEIKELKKAIEELK-KAKGKCPVCgreltEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 605 SSELQRQEKELhnSQKQSLELTsdlsilqmsrKELENQVGSLK----EQHLRDSADLKTLLSKAENQAKDVQKEYEKtqt 680
Cdd:PRK03918 486 EKVLKKESELI--KLKELAEQL----------KELEEKLKKYNleelEKKAEEYEKLKEKLIKLKGEIKSLKKELEK--- 550
|
410 420 430
....*....|....*....|....*....|....*..
gi 1799135526 681 vLSELKLKFEMTEQEKQSITDELkqcKNNLKLLREKG 717
Cdd:PRK03918 551 -LEELKKKLAELEKKLDELEEEL---AELLKELEELG 583
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
25-108 |
3.88e-05 |
|
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar proteins; ZEP, also called protein ABA DEFICIENT 1, ABA1, protein IMPAIRED IN BABA-INDUCED STERILITY 3, protein LOW EXPRESSION OF OSMOTIC STRESS-RESPONSIVE GENES 6, or protein NON-PHOTOCHEMICAL QUENCHING 2, plays an important role in the xanthophyll cycle and abscisic acid (ABA) biosynthesis. It converts zeaxanthin into antheraxanthin and subsequently violaxanthin. ZEP is required for resistance to osmotic and drought stresses, ABA-dependent stomatal closure, seed development and dormancy, modulation of defense gene expression, and disease resistance and non-photochemical quencing (NPQ). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438754 [Multi-domain] Cd Length: 123 Bit Score: 43.57 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 25 DEPIKIGRsvarcRPAQNNAT----FDCKVLSRNHALVWFdhKTGKFYLQDTKSSNGTFINSQRLSR-GSEESPPCEILS 99
Cdd:cd22702 31 KQPCIIGS-----DPHQAISGisvvIPSPQVSELHARITC--KNGAFFLTDLGSEHGTWINDNEGRRyRAPPNFPVRLHP 103
|
....*....
gi 1799135526 100 GDIIQFGVD 108
Cdd:cd22702 104 SDVIEFGSD 112
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
18-86 |
4.68e-05 |
|
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the first FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438746 [Multi-domain] Cd Length: 93 Bit Score: 42.70 E-value: 4.68e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135526 18 QERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhkTGKFYLQDTKSSNGTFINSQRLS 86
Cdd:cd22694 8 GELRFDPGSSVRIGRD------PDADVRLDDPRVSRRHALLEFD--GDGWVYTDLGSRNGTYLNGRRVQ 68
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
13-110 |
6.25e-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: 6.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 13 NSHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTgkFYLQDTKSSNGTFINSQRLSrgsee 91
Cdd:cd22665 7 SQAHGPEKDFPLYEgENVIGRD------PSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRL----- 73
|
90 100
....*....|....*....|.
gi 1799135526 92 SPPC--EILSGDIIQFGvDVT 110
Cdd:cd22665 74 KPNVryELIDGDLLLFG-DVK 93
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
260-695 |
6.27e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.61 E-value: 6.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 260 RVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEK 339
Cdd:COG5022 954 PELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASK 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 340 ------------KELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGhltkaveetklsKENQTRAKES 407
Cdd:COG5022 1034 iissestelsilKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTEN------------LLKTINVKDL 1101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 408 DFSDTLSpSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEK 487
Cdd:COG5022 1102 EVTNRNL-VKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEK 1180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 488 DSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAElERWRKAASEYEKEITSLQNSFQLRCQQCED 567
Cdd:COG5022 1181 RLYQSALYDEKSKLSSSEVNDLKNELIALFSKIFSGWPRGDKLKKLISE-GWVPTEYSTSLKGFNNLNKKFDTPASMSNE 1259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 568 QQREEATRLQGELEKLRKEWNALETECHSLKRE-NVLLSSELQRQEKELhnSQKQSLELTSDLSILQMSRKELENQVGSL 646
Cdd:COG5022 1260 KLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYiNVGLFNALRTKASSL--RWKSATEVNYNSEELDDWCREFEISDVDE 1337
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1799135526 647 KEQHLRDSADLKTLLSKAENQAKDV-QKEYEKTQTVLSELKLKFEMTEQE 695
Cdd:COG5022 1338 ELEELIQAVKVLQLLKDDLNKLDELlDACYSLNPAEIQNLKSRYDPADKE 1387
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
443-593 |
7.83e-05 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 46.21 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 443 LLKALLEEERK--AYRNQVEESTKQIQVLQAQLQRLHIDTENLREE--KDSEITSTRDELLSARDEILLLHQAAAKvASE 518
Cdd:pfam13166 305 QLPAVSDLASLlsAFELDVEDIESEAEVLNSQLDGLRRALEAKRKDpfKSIELDSVDAKIESINDLVASINELIAK-HNE 383
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799135526 519 RDTDIASLQEELKKvraelERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREeATRLQGELEKLRKEWNALETE 593
Cdd:pfam13166 384 ITDNFEEEKNKAKK-----KLRLHLVEEFKSEIDEYKDKYAGLEKAINSLEKE-IKNLEAEIKKLREEIKELEAQ 452
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
153-381 |
2.07e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 153 VAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQAcSKNQT 232
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA-ELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 233 EDSLRKELIALQEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEdectHLKEMNERTQEELRELANKyngaVN 312
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ----YLKYLAPARREQAEELRAD----LA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135526 313 EIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKL 381
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
243-715 |
2.09e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.04 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 243 LQEDKHNYETTAKeSLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMN--ERTQEELRELANKYNGAVNEIKDLSdk 320
Cdd:TIGR01612 1231 IDEEKKKSEHMIK-AMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNisHDDDKDHHIISKKHDENISDIREKS-- 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 321 LKVAEGKQEEiqQKGQAEKKELQHKIDEMEEKEQELQAKIEALQadNDFTNERLTALQEKLIVEGHLTKAVEETklskeN 400
Cdd:TIGR01612 1308 LKIIEDFSEE--SDINDIKKELQKNLLDAQKHNSDINLYLNEIA--NIYNILKLNKIKKIIDEVKEYTKEIEEN-----N 1378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 401 QTRAKESDFSDTLSPS-KEKSSDDT----TDAQMDEQDLNEPLAKVSLLKA-LLEEERK--AYRNQVEESTKQIQVLQAQ 472
Cdd:TIGR01612 1379 KNIKDELDKSEKLIKKiKDDINLEEckskIESTLDDKDIDECIKKIKELKNhILSEESNidTYFKNADENNENVLLLFKN 1458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 473 LQRLHIDTENLREEKDSEITSTRDELLSARDEilllHQAAAKvaserdtdiaSLQEELKKVRAELERWRKAASEYEKEIT 552
Cdd:TIGR01612 1459 IEMADNKSQHILKIKKDNATNDHDFNINELKE----HIDKSK----------GCKDEADKNAKAIEKNKELFEQYKKDVT 1524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 553 SLQNSF-QLRCQQCEDQQREEATRLQGELEKLRK----EWNALETECHSLKRENVLLSSELQRQEKE----------LHN 617
Cdd:TIGR01612 1525 ELLNKYsALAIKNKFAKTKKDSEIIIKEIKDAHKkfilEAEKSEQKIKEIKKEKFRIEDDAAKNDKSnkaaidiqlsLEN 1604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 618 SQKQSLELTSDLSILQMSRKE---LENQVGSL----KEQHLRDSAD----LKTLLSKAENQAKDVQKEYEKTQTVLSELK 686
Cdd:TIGR01612 1605 FENKFLKISDIKKKINDCLKEtesIEKKISSFsidsQDTELKENGDnlnsLQEFLESLKDQKKNIEDKKKELDELDSEIE 1684
|
490 500 510
....*....|....*....|....*....|....*..
