|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
3-130 |
6.96e-81 |
|
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and similar proteins; SLMAP, also called sarcolemmal-associated protein (SLAP), is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. It is a cardiac membrane protein that plays an important role in E-C coupling and the adrenergic response of the heart. Overexpression of the SLMAP gene has been associated with diabetes and endothelial dysfunction of macro- and micro-blood vessels. SLMAP contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438731 [Multi-domain] Cd Length: 126 Bit Score: 255.27 E-value: 6.96e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 3 SALAVFSCRPNSHPFQERHVYLDEPVKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINS 82
Cdd:cd22679 1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 528494938 83 QRLSRGSEESPPCEVLSGDIIQFGVDVTENTRKVTHGCIVSTIKLFLP 130
Cdd:cd22679 79 QRLSKGSEESEPRELHSGDIVQFGVDVVENSRKVTHGCIVATVTLFLP 126
|
|
| CC1_SLMAP |
cd21911 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal ... |
163-225 |
7.64e-27 |
|
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: 103.92 E-value: 7.64e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528494938 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLASTQEASESSWQALIDEDRLLSRLEVMGNQLQ 225
Cdd:cd21911 1 QELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQLS 63
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
163-793 |
1.30e-20 |
|
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: 97.82 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLASTQEASESSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGirKELVA 242
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL--EELEA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 243 LTEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKY-NGAVNEIKDLTEKI 321
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEEL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 322 KLAEDKHEELTQKGLNEKKELQMRIEEMEEKEQALQARIEALQAdndftneRLTALQVRLEQLQEKSIKENNSFAVRQLK 401
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA-------RLDSLERLQENLEGFSEGVKALLKNQSGL 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 402 EAVDSSINKLSNFDE----VIDAHLQNN-QTTVDNSLPSPDR----LKENQIdAKECDMSDTLSPSKEKSSDDTSDGQME 472
Cdd:TIGR02168 519 SGILGVLSELISVDEgyeaAIEAALGGRlQAVVVENLNAAKKaiafLKQNEL-GRVTFLPLDSIKGTEIQGNDREILKNI 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 473 EQELNEPQNRVSLLKEMDRSLEA--GDTeqvipHIHRELQEAQELAN----------------------TGKQKCLELQA 528
Cdd:TIGR02168 598 EGFLGVAKDLVKFDPKLRKALSYllGGV-----LVVDDLDNALELAKklrpgyrivtldgdlvrpggviTGGSAKTNSSI 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 529 M-LEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQREN---TITTTREELYSAQEEILVLRHAMEAATAERER- 603
Cdd:TIGR02168 673 LeRRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQlrkELEELSRQISALRKDLARLEAEVEQLEERIAQl 752
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 604 --EITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASF-QLQSQHQ---ERASQLQGEVEKLQADCSGLQNECDSLRAE 677
Cdd:TIGR02168 753 skELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIeQLKEELKalrEALDELRAELTLLNEEAANLRERLESLERR 832
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 678 KSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLgsiqDQHQQDASKLKIQLAQAESRTRDLQKEYDDTQS 757
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL----EALLNERASLEEALALLRSELEELSEELRELES 908
|
650 660 670
....*....|....*....|....*....|....*.
gi 528494938 758 LLSDLRQRYEQTEQEKRSINDELEQCKVNLKLLQDK 793
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| FHA_DMA-like |
cd22692 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest ... |
27-108 |
1.14e-17 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest protein 1 (DMA1), 2 (DMA2) and similar proteins; DMA1 (also known as checkpoint forkhead associated with RING domains-containing protein 1, or CHF1) and DMA2 (also known as checkpoint forkhead associated with RING domains-containing protein 2, or CHF2) are E3 ubiquitin-protein ligases which function in cell cycle retarding in conjunction with the UBC4 and UBC13/MMS2 complex, two E2 ubiquitin conjugating enzymes. They are involved in nutritional control of the cell cycle and required for proper spindle positioning, likely regulating septin ring deposition at the bud neck. DMA1 targets the degradation of G1 cyclin PCL1. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438744 [Multi-domain] Cd Length: 139 Bit Score: 80.30 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 27 PVKIGRSVARCRPAQNNAT-FDCKVLSRNHALVWfdHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCEVLSGDIIQF 105
Cdd:cd22692 38 QIHIGRYTERVRQAIYHPVvFKSKVVSRTHGCIK--VDEGNWYIKDVKSSSGTFLNHQRLSPASRTSKPYPLRDGDILQL 115
|
...
gi 528494938 106 GVD 108
Cdd:cd22692 116 GMD 118
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
172-793 |
1.34e-16 |
|
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: 84.72 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 172 LQEALHREQMLEQKLATLQRLLASTQEASESSWQALIDEDRllsrlevmgnqlqaySKNQTEDGIRKELVALTEDKHNYE 251
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS---------------ELEEEIEELQKELYALANEISRLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 252 ttakeslrrvlQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEEL 331
Cdd:TIGR02168 302 -----------QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 332 TQKglneKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEkSIKENNSFAVRQLKEAVDSSINKL 411
Cdd:TIGR02168 371 ESR----LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ-EIEELLKKLEEAELKELQAELEEL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 412 SNFDEVIDAHLQNNQTTVdnslpspdRLKENQIDAKECDMSDTLSPSKEKSSDDTSDGQMEEQELNEPQNRVSLLKEmdR 491
Cdd:TIGR02168 446 EEELEELQEELERLEEAL--------EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN--Q 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 492 SLEAGDTEQVIPHIH----------------------------RELQEAQELANTGKQKCLEL----------------- 526
Cdd:TIGR02168 516 SGLSGILGVLSELISvdegyeaaieaalggrlqavvvenlnaaKKAIAFLKQNELGRVTFLPLdsikgteiqgndreilk 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 527 ------------------------------------QAMLEEERKTNRQQT-------------------EESAKQIRFL 551
Cdd:TIGR02168 596 niegflgvakdlvkfdpklrkalsyllggvlvvddlDNALELAKKLRPGYRivtldgdlvrpggvitggsAKTNSSILER 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 552 QTQLAKLQTDMEALrEQRENTITTTREELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEV 631
Cdd:TIGR02168 676 RREIEELEEKIEEL-EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 632 EISNLQASFQLQSQH----QERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLN 707
Cdd:TIGR02168 755 ELTELEAEIEELEERleeaEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 708 ALEKSQGDLENKLGSIQDQHQQDA---SKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCK 784
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
....*....
gi 528494938 785 VNLKLLQDK 793
Cdd:TIGR02168 915 RELEELREK 923
|
|
| FHA_VPS64-like |
cd22695 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ... |
6-126 |
1.07e-14 |
|
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: 71.56 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 6 AVFSCRPNSHPFQERHV---YLDEPVKIGRSVARCRPAQN---------------NATFDCKVLSRNHALVWFDHKTGKF 67
Cdd:cd22695 2 HILVLKSLNATFETKFLvvpFKPDGLKLGRPVTNSVNKNNsgskrdlfsqqvrpdNGNFDSRVLSRNHACLSCDPTTGKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 528494938 68 YLQDTKSSNGTFINSQRLSRGSeesppCEVLSGDIIQFGVDVTEntrKVTHGCIVSTIK 126
Cdd:cd22695 82 YIRDLKSSNGTFVNGQKIRQND-----VELKVGDEVDLGTDIDS---KIEHRKISAYVE 132
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
485-792 |
1.07e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 78.56 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 485 LLKEMDRSLEagdteqvipHIHRELQEAQ---ELANTGKQKCLELQAMLEEERKTNRQQTEESAKQirfLQTQLAKLQTD 561
Cdd:TIGR02168 194 ILNELERQLK---------SLERQAEKAErykELKAELRELELALLVLRLEELREELEELQEELKE---AEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 562 MEALREQrentITTTREELYSAQEEILVLRHAMEAATAErereITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQ 641
Cdd:TIGR02168 262 LQELEEK----LEELRLEVSELEEEIEELQKELYALANE----ISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 642 LQsqhQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLG 721
Cdd:TIGR02168 334 EL---AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 722 SIQDQHQQ---------------DASKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVN 786
Cdd:TIGR02168 411 RLEDRRERlqqeieellkkleeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
....*.
gi 528494938 787 LKLLQD 792
Cdd:TIGR02168 491 LDSLER 496
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
13-106 |
1.47e-13 |
|
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.
Pssm-ID: 438714 [Multi-domain] Cd Length: 92 Bit Score: 66.92 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 13 NSHPFQERHVYLDEPVKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINSQRLsrgseeS 92
Cdd:cd00060 6 DGDGGGREFPLTKGVVTIGRS------PDCDIVLDDPSVSRRHARIEVDG--GGVYLEDLGSTNGTFVNGKRI------T 71
|
90
....*....|....
gi 528494938 93 PPCEVLSGDIIQFG 106
Cdd:cd00060 72 PPVPLQDGDVIRLG 85
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
28-105 |
2.74e-13 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 65.29 E-value: 2.74e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528494938 28 VKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRLSRgseesPPCEVLSGDIIQF 105
Cdd:pfam00498 1 VTIGRS------PDCDIVLDDPSVSRRHAEIRYD-GGGRFYLEDLGSTNGTFVNGQRLGP-----EPVRLKDGDVIRL 66
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
174-783 |
3.55e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 73.56 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 174 EALHREQMLEQKLATLQRLLASTQEASESSwQALIDEDRL-LSRLEVMGNQLQAYSKNQTED---GIRKELVALT----- 244
Cdd:TIGR02169 227 ELLKEKEALERQKEAIERQLASLEEELEKL-TEEISELEKrLEEIEQLLEELNKKIKDLGEEeqlRVKEKIGELEaeias 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 245 ------------EDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVN 312
Cdd:TIGR02169 306 lersiaekerelEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 313 EIKDLTEKIKLAEDKHEEL---TQKGLNEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEKSI 389
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELkreLDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 390 KENNS-FAVRQLKEAVDSSINKLSNFDEVIDAHLQNNQTTVDNSLPSPDRLK---------------------------- 440
Cdd:TIGR02169 466 KYEQElYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKasiqgvhgtvaqlgsvgeryataievaa 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 441 ---------ENQIDAKEC---------------------DMSDTLSPSKEKSSDD------------------------- 465
Cdd:TIGR02169 546 gnrlnnvvvEDDAVAKEAiellkrrkagratflplnkmrDERRDLSILSEDGVIGfavdlvefdpkyepafkyvfgdtlv 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 466 -----------------TSDGQMEEQ--------------ELNEPQNRVSL------LKEMDRSLEAGDTEQviPHIHRE 508
Cdd:TIGR02169 626 vedieaarrlmgkyrmvTLEGELFEKsgamtggsraprggILFSRSEPAELqrlrerLEGLKRELSSLQSEL--RRIENR 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 509 LQEAQELANTGKQKCLELQA---MLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALR---EQRENTITTTREELYS 582
Cdd:TIGR02169 704 LDELSQELSDASRKIGEIEKeieQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEariEELEEDLHKLEEALND 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 583 -----AQEEILVLRHAMEAATAERER------EITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQ-----LQSQH 646
Cdd:TIGR02169 784 learlSHSRIPEIQAELSKLEEEVSRiearlrEIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEkeienLNGKK 863
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 647 QERASQL---QGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSI 723
Cdd:TIGR02169 864 EELEEELeelEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528494938 724 QDQHQQDAS--KLKIQLAQAESRTRDLQ-------KEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQC 783
Cdd:TIGR02169 944 EEIPEEELSleDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| CC1_SLMAP-like |
cd21868 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ... |
167-204 |
4.86e-13 |
|
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: 63.66 E-value: 4.86e-13
10 20 30
....*....|....*....|....*....|....*...
gi 528494938 167 QLSQYLQEALHREQMLEQKLATLQRLLASTQEASESSW 204
Cdd:cd21868 1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
506-782 |
1.61e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 506 HRELQEAQELantgkqkcLELQAMLEEERKTNRQQtEESAKQIRFLQTQLAKLQTD---MEALREQRENTITTTREELYS 582
Cdd:COG1196 215 YRELKEELKE--------LEAELLLLKLRELEAEL-EELEAELEELEAELEELEAElaeLEAELEELRLELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 583 AQEEILVLRHAMEAATAERERE---ITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQ-LQSQHQERASQLQGEVE 658
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLeerRRELEERLEELEEELAELEEELEELEEELEELEEELEeAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 659 KLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKsqgdLENKLGSIQDQHQQDASKLKIQL 738
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER----LEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 528494938 739 AQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQ 782
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
14-106 |
1.04e-11 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 61.90 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 14 SHPFQERHVYLDE-PVKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716 8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
|
90
....*....|....
gi 528494938 93 pPCEVLSGDIIQFG 106
Cdd:COG1716 75 -PAPLRDGDVIRLG 87
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
52-106 |
1.26e-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: 1.26e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 528494938 52 SRNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCEVLSGDIIQFG 106
Cdd:cd22686 48 SKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPYPLTHGDELKIG 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
205-772 |
2.15e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 205 QALIDEDRLLsRLEVMGNQLQAYSKNQTEDGIRKELVALTEDKHNYETTAKESLRRVLQEKIEVVRK--------LSEVE 276
Cdd:COG1196 216 RELKEELKEL-EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELeleeaqaeEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 277 RSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEELTQKGLNEKKELQMRIEEMEEKEQAL 356
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 357 QARIEALQADNDFTNERLTALQVRLEQLQEKSIKENNSFAVR-QLKEAVDSSINKLSNFDEVIDAHLQNNQTtvdnslps 435
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLeRLEEELEELEEALAELEEEEEEEEEALEE-------- 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 436 pDRLKENQIDAKECDMSDTLSPSKEKSSDDTSDGQMEEQELNEPQNRVSLLKEMDRSLEAGDT----EQVIPHIHRELQE 511
Cdd:COG1196 447 -AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEgvkaALLLAGLRGLAGA 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 512 AQELANTGKQKCLELQAMLEEERKTNRQQTEESAKQ-IRFLQTQLAKLQTDMEALREQRENTITTTREELYSAQEEILVL 590
Cdd:COG1196 526 VAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAaIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVA 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 591 RHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQAdcsglqne 670
Cdd:COG1196 606 SDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEA-------- 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 671 cdslRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESRTRDLQK 750
Cdd:COG1196 678 ----EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAL 753
|
570 580
....*....|....*....|..