gi 1799135526 687 -LKFEMTEQEK-------QSITDELKQCKNNLKLLRE 715
Cdd:TIGR01612 1685 kIEIDVDQHKKnyeigiiEKIKEIAIANKEEIESIKE 1721
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
52-107 |
2.19e-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: 2.19e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799135526 52 SRNHALVWFDHKTG---------KFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQFGV 107
Cdd:cd22667 40 SRKHATLTVLHPEAnlsdpdtrpELTLKDL-SKYGTFVNGEKLKGGSE----VTLKDGDVITFGV 99
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
338-601 |
2.19e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.03 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 338 EKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLI-VEGHLTKAV-EETKLSKENQTRAKE-SDFSDTLS 414
Cdd:pfam15905 60 ELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEkVEAKLNAAVrEKTSLSASVASLEKQlLELTRVNE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 415 PSKEKSSDDTTDAQMdeqdlNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLRE---EKDSEI 491
Cdd:pfam15905 140 LLKAKFSEDGTQKKM-----SSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEklvSTEKEK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 492 TSTRDELLSARDEILLLHQAAAKVASERdTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQRE 571
Cdd:pfam15905 215 IEEKSETEKLLEYITELSCVSEQVEKYK-LDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEE 293
|
250 260 270
....*....|....*....|....*....|
gi 1799135526 572 EATRLQGELEKLRKEWNALETECHSLKREN 601
Cdd:pfam15905 294 LLREYEEKEQTLNAELEELKEKLTLEEQEH 323
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
251-705 |
2.22e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 251 ETTAKESLRRVLQ-EKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELR-ELANKYNGA--VNEIKDLSDKLKVAE- 325
Cdd:PTZ00121 1114 ARKAEEAKKKAEDaRKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKaEEARKAEDAkkAEAARKAEEVRKAEEl 1193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 326 GKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKI------------EALQADNDFTNERLTALQEKLIVEGHLTKAVE- 392
Cdd:PTZ00121 1194 RKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAvkkaeeakkdaeEAKKAEEERNNEEIRKFEEARMAHFARRQAAIk 1273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 393 -ETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQdlneplAKVSLLKALLEEERK---AYRNQVEESTKQIQV 468
Cdd:PTZ00121 1274 aEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA------KKADEAKKKAEEAKKkadAAKKKAEEAKKAAEA 1347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 469 LQAQLQRLHIDTENLREE------KDSEITSTRDELLSARDEILLLHQAAAKvaSERDTDIAslqEELKKVRAElerwRK 542
Cdd:PTZ00121 1348 AKAEAEAAADEAEAAEEKaeaaekKKEEAKKKADAAKKKAEEKKKADEAKKK--AEEDKKKA---DELKKAAAA----KK 1418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 543 AASEYEKEITSLQNSFQLRCQQCEDQQREEATRlqgELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQS 622
Cdd:PTZ00121 1419 KADEAKKKAEEKKKADEAKKKAEEAKKADEAKK---KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEA 1495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 623 LELTSDLSILQMSRKELENqvgSLKEQHLRDSADLKtllsKAEN--QAKDVQKEYEKTQTvlSELKLKFEMTEQEKQSIT 700
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADE---AKKAEEAKKADEAK----KAEEakKADEAKKAEEKKKA--DELKKAEELKKAEEKKKA 1566
|
....*
gi 1799135526 701 DELKQ 705
Cdd:PTZ00121 1567 EEAKK 1571
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
181-716 |
2.76e-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: 44.33 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 181 MLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQT--EDSLR---KELIALQEDKHNY---ET 252
Cdd:pfam05483 262 LLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKalEEDLQiatKTICQLTEEKEAQmeeLN 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 253 TAKESLRRVLQEKIEVVRKLSEVERS----LSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLsdKLKVAEgkq 328
Cdd:pfam05483 342 KAKAAHSFVVTEFEATTCSLEELLRTeqqrLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEEL--KKILAE--- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 329 eeiQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKlivEGHLTKAVEE--TKLSKENQTRAKE 406
Cdd:pfam05483 417 ---DEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTS---EEHYLKEVEDlkTELEKEKLKNIEL 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 407 SDFSDTLSPSKEKSSDDTTDAQMdeqdlneplakvsllkalleeERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREE 486
Cdd:pfam05483 491 TAHCDKLLLENKELTQEASDMTL---------------------ELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 487 kdseITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLqnsfqlrcqqce 566
Cdd:pfam05483 550 ----LESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEEL------------ 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 567 dQQREEATRLQGELEKlrKEWNALETECHSLKREnvlLSSELQRQEKELHNSQKQ----SLELTSDLSILQMSRKELENQ 642
Cdd:pfam05483 614 -HQENKALKKKGSAEN--KQLNAYEIKVNKLELE---LASAKQKFEEIIDNYQKEiedkKISEEKLLEEVEKAKAIADEA 687
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799135526 643 VGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 716
Cdd:pfam05483 688 VKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQ 761
|
|
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
53-106 |
2.97e-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: 2.97e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1799135526 53 RNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPceilsGDIIQFG 106
Cdd:cd22700 36 EQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAP-----GDVLRFG 84
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
1-106 |
3.36e-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: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 1 MPSALAIFTCRPNSHPFQERHVYLDEPIKIGRSvARC-----RPAQnnatfdckVLSRNHALVWFDHktGKFYLQDTkSS 75
Cdd:COG3456 1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRS-ADCdwvlpDPDR--------SVSRRHAEIRFRD--GAFCLTDL-ST 68
|
90 100 110
....*....|....*....|....*....|...
gi 1799135526 76 NGTFIN--SQRLSRGSEEsppcEILSGDIIQFG 106
Cdd:COG3456 69 NGTFLNgsDHPLGPGRPV----RLRDGDRLRIG 97
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
426-614 |
3.75e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 426 DAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEI--------TSTRDE 497
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLralyrlgrQPPLAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 498 LLSARD-----EILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFqlrcQQCEDQQREE 572
Cdd:COG4942 125 LLSPEDfldavRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL----EALKAERQKL 200
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1799135526 573 ATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKE 614
Cdd:COG4942 201 LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
245-629 |
3.83e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 245 EDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEmnertqeELRELANKYNGAVNEIKDLSDKLKVA 324
Cdd:TIGR00618 534 EQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDN-------RSKEDIPNLQNITVRLQDLTEKLSEA 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 325 EGKQEEIQQkgqAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKENQTRA 404
Cdd:TIGR00618 607 EDMLACEQH---ALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQ 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 405 KESDFSDTLSPSKEkssddttdaqmdeqDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLR 484
Cdd:TIGR00618 684 KMQSEKEQLTYWKE--------------MLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELM 749
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 485 EEkdseitstRDELLSARDEILLLHQAAAKVASERDTdiaslqeELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQ 564
Cdd:TIGR00618 750 HQ--------ARTVLKARTEAHFNNNEEVTAALQTGA-------ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPS 814
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799135526 565 CEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEkELHNSQKQSLELTSDL 629
Cdd:TIGR00618 815 DEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA-QLTQEQAKIIQLSDKL 878
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
572-718 |
4.43e-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: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 572 EATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNsQKQSLELTSDLSilqmsrkELENQVGSLKeqhl 651
Cdd:pfam15294 134 EIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGA-KKDVKSNLKEIS-------DLEEKMAALK---- 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135526 652 rdsADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGN 718
Cdd:pfam15294 202 ---SDLEKTLNASTALQKSLEEDLASTKHELLKVQEQLEMAEKELEKKFQQTAAYRNMKEMLTKKNE 265
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
517-716 |
5.23e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 517 SERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQ--LRCQQCEDQQRE-EATRLQGELEKLRKEWNALETE 593
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREkaERYQALLKEKREyEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 594 CHSLKRENVLLSSELQRQEKELHNS----------------------QKQSLELTSDLSILQMSRKELENQVGSLKEQHL 651
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIeqlleelnkkikdlgeeeqlrvKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135526 652 RDSADLKTLLSKAENQAKDV---QKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 716
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIeeeRKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
427-716 |
5.75e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 427 AQMDE------QDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHidTENLREEKD--SEITSTRDEL 498
Cdd:PHA02562 166 SEMDKlnkdkiRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKY--DELVEEAKTikAEIEELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 499 LSARDEIlllhqaaakvaSERDTDIASLQEELKKVRAELERWRKAASEYEKEITslqnsfqlrCQQCEDQQREEATRLQG 578
Cdd:PHA02562 244 LNLVMDI-----------EDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGV---------CPTCTQQISEGPDRITK 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 579 ELEKLrkewnaletechslkrenvllsSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQhlrdsadlk 658
Cdd:PHA02562 304 IKDKL----------------------KELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQS--------- 352
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799135526 659 tlLSKAENQAKDVQKEYEKTQTvlselklkfemteqEKQSITDELKQCKNNLKLLREK 716
Cdd:PHA02562 353 --LITLVDKAKKVKAAIEELQA--------------EFVDNAEELAKLQDELDKIVKT 394
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
49-112 |
5.94e-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: 5.94e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799135526 49 KVLSRNHALVWFDHKTG--KFYLQDTKSSNGTFINsqrlsrgSEESPPC---EILSGDIIQFGVDVTEN 112
Cdd:cd22681 64 ETCSKQHCVIQFRNVKGilKPYIMDLDSSNGTCLN-------DNVIPSSryvELRSGDVITFSKSNDYE 125
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
213-506 |
6.22e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.50 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 213 LLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTAKEslrrvlqeKIEVVRKLSEVERSlsntedecthlKEM 292
Cdd:TIGR01612 1455 LFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSKGC--------KDEADKNAKAIEKN-----------KEL 1515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 293 NERTQEELRELANKY----------------NGAVNEIKDLSDKLKVAEGKQEeiqQKGQAEKKElqhkidemeekeqel 356
Cdd:TIGR01612 1516 FEQYKKDVTELLNKYsalaiknkfaktkkdsEIIIKEIKDAHKKFILEAEKSE---QKIKEIKKE--------------- 1577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 357 QAKIEALQADNDFTNerltalqeKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQmdEQDLNE 436
Cdd:TIGR01612 1578 KFRIEDDAAKNDKSN--------KAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQ--DTELKE 1647
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135526 437 PLAKVSLLKALLEEERKAYRNqVEESTKQIQVLQAQLQRLHIDTENLRE-------EKDSEITSTRDELLSARDEIL 506
Cdd:TIGR01612 1648 NGDNLNSLQEFLESLKDQKKN-IEDKKKELDELDSEIEKIEIDVDQHKKnyeigiiEKIKEIAIANKEEIESIKELI 1723
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
16-111 |
6.35e-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: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 16 PFQERHVYLD-EPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFdhKTGKFYLQDTKSSNGTFINSQRLSRgseespP 94
Cdd:cd22693 7 TLQGQTFPIDkSGITIGRA------DDNDLVLSDDFVSSRHARIYL--QGSSWYLEDLGSTNGTFVNGNRVTQ------P 72
|
90
....*....|....*..