gi 528494938 751 EYDDTQSLLSDLRQRYEQTEQE 772
Cdd:COG1196 754 EELPEPPDLEELERELERLERE 775
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
275-782 |
2.51e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.37 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 275 VERSLSNTEDECTHLREMNERTQEelRELANKYNGAVNEIKDLTEKIKLAEDKHEELTQKglneKKELQMRIEEMEEKEQ 354
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEE--KDLHERLNGLESELAELDEEIERYEEQREQARET----RDEADEVLEEHEERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 355 ALQ---ARIEALQADNDFTNERLTALQVRLEQLQEK--SIKENNSFAVRQLK------EAVDSSINKLSNFDEVIDAHLQ 423
Cdd:PRK02224 252 ELEtleAEIEDLRETIAETEREREELAEEVRDLRERleELEEERDDLLAEAGlddadaEAVEARREELEDRDEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 424 NNQTTVDNSLPSPDRLKENQIDAKEcdMSDTLspsKEKSSDDTSDGQMEEQELNEPQNRVSLLKEMDRSLEA--GDTEQV 501
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLEE--RAEEL---REEAAELESELEEAREAVEDRREEIEELEEEIEELRErfGDAPVD 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 502 IPHIHRELQEAQELANTGKQKCLELQAMLEEERKTNR---------------QQTEES--AKQIRFLQTQLAKLQTDMEA 564
Cdd:PRK02224 407 LGNAEDFLEELREERDELREREAELEATLRTARERVEeaealleagkcpecgQPVEGSphVETIEEDRERVEELEAELED 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 565 LREQREntittTREElysaqeeilvlRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQasfqlqs 644
Cdd:PRK02224 487 LEEEVE-----EVEE-----------RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELR------- 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 645 qhqERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLnrleEELDSSRERSATLSSNLNALEksqgDLENKLGSIQ 724
Cdd:PRK02224 544 ---ERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL----AELKERIESLERIRTLLAAIA----DAEDEIERLR 612
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528494938 725 DQHQQDASK---LKIQLAQAESRTRDLQKEYDDTQslLSDLRQRYEQTEQEKRSINDELEQ 782
Cdd:PRK02224 613 EKREALAELndeRRERLAEKRERKRELEAEFDEAR--IEEAREDKERAEEYLEQVEEKLDE 671
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
510-775 |
3.85e-11 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 66.58 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 510 QEAQELANTgkqkcLeLQAMLEEERKTNRQQTEESakqIRFLQTQLAKLQTDMEALRE-----QRENTITTTREELYSAQ 584
Cdd:COG3206 148 ELAAAVANA-----L-AEAYLEQNLELRREEARKA---LEFLEEQLPELRKELEEAEAaleefRQKNGLVDLSEEAKLLL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 585 EEIlvlrhameaatAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERAsQLQGEVEKLQADc 664
Cdd:COG3206 219 QQL-----------SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLA-ELEAELAELSAR- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 665 sgLQNECDSLRAekstLMQKLNRLEEELDSSRERS-ATLSSNLNALEKSQGDLENKLGSIQDQHQQdasklkiqLAQAES 743
Cdd:COG3206 286 --YTPNHPDVIA----LRAQIAALRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAE--------LPELEA 351
|
250 260 270
....*....|....*....|....*....|..
gi 528494938 744 RTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRS 775
Cdd:COG3206 352 ELRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
121-743 |
4.29e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 67.07 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 121 IVSTIKLFLPDGMEARRRSDVVPAPLPLAIDKVSANtpsmYSQELFQLSQYLQEA--LHREQ--MLEQKLATLQRLLAST 196
Cdd:pfam15921 47 TFTQIPIFPKYEVELDSPRKIIAYPGKEHIERVLEE----YSHQVKDLQRRLNESneLHEKQkfYLRQSVIDLQTKLQEM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 197 QEASEsswqALIDedrlLSRLEvmgNQLQAYSKNQTEDGIRKELVA--LTEDKHNYETTAKESLRR-------VLQEKIE 267
Cdd:pfam15921 123 QMERD----AMAD----IRRRE---SQSQEDLRNQLQNTVHELEAAkcLKEDMLEDSNTQIEQLRKmmlshegVLQEIRS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 268 VVRKLSEVERSLSNTEDECT--HLREMNERTQEELRELANkyngavnEIKDLTEKIKLAEDKHEELTQKGLNEKKEL-QM 344
Cdd:pfam15921 192 ILVDFEEASGKKIYEHDSMStmHFRSLGSAISKILRELDT-------EISYLKGRIFPVEDQLEALKSESQNKIELLlQQ 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 345 RIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEKSiKENNSFAVRQLKEaVDSSINKLSN--------FDE 416
Cdd:pfam15921 265 HQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQA-RNQNSMYMRQLSD-LESTVSQLRSelreakrmYED 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 417 VIDAhlQNNQTTVDNSLPSPDRLKENQIDAKECDMSDTLSP--------SKEKSSDDTSDGQMEEQELNEPQNRVSLLKE 488
Cdd:pfam15921 343 KIEE--LEKQLVLANSELTEARTERDQFSQESGNLDDQLQKlladlhkrEKELSLEKEQNKRLWDRDTGNSITIDHLRRE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 489 MD-RSLEAGDTEQVIPHIHRELQ---EAQELANTGKQKCLE----LQAMLEEERKTNRQQTEE-SAKQIRFLQTQlaKLQ 559
Cdd:pfam15921 421 LDdRNMEVQRLEALLKAMKSECQgqmERQMAAIQGKNESLEkvssLTAQLESTKEMLRKVVEElTAKKMTLESSE--RTV 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 560 TDMEALREQRENTITTTR--------------EELYSAQEEILVLRH------AMEAATAEREREITALQGDLSIVTAEL 619
Cdd:pfam15921 499 SDLTASLQEKERAIEATNaeitklrsrvdlklQELQHLKNEGDHLRNvqteceALKLQMAEKDKVIEILRQQIENMTQLV 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 620 DKWRQTAAKYEVEISnlqasfQLQSQHQERASQLQ----------GEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLE 689
Cdd:pfam15921 579 GQHGRTAGAMQVEKA------QLEKEINDRRLELQefkilkdkkdAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIK 652
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 528494938 690 EELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAES 743
Cdd:pfam15921 653 QERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQS 706
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
312-612 |
5.29e-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: 66.62 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 312 NEIKDLTEKIKLAEDKHEELTQKgLNEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEKSIKE 391
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKA-LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 392 NNSFAVRqlKEAVDSSINKLSNFDEVIDAHLQNNQTTVDNSLPSPDRLKEnQIDAKECDMSDT---LSPSKEKSSDDTSD 468
Cdd:TIGR02168 756 LTELEAE--IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE-ALDELRAELTLLneeAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 469 GQMEEQELNEPQNRVSLLKEMDRSLEA--GDTEQVIPHIHRELQEAQELANTGKQKCLELQAMLEEERKTNR---QQTEE 543
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELReleSKRSE 912
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528494938 544 SAKQIRFLQTQLAKLQTDMEALREQRENTITTTREELYSAQEEILVLRHAMEAATAEREREITALQGDL 612
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
163-718 |
8.49e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 8.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLASTQEASEsswQALIDEDRLLSRLEVMGNQLQAYSKNQTEdgIRKELVA 242
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRR---ELEERLEELEEELAELEEELEELEEELEE--LEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 243 LTEDkhnyETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKIK 322
Cdd:COG1196 349 AEEE----LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 323 LAEDKHEELTQkglnEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEKSIKENNSFAVRQLKE 402
Cdd:COG1196 425 ELEEALAELEE----EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 403 AVDSSInklsnFDEVIDAHLQNNQTTVDNSLPSPDRLKENQIDAKECDMSDTLSPSKEKssDDTSDGQMEEQELNEPQNR 482
Cdd:COG1196 501 ADYEGF-----LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE--DDEVAAAAIEYLKAAKAGR 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 483 VSLL---KEMDRSLEAGDTEQVIPHIHRELQEAQELANTGKQKCLELQAMLEEERKTNRQQTEESAKQIRFLQTQLAKLQ 559
Cdd:COG1196 574 ATFLpldKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 560 TDMEALREQRENTITTTREELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQAS 639
Cdd:COG1196 654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 640 FQLQSQHQERASQLQGEVEKLQADcsGLQNEcDSLRAEKSTLMQKLNRL-------EEELDSSRERSATLSSNLNALEKS 712
Cdd:COG1196 734 REELLEELLEEEELLEEEALEELP--EPPDL-EELERELERLEREIEALgpvnllaIEEYEELEERYDFLSEQREDLEEA 810
|
....*.
gi 528494938 713 QGDLEN 718
Cdd:COG1196 811 RETLEE 816
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
507-782 |
3.24e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 507 RELQEAQELAntgkQKCLELQAMLEEERKTNRQQTEesaKQIRFLQTQLAKLQTDMEALREqRENTITTTREELYSAQEE 586
Cdd:COG1196 235 RELEAELEEL----EAELEELEAELEELEAELAELE---AELEELRLELEELELELEEAQA-EEYELLAELARLEQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 587 ILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQADcsg 666
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE--- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 667 LQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESRTR 746
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270
....*....|....*....|....*....|....*.
gi 528494938 747 DLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQ 782
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| CC1_T3JAM |
cd21912 |
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ... |
164-204 |
4.19e-10 |
|
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: 55.43 E-value: 4.19e-10
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 528494938 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLASTQEASESSW 204
Cdd:cd21912 5 EILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
179-796 |
4.35e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.55 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 179 EQMLEQKLATLQRLLASTQEASEssWQALIDEDR------LLSRLEVMGNQLQAYSKNQteDGIRKELVALTE--DKHNY 250
Cdd:TIGR02169 190 DLIIDEKRQQLERLRREREKAER--YQALLKEKReyegyeLLKEKEALERQKEAIERQL--ASLEEELEKLTEeiSELEK 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 251 ETTAKESLRRVLQEKIE---------VVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKI 321
Cdd:TIGR02169 266 RLEEIEQLLEELNKKIKdlgeeeqlrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREI 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 322 KlaedkheelTQKGlnEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEK--SIKENNSFAVRQ 399
Cdd:TIGR02169 346 E---------EERK--RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREinELKRELDRLQEE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 400 LKEAvDSSINKLSNFDEVIDAHLQNNQTTVDNSlpspdRLKENQIDAKECDMSDTLSPSKEKSSDDTSDGQMEEQELNEP 479
Cdd:TIGR02169 415 LQRL-SEELADLNAAIAGIEAKINELEEEKEDK-----ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 480 QNRVSLLKE-----MDRSLEAGDTEQV----IPHIH----------RELQEAQELANTGK------------QKCLE--- 525
Cdd:TIGR02169 489 QRELAEAEAqarasEERVRGGRAVEEVlkasIQGVHgtvaqlgsvgERYATAIEVAAGNRlnnvvveddavaKEAIEllk 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 526 -----------LQAMLEEERKTNRQQTE---------------------------------ESAKQI------------- 548
Cdd:TIGR02169 569 rrkagratflpLNKMRDERRDLSILSEDgvigfavdlvefdpkyepafkyvfgdtlvvediEAARRLmgkyrmvtlegel 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 549 ---------------------RFLQTQLAKLQTDMEALREQREntitTTREELYSAQEEILVLRHAMEAATA---ERERE 604
Cdd:TIGR02169 649 feksgamtggsraprggilfsRSEPAELQRLRERLEGLKRELS----SLQSELRRIENRLDELSQELSDASRkigEIEKE 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 605 ITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQ----LQSQHQERASQLQGEVEKLQADCSG-----LQNECDSLR 675
Cdd:TIGR02169 725 IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKeleaRIEELEEDLHKLEEALNDLEARLSHsripeIQAELSKLE 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 676 AEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQH---QQDASKLKIQLAQAESRTRDLQKEY 752
Cdd:TIGR02169 805 EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIenlNGKKEELEEELEELEAALRDLESRL 884
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 528494938 753 DDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLKLLQDKGSN 796
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
161-774 |
1.01e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 161 YSQELFQLSQYLqeALHREQMLEQKLATLQRLLASTQEASEsswqalidedRLLSRLEVMGNQLQAYSKNQTEdgIRKEL 240
Cdd:COG1196 218 LKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELE----------ELEAELAELEAELEELRLELEE--LELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 241 VALTEDkhnyETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEK 320
Cdd:COG1196 284 EEAQAE----EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 321 IKLAEDKHEELTQkglnEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEKSIKENnsfavRQL 400
Cdd:COG1196 360 LAEAEEALLEAEA----ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE-----EAL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 401 KEAVDSSINKLSNFDEVIDAHLQNNQTTVDNSLPSPDRLKENQIDAKEcdMSDTLSPSKEKSSDDTSDGQMEEQELNEPQ 480
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA--LAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 481 N--RVSLLKEMDRSLEAGDTEQVIPHIHRELQEAQELANTGK---------QKCLELQAMLEEERKTNRQQTEESAKQIR 549
Cdd:COG1196 509 GvkAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNivveddevaAAAIEYLKAAKAGRATFLPLDKIRARAAL 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 550 FLQTQLAKLQTDMEALREQREntittTREELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKY 629
Cdd:COG1196 589 AAALARGAIGAAVDLVASDLR-----EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 630 EVEISNLQASFQLQSQHQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDssRERSATLSSNLNAL 709
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE--EQLEAEREELLEEL 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 710 EKSQGDLENKLGSIQ------DQHQQDASKLKIQL--------------AQAESRTRDLQKEYDDTQSLLSDLRQRYEQT 769
Cdd:COG1196 742 LEEEELLEEEALEELpeppdlEELERELERLEREIealgpvnllaieeyEELEERYDFLSEQREDLEEARETLEEAIEEI 821
|
....*
gi 528494938 770 EQEKR 774
Cdd:COG1196 822 DRETR 826
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
505-709 |
1.22e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 505 IHRELQEAQElantgKQKCLE-----LQAMLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQRENT---ITTT 576
Cdd:COG4913 240 AHEALEDARE-----QIELLEpirelAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLeaeLERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 577 REELYSAQEEILVLRHAMEAATAER----EREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQlqsqhqERASQ 652
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRleqlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA------ALRAE 388
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 528494938 653 LQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNAL 709
Cdd:COG4913 389 AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
535-792 |
2.77e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 535 KTNRQQTEesaKQIRFLQTQLAKLQ-------TDMEALREQRENTIT--TTREELYSAQEEILVLR-HAMEAATAERERE 604
Cdd:TIGR02168 171 KERRKETE---RKLERTRENLDRLEdilneleRQLKSLERQAEKAERykELKAELRELELALLVLRlEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 605 ITALQGDLSIVTAELDKwrqtaakYEVEISNLQASFQlqsQHQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQK 684
Cdd:TIGR02168 248 LKEAEEELEELTAELQE-------LEEKLEELRLEVS---ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 685 LNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHqqdaSKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQ 764
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL----EELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
250 260
....*....|....*....|....*...