gi 1799135526 95 CEILSGDIIQFGVDVTE 111
Cdd:cd22693 73 VVVQPGDTIRIGATVFE 89
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
419-685 |
8.13e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 419 KSSDDTTDAQMDEQDLNEPLAKVSLLKALlEEERKAYRNQVEESTKQIQVLQAQLQRLhidtenlreeKDSEITSTRDEL 498
Cdd:PRK11281 50 KQKLLEAEDKLVQQDLEQTLALLDKIDRQ-KEETEQLKQQLAQAPAKLRQAQAELEAL----------KDDNDEETRETL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 499 lsardeilllhqaaakvaseRDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQN----------SFQLRCQQCEDQ 568
Cdd:PRK11281 119 --------------------STLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTqperaqaalyANSQRLQQIRNL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 569 ----QREEATRLQGELEKLRKEWNALEtechslkrenvlLSSELQRQEKElHNSQKQSL-ELTSDLSILQMSRKELENQv 643
Cdd:PRK11281 179 lkggKVGGKALRPSQRVLLQAEQALLN------------AQNDLQRKSLE-GNTQLQDLlQKQRDYLTARIQRLEHQLQ- 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1799135526 644 gslkeqhlrdsaDLKTL-----LSKAENQAKDVQKEYEKTQTVLSEL 685
Cdd:PRK11281 245 ------------LLQEAinskrLTLSEKTVQEAQSQDEAARIQANPL 279
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
163-362 |
9.35e-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: 42.06 E-value: 9.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALID--------EDRLLSRLEVMGNQLQACSKNQTED 234
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekeiaelRAELEAQKEELAELLRALYRLGRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 235 SLrkELIALQEDKHNYETTAK--ESLRRVLQEKIEVVRK-LSEVERSLSNTEDECTHLKEMNERTQEELRELANkyngAV 311
Cdd:COG4942 121 PL--ALLLSPEDFLDAVRRLQylKYLAPARREQAEELRAdLAELAALRAELEAERAELEALLAELEEERAALEA----LK 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1799135526 312 NEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEA 362
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
415-638 |
1.06e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 415 PSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREE-------- 486
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgeraral 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 487 -KDSEITSTRDELLSARDEILLLHQAAA-KVASERDTDIAslqEELKKVRAELERWRKAASEYEKEITSLQnsfqlrcqq 564
Cdd:COG3883 96 yRSGGSVSYLDVLLGSESFSDFLDRLSAlSKIADADADLL---EELKADKAELEAKKAELEAKLAELEALK--------- 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799135526 565 ceDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKE 638
Cdd:COG3883 164 --AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
274-381 |
1.17e-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: 42.15 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 274 EVERSLSNTEDECTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEK----------K 340
Cdd:pfam06160 288 YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEvayselqeelE 367
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1799135526 341 ELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKL 381
Cdd:pfam06160 368 EILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLEL 408
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
263-591 |
1.40e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 263 QEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKgqaeKKEL 342
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEK----VKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 343 QHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEkliveghLTKAVEetKLSKENQTRakesdfsdTLSPSKEKssd 422
Cdd:COG1340 77 KEERDELNEKLNELREELDELRKELAELNKAGGSIDK-------LRKEIE--RLEWRQQTE--------VLSPEEEK--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 423 dttdaqmdeqdlnEPLAKVSLLKALLEEERKAyrnqvEESTKQIQVLQAQLQRLHIDTENLREekdsEITSTRDELLSAR 502
Cdd:COG1340 137 -------------ELVEKIKELEKELEKAKKA-----LEKNEKLKELRAELKELRKEAEEIHK----KIKELAEEAQELH 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 503 DEILLLHQAAAKVASERDT---DIASLQEELKKVRAELERWRKAASEYEKEITSLqnsfqlrcqqcedQQREEATRLQGE 579
Cdd:COG1340 195 EEMIELYKEADELRKEADElhkEIVEAQEKADELHEEIIELQKELRELRKELKKL-------------RKKQRALKREKE 261
|
330
....*....|..
gi 1799135526 580 LEKLRKEWNALE 591
Cdd:COG1340 262 KEELEEKAEEIF 273
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
231-716 |
1.47e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.13 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 231 QTEDSLRKELIALQEDKHNYETTAKEslRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEEL-RELANKYNG 309
Cdd:pfam12128 353 QSELENLEERLKALTGKHQDVTAKYN--RRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALeSELREQLEA 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 310 AVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKEL------QHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIV 383
Cdd:pfam12128 431 GKLEFNEEEYRLKSRLGELKLRLNQATATPELLlqlenfDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQ 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 384 EGHLTKAVEETKLSKENQTRAKESDFSDTLSpskekssddtTDAQMDEQDLNEPLAKVSLLKALLEEErkayrnQVEEST 463
Cdd:pfam12128 511 ASRRLEERQSALDELELQLFPQAGTLLHFLR----------KEAPDWEQSIGKVISPELLHRTDLDPE------VWDGSV 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 464 KQIQVLQAQlqRLHIDTENLREEKDSEitstrDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKA 543
Cdd:pfam12128 575 GGELNLYGV--KLDLKRIDVPEWAASE-----EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTA 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 544 aseyekeitsLQNSfQLRCQQCEDQQREEATRLQGELE----KLRKEWNALETECHSLKRENVLLSSELQRQEKEL---H 616
Cdd:pfam12128 648 ----------LKNA-RLDLRRLFDEKQSEKDKKNKALAerkdSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREArteK 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 617 NSQKQSLELTSDLSILQMS------RKELENQVGSLKEQHLRD--------------SADLKTLLSKAENQAKDVQK--E 674
Cdd:pfam12128 717 QAYWQVVEGALDAQLALLKaaiaarRSGAKAELKALETWYKRDlaslgvdpdviaklKREIRTLERKIERIAVRRQEvlR 796
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1799135526 675 YEKTQ--TVLSE---LKLKFEMTEQEKQSITDELKQCKNNLKLLREK 716
Cdd:pfam12128 797 YFDWYqeTWLQRrprLATQLSNIERAISELQQQLARLIADTKLRRAK 843
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
322-698 |
1.66e-03 |
|
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: 41.65 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 322 KVAEGKQEEIQQKGQAEKKELQHK----------------IDEMEEKEQELQAKIEALQADNdftNERLTALQEKlIVEG 385
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKrarielekkasalkrqLDRESDRNQELQKRIRLLEKRE---AEAEEALREQ-AELN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 386 HLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRN---QVEES 462