gi 528494938 765 RYEQTEQEKRSINDELEQCKVNLKLLQD 792
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQ 421
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
177-780 |
3.47e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.42 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 177 HREQMLEQKLATLQRLLASTQEASESSWQALIDEDRLLSRLEVMGNQLQAYSK---------NQTEDGIRKELVALTED- 246
Cdd:TIGR04523 33 TEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKdlndklkknKDKINKLNSDLSKINSEi 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 247 --KHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKIKLA 324
Cdd:TIGR04523 113 knDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 325 EDKHEELTQKGLNEK------KELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEKSIKENNSFAVR 398
Cdd:TIGR04523 193 KNKLLKLELLLSNLKkkiqknKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 399 QLK-EAVDSSINKLSNFDEVIDAHLQ--NNQTTVD--NSLPSPDRLKENQIDAKECDMS----------DTLSPSKEKSS 463
Cdd:TIGR04523 273 QKElEQNNKKIKELEKQLNQLKSEISdlNNQKEQDwnKELKSELKNQEKKLEEIQNQISqnnkiisqlnEQISQLKKELT 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 464 DDTSDGQMEEQELNEPQNRVSLLKEMDRSL--EAGDTEQVIPHIHRELQEAQELANTGKQKCLELQA---MLEEERKTNR 538
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYkqEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQekeLLEKEIERLK 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 539 QQTEESAKQIRFLQTQLAKLQTDMEALREQREntitttreelySAQEEILVLrhameaataerEREITALQGDLSIVTAE 618
Cdd:TIGR04523 433 ETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE-----------SLETQLKVL-----------SRSINKIKQNLEQKQKE 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 619 LDKWRQTAAKYEVEISNLQASFQLQSQHQeraSQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNR--LEEELDSSR 696
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLTKKI---SSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenLEKEIDEKN 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 697 ERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESRTRDL---QKEYDDTQSLLSDLRQRYEQTEQEK 773
Cdd:TIGR04523 568 KEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELekaKKENEKLSSIIKNIKSKKNKLKQEV 647
|
....*..
gi 528494938 774 RSINDEL 780
Cdd:TIGR04523 648 KQIKETI 654
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
162-587 |
9.64e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 9.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 162 SQELFQLSQY--LQEALHREQMLEQKLATLQRLLASTQEASESSWQALIDEDRLLSRLEVMGNQLQAYSKNQTE--DGIR 237
Cdd:TIGR02169 664 GGILFSRSEPaeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKErlEELE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 238 KELVALTEDKHNYETTAKEsLRRVLQEKIEvvrKLSEVERSLSNTEDECTHlremnertqEELRELANKYNGAVNEIKDL 317
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKE-LEARIEELEE---DLHKLEEALNDLEARLSH---------SRIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 318 TEKIKLAEDKHEELTQKGL---NEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEKSIKenns 394
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEyleKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD---- 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 395 favrqLKEAVDSSINKLSNfdevidahLQNNQTTVdnslpspdrlkENQIDAKECDMSDTLSPSKEKSSDDTSDGQMEEQ 474
Cdd:TIGR02169 887 -----LKKERDELEAQLRE--------LERKIEEL-----------EAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE 942
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 475 ELNEPQNRVSLlkemdrsleaGDTEQVIPHIHRELQEaqelantgkqkcLELQAMLEEerktnrQQTEESAKQIRFLQTQ 554
Cdd:TIGR02169 943 DEEIPEEELSL----------EDVQAELQRVEEEIRA------------LEPVNMLAI------QEYEEVLKRLDELKEK 994
|
410 420 430
....*....|....*....|....*....|...
gi 528494938 555 LAKLQTDMEALREQRENTITTTREELYSAQEEI 587
Cdd:TIGR02169 995 RAKLEEERKAILERIEEYEKKKREVFMEAFEAI 1027
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
529-787 |
1.28e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 529 MLEEerktnrQQTEESAKQIRFLQTQLAKLQTDMEALREQRE--NTITTTREELYSAQEEILVLRHAMEAATAEREREit 606
Cdd:COG4913 217 MLEE------PDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAQR-- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 607 alqgdlsivtaELDKWRQTAAKYEVEISNLQASfqlQSQHQERASQLQGEVEKLQADCSGLQNEcdslraEKSTLMQKLN 686
Cdd:COG4913 289 -----------RLELLEAELEELRAELARLEAE---LERLEARLDALREELDELEAQIRGNGGD------RLEQLEREIE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 687 RLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQdasklkiQLAQAESRTRDLQKEYDDTQSLLSDLRQRY 766
Cdd:COG4913 349 RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA-------LLEALEEELEALEEALAEAEAALRDLRREL 421
|
250 260
....*....|....*....|.
gi 528494938 767 EQTEQEKRSindeLEQCKVNL 787
Cdd:COG4913 422 RELEAEIAS----LERRKSNI 438
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
301-782 |
1.40e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 301 RELANKYNGAVNEIKDLTEKIKLAEDKHEELTQKGLNEK-----------------------------KELQMRIEEMEE 351
Cdd:COG1196 209 AEKAERYRELKEELKELEAELLLLKLRELEAELEELEAEleeleaeleeleaelaeleaeleelrlelEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 352 KEQALQARIEALQADNDFTNERLTALQVRLEQLQEKsiKENNSFAVRQLKEAVDSSINKLSNFDEVIDAhLQNNQTTVDN 431
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEE--LAELEEELEELEEELEELEEELEEAEEELEE-AEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 432 SLPSPDRLKENQIDAKECDMSDTLSPSKEKSSDDTSDGQMEEQELNEPQNRVSLLKEM-DRSLEAGDTEQVIPHIHRELQ 510
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELeELEEALAELEEEEEEEEEALE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 511 EAQELANTGKQKCLELQAMLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQRENTITTTREELYSAQEEILVL 590
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 591 RHAMEAATAEREREI-TALQGDLSIVTAELDKWRQTAAKYEVEISNLQASF-QLQSQHQERASQLQGEVEKLQADCSGLQ 668
Cdd:COG1196 526 VAVLIGVEAAYEAALeAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFlPLDKIRARAALAAALARGAIGAAVDLVA 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 669 NECDSLRAEKSTLMQKL---NRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESRT 745
Cdd:COG1196 606 SDLREADARYYVLGDTLlgrTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685
|
490 500 510
....*....|....*....|....*....|....*..
gi 528494938 746 RDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQ 782
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEERELAEAEEERLEEELE 722
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
135-737 |
1.55e-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: 58.59 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 135 ARRRSDVVPAPLPLaIDKVSANTPSMYSQELFQL----SQYLQEALHREQMLEQKLATLQR-LLASTQEASEsswqALID 209
Cdd:pfam15921 290 ARSQANSIQSQLEI-IQEQARNQNSMYMRQLSDLestvSQLRSELREAKRMYEDKIEELEKqLVLANSELTE----ARTE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 210 EDRLLSRLEVMGNQLQAY----SKNQTEDGIRKELVALTEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNtede 285
Cdd:pfam15921 365 RDQFSQESGNLDDQLQKLladlHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKS---- 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 286 cthlrEMNERTQEELRELANKyNGAVNEIKDLTEKIklaeDKHEELTQKGLNEKKELQMRIEEMEEKEQALQARIEALQA 365
Cdd:pfam15921 441 -----ECQGQMERQMAAIQGK-NESLEKVSSLTAQL----ESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKER 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 366 DNDFTNERLTALQVRLE-QLQEksikennsfaVRQLKEAVDssinklsnfdevidaHLQNNQTtvdnslpspdrlkenqi 444
Cdd:pfam15921 511 AIEATNAEITKLRSRVDlKLQE----------LQHLKNEGD---------------HLRNVQT----------------- 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 445 dakECDMSDTLSPSKEKssddtsdgqMEEQELNEPQNRVSLLKEMDRS-----LEAGDTEQVIPHIHRELQEAQELANTG 519
Cdd:pfam15921 549 ---ECEALKLQMAEKDK---------VIEILRQQIENMTQLVGQHGRTagamqVEKAQLEKEINDRRLELQEFKILKDKK 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 520 KQKCLELQAMLEEERKTNRQQTEESAKQIRFLQtqlaklqtDMEALREQRENTITTTREELYSAQEEILVLRHAMEAATA 599
Cdd:pfam15921 617 DAKIRELEARVSDLELEKVKLVNAGSERLRAVK--------DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSE 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 600 EREREITALQGDLSIVTAELDKWRQTAAKYE-VEISNLQASFQLQSQHQERASQ---LQGEVEKLQADCSGLQNECDSLR 675
Cdd:pfam15921 689 EMETTTNKLKMQLKSAQSELEQTRNTLKSMEgSDGHAMKVAMGMQKQITAKRGQidaLQSKIQFLEEAMTNANKEKHFLK 768
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528494938 676 AEKSTLMQKL-------NRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQD---QHQQDASKLKIQ 737
Cdd:pfam15921 769 EEKNKLSQELstvatekNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDiiqRQEQESVRLKLQ 840
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
182-765 |
2.06e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 182 LEQKLATLQRLLASTQEASESSWQALIDEDRLLSRLEvmgnqlqaySKNQTEDGIRKELVALTEDKHNYETTaKESLRRV 261
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHE---------ERREELETLEAEIEDLRETIAETERE-REELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 262 LQEKIEVVRKLSE------VERSLSNTEDECTHLR-----EMNERTQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEE 330
Cdd:PRK02224 281 VRDLRERLEELEEerddllAEAGLDDADAEAVEARreeleDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 331 LTQKGLNEKKELQ---MRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEKsikennsfavrqlKEAVDSS 407
Cdd:PRK02224 361 LREEAAELESELEearEAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREE-------------RDELRER 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 408 INKLSnfdevidAHLQNNQttvdnslpspDRLKENQ--IDA---KECDMSDTLSPSKEKSSDDTSDGQMEEQELNEPQNR 482
Cdd:PRK02224 428 EAELE-------ATLRTAR----------ERVEEAEalLEAgkcPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 483 VSLLKEMDRSLEagdteqviphihrELQEAQELANTGKQKCLELQAMLEEERKTnrqqTEESAKQIRFLQTQLAKLQTDM 562
Cdd:PRK02224 491 VEEVEERLERAE-------------DLVEAEDRIERLEERREDLEELIAERRET----IEEKRERAEELRERAAELEAEA 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 563 EALREQrentITTTREELYSAQEEILVLRHAMEAATAERER--EITALQGDLSIVTAELDKWR-QTAAKYEVeisNLQAS 639
Cdd:PRK02224 554 EEKREA----AAEAEEEAEEAREEVAELNSKLAELKERIESleRIRTLLAAIADAEDEIERLReKREALAEL---NDERR 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 640 FQLQSQhQERASQLQGEVEklqadcsglQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENk 719
Cdd:PRK02224 627 ERLAEK-RERKRELEAEFD---------EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE- 695
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 528494938 720 lgsiqdqhqqdaskLKIQLAQAESRTRDLQKEYDDTQSLLS-------DLRQR 765
Cdd:PRK02224 696 --------------LRERREALENRVEALEALYDEAEELESmygdlraELRQR 734
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
28-85 |
2.44e-08 |
|
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.
Pssm-ID: 214578 [Multi-domain] Cd Length: 52 Bit Score: 50.64 E-value: 2.44e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 528494938 28 VKIGRSvarcrPAQNNATFDCKVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRL 85
Cdd:smart00240 1 VTIGRS-----SEDCDIQLDGPSISRRHAVIVYD-GGGRFYLIDLGSTNGTFVNGKRI 52
|
|
| FHA_TCF19 |
cd22685 |
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ... |
28-119 |
2.61e-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: 53.19 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 28 VKIGRSVARCRPAQNNATFDcKVLSRNHALVW---FDHKTGKFYLQDTkSSNGTFINSQRLSRGSEEsppcEVLSGDIIQ 104
Cdd:cd22685 30 YRIGRNPEVCDVFLCSSQHP-NLISREHAEIHaerDGNGNWKVLIEDR-STNGTYVNDVRLQDGQRR----ELSDGDTIT 103
|
90
....*....|....*..
gi 528494938 105 FG--VDVTENTRKVTHG 119
Cdd:cd22685 104 FGhkNGRRVKQWPYQKS 120
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
595-782 |
5.34e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 595 EAATAEREREitaLQGDLSIVTAEL--DKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQADCSGLQNECD 672
Cdd:COG1196 208 QAEKAERYRE---LKEELKELEAELllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 673 SLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLgsiqDQHQQDASKLKIQLAQAESRTRDLQKEY 752
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL----EELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190
....*....|....*....|....*....|
gi 528494938 753 DDTQSLLSDLRQRYEQTEQEKRSINDELEQ 782
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLE 390
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
276-782 |
7.75e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 56.34 E-value: 7.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 276 ERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKIKLAED---KHEELTQKGLNEKKELQMRIEEMEEK 352
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETElcaEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 353 EQALQARIEALQADNDFTNERLTALQvrlEQLQEKSikennsfAVRQL----KEAVDSSINKLSnfDEVIDAHLQNNQTT 428
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLE---EQLDEEE-------AARQKlqleKVTTEAKIKKLE--EDILLLEDQNSKLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 429 VDNSLPSpDRLKENQID-AKECDMSDTLSPSKEKSSDDTSDgqMEEQELNEPQNRVSLLKeMDRSLEaGDTEQVIPHIHR 507
Cdd:pfam01576 152 KERKLLE-ERISEFTSNlAEEEEKAKSLSKLKNKHEAMISD--LEERLKKEEKGRQELEK-AKRKLE-GESTDLQEQIAE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 508 ELQEAQELANTGKQKCLELQAMLEEERKTNRQQTeESAKQIRFLQTQLAKLQTDMEALREQRENTITTTR------EELY 581
Cdd:pfam01576 227 LQAQIAELRAQLAKKEEELQAALARLEEETAQKN-NALKKIRELEAQISELQEDLESERAARNKAEKQRRdlgeelEALK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 582 SAQEEILVLRHAMEAATAEREREITALQGDLsivtaELDKWRQTAAKYEVEISNLQASFQLQSQhQERASQLQGEVEK-- 659
Cdd:pfam01576 306 TELEDTLDTTAAQQELRSKREQEVTELKKAL-----EEETRSHEAQLQEMRQKHTQALEELTEQ-LEQAKRNKANLEKak 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 660 --LQADCSGLQNECDSLRAEKSTLMQKLNRLEEELdssrersATLSSNLNALEKSQGDLENKLGSIQDQHQQDASklkiQ 737
Cdd:pfam01576 380 qaLESENAELQAELRTLQQAKQDSEHKRKKLEGQL-------QELQARLSESERQRAELAEKLSKLQSELESVSS----L 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 528494938 738 LAQAESRTRDLQKEYD-------DTQSLLSD-------LRQRYEQTEQEKRSINDELEQ 782
Cdd:pfam01576 449 LNEAEGKNIKLSKDVSslesqlqDTQELLQEetrqklnLSTRLRQLEDERNSLQEQLEE 507
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
525-745 |
1.24e-07 |
|
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: 54.77 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 525 ELQAMLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQ---RENTITTTREELYSAQEEILVLRHAMEAAtaer 601
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiaaLARRIRALEQELAALEAELAELEKEIAEL---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 602 EREITALQGDLSIVTAELDKW-RQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQADCSGLQNECDSLRAEKST 680
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528494938 681 LMQKLNRLEEE---LDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESRT 745
Cdd:COG4942 176 LEALLAELEEEraaLEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
164-791 |
2.28e-07 |
|
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: 54.84 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLASTQEASESSWQALIDEDRL------------LSRLEVMGNQLQAYSKNQ 231
Cdd:pfam12128 259 RLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGelsaadaavakdRSELEALEDQHGAFLDAD 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 232 TE---------DGIRKEL------VALTEDKHNYETTAKEslRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERT 296
Cdd:pfam12128 339 IEtaaadqeqlPSWQSELenleerLKALTGKHQDVTAKYN--RRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDD 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 297 QEEL-RELANKYNGAVNEIKDLTEKIKLA--EDK---------HEELTQKGLNekkelQMRIEEMEEKEQALQARIEALQ 364
Cdd:pfam12128 417 LQALeSELREQLEAGKLEFNEEEYRLKSRlgELKlrlnqatatPELLLQLENF-----DERIERAREEQEAANAEVERLQ 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 365 ADN--------------DFTNERLTALQVRLEQLQEKSIKENNSFAVRQLKEAVD--SSINKL--------SNFDEVIDA 420
Cdd:pfam12128 492 SELrqarkrrdqasealRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDweQSIGKVispellhrTDLDPEVWD 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 421 H------------LQNNQTTVDNSLPSPDRLKEnQIDAKECDMSDTLSPSKEKSSD-DTSDGQMEEQELNEP-------Q 480
Cdd:pfam12128 572 GsvggelnlygvkLDLKRIDVPEWAASEEELRE-RLDKAEEALQSAREKQAAAEEQlVQANGELEKASREETfartalkN 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 481 NRVSL--LKEMDRSLEAGDTEQVIPHIHRELQEAQELANTGKQKCLELQAMLEEERKTNRQQTEESAKQIRFLQ----TQ 554
Cdd:pfam12128 651 ARLDLrrLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEgaldAQ 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 555 LAKLQTDMEALREQRENTITTTREELYSAqeeiLVLRHAMEAATAEREREITALQGDLSivtaELDKWRQTAAKYEVeis 634
Cdd:pfam12128 731 LALLKAAIAARRSGAKAELKALETWYKRD----LASLGVDPDVIAKLKREIRTLERKIE----RIAVRRQEVLRYFD--- 799
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 635 nlqasfQLQSQHQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRleeELDSSRERSATLSSNLNALEKSQG 714
Cdd:pfam12128 800 ------WYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEM---ERKASEKQQVRLSENLRGLRCEMS 870
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 715 DL-ENKLGSIQDQHQQDASKLKIQLAQ----AESRTRDLQKEYDDTQSLLSDLR-----QRYEQTEQEKRSINDELEQCK 784
Cdd:pfam12128 871 KLaTLKEDANSEQAQGSIGERLAQLEDlklkRDYLSESVKKYVEHFKNVIADHSgsglaETWESLREEDHYQNDKGIRLL 950
|
....*..
gi 528494938 785 VNLKLLQ 791
Cdd:pfam12128 951 DYRKLVP 957
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
14-110 |
2.33e-07 |
|
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: 49.53 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 14 SHPFQERHV---YLDEPVKIGRSvARCRPAQNNATfdckvLSRNHALVW---FDHKTG-KFYLQDTkSSNGTFINSQRLS 86
Cdd:cd22670 7 SSPGSTDIVlpiYKNQVITIGRS-PSCDIVINDPF-----VSRTHCRIYsvqFDESSApLVYVEDL-SSNGTYLNGKLIG 79
|
90 100
....*....|....*....|....*
gi 528494938 87 RGseespPCEVLS-GDIIQFGVDVT 110
Cdd:cd22670 80 RN-----NTVLLSdGDVIEIAHSAT 99
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
25-114 |
2.70e-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: 49.66 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 25 DEPVKIGRSVArcrpAQNNATFDC-KVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRLsrgsEESPPCEVLSGDII 103
Cdd:cd22663 20 GKEVTVGRGLG----VTYQLVSTCpLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERI----EPLKPYPLNEGDLI 90
|
90
....*....|.
gi 528494938 104 QFGVDVTENTR 114
Cdd:cd22663 91 QLGVPPENKEP 101
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
289-775 |
2.88e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 289 LREMNERTQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEELTQKgLNEKKELQMRIEEMEEKEQALQARIEALQADND 368
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 369 F---------TNERLTALQVRLEQLQEKsIKEnnsfaVRQLKEAVDSSINKLSNFDEVIDAHLQnnqttvDNSLPSPDRL 439
Cdd:COG4717 127 LlplyqeleaLEAELAELPERLEELEER-LEE-----LRELEEELEELEAELAELQEELEELLE------QLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 440 KENQIDAKECDmsdtlspskekssddtSDGQMEEQELNEPQNRVSLLKEmdrSLEAGDTEQVIPHIHRELQEAQELANTG 519
Cdd:COG4717 195 QDLAEELEELQ----------------QRLAELEEELEEAQEELEELEE---ELEQLENELEAAALEERLKEARLLLLIA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 520 KQKCLeLQAMLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQRENTITTTREELYSAQE--EILVLRHAMEAA 597
Cdd:COG4717 256 AALLA-LLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEEleELLAALGLPPDL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 598 TAEREREITALQGDLSIVTAELDKWRQTA--AKYEVEISNLQASFQLQS--------QHQERASQLQGEVEKLQADCSGL 667
Cdd:COG4717 335 SPEELLELLDRIEELQELLREAEELEEELqlEELEQEIAALLAEAGVEDeeelraalEQAEEYQELKEELEELEEQLEEL 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 668 QNECDSLRA--EKSTLMQKLNRLEEELDSSRERsatlssnLNALEKSQGDLENKLGSIQDQHqqDASKLKIQLAQAESRT 745
Cdd:COG4717 415 LGELEELLEalDEEELEEELEELEEELEELEEE-------LEELREELAELEAELEQLEEDG--ELAELLQELEELKAEL 485
|
490 500 510
....*....|....*....|....*....|
gi 528494938 746 RDLQKEYDDTQSLLSDLRQRYEQTEQEKRS 775
Cdd:COG4717 486 RELAEEWAALKLALELLEEAREEYREERLP 515
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
27-106 |
3.57e-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: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 27 PVKIGRSVARcRPAQNNATFDC-----KVLSRNHALVWFDHKTGKFYLQdTKSSNGTFINSQRLSRGseeSPPCEVLSGD 101
Cdd:cd22701 18 EVVLGRNSKN-SSSTAADSVDIdlgpsKKISRRHARIFYDFTTQCFELS-VLGRNGVKVDGILVKPG---SPPVPLRSGS 92
|
....*
gi 528494938 102 IIQFG 106
Cdd:cd22701 93 LIQIG 97
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
612-779 |
4.16e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 612 LSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKL--QADCSGLQNECDSLRAEKSTLMQKLNRLE 689
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 690 EELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQT 769
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170
....*....|
gi 528494938 770 EQEKRSINDE 779
Cdd:COG4717 233 ENELEAAALE 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
152-604 |
4.34e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 152 KVSANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLASTQEASEsswqaliDEDRLLSRLEVMGNQLQAYSKNQ 231
Cdd:COG4717 60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA-------ELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 232 TEDGIRKELVALTEdkhnyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDEC-THLREMNERTQEELRELANKYNGA 310
Cdd:COG4717 133 ELEALEAELAELPE--------RLEELEERLEELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 311 VNEIKDLTEKIKLAEDKHEELTQkglnEKKELQMRIEEMEEKEQALQARIEALQAdndftNERLTALQVRLEQLQEKSIK 390
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEE----ELEQLENELEAAALEERLKEARLLLLIA-----AALLALLGLGGSLLSLILTI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 391 ENNSFAVRQLKEAVDSSINKlsnfdeviDAHLQNNQTTVDNSLPSPDRLKENQID--AKECDMSDTLSPSK-EKSSDDTS 467
Cdd:COG4717 276 AGVLFLVLGLLALLFLLLAR--------EKASLGKEAEELQALPALEELEEEELEelLAALGLPPDLSPEElLELLDRIE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 468 DGQMEEQELNEPQNRV---SLLKEMDRSLEAG--DTEQVIPHIHRELQEAQELantgKQKCLELQAMLEEERKTNRQQTE 542
Cdd:COG4717 348 ELQELLREAEELEEELqleELEQEIAALLAEAgvEDEEELRAALEQAEEYQEL----KEELEELEEQLEELLGELEELLE 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528494938 543 ESAKQirFLQTQLAKLQTDMEALREQRENtittTREELYSAQEEILVLRHAMEAATAERERE 604
Cdd:COG4717 424 ALDEE--ELEEELEELEEELEELEEELEE----LREELAELEAELEQLEEDGELAELLQELE 479
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
256-694 |
4.47e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.75 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 256 ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERtQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEELTQKG 335
Cdd:PRK01156 315 SNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQ-ILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 336 LNEKK-------ELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEKSIKE--NNSFAVRQLKEAVDS 406
Cdd:PRK01156 394 SEILKiqeidpdAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPvcGTTLGEEKSNHIINH 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 407 SINKLSNFDEVIDaHLQNNQTTVDNSLPSPDRLKEnQIDAKECDMSDTLSPSKEKSSDDTSDGQMEEQELNEPQNRVSLL 486
Cdd:PRK01156 474 YNEKKSRLEEKIR-EIEIEVKDIDEKIVDLKKRKE-YLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEI 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 487 KEMDRSLEAGDTEQviphihrelqeaqelANTGKQKCLELQAMLEEErkTNRQQTEESAKQIRFLQTQLAKLQTDMEALR 566
Cdd:PRK01156 552 KNRYKSLKLEDLDS---------------KRTSWLNALAVISLIDIE--TNRSRSNEIKKQLNDLESRLQEIEIGFPDDK 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 567 EQRENTITTTREELYSAQEEILVLRhameaataEREREITALQGDLSivtaelDKWRQTAAKYEVEISNLQASFQLqSQH 646
Cdd:PRK01156 615 SYIDKSIREIENEANNLNNKYNEIQ--------ENKILIEKLRGKID------NYKKQIAEIDSIIPDLKEITSRI-NDI 679
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 528494938 647 QERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDS 694
Cdd:PRK01156 680 EDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLES 727
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
267-788 |
5.98e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.10 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 267 EVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEELTQKGLNEKKELQMRI 346
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 347 EEMEEKEQalqaRIEALQADNDFTNERLTALQVRLEQLQEKSIKENNSFA-VRQLKEAVDSSINKLSNFDEVIDAHLQN- 424
Cdd:TIGR04523 117 EQKNKLEV----ELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNdLKKQKEELENELNLLEKEKLNIQKNIDKi 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 425 -NQTTVDNSLPSPDRLKENQIDAKECDMSDtlspSKEKSSDDTSDGQMEEQELNEPQNRVSLLKEmdrslEAGDTEQVIP 503
Cdd:TIGR04523 193 kNKLLKLELLLSNLKKKIQKNKSLESQISE----LKKQNNQLKDNIEKKQQEINEKTTEISNTQT-----QLNQLKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 504 HIHRELQEAQELANTGKQKCLELQAMLEE-ERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQ---RENTITTTREE 579
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEKQLNQlKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQisqNNKIISQLNEQ 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 580 LYSAQEEILVLrhamEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQsqhQERASQLQGEVEK 659
Cdd:TIGR04523 344 ISQLKKELTNS----ESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQ---EKLNQQKDEQIKK 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 660 LQADCSGLQNECDSLRAEKSTLMQKLNRLEEE----------LDSSRErsaTLSSNLNALEKSQGDLENKLGSIQ---DQ 726
Cdd:TIGR04523 417 LQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkeliiknLDNTRE---SLETQLKVLSRSINKIKQNLEQKQkelKS 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528494938 727 HQQDASKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLK 788
Cdd:TIGR04523 494 KEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK 555
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
212-793 |
6.55e-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: 53.13 E-value: 6.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 212 RLLSRLEVMGNQLQAYSKNQTEDGIRKELVALTEDKHNYETTAKESLRRVLQEKIEvvrkLSEVERSlSNTEDECTHLRE 291
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE----LDGFERG-PFSERQIKNFHT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 292 MNERTQEELRELANKyngavnEIKDLTEKIKLAEDKHEELTQKGLNEKKELQMRIEEMEEKEQALQARIEALQADNDFTN 371
Cdd:TIGR00606 398 LVIERQEDEAKTAAQ------LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 372 ERLTALQVRLEQLQEKSIKENNSFAVRQLKEAVdssinklsnfdevidaHLQNNQTTVDNSLPSPDRlKENQIDAKECDM 451
Cdd:TIGR00606 472 RILELDQELRKAERELSKAEKNSLTETLKKEVK----------------SLQNEKADLDRKLRKLDQ-EMEQLNHHTTTR 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 452 SDTLSPSKEKSsddTSDGQMEEQELNEPQNRVSLLKEMDRSLEAGDTeqviphIHRELQEAQELANTGKQKCLELQAMLE 531
Cdd:TIGR00606 535 TQMEMLTKDKM---DKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDW------LHSKSKEINQTRDRLAKLNKELASLEQ 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 532 EERKTNrqqteesaKQIRFLQTQLAKLQTDMEAL--REQRENTITTTREELYSAQEEilvlRHAMEAATAEREREITALQ 609
Cdd:TIGR00606 606 NKNHIN--------NELESKEEQLSSYEDKLFDVcgSQDEESDLERLKEEIEKSSKQ----RAMLAGATAVYSQFITQLT 673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 610 GDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQADCSGL----QNECDSLRAEKSTL---M 682
Cdd:TIGR00606 674 DENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLapgrQSIIDLKEKEIPELrnkL 753
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 683 QKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQD-QHQQDASKLKIQLAQAESRTRDLQKEYddtqsllSD 761
Cdd:TIGR00606 754 QKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERfQMELKDVERKIAQQAAKLQGSDLDRTV-------QQ 826
|
570 580 590
....*....|....*....|....*....|..