Cdd:pfam05557 79 RLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEaeqLRQNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 463 TKQIQVLQAQLQRLH-IDTENLREEKDSEITST-RDELLS---------------------ARDEILL---LHQAAAKVA 516
Cdd:pfam05557 159 EKQQSSLAEAEQRIKeLEFEIQSQEQDSEIVKNsKSELARipelekelerlrehnkhlnenIENKLLLkeeVEDLKRKLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 517 SERDT--DIASLQEELKKVRAELERWRKAASEYEKEITS--LQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALET 592
Cdd:pfam05557 239 REEKYreEAATLELEKEKLEQELQSWVKLAQDTGLNLRSpeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 593 ECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDL----SILQMSRKELENQVGSlkEQHLRDSADLKTLLSKAENQA 668
Cdd:pfam05557 319 ELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgyrAILESYDKELTMSNYS--PQLLERIEEAEDMTQKMQAHN 396
|
410 420 430
....*....|....*....|....*....|
gi 1799135526 669 KDVQKEYEKTQTVLSELKLKFEMTEQEKQS 698
Cdd:pfam05557 397 EEMEAQLSVAEEELGGYKQQAQTLERELQA 426
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
27-106 |
1.71e-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: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 27 PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTGkfYLQDTKSSNGTFINSQRLsrgseeSPPCEILSGDIIQFG 106
Cdd:cd22668 19 SNIIGRG------SDADFRLPDTGVSRRHAEIRWDGQVA--HLTDLGSTNGTTVNNAPV------TPEWRLADGDVITLG 84
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
253-539 |
1.74e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 253 TAKESLRRVLQEKIEVVRKLSEvERSLSNTEDECTHLKEMNERTQ--------------EELRELANKYNGavnEIKDLS 318
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKLKkynleelekkaeeyEKLKEKLIKLKG---EIKSLK 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 319 DKLKvaegKQEEIQQKgqaeKKELQHKIDEMEEKEQELQAKIEALQ-ADNDFTNERLTALQEKLIVEGHLTKAVEETKLS 397
Cdd:PRK03918 546 KELE----KLEELKKK----LAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKELERE 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 398 KENQTRAKEsdfsdTLSPSKEKSSDDTTDAQMDEQDLNEplakvsLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLh 477
Cdd:PRK03918 618 EKELKKLEE-----ELDKAFEELAETEKRLEELRKELEE------LEKKYSEEEYEELREEYLELSRELAGLRAELEEL- 685
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799135526 478 idtENLREEKDS---EITSTRDELLSARDEILLLHQAAAKVaserdtdiASLQEELKKVRAELER 539
Cdd:PRK03918 686 ---EKRREEIKKtleKLKEELEEREKAKKELEKLEKALERV--------EELREKVKKYKALLKE 739
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
258-620 |
1.88e-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: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 258 LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRElankyngavnEIKDLSDKLKVAEGKQEEIQQKgqa 337
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELES----------RVAELKEELRQSREKHEELEEK--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 338 eKKELQHKIDEM-EEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKeNQTRAKESDfsdtlsps 416
Cdd:pfam07888 103 -YKELSASSEELsEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAG-AQRKEEEAE-------- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 417 kekSSDDTTDAQMDEQDLNEPLAKVSLLKALLeEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREekdsEITSTRD 496
Cdd:pfam07888 173 ---RKQLQAKLQQTEEELRSLSKEFQELRNSL-AQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE----ELRSLQE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 497 ELLSARDEILLLHQAAAKVASERDTDIASL-QEELKKVRAELE------RWRKAASEYEKEITSLQNSFQLRCQQCEdQQ 569
Cdd:pfam07888 245 RLNASERKVEGLGEELSSMAAQRDRTQAELhQARLQAAQLTLQladaslALREGRARWAQERETLQQSAEADKDRIE-KL 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1799135526 570 REEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQK 620
Cdd:pfam07888 324 SAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLR 374
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
518-719 |
1.93e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 518 ERDT--DIASLQEELKkvraELERWRKAASEYEKEITSLQnsfQLRcqqcedQQREEATRLQGELEKLRKEWNALETECH 595
Cdd:COG4913 220 EPDTfeAADALVEHFD----DLERAHEALEDAREQIELLE---PIR------ELAERYAAARERLAELEYLRAALRLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 596 SLKREnvLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQvgsLKEQHLRDSADLKTLLSKAENQAKDVQKEY 675
Cdd:COG4913 287 QRRLE--LLEAELEELRAELARLEAELERLEARLDALREELDELEAQ---IRGNGGDRLEQLEREIERLERELEERERRR 361
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1799135526 676 EKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNN 719
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
300-428 |
1.95e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 300 LRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQE 379
Cdd:COG3883 124 LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1799135526 380 KLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQ 428
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
253-716 |
1.95e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 41.74 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 253 TAKESLRRVLQEKIEVVRKLSEVERSLSN--------TEDECTHLKEMNERTQEELRE-LANKYNGAVNEIKDLSDKLKV 323
Cdd:PTZ00440 894 SNKQLVEHLLNNKIDLKNKLEQHMKIINTdniiqkneKLNLLNNLNKEKEKIEKQLSDtKINNLKMQIEKTLEYYDKSKE 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 324 A-EGKQEEIQQKGQAEKKELQH---KIDEMEEKEQELQAKIealqadNDFTNER---LTALQEKLIvEGHLTKAVEETKL 396
Cdd:PTZ00440 974 NiNGNDGTHLEKLDKEKDEWEHfksEIDKLNVNYNILNKKI------DDLIKKQhddIIELIDKLI-KEKGKEIEEKVDQ 1046
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 397 SKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDE---------QDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQ 467
Cdd:PTZ00440 1047 YISLLEKMKTKLSSFHFNIDIKKYKNPKIKEEIKLleekveallKKIDENKNKLIEIKNKSHEHVVNADKEKNKQTEHYN 1126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 468 VLQAQLQRLHIDTENLREEKDS----EITSTRDELLSARDEILLLHQAAAKVASERdTDIASLQEELKKVRAELERWRKA 543
Cdd:PTZ00440 1127 KKKKSLEKIYKQMEKTLKELENmnleDITLNEVNEIEIEYERILIDHIVEQINNEA-KKSKTIMEEIESYKKDIDQVKKN 1205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 544 ASEYEKEITSLQNSfqlrcqqceDQQREEATRLQGELEKLRKEWNALETECHSLKRENvllssELQRQEKELHNSQKQSL 623
Cdd:PTZ00440 1206 MSKERNDHLTTFEY---------NAYYDKATASYENIEELTTEAKGLKGEANRSTNVD-----ELKEIKLQVFSYLQQVI 1271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 624 ELTSDLsilQMSRKELENQVGSLKEQHLRD-SADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQ--SIT 700
Cdd:PTZ00440 1272 KENNKM---ENALHEIKNMYEFLISIDSEKiLKEILNSTKKAEEFSNDAKKELEKTDNLIKQVEAKIEQAKEHKNkiYGS 1348
|
490
....*....|....*.