gi 528494938 762 LRQRYEQTEQEKRSINDELEQckvNLKLLQDK 793
Cdd:TIGR00606 827 VNQEKQEKQHELDTVVSKIEL---NRKLIQDQ 855
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
250-786 |
1.04e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 250 YETTAKES--LRRVLQEKIEVVRKL----SEVERSLSNTEDECTH-LREMNErTQEELRELANKYNGAVNEIKDLtEKIK 322
Cdd:PRK03918 160 YENAYKNLgeVIKEIKRRIERLEKFikrtENIEELIKEKEKELEEvLREINE-ISSELPELREELEKLEKEVKEL-EELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 323 laedkhEELTQKGLnEKKELQMRIEEMEEKEQALQARIEALQadndftnERLTALQVRLEQLQEKSIKENNSFAVRQLKE 402
Cdd:PRK03918 238 ------EEIEELEK-ELESLEGSKRKLEEKIRELEERIEELK-------KEIEELEEKVKELKELKEKAEEYIKLSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 403 AVDSSINKLSNFDEVIDAHLQNNQTTVDNSLPSPDRLKEnqidakecdmsdtlspsKEKSSDDTSDGQMEEQELNEPQNR 482
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE-----------------LKKKLKELEKRLEELEERHELYEE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 483 VSLLKEMDRSLEAGDTEQVIPHIHRELQEaqelantgkqkclelqamLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDM 562
Cdd:PRK03918 367 AKAKKEELERLKKRLTGLTPEKLEKELEE------------------LEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 563 EALREQRENTITTTREELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYeveISNLQASFQL 642
Cdd:PRK03918 429 EELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEL---IKLKELAEQL 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 643 QSQHQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEeldsSRERSATLSSNLNALEKSQGDLENKLGS 722
Cdd:PRK03918 506 KELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEE 581
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528494938 723 IQ-DQHQQDASKLK---------IQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVN 786
Cdd:PRK03918 582 LGfESVEELEERLKelepfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
602-783 |
1.40e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 602 EREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQgEVEKLQADCSGLQNECDSLRAEKSTL 681
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-DVASAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 682 M---QKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESRTRDLQKEYDDTQSL 758
Cdd:COG4913 688 AaleEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
|
170 180
....*....|....*....|....*
gi 528494938 759 LSDLRQRYEQTEQEKRSINDELEQC 783
Cdd:COG4913 768 RENLEERIDALRARLNRAEEELERA 792
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
505-703 |
1.85e-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: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 505 IHRELQEAQELANTGKQKclelQAMLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQR---ENTITTTREEL- 580
Cdd:COG4942 32 LQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIaelRAELEAQKEELa 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 581 --------YSAQEEILVLRHA------------MEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQAS- 639
Cdd:COG4942 108 ellralyrLGRQPPLALLLSPedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEEr 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528494938 640 FQLQSQHQERASQLQgeveKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLS 703
Cdd:COG4942 188 AALEALKAERQKLLA----RLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
55-108 |
3.42e-06 |
|
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) family; The Cep170 family includes Cep170 and Cep170B. Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438756 [Multi-domain] Cd Length: 102 Bit Score: 46.16 E-value: 3.42e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 528494938 55 HALVWFDHKTGKFYLQDTKSSNGTFINSQRLSrgseESPPCEVLSGDIIQFGVD 108
Cdd:cd22704 39 HAVITYDQIDNEFKIKDLGSLNGTFVNDSRIP----EQTYITLKLGDSIRFGYD 88
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
30-106 |
3.59e-06 |
|
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438750 [Multi-domain] Cd Length: 93 Bit Score: 45.87 E-value: 3.59e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528494938 30 IGRSVArcrpaqNNATFDCKVLSRNHALVwfDHKTGKFYLQDTKSSNGTFINSQRLSRGseesppcEVLSGDIIQFG 106
Cdd:cd22698 25 IGRSSN------NDIRLNDHSVSRHHARI--VRQGDKCNLTDLGSTNGTFLNGIRVGTH-------ELKHGDRIQLG 86
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
257-793 |
4.41e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 257 SLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEELTQkgL 336
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE--L 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 337 NEKKELQMRIEEMEEKEQALQARIEALQADndfTNERLTALQVRLEQLQEKSIKennsfaVRQLKEAVDSSINKLSNFDE 416
Cdd:PRK03918 289 KEKAEEYIKLSEFYEEYLDELREIEKRLSR---LEEEINGIEERIKELEEKEER------LEELKKKLKELEKRLEELEE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 417 VIDAhLQNNQTTVDNSLPSPDRLKENQIDAKEcDMSDTLSPSKEKSSDDTSDgqmEEQELNEPQNRVSLLKEMDRSLEAG 496
Cdd:PRK03918 360 RHEL-YEEAKAKKEELERLKKRLTGLTPEKLE-KELEELEKAKEEIEEEISK---ITARIGELKKEIKELKKAIEELKKA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 497 dtEQVIPHIHRELQEAQElantgkqkcLELQAMLEEERKTNRQQTEESAKQIRFLQTQLAKLqtDMEALREQRENTITTT 576
Cdd:PRK03918 435 --KGKCPVCGRELTEEHR---------KELLEEYTAELKRIEKELKEIEEKERKLRKELREL--EKVLKKESELIKLKEL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 577 REELYSAQEEILVLR-HAMEAATAERE---REITALQGDLSIVTAELDKWRQTAAKYEVEISNLQ-ASFQLQSQHQERAS 651
Cdd:PRK03918 502 AEQLKELEEKLKKYNlEELEKKAEEYEklkEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDeLEEELAELLKELEE 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 652 QLQGEVEKLQADCSGLQ---NECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQ 728
Cdd:PRK03918 582 LGFESVEELEERLKELEpfyNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEY 661
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528494938 729 QDAS----KLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDeLEQCKVNLKLLQDK 793
Cdd:PRK03918 662 EELReeylELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK-LEKALERVEELREK 729
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
51-106 |
5.64e-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: 45.62 E-value: 5.64e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528494938 51 LSRNHALVWF----DHKTGKFYLQDTKSSNGTFINSQRLsrgseesPP---CEVLSGDIIQFG 106
Cdd:cd22677 41 ISRYHAVLQYrgdaDDHDGGFYLYDLGSTHGTFLNKQRI-------PPkqyYRLRVGHVLKFG 96
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
582-752 |
5.76e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 582 SAQEEILVLRHAMEAATAER---EREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERAS------- 651
Cdd:COG4913 607 DNRAKLAALEAELAELEEELaeaEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERldassdd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 652 --QLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGD-------LENKLGS 722
Cdd:COG4913 687 laALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEerfaaalGDAVERE 766
|
170 180 190
....*....|....*....|....*....|
gi 528494938 723 IQDQHQQDASKLKIQLAQAESRTRDLQKEY 752
Cdd:COG4913 767 LRENLEERIDALRARLNRAEEELERAMRAF 796
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
52-106 |
7.70e-06 |
|
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: 45.33 E-value: 7.70e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 528494938 52 SRNH-ALVWfdHK-TGKFYLQDTKSSNGTFINSQRLsrgsEESPPCEVLSGDIIQFG 106
Cdd:cd22674 48 SRVHaALVY--HKhLNRVFLIDLGSTHGTFVGGIRL----EPHKPQQLPIDSTLRFG 98
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
178-730 |
1.16e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 178 REQML--EQKLATLQRLLASTQEAsESSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGIRKELVALTEDKHNYE---T 252
Cdd:COG4913 241 HEALEdaREQIELLEPIRELAERY-AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEarlD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 253 TAKESLRRV--------------LQEKIE-VVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDL 317
Cdd:COG4913 320 ALREELDELeaqirgnggdrleqLEREIErLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 318 TEKIKLAEDKHEELTQKGLNEKKELQMRIEEME-------EKEQALQARI-EALQADND---FTNErltALQVRLEQLQ- 385
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLErrksnipARLLALRDALaEALGLDEAelpFVGE---LIEVRPEEERw 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 386 ----EKSIkenNSFAVR---------QLKEAVDSsiNKLS---NFDEV-IDAHLQNNQTTVDNSLPspdrlkeNQIDAKE 448
Cdd:COG4913 477 rgaiERVL---GGFALTllvppehyaAALRWVNR--LHLRgrlVYERVrTGLPDPERPRLDPDSLA-------GKLDFKP 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 449 CDMSDTLspskekssddtsdgqmeEQELNEPQNRVSL-----LKEMDRSL-EAGDTEQviPHIHRELQEAQELA------ 516
Cdd:COG4913 545 HPFRAWL-----------------EAELGRRFDYVCVdspeeLRRHPRAItRAGQVKG--NGTRHEKDDRRRIRsryvlg 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 517 -NTGKQKclelqAMLEEERktnrqqtEESAKQIRFLQTQLAKLQTDMEALREQREntITTTREELYSAQEEILVLRHAME 595
Cdd:COG4913 606 fDNRAKL-----AALEAEL-------AELEEELAEAEERLEALEAELDALQERRE--ALQRLAEYSWDEIDVASAEREIA 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 596 AATAEREReITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQADCSGLQNECDSLR 675
Cdd:COG4913 672 ELEAELER-LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 528494938 676 AEKstlmqklnRLEEELDSSRER--SATLSSNLNALEKSQGDLENKLGSIQDQHQQD 730
Cdd:COG4913 751 LEE--------RFAAALGDAVERelRENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
564-783 |
1.36e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.18 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 564 ALREQRENTITTTREELYSAQEEILVLRHAMEAATAEREREIT-----ALQGDLSivtAELDKWRQTAAKYEVEISNLQA 638
Cdd:COG3096 781 AAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGghlavAFAPDPE---AELAALRQRRSELERELAQHRA 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 639 SFQlqsQHQERASQLQGEVEKLQadcsGLQNECDSLRAEksTLMQKLNRLEEELDSSRERSATLSSNLNALEKsqgdLEN 718
Cdd:COG3096 858 QEQ---QLRQQLDQLKEQLQLLN----KLLPQANLLADE--TLADRLEELREELDAAQEAQAFIQQHGKALAQ----LEP 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 719 KLGSIQDQHQQDASkLKIQLAQAESRTRDLQKE---------------YDDTQSLLSD-------LRQRYEQTEQEKRSI 776
Cdd:COG3096 925 LVAVLQSDPEQFEQ-LQADYLQAKEQQRRLKQQifalsevvqrrphfsYEDAVGLLGEnsdlnekLRARLEQAEEARREA 1003
|
....*..