gi 1799135526 701 DELKQCKNNLKLLREK 716
Cdd:PTZ00440 1349 LEDKQIDDEIKKIEQI 1364
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
448-607 |
1.98e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 448 LEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDseitstrdELlsaRDEILllhqaaakvasERDTDIASLQ 527
Cdd:COG2433 390 LPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE--------EL---EAELE-----------EKDERIERLE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 528 EELKKVRAElerwRKAASEYEKEITSLQNsfqlrcqqcedqqreEATRLQGELEKLRKEWNALETECHSLKRENVLLSSE 607
Cdd:COG2433 448 RELSEARSE----ERREIRKDREISRLDR---------------EIERLERELEEERERIEELKRKLERLKELWKLEHSG 508
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
438-674 |
2.14e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 438 LAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVAS 517
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 518 ErdtdIASLQEELKKVRAELER-----WRKAASEYEKEITSLQNSFQL-----RCQQCEDQQREEATRLQGELEKLRKew 587
Cdd:COG4942 91 E----IAELRAELEAQKEELAEllralYRLGRQPPLALLLSPEDFLDAvrrlqYLKYLAPARREQAEELRADLAELAA-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 588 naletechslkrenvlLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQH-------LRDSADLKTL 660
Cdd:COG4942 165 ----------------LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELaaelaelQQEAEELEAL 228
|
250
....*....|....
gi 1799135526 661 LSKAENQAKDVQKE 674
Cdd:COG4942 229 IARLEAEAAAAAER 242
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
253-560 |
2.23e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 253 TAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQ 332
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 333 ---QKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKENQTRAKESDF 409
Cdd:COG4372 115 eelEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 410 SDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDS 489
Cdd:COG4372 195 NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799135526 490 EITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQL 560
Cdd:COG4372 275 EEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQL 345
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
449-680 |
2.49e-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: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 449 EEERKAYRNQVEESTKQIQVLQAQLQRLhidtenlreekDSEITSTRDELLSARDEILLLHQAAAKVASErdtdIASLQE 528
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDAL-----------QAELEELNEEYNELQAELEALQAEIDKLQAE----IAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 529 ELKKVRAELERWRKAASEYEKEITSLQ-----NSFQ------LRCQQCEDQQREE---ATRLQGELEKLRKEWNALETEC 594
Cdd:COG3883 80 EIEERREELGERARALYRSGGSVSYLDvllgsESFSdfldrlSALSKIADADADLleeLKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 595 HSLKRENVLLSSELQRQEKELhnsQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKE 674
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQ---EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
....*.
gi 1799135526 675 YEKTQT 680
Cdd:COG3883 237 AAAAAA 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
343-600 |
2.53e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 343 QHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETK--LSKENQTRAKESDFSDTlspskEKS 420
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERL-----DAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 421 SDDTTDAQMDEQDLNEPLAKvsllkalLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLS 500
Cdd:COG4913 684 SDDLAALEEQLEELEAELEE-------LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 501 ARDEILLLHQAAAKVASERD---TDIASLQEELKKVRAE-LERWRKAASEYEKEITSLqNSFQlrcQQCEDQQREEATRL 576
Cdd:COG4913 757 AALGDAVERELRENLEERIDalrARLNRAEEELERAMRAfNREWPAETADLDADLESL-PEYL---ALLDRLEEDGLPEY 832
|
250 260
....*....|....*....|....*.
gi 1799135526 577 QGELEKLRKEW--NALETECHSLKRE 600
Cdd:COG4913 833 EERFKELLNENsiEFVADLLSKLRRA 858
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
569-716 |
2.63e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 569 QREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKE 648
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 649 QHLRDSADLKTLLSKAE-------------------------------NQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQ 697
Cdd:COG4942 98 ELEAQKEELAELLRALYrlgrqpplalllspedfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAELE 177
|
170
....*....|....*....
gi 1799135526 698 SITDELKQCKNNLKLLREK 716
Cdd:COG4942 178 ALLAELEEERAALEALKAE 196
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
256-716 |
2.65e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.58 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 256 ESLRRVLQEKIEVVRK--LSEVERSLSNTEDECTHLKEMN--ERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEI 331
Cdd:TIGR01612 1058 DEIEKEIGKNIELLNKeiLEEAEINITNFNEIKEKLKHYNfdDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEI 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 332 QQKGQAEKKELQHKIDEME---------EKEQELQAKIEALqadndftnerLTALQEKLIVEGHLTKAVEETKLSKENQT 402
Cdd:TIGR01612 1138 KKKSENYIDEIKAQINDLEdvadkaisnDDPEEIEKKIENI----------VTKIDKKKNIYDEIKKLLNEIAEIEKDKT 1207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 403 RAKEsdfSDTLSPSKEKSSDDTTDAQMDEQDlNEPLAKVSLLKALLE--EERKAYRNQVEESTKQIQVLQAQLQRLHIDT 480
Cdd:TIGR01612 1208 SLEE---VKGINLSYGKNLGKLFLEKIDEEK-KKSEHMIKAMEAYIEdlDEIKEKSPEIENEMGIEMDIKAEMETFNISH 1283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 481 EnlrEEKDSEITSTR-DELLS-ARDEILLLHQaaakvASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSF 558
Cdd:TIGR01612 1284 D---DDKDHHIISKKhDENISdIREKSLKIIE-----DFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNIL 1355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 559 QL-RCQQCEDQQREEATRLQGELEKLRKEWNALET------------ECHSlKRENVL--------------LSSELQRQ 611
Cdd:TIGR01612 1356 KLnKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKlikkikddinleECKS-KIESTLddkdidecikkikeLKNHILSE 1434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 612 EKELHNSQKQSLELTSDLSIL--------QMSRKELENQ-----------VGSLKEqHLRDSADLKTLLSKAENQA---K 669
Cdd:TIGR01612 1435 ESNIDTYFKNADENNENVLLLfkniemadNKSQHILKIKkdnatndhdfnINELKE-HIDKSKGCKDEADKNAKAIeknK 1513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1799135526 670 DVQKEYEKTQTVL------SELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 716
Cdd:TIGR01612 1514 ELFEQYKKDVTELlnkysaLAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEK 1566
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
263-656 |
2.67e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 263 QEKIEVVRKLSEVERS----LSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGkqEEIQQKGQAE 338
Cdd:PLN02939 45 QQKKKRGKNIAPKQRSsnskLQSNTDENGQLENTSLRTVMELPQKSTSSDDDHNRASMQRDEAIAAID--NEQQTNSKDG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 339 KKELQHKIDEMEEKEQELQAKIEALQADNDFTNERL-TALQEKLIVEGHLTkaVEETKLSkENQTRAKESdfsdtlspSK 417
Cdd:PLN02939 123 EQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLeKILTEKEALQGKIN--ILEMRLS-ETDARIKLA--------AQ 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 418 EKSSDDTTDAQMDEqdlneplakvslLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKdSEITSTRDE 497
Cdd:PLN02939 192 EKIHVEILEEQLEK------------LRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAEL-IEVAETEER 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 498 LlsardeilllhqaaAKVASERDTDIASLQE-ELKKVRAELERWRKAASEYE---KEITSLQNSFQlrcqqCEDQQREEA 573
Cdd:PLN02939 259 V--------------FKLEKERSLLDASLRElESKFIVAQEDVSKLSPLQYDcwwEKVENLQDLLD-----RATNQVEKA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 574 TRLQGELEKLRKEWNALETechSLKRENVL-LSSE----LQRQEKELHNS-QKQSLELTSDLSILQMSRKELENQVGSLK 647
Cdd:PLN02939 320 ALVLDQNQDLRDKVDKLEA---SLKEANVSkFSSYkvelLQQKLKLLEERlQASDHEIHSYIQLYQESIKEFQDTLSKLK 396
|
....*....
gi 1799135526 648 EQHLRDSAD 656
Cdd:PLN02939 397 EESKKRSLE 405
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
163-393 |
2.88e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.83 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEasdtsWQALIDEDRLLSR----LEVMGNQLQACSKNQT--EDSL 236
Cdd:COG0497 172 KELEELRADEAERARELDLLRFQLEELEAAALQPGE-----EEELEEERRRLSNaeklREALQEALEALSGGEGgaLDLL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 237 RKELIALQEDKHnYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERtQEELRELANKYNGAVNEIKD 316
Cdd:COG0497 247 GQALRALERLAE-YDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEER-LALLRRLARKYGVTVEELLA 324
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799135526 317 LSDKLkvaegkqeeiqqkgQAEKKELQHKIDEMEEKEQELQAKIEALQAdndfTNERLTALQEKLIVEghLTKAVEE 393
Cdd:COG0497 325 YAEEL--------------RAELAELENSDERLEELEAELAEAEAELLE----AAEKLSAARKKAAKK--LEKAVTA 381
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
172-361 |
2.88e-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: 39.50 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 172 LQEALHREQMLEQKLATLQRLLaitqeasdtswQALIDEDRLLSRLEVmgNQLQACSKNQTEDSLRKELIAlqedKHNYE 251
Cdd:pfam15619 6 LSARLHKIKELQNELAELQSKL-----------EELRKENRLLKRLQK--RQEKALGKYEGTESELPQLIA----RHNEE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 252 T-TAKESLRRvLQEKIEVV-RKLSEVERSLSNTEDECTHL------KEMNERT--QEELRELANKYNGAVNEIKDLSDKL 321
Cdd:pfam15619 69 VrVLRERLRR-LQEKERDLeRKLKEKEAELLRLRDQLKRLeklsedKNLAEREelQKKLEQLEAKLEDKDEKIQDLERKL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1799135526 322 KVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIE 361
Cdd:pfam15619 148 ELENKSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLK 187
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
256-365 |
3.06e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 256 ESLRRVLQEKI-EVVRKLSEVERSLSNTEDEcthLKEMNERTQEELRELANKYNGAVNE--------IKDLSD--KLKVA 324
Cdd:PRK00409 526 EELERELEQKAeEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLEEAEKEAQQAIKEakkeadeiIKELRQlqKGGYA 602
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1799135526 325 EGKQEEIQQKgqaeKKELQHKIDEMEEKEQELQAKIEALQA 365
Cdd:PRK00409 603 SVKAHELIEA----RKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
262-582 |
3.43e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 262 LQEKIEVVRKLSEVERSLSNTEDECTHLKEMNE-RTQEELRELANKYNGavNEIKDLSDKLKVAEGKQEEIQQKGQaEKK 340
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEaKKADEAKKAEEAKKA--DEAKKAEEKKKADELKKAEELKKAE-EKK 1564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 341 ELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKEnQTRAKESDFSDTLSPSKEKS 420
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE-ELKKAEEEKKKVEQLKKKEA 1643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 421 SDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQlqrlhidtenlreeKDSEITSTRDELLS 500
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK--------------KEAEEAKKAEELKK 1709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 501 ARDEILLLHQAAAKVASERDTDIaslqEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGEL 580
Cdd:PTZ00121 1710 KEAEEKKKAEELKKAEEENKIKA----EEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
..
gi 1799135526 581 EK 582
Cdd:PTZ00121 1786 DE 1787
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
327-682 |
3.51e-03 |
|
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: 40.93 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 327 KQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALqadndftNERLTALQEKLIVEGHLTKAVEETKLSKENQtrake 406
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQL-------CEEKNALQEQLQAETELCAEAEEMRARLAAR----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 407 sdfsdtlspskekssddttdaqmdEQDLNEPLAKvslLKALLEEERKAYRNQVEESTK---QIQVLQAQLQrlhiDTENL 483
Cdd:pfam01576 70 ------------------------KQELEEILHE---LESRLEEEEERSQQLQNEKKKmqqHIQDLEEQLD----EEEAA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 484 REEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTdiasLQEELkkvrAELERWRKAASEYEKEITSLQNSFQLRCQ 563
Cdd:pfam01576 119 RQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKL----LEERI----SEFTSNLAEEEEKAKSLSKLKNKHEAMIS 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 564 QCEDQ-QREEATRLqgELEKLRKEWNALETECHS----LKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKE 638
Cdd:pfam01576 191 DLEERlKKEEKGRQ--ELEKAKRKLEGESTDLQEqiaeLQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRE 268
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1799135526 639 LENQVGSLKEqhlrDSADLKTLLSKAENQAKDVQKEYEKTQTVL 682
Cdd:pfam01576 269 LEAQISELQE----DLESERAARNKAEKQRRDLGEELEALKTEL 308
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
208-381 |
4.00e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.59 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 208 IDEDRLLSRLEVMGNQLQACSKNQTE---DSLRKELIALQED-KHNYETTAKEslrrvLQEKIEVVRKLSEVERSLsnte 283
Cdd:PRK04778 249 LDHLDIEKEIQDLKEQIDENLALLEEldlDEAEEKNEEIQERiDQLYDILERE-----VKARKYVEKNSDTLPDFL---- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 284 decTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKG----------QAEKKELQHKIDEME 350
Cdd:PRK04778 320 ---EHAKEQNKELKEEIDRVKQSYtlnESELESVRQLEKQLESLEKQYDEITERIaeqeiayselQEELEEILKQLEEIE 396
|
170 180 190
....*....|....*....|....*....|.