gi 528494938 777 NDELEQC 783
Cdd:COG3096 1004 REQLRQA 1010
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
650-793 |
1.37e-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: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 650 ASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGS-IQDQHQ 728
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErARALYR 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528494938 729 QDASKLKI-QLAQAES------RTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLKLLQDK 793
Cdd:COG3883 98 SGGSVSYLdVLLGSESfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
592-793 |
2.24e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 592 HAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQAsfqlqsqhqeRASQLQGEVEKLQADCSGLQNEC 671
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER----------RIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 672 DSLRAEKSTLMQKLNRLEEELdSSRERSATLSSNLNALE--KSQGDLENK------LGSIQDQHQQDASKLKIQLAQAES 743
Cdd:COG4942 86 AELEKEIAELRAELEAQKEEL-AELLRALYRLGRQPPLAllLSPEDFLDAvrrlqyLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 528494938 744 RTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLKLLQDK 793
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
28-106 |
2.35e-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: 2.35e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528494938 28 VKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDhkTGKFYLQDTKSSNGTFINSQRlsrgsEESPPCEVLSGDIIQFG 106
Cdd:cd22680 23 VSIGRDP------ENVIVIPDPFVSRNHARITVD--SNEIYIEDLGSTNGTFVNDFK-----RIKGPAKLHPNDIIKLG 88
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
27-117 |
2.43e-05 |
|
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: 43.89 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 27 PVKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLsrgSEESPPCEVLSGDIIQFG 106
Cdd:cd22678 24 PLTIGRIQ------RGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESI---SPNGRPVVLSSGDVITLG 94
|
90
....*....|.
gi 528494938 107 vdvTENTRKVT 117
Cdd:cd22678 95 ---SETKILVR 102
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
229-785 |
3.31e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 229 KNQTEDGIRKELVALTEDKHNYETTAKESL-RRVLQEKIEVVRKLSEVERSLSNTEDEctHLREMNE-RTQEELRELANK 306
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFaRRQAAIKAEEARKADELKKAEEKKKAD--EAKKAEEkKKADEAKKKAEE 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 307 YNGAvneiKDLTEKIKLAEDKHEELTQKGLNEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERltalQVRLEQLQE 386
Cdd:PTZ00121 1314 AKKA----DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA----KKKADAAKK 1385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 387 KSIKennsfaVRQLKEAVDSSINKLSNFDEVIDAHLQNNQTtvdnslpspDRLKENQIDAKECDmsDTLSPSKEKSSDDT 466
Cdd:PTZ00121 1386 KAEE------KKKADEAKKKAEEDKKKADELKKAAAAKKKA---------DEAKKKAEEKKKAD--EAKKKAEEAKKADE 1448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 467 SDGQMEEQELNEPQNRVSLLKEMDRSLEAGDTEQviphihRELQEAQELANTGKQKCLELQAMLEEERKTNR-QQTEESA 545
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEA------KKADEAKKKAEEAKKKADEAKKAAEAKKKADEaKKAEEAK 1522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 546 KQIRFLQTQLAKLQTDMEALREQRENTITTTREELYSAQEeilvlRHAMEAATAEREREITALQGDLSIVTAELDKWRQT 625
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEE-----KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 626 AAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQADCSGLQNECDSLR-AEKSTLMQKLNRLE-EELDSSRERSATLS 703
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKkAEELKKAEEENKIKaAEEAKKAEEDKKKA 1677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 704 SNLNALEKSQGDLENKLGSiQDQHQQDASKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSIN-DELEQ 782
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKK-EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKkDEEEK 1756
|
...
gi 528494938 783 CKV 785
Cdd:PTZ00121 1757 KKI 1759
|
|
| FHA_CHFR |
cd22672 |
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ... |
49-105 |
3.51e-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: 3.51e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 528494938 49 KVLSRNHALVWFDHKtGKFYLQDTkSSNGTFINSQRLSRGSEesppCEVLSGDIIQF 105
Cdd:cd22672 39 KLVSGDHCKIIRDEK-GQVWLEDT-STNGTLVNKVKVVKGQK----VELKHGDVIYL 89
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
18-86 |
3.60e-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: 43.09 E-value: 3.60e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528494938 18 QERHVYLDEPVKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhkTGKFYLQDTKSSNGTFINSQRLS 86
Cdd:cd22694 8 GELRFDPGSSVRIGRD------PDADVRLDDPRVSRRHALLEFD--GDGWVYTDLGSRNGTYLNGRRVQ 68
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
25-108 |
4.38e-05 |
|
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar proteins; ZEP, also called protein ABA DEFICIENT 1, ABA1, protein IMPAIRED IN BABA-INDUCED STERILITY 3, protein LOW EXPRESSION OF OSMOTIC STRESS-RESPONSIVE GENES 6, or protein NON-PHOTOCHEMICAL QUENCHING 2, plays an important role in the xanthophyll cycle and abscisic acid (ABA) biosynthesis. It converts zeaxanthin into antheraxanthin and subsequently violaxanthin. ZEP is required for resistance to osmotic and drought stresses, ABA-dependent stomatal closure, seed development and dormancy, modulation of defense gene expression, and disease resistance and non-photochemical quencing (NPQ). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438754 [Multi-domain] Cd Length: 123 Bit Score: 43.57 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 25 DEPVKIGRsvarcRPAQNNAT----FDCKVLSRNHALVWFdhKTGKFYLQDTKSSNGTFINSQRLSR-GSEESPPCEVLS 99
Cdd:cd22702 31 KQPCIIGS-----DPHQAISGisvvIPSPQVSELHARITC--KNGAFFLTDLGSEHGTWINDNEGRRyRAPPNFPVRLHP 103
|
....*....
gi 528494938 100 GDIIQFGVD 108
Cdd:cd22702 104 SDVIEFGSD 112
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
531-746 |
5.02e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 531 EEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQRENT---ITTTREELYSAQEEILVLRHAMEAATAEREREITA 607
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELqaeLEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 608 LQ---GDLSIVTAELDkwrqtAAKYEVEISNLQASFQLQSQHQErasqlqgEVEKLQADCSGLQNECDSLRAEKSTLMQK 684
Cdd:COG3883 95 LYrsgGSVSYLDVLLG-----SESFSDFLDRLSALSKIADADAD-------LLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528494938 685 LNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESRTR 746
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
658-787 |
5.43e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 658 EKLQAdcsgLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLS--SNLNALEKSQGDLENKLGSIQDQHQQ-DASKl 734
Cdd:COG4913 610 AKLAA----LEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERlDASS- 684
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 528494938 735 kIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNL 787
Cdd:COG4913 685 -DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-709 |
5.77e-05 |
|
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: 46.97 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 263 QEKIEVVRKLSEVERSLSNTEDEcthLREMNERTQ--EELRELANKYNGAVNEIKDLtEKIKLAEDKHEELtqkglNEKK 340
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDI---LNELERQLKslERQAEKAERYKELKAELREL-ELALLVLRLEELR-----EELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 341 ELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEKSikennsFAVRQLKEAVDSSINKLSNFDEVIDA 420
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL------YALANEISRLEQQKQILRERLANLER 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 421 HLQNNQTTVDNSLPSPDRLKENqidakecdmsdtLSPSKEKSSDDTSDGQMEEQELNEpqnrvsllkemdrsleagdTEQ 500
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEE------------LAELEEKLEELKEELESLEAELEE-------------------LEA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 501 VIPHIHRELQEAQELANTGKQKCLELqamleeerktnRQQTEESAKQIRFLQTQLaklqtdmEALREQRENTITTTREEL 580
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQL-----------ELQIASLNNEIERLEARL-------ERLEDRRERLQQEIEELL 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 581 YSAQEeilVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEveisnlQASFQLQSQHQERASQLQGeVEKL 660
Cdd:TIGR02168 428 KKLEE---AELKELQAELEELEEELEELQEELERLEEALEELREELEEAE------QALDAAERELAQLQARLDS-LERL 497
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 528494938 661 QADCSGLQNECDSLRAEKSTLMQKLNRLEE--ELDSSRER--SATLSSNLNAL 709
Cdd:TIGR02168 498 QENLEGFSEGVKALLKNQSGLSGILGVLSEliSVDEGYEAaiEAALGGRLQAV 550
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
289-781 |
6.90e-05 |
|
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: 46.50 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 289 LREMNERTQEELRELANKyNGAVNEIKDLTEKIKLAEDKHEELTQKGLNEKKELQMRIEEMEEKEQALQARIEALQADND 368
Cdd:TIGR00618 172 LFPLDQYTQLALMEFAKK-KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKRE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 369 FTNERLTALQVRLEQLQEKSIKENNSFAVRQLKEAVDSSINKLSNFDEVID-AHLQNNQTTVDNSLPSPDRLKENQIDAK 447
Cdd:TIGR00618 251 AQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAvTQIEQQAQRIHTELQSKMRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 448 ECDMSDTLSPSKEKSSDDTsdgQMEEQELNEPQNRVSLLKEMDRSLEAGDTEqvipHIHRElqeaQELANTGKQKCLELQ 527
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQT---LHSQEIHIRDAHEVATSIREISCQQHTLTQ----HIHTL----QQQKTTLTQKLQSLC 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 528 AMLEEERKTNRQQTEESAKQiRFLQTQLAKLQTDMEALREQRENTITTTREElysAQEEILVLRHAMEAATAEREREitA 607
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAF-RDLQGQLAHAKKQQELQQRYAELCAAAITCT---AQCEKLEKIHLQESAQSLKERE--Q 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 608 LQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQADCSG-------LQNECDSLRAEKST 680
Cdd:TIGR00618 474 QLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRgeqtyaqLETSEEDVYHQLTS 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 681 LMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDaSKLKIQLAQAESRTRDLQKEYDDTQSLLS 760
Cdd:TIGR00618 554 ERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKL-SEAEDMLACEQHALLRKLQPEQDLQDVRL 632
|
490 500
....*....|....*....|.
gi 528494938 761 DLRQRYEQTEQEKRSINDELE 781
Cdd:TIGR00618 633 HLQQCSQELALKLTALHALQL 653
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
256-386 |
6.98e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.39 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 256 ESLRRVLQEKIEvvrklSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEELTQKg 335
Cdd:COG2433 376 LSIEEALEELIE-----KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERE- 449
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 528494938 336 LNEKKElQMRIEEMEEKE-QALQARIEALQADNDFTNERLTALQVRLEQLQE 386
Cdd:COG2433 450 LSEARS-EERREIRKDREiSRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
683-793 |
8.96e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 8.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 683 QKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQ------------DQHQQDASKLKIQLAQAESRTRD--- 747
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlaeyswdeidvASAEREIAELEAELERLDASSDDlaa 689
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 528494938 748 LQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLKLLQDK 793
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
473-663 |
9.11e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 9.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 473 EQELNEPQNRVSLLKEMDRSLEAG--DTEQVIPHIHRELQEAQELANTGKQKCLELQAMLEEERKTNRQQTEESAKQIRF 550
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQlaALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 551 LQ-----------------TQLAKLQTDMEAL---REQRENTITTTREELYSAQEEILVLRHAMEAATAEREREITALQG 610
Cdd:COG4942 113 LYrlgrqpplalllspedfLDAVRRLQYLKYLapaRREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 528494938 611 DLSIVTAELDKWRQTAAKYEVEISNLQASfqlqsqhqerASQLQGEVEKLQAD 663
Cdd:COG4942 193 LKAERQKLLARLEKELAELAAELAELQQE----------AEELEALIARLEAE 235
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
30-106 |
9.56e-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: 42.13 E-value: 9.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528494938 30 IGRSVarcrpaQNNATFDCKVLSRNHALvwFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEesppCEVLSGDIIQFG 106
Cdd:cd22682 24 IGRSV------ESQVQIDDDSVSRYHAK--LAVNPSAVSIIDLGSTNGTIVNGKKIPKLAS----CDLQNGDQIKIG 88
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
617-782 |
1.09e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 617 AELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQADCSGLQNEcdslraeksTLMQKLNRLEEELDSSR 696
Cdd:PRK04863 837 AELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADE---------TLADRVEEIREQLDEAE 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 697 ERSATLSSNLNALEKsqgdLENKLGSIQdQHQQDASKLKIQLAQAESRTRDLQKE---------------YDDTQSLLSD 761
Cdd:PRK04863 908 EAKRFVQQHGNALAQ----LEPIVSVLQ-SDPEQFEQLKQDYQQAQQTQRDAKQQafaltevvqrrahfsYEDAAEMLAK 982
|
170 180
....*....|....*....|....*...
gi 528494938 762 -------LRQRYEQTEQEKRSINDELEQ 782
Cdd:PRK04863 983 nsdlnekLRQRLEQAEQERTRAREQLRQ 1010
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
253-782 |
1.10e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.10 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 253 TAKESLRR------VLQEKIEVVRKLSEVERSLSNtedecthlremNERTQEELRELANKYNGAVNEIKDLTEKIKLAED 326
Cdd:COG3096 496 TARELLRRyrsqqaLAQRLQQLRAQLAELEQRLRQ-----------QQNAERLLEEFCQRIGQQLDAAEELEELLAELEA 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 327 KHEELTQKgLNEKKELQMrieEMEEKEQALQARI--------------EALQADNDFTNERLT-------ALQVRLEQLQ 385
Cdd:COG3096 565 QLEELEEQ-AAEAVEQRS---ELRQQLEQLRARIkelaarapawlaaqDALERLREQSGEALAdsqevtaAMQQLLERER 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 386 EKSIKENNsfaVRQLKEAVDSSINKLSNFDEVIDAHLQN--------------NQTTVDNS---------------LPSP 436
Cdd:COG3096 641 EATVERDE---LAARKQALESQIERLSQPGGAEDPRLLAlaerlggvllseiyDDVTLEDApyfsalygparhaivVPDL 717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 437 DRLKEnQIDAKECDMSDTLSPSKEKSSDDTSDGQMEEQE------LNEPQNRVSLLKEMDRSLEAGdTEQVIPHIHRELQ 510
Cdd:COG3096 718 SAVKE-QLAGLEDCPEDLYLIEGDPDSFDDSVFDAEELEdavvvkLSDRQWRYSRFPEVPLFGRAA-REKRLEELRAERD 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 511 E-AQELANT--GKQKCLELQAMLEEERKTNRQQTEES--AKQIRFLQTQLAKLQTDMEALREQrentITTTREELYSAQE 585
Cdd:COG3096 796 ElAEQYAKAsfDVQKLQRLHQAFSQFVGGHLAVAFAPdpEAELAALRQRRSELERELAQHRAQ----EQQLRQQLDQLKE 871
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 586 EILVLR------HAMEAAT-AEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVE 658
Cdd:COG3096 872 QLQLLNkllpqaNLLADETlADRLEELREELDAAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQR 951
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 659 KLQA------------------DCSGLQNECDSLrAEKstLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKL 720
Cdd:COG3096 952 RLKQqifalsevvqrrphfsyeDAVGLLGENSDL-NEK--LRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSR 1028
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528494938 721 GSIQDQHQ---QDASKLKIQL-AQAESRTRDlqkEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQ 782
Cdd:COG3096 1029 DAKQQTLQeleQELEELGVQAdAEAEERARI---RRDELHEELSQNRSRRSQLEKQLTRCEAEMDS 1091
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
579-753 |
1.10e-04 |
|
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: 44.53 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 579 ELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQAsfqlqsqHQERASQLQGEVE 658
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA-------RIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 659 K---LQAdcsgLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLK 735
Cdd:COG1579 87 NnkeYEA----LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|....*....
gi 528494938 736 IQLAQAESRT-RDLQKEYD 753
Cdd:COG1579 163 AEREELAAKIpPELLALYE 181
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
5-110 |
1.49e-04 |
|
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: 41.45 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 5 LAVFSCRPnshpFQERHVYLDE-PVKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTgkFYLQDTKSSNGTFINSQ 83
Cdd:cd22665 3 LKVFSQAH----GPEKDFPLYEgENVIGRD------PSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNK 70
|
90 100
....*....|....*....|....*....
gi 528494938 84 RLSrgseeSPPC--EVLSGDIIQFGvDVT 110
Cdd:cd22665 71 VRL-----KPNVryELIDGDLLLFG-DVK 93
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
450-782 |
1.53e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.71 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 450 DMSDTLSPSKEKSSDDTSDGQMEEQELNEPQNRVSLLKEMDRSLEAGDteqviphihrELQEAQELANtgkqkclELQAM 529
Cdd:COG3096 310 EMARELEELSARESDLEQDYQAASDHLNLVQTALRQQEKIERYQEDLE----------ELTERLEEQE-------EVVEE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 530 LEEERKTNRQQTEESAKQIRFLQTQLAKLQTDME--------------ALREQR-------------ENTITTTREELYS 582
Cdd:COG3096 373 AAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDvqqtraiqyqqavqALEKARalcglpdltpenaEDYLAAFRAKEQQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 583 AQEEILVLRHAMEAATAEREREITALQGDLSIV--TAELDKW---RQTAAKYEVEISNLQASFQLQSQHQE--RASQLQG 655
Cdd:COG3096 453 ATEEVLELEQKLSVADAARRQFEKAYELVCKIAgeVERSQAWqtaRELLRRYRSQQALAQRLQQLRAQLAEleQRLRQQQ 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 656 EVEKLQADCSGLQNEC----DSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLEnKLGSIQDQHQQDA 731
Cdd:COG3096 533 NAERLLEEFCQRIGQQldaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELA-ARAPAWLAAQDAL 611
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 528494938 732 SKLKIQLAQAESRTRDLQkeyDDTQSLLSDLRQRY---EQTEQEKRSINDELEQ 782
Cdd:COG3096 612 ERLREQSGEALADSQEVT---AAMQQLLEREREATverDELAARKQALESQIER 662
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
172-603 |
1.61e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 45.51 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 172 LQEALHREqmLEQKLATLQRLLASTQEASESSWQALIDE----DRLLSRLEVM-GNQLQAYSKNQTEDGIRKELVALTED 246
Cdd:pfam07111 134 LEEGSQRE--LEEIQRLHQEQLSSLTQAHEEALSSLTSKaeglEKSLNSLETKrAGEAKQLAEAQKEAELLRKQLSKTQE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 247 KHNYETTAKESLRRVLQEKI--EVVRKLSEVERSlsNTEDECTHLREMNERTQEELRELANKYNGAVNEI----KDLTEK 320
Cdd:pfam07111 212 ELEAQVTLVESLRKYVGEQVppEVHSQTWELERQ--ELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLalqeEELTRK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 321 IKLAEDKHEELTQKG---LNEKKE------LQMRIEEMEEKEQALQARIEALQADNDFTN-------------------- 371
Cdd:pfam07111 290 IQPSDSLEPEFPKKCrslLNRWREkvfalmVQLKAQDLEHRDSVKQLRGQVAELQEQVTSqsqeqailqralqdkaaeve 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 372 -ERLTA--LQVRLEQLQEK---------SIKENNSFAVRQLKEAVDSSINKLSNFDEVID--AHLQNNQTTVDNSLPSPD 437
Cdd:pfam07111 370 vERMSAkgLQMELSRAQEArrrqqqqtaSAEEQLKFVVNAMSSTQIWLETTMTRVEQAVAriPSLSNRLSYAVRKVHTIK 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 438 RLKENQIDAKECDMSDtlSPSKEKSSDDTSDGQMEEQELNEPQNRVS---------LLKEMDRSLEAGDTE-----QVIP 503
Cdd:pfam07111 450 GLMARKVALAQLRQES--CPPPPPAPPVDADLSLELEQLREERNRLDaelqlsahlIQQEVGRAREQGEAErqqlsEVAQ 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 504 HIHRELQEAQE-LANTGKQKCLELQAMLE--EERKTNRQQ-TEESAKQIRFLQTQLAKLQTdmeALREQRENTITTTREE 579
Cdd:pfam07111 528 QLEQELQRAQEsLASVGQQLEVARQGQQEstEEAASLRQElTQQQEIYGQALQEKVAEVET---RLREQLSDTKRRLNEA 604
|
490 500
....*....|....*....|....
gi 528494938 580 LYSAQEEILVLRHAMEAATAERER 603
Cdd:pfam07111 605 RREQAKAVVSLRQIQHRATQEKER 628
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
52-107 |
1.64e-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: 41.54 E-value: 1.64e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528494938 52 SRNHALVWFDHKTG---------KFYLQDTkSSNGTFINSQRLSRGSEesppCEVLSGDIIQFGV 107
Cdd:cd22667 40 SRKHATLTVLHPEAnlsdpdtrpELTLKDL-SKYGTFVNGEKLKGGSE----VTLKDGDVITFGV 99
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
253-692 |
2.14e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 253 TAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRelankyngavneikdLTEKIKLAEDKHEELT 332
Cdd:PRK04863 297 TSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALR---------------QQEKIERYQADLEELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 333 QKgLNEKKELqmrIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEKSIKENNsfAVRQLKEAvdSSINKLS 412
Cdd:PRK04863 362 ER-LEEQNEV---VEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQ--AVQALERA--KQLCGLP 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 413 NFdevidahlqnnqtTVDNslpSPDRLKENQidAKECDMSDTLSPSKEK-SSDDTSDGQMEEQElnepQNRVSLLKEMDR 491
Cdd:PRK04863 434 DL-------------TADN---AEDWLEEFQ--AKEQEATEELLSLEQKlSVAQAAHSQFEQAY----QLVRKIAGEVSR 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 492 SlEAGDTEQVIPHIHRELQEAQELANTGKQKCLELQAMLEEERKTNRQQTEESAKQIRFLQTqlaklQTDMEALREQREN 571
Cdd:PRK04863 492 S-EAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDD-----EDELEQLQEELEA 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 572 TITTTREELYSAQEEILVLRHAMEAATAEREReitalqgdlsiVTAELDKWR--QTAAKYEVEIS-----NLQASFQLQS 644
Cdd:PRK04863 566 RLESLSESVSEARERRMALRQQLEQLQARIQR-----------LAARAPAWLaaQDALARLREQSgeefeDSQDVTEYMQ 634
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 528494938 645 QHQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEEL 692
Cdd:PRK04863 635 QLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAERF 682
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
258-387 |
2.44e-04 |
|
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: 43.37 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 258 LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEEL-TQKGL 336
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrNNKEY 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 528494938 337 N----EKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEK 387
Cdd:COG1579 92 EalqkEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
234-387 |
2.77e-04 |
|
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: 43.37 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 234 DGIRKELVALTEdkhnyETTAKESLRRVLQEKIEVVRK-LSEVERSLSNTEDECTHLREMNERTQEELRELAN--KYNGA 310
Cdd:COG1579 20 DRLEHRLKELPA-----ELAELEDELAALEARLEAAKTeLEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEAL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528494938 311 VNEIKDLTEKIKLAEDKHEELtqkgLNEKKELQMRIEEMEEKEQALQARIEALQADNDftnERLTALQVRLEQLQEK 387
Cdd:COG1579 95 QKEIESLKRRISDLEDEILEL----MERIEELEEELAELEAELAELEAELEEKKAELD---EELAELEAELEELEAE 164
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
1-106 |
3.07e-04 |
|
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442679 [Multi-domain] Cd Length: 402 Bit Score: 43.98 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 1 MPSALAVFSCRPNSHPFQERHVYLDEPVKIGRSvARC-----RPAQnnatfdckVLSRNHALVWFDHktGKFYLQDTkSS 75
Cdd:COG3456 1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRS-ADCdwvlpDPDR--------SVSRRHAEIRFRD--GAFCLTDL-ST 68
|
90 100 110
....*....|....*....|....*....|....
gi 528494938 76 NGTFIN--SQRLSRGSEesppcEVLS-GDIIQFG 106
Cdd:COG3456 69 NGTFLNgsDHPLGPGRP-----VRLRdGDRLRIG 97
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
578-788 |
3.76e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 578 EELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQtaakyevEISNLQASFQLQSQHQERASQLQGEV 657
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEK-------EVKELEELKEEIEELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 658 EKLQADCSGLQNECDSLRAEKSTLMQKLNRLeEELDSSRERSATLS-------SNLNALEKSQGDLENKLGSIQDQHQQD 730
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSefyeeylDELREIEKRLSRLEEEINGIEERIKEL 333
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 528494938 731 ASKlkiqlaqaESRTRDLQKEYDDTQSLLSDLRQRyEQTEQEKRSINDELEQCKVNLK 788
Cdd:PRK03918 334 EEK--------EERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLT 382
|
|
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
53-106 |
3.91e-04 |
|
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 (FHAD1) and similar proteins; FHAD1, also called FHA domain-containing protein 1, is an uncharacterized FHA domain-containing protein. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438752 [Multi-domain] Cd Length: 96 Bit Score: 40.32 E-value: 3.91e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 528494938 53 RNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPcevlsGDIIQFG 106
Cdd:cd22700 36 EQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAP-----GDVLRFG 84
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
298-793 |
4.00e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 298 EELRELANKYNGAVNEIKDLTEKIKL---AEDKHEELTQKG--LNEKKELQ--MRIEEMEEKEQALQARIEALQADNDFT 370
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELlepIRELAERYAAARerLAELEYLRaaLRLWFAQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 371 NERLTALQVRLEQLQEKsikennsfaVRQLKEAvdssinklsnfdevidahLQNNQTtvdnslpspDRLK--ENQIDAKe 448
Cdd:COG4913 308 EAELERLEARLDALREE---------LDELEAQ------------------IRGNGG---------DRLEqlEREIERL- 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 449 cdmsdtlspskekssddtsdgqmeEQELNEPQNRVSLLKEMDRSLEAGdteqvIPHIHRELQEAQELANtgkqkclELQA 528
Cdd:COG4913 351 ------------------------ERELEERERRRARLEALLAALGLP-----LPASAEEFAALRAEAA-------ALLE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 529 MLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALReQRENTITttreelysaqEEILVLRHAMEAATAEREREITAL 608
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE-RRKSNIP----------ARLLALRDALAEALGLDEAELPFV 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 609 qGDLSIVTAELDKWRQTA--------------AKYEVE----ISNLQASFQLQSQH-QERASQLQGE-------VEKLQA 662
Cdd:COG4913 464 -GELIEVRPEEERWRGAIervlggfaltllvpPEHYAAalrwVNRLHLRGRLVYERvRTGLPDPERPrldpdslAGKLDF 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 663 DCSGLQN-----------------------------------------ECDSLRAEKSTLM------QKLNRLEEELDSS 695
Cdd:COG4913 543 KPHPFRAwleaelgrrfdyvcvdspeelrrhpraitragqvkgngtrhEKDDRRRIRSRYVlgfdnrAKLAALEAELAEL 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 696 RERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAE-SRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKR 774
Cdd:COG4913 623 EEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiAELEAELERLDASSDDLAALEEQLEELEAELE 702
|
570
....*....|....*....
gi 528494938 775 SINDELEQCKVNLKLLQDK 793
Cdd:COG4913 703 ELEEELDELKGEIGRLEKE 721
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
16-111 |
5.54e-04 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaB and similar proteins; FhaB, also called FtsZ-interacting protein A (FipA), is a putative virulence factor involved in regulating cell shape. It can interact with polyketide-associated protein PapA5, a putative membrane protein involved in the biosynthesis of virulence enhancing lipids. FhaB regulates growth and cell division. It is probably required for divisomal protein assembly under oxidative stress. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438745 [Multi-domain] Cd Length: 91 Bit Score: 39.59 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 16 PFQERHVYLD-EPVKIGRSvarcrpAQNNATFDCKVLSRNHALVWFdhKTGKFYLQDTKSSNGTFINSQRLSRgseespP 94
Cdd:cd22693 7 TLQGQTFPIDkSGITIGRA------DDNDLVLSDDFVSSRHARIYL--QGSSWYLEDLGSTNGTFVNGNRVTQ------P 72
|
90
....*....|....*..