gi 1799135526 351 EKEQELQAKIEALQADNDFTNERLTALQEKL 381
Cdd:PRK04778 397 KEQEKLSEMLQGLRKDELEAREKLERYRNKL 427
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
479-718 |
4.68e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 479 DTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVaSERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNsf 558
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKL-EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE-- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 559 QLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSD---LSILQMS 635
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKeerLEELKKK 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 636 RKELENQVGSLKEQHlRDSADLKTLLSKAENQAKdvqkeyEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLRE 715
Cdd:PRK03918 347 LKELEKRLEELEERH-ELYEEAKAKKEELERLKK------RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
...
gi 1799135526 716 KGN 718
Cdd:PRK03918 420 EIK 422
|
|
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
448-537 |
5.20e-03 |
|
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.
Pssm-ID: 462015 [Multi-domain] Cd Length: 198 Bit Score: 38.83 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 448 LEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLRE---EKDSEITSTRDEL--LSARDEILLLHQAAAKVASERDTD 522
Cdd:pfam06818 50 KEEQIQELEDSLRSKTLELEVCENELQRKKNEAELLREkvgKLEEEVSGLREALsdVSPSGYESVYESDEAKEQRQEEAD 129
|
90
....*....|....*
gi 1799135526 523 IASLQEELKKVRAEL 537
Cdd:pfam06818 130 LGSLRREVERLRAEL 144
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
163-413 |
5.57e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWqALIDEDRLLSRLEVMGNQLQACSKNQTE-DSLRKELI 241
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-DEIDVASAEREIAELEAELERLDASSDDlAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 242 ALQEDkhnyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLK----EMNERTQEELRELANKYNGAVNEIkdl 317
Cdd:COG4913 696 ELEAE-----------LEELEEELDELKGEIGRLEKELEQAEEELDELQdrleAAEDLARLELRALLEERFAAALGD--- 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 318 sdklKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKL--IVEGHLTKAVEETK 395
Cdd:COG4913 762 ----AVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLdrLEEDGLPEYEERFK 837
|
250
....*....|....*...
gi 1799135526 396 LSKENQTRAKESDFSDTL 413
Cdd:COG4913 838 ELLNENSIEFVADLLSKL 855
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
52-106 |
5.67e-03 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein kinase DUN1 and similar proteins; DUN1 is a protein kinase that controls the DNA damage response in yeast. It phosphorylates SML1 on serine residues and cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438735 [Multi-domain] Cd Length: 96 Bit Score: 36.70 E-value: 5.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799135526 52 SRNHALVWFDHKTGKFYLQ-----------DTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFG 106
Cdd:cd22683 28 SRSCDLVLSDPSISRFHAElrleqnginviDNNSANGTFINGKRIKGKT-----YILKNGDIIVFG 88
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
372-714 |
5.90e-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: 39.88 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 372 ERLTALQEKLIVEGHLTKAVEETKLSK---ENQTRAKESDFSDtLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALL 448
Cdd:pfam07888 42 ERAELLQAQEAANRQREKEKERYKRDReqwERQRRELESRVAE-LKEELRQSREKHEELEEKYKELSASSEELSEEKDAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 449 EEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAaakvaserdtdiaslQE 528
Cdd:pfam07888 121 LAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQT---------------EE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 529 ELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATR--LQGELEKLRKEWNALETECHSLKRENVLLSS 606
Cdd:pfam07888 186 ELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENeaLLEELRSLQERLNASERKVEGLGEELSSMAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 607 ELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQvGSLKEQHLRDSADLKTllSKAENQAKDVQKEYEKTQTVLSE-L 685
Cdd:pfam07888 266 QRDRTQAELHQARLQAAQLTLQLADASLALREGRAR-WAQERETLQQSAEADK--DRIEKLSAELQRLEERLQEERMErE 342
|
330 340
....*....|....*....|....*....
gi 1799135526 686 KLKFEMTeQEKQSITDELKQCKNNLKLLR 714
Cdd:pfam07888 343 KLEVELG-REKDCNRVQLSESRRELQELK 370
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
234-381 |
5.91e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 234 DSLRKELIALQEDKhnyeTTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKE--MNERTQEELRELANKYNGAV 311
Cdd:COG1579 27 KELPAELAELEDEL----AALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNNKEYEALQKEIESLK 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 312 NEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKL 381
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
173-366 |
7.88e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.75 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 173 QEALHREQMLEQKLATLQRLLAitqeasdtswqalidedRLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYET 252
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLK-----------------ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 253 TAKESLRRVLQEKIEVVRKlsevERSLSNTEDECTHLKEMNERTQEELRELankyngaVNEIKDLSDKLKVAEGKQEEIQ 332
Cdd:COG1579 69 EEVEARIKKYEEQLGNVRN----NKEYEALQKEIESLKRRISDLEDEILEL-------MERIEELEEELAELEAELAELE 137
|
170 180 190
....*....|....*....|....*....|....
gi 1799135526 333 QKGQAEKKELQHKIDEMEEKEQELQAKIEALQAD 366
Cdd:COG1579 138 AELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
172-380 |
7.91e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 38.86 E-value: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 172 LQEALHREQMLEQKLATLQRLLAITQEASDTSwqalidEDRLLSRLEvmgNQLQACSKNQTEDSLRKELialqEDKHNYE 251
Cdd:pfam00261 24 LEEAEKRAEKAEAEVAALNRRIQLLEEELERT------EERLAEALE---KLEEAEKAADESERGRKVL----ENRALKD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799135526 252 TTAKESLRRVLQEKIEVV----RKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDlsdkLKVAEGK 327
Cdd:pfam00261 91 EEKMEILEAQLKEAKEIAeeadRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKS----LEASEEK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1799135526 328 QEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEK 380
Cdd:pfam00261 167 ASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEK 219
|
|
| VI_FHA |
TIGR03354 |
type VI secretion system FHA domain protein; Members of this protein family are FHA ... |
49-106 |
8.45e-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: 8.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799135526 49 KVLSRNHALV-WFDhktGKFYLQDTkSSNGTFINS--QRLSRGSEesppcEILS-GDIIQFG 106
Cdd:TIGR03354 43 RHVSGRHARIrYRD---GAYLLTDL-STNGVFLNGsgSPLGRGNP-----VRLEqGDRLRLG 95
|
|
| |