gi 528494938 95 CEVLSGDIIQFGVDVTE 111
Cdd:cd22693 73 VVVQPGDTIRIGATVFE 89
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
190-799 |
5.82e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 190 QRLLASTQEASESSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGIRKELVALTEDKHNYET----TAKESLRRVLQEK 265
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNeeriDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 266 IEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTE-KIKLAEDKHEELTQKGLNEKKELQM 344
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLErRKVDDEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 345 RIEEMEEKEQALqARIEALQADNDFTNERLTALQVRLEQLQEKSIKENNSFAVRQLKEAVDSSINKLsnfdevidahLQN 424
Cdd:pfam02463 333 EKEEIEELEKEL-KELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE----------LKS 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 425 NQTTVDNSLpspDRLKENQIDAKEcdmsdtlspSKEKSSDDTSDGQMEEQELNEPQNRVSLLKEMDRSLEAGDTEQVIPH 504
Cdd:pfam02463 402 EEEKEAQLL---LELARQLEDLLK---------EEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 505 IHRELQEAQELANTGKQKcLELQAMLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQRENTITTTREELYSAQ 584
Cdd:pfam02463 470 SEDLLKETQLVKLQEQLE-LLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTA 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 585 EEILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAK---------------------YEVEISNLQASFQLQ 643
Cdd:pfam02463 549 VIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKsiavleidpilnlaqldkatlEADEDDKRAKVVEGI 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 644 SQHQERASQLQGEVEKLQADCSGLQNEcdSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSI 723
Cdd:pfam02463 629 LKDTELTKLKESAKAKESGLRKGVSLE--EGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQ 706
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528494938 724 QDQHQQDASKLKIQLAQAESRTRDLQK---EYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLKLLQDKGSNSGW 799
Cdd:pfam02463 707 REKEELKKLKLEAEELLADRVQEAQDKineELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEK 785
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
645-782 |
5.87e-04 |
|
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: 42.22 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 645 QHQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALeKSQGDLENKLGSIQ 724
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNNKEYEALQKEIE 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 528494938 725 DQhQQDASKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQ 782
Cdd:COG1579 100 SL-KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| FHA_RAD53-like_rpt2 |
cd22690 |
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
12-103 |
6.00e-04 |
|
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: 39.97 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 12 PNSHPfqerHVYL-DEPVKIGRSvarcrpAQNNATFDCKVLSRNHALVWFD-HKTGK--FYLQDTkSSNGTFINSQRLSR 87
Cdd:cd22690 8 NPSYP----DIELtQNTTFIGRS------KDCDEEITDPRISKHHCIITRKrSGKGLddVYVTDT-STNGTFINNNRLGK 76
|
90
....*....|....*.
gi 528494938 88 GSEesppCEVLSGDII 103
Cdd:cd22690 77 GSQ----SLLQDGDEI 88
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
49-112 |
7.24e-04 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 (PML1) and similar proteins; PML1 is an FHA domain-containing protein required for efficient splicing and pre-mRNA nuclear retention. It is a component of the pre-mRNA retention and splicing (RES) complex composed of at least BUD13, IST3, and PML1. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438733 [Multi-domain] Cd Length: 129 Bit Score: 40.50 E-value: 7.24e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528494938 49 KVLSRNHALVWFDHKTG--KFYLQDTKSSNGTFINsqrlsrgSEESPPC---EVLSGDIIQFGVDVTEN 112
Cdd:cd22681 64 ETCSKQHCVIQFRNVKGilKPYIMDLDSSNGTCLN-------DNVIPSSryvELRSGDVITFSKSNDYE 125
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
469-790 |
7.71e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.42 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 469 GQMEEQELNEPQNRVSLLKEMDRSLEAGDTEQVIPHIHRELQEAQELANTGKQKCLELQAMLEEERKTNRQQtEESAKQI 548
Cdd:pfam02463 142 GKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYY-QLKEKLE 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 549 RFLQTQLAKLQTDMEALREQRENTITTTREELYSAQEEILVLRHAMEAATAEREREITALQGDLSivtaelDKWRQTAAK 628
Cdd:pfam02463 221 LEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE------EELKLLAKE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 629 YEVEISNLQASFQLQSQHQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNA 708
Cdd:pfam02463 295 EEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 709 LEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLK 788
Cdd:pfam02463 375 LLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELE 454
|
..
gi 528494938 789 LL 790
Cdd:pfam02463 455 KQ 456
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
532-793 |
8.29e-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: 43.13 E-value: 8.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 532 EERKTNRQQTEESAKQIRFLQTQLAKLQTDmealREQRENTITTTREELYSAQEEILVLRHAMEAATAEREREITALQGD 611
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 612 LSIVTAELDKWRQTAAKYEVEISNLQAsfQLQSQHQERASQLQGEVEKLQADcsglQNECDSLRAEKSTLMQKLNRLEEE 691
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELNK--KIKDLGEEEQLRVKEKIGELEAE----IASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 692 LDSSRErsatlssnlnaleKSQGDLENKLGSIQDQhqqdasklKIQLAQAESRTRDLQKEYDDtqsllsdLRQRYEQTEQ 771
Cdd:TIGR02169 327 LEAEID-------------KLLAEIEELEREIEEE--------RKRRDKLTEEYAELKEELED-------LRAELEEVDK 378
|
250 260
....*....|....*....|..
gi 528494938 772 EKRSINDELEQCKVNLKLLQDK 793
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKRE 400
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
507-773 |
9.63e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 9.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 507 RELQEAQELANTGKQKCLELQAmleeERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQRENTITTTREELYSAQEE 586
Cdd:pfam15921 135 RESQSQEDLRNQLQNTVHELEA----AKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSM 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 587 ILVLRHAMEAATA----EREREITALQGDLSIVTAELDKWRqTAAKYEVEIsnlqasfqLQSQHQERASQLQGEVEklqA 662
Cdd:pfam15921 211 STMHFRSLGSAISkilrELDTEISYLKGRIFPVEDQLEALK-SESQNKIEL--------LLQQHQDRIEQLISEHE---V 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 663 DCSGLQNECDSLRAEKSTLMQKLNRLEEEldsSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAE 742
Cdd:pfam15921 279 EITGLTEKASSARSQANSIQSQLEIIQEQ---ARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLAN 355
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 528494938 743 SRTRDLQKEYDD-----------TQSLLSDLRQRYEQTEQEK 773
Cdd:pfam15921 356 SELTEARTERDQfsqesgnlddqLQKLLADLHKREKELSLEK 397
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
163-366 |
1.36e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.98 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 163 QELFQLSQYLQEALHREQMLEQKLATLQRLlastqEASESSWQALIDEDRLLSRLEVMGNQLQ-AYSK-NQTEDGI---- 236
Cdd:COG0497 172 KELEELRADEAERARELDLLRFQLEELEAA-----ALQPGEEEELEEERRRLSNAEKLREALQeALEAlSGGEGGAldll 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 237 ---RKELVALTEDKHNYETTAkESLRRVLQEKIEVVRklsEVERSLSNTEDECTHLREMNERtQEELRELANKYNGAVNE 313
Cdd:COG0497 247 gqaLRALERLAEYDPSLAELA-ERLESALIELEEAAS---ELRRYLDSLEFDPERLEEVEER-LALLRRLARKYGVTVEE 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 528494938 314 IKDLTEKIKlaedkhEELTQkglnekkelqmrIEEMEEKEQALQARIEALQAD 366
Cdd:COG0497 322 LLAYAEELR------AELAE------------LENSDERLEELEAELAEAEAE 356
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
667-793 |
1.74e-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: 40.68 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 667 LQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLgsiqDQHQQDASKLKIQLAQAESrtr 746
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI----EEVEARIKKYEEQLGNVRN--- 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 528494938 747 dlQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLKLLQDK 793
Cdd:COG1579 88 --NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE 132
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
590-782 |
1.87e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 590 LRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEiSNLQASFQLQSQHQERASQLQGEVEKLQADCSGLQN 669
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQK-NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 670 ECDSLRAEKSTLMQKLNRLEE--ELDSSRERSATLSSNLNALEKSQGD-------LENKLGSIQDQHQQDASK----LKI 736
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPnhpdviaLRAQIAALRAQLQQEAQRilasLEA 320
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 528494938 737 QLAQAESRTRDLQKEYDDTQSLLSDL---RQRYEQTEQEKRSINDELEQ 782
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELYES 369
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
665-785 |
1.98e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.16 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 665 SGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESR 744
Cdd:smart00787 147 EGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKK 226
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 528494938 745 TRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKV 785
Cdd:smart00787 227 LEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
535-794 |
2.13e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 535 KTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQRENTITTTREELYSAQEEILvlrhAMEAATAEREREITALQGDLSI 614
Cdd:PHA02562 177 RELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAK----TIKAEIEELTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 615 VTAELDKWRQTAAKYEVEISNLQASFQLQSQHQER---ASQLQGEVEKLQadcsglqnecdSLRAEKSTLMQKLNRLEEE 691
Cdd:PHA02562 253 PSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGVCptcTQQISEGPDRIT-----------KIKDKLKELQHSLEKLDTA 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 692 LDSSRERSatlsSNLNALEKSQGDLENKLgsiqDQHQQDASKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQ 771
Cdd:PHA02562 322 IDELEEIM----DEFNEQSKKLLELKNKI----STNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVK 393
|
250 260
....*....|....*....|...
gi 528494938 772 EKRSINDELEQCKVNLKLLQDKG 794
Cdd:PHA02562 394 TKSELVKEKYHRGIVTDLLKDSG 416
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
256-398 |
2.25e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 256 ESLRRVLQEKI-EVVRKLSEVERSLSNTEDEcthLREMNERTQEELRELANKYNGAVNE--------IKDLTEKIKL--A 324
Cdd:PRK00409 526 EELERELEQKAeEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLEEAEKEAQQAIKEakkeadeiIKELRQLQKGgyA 602
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528494938 325 EDKHEELTQKglneKKELQMRIEEMEEKEQALQARIEALQAdndftNERltalqVRLEQLQEK----SIKENNSFAVR 398
Cdd:PRK00409 603 SVKAHELIEA----RKRLNKANEKKEKKKKKQKEKQEELKV-----GDE-----VKYLSLGQKgevlSIPDDKEAIVQ 666
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
507-787 |
2.67e-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: 41.31 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 507 RELQEAQELANTGKQKCL----ELQAMLEEERKTNRQQT------------------------EESAKQIRFLQTQLAKL 558
Cdd:pfam01576 731 RDLQARDEQGEEKRRQLVkqvrELEAELEDERKQRAQAVaakkkleldlkeleaqidaankgrEEAVKQLKKLQAQMKDL 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 559 QTDMEALREQRENTITTTRE----------ELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAK 628
Cdd:pfam01576 811 QRELEEARASRDEILAQSKEsekklknleaELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEAR 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 629 ---YEVEISNLQASFQLQSQHQERASQlqgEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELdssRERSATLSSN 705
Cdd:pfam01576 891 iaqLEEELEEEQSNTELLNDRLRKSTL---QVEQLTTELAAERSTSQKSESARQQLERQNKELKAKL---QEMEGTVKSK 964
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 706 LNAlekSQGDLENKLGSIQDQHQQDASklkiQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKV 785
Cdd:pfam01576 965 FKS---SIAALEAKIAQLEEQLEQESR----ERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKR 1037
|
..
gi 528494938 786 NL 787
Cdd:pfam01576 1038 QL 1039
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
509-793 |
2.85e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 509 LQEAQELANTGKQKCLELQAMLEEERKTNRQQTEES------AKQIRFLQTQLAKLQTDMEAL------REQRENTITTT 576
Cdd:TIGR00606 212 LKQYKEKACEIRDQITSKEAQLESSREIVKSYENELdplknrLKEIEHNLSKIMKLDNEIKALksrkkqMEKDNSELELK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 577 REELYSAQEEILV-LRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQsQHQERASQLQG 655
Cdd:TIGR00606 292 MEKVFQGTDEQLNdLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRH-QEHIRARDSLI 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 656 EVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLK 735
Cdd:TIGR00606 371 QSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILE 450
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 528494938 736 IQLAQAESRTRDLQKEYDDTQSLLS-DLRQRYEQTEQEKRSINDELEQCKVNLKLLQDK 793
Cdd:TIGR00606 451 KKQEELKFVIKELQQLEGSSDRILElDQELRKAERELSKAEKNSLTETLKKEVKSLQNE 509
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
172-383 |
3.11e-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: 40.01 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 172 LQEALHREQMLEQKLATLQRLLASTQEASESSwqalidEDRLLSRLEvmgNQLQAYSKNQTEDGIRKELvaltEDKHNYE 251
Cdd:pfam00261 24 LEEAEKRAEKAEAEVAALNRRIQLLEEELERT------EERLAEALE---KLEEAEKAADESERGRKVL----ENRALKD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 252 TTAKESLRRVLQEKIEVV----RKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDL---TEKIKLA 324
Cdd:pfam00261 91 EEKMEILEAQLKEAKEIAeeadRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLeasEEKASER 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 325 EDKHEElTQKGLNEK-KELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQ 383
Cdd:pfam00261 171 EDKYEE-QIRFLTEKlKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQ 229
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
310-687 |
3.54e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 310 AVNEIKDLTekiklAEDKheeLTQKGLNEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQvrlEQLQEKSI 389
Cdd:PRK11281 47 ALNKQKLLE-----AEDK---LVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALK---DDNDEETR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 390 KENNSFAVRQLKEAVDSSINKLSNfdevidahLQNNQTTVDNSLPS----PDR----LKENQIDAKEcdMSDTLSPSKEK 461
Cdd:PRK11281 116 ETLSTLSLRQLESRLAQTLDQLQN--------AQNDLAEYNSQLVSlqtqPERaqaaLYANSQRLQQ--IRNLLKGGKVG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 462 SSDDTSDGQME---EQELNEPQNrvSLLKemdRSLEAGDTEQVIphihreLQEAQELAnTGKQKCLE-----LQAMLEEE 533
Cdd:PRK11281 186 GKALRPSQRVLlqaEQALLNAQN--DLQR---KSLEGNTQLQDL------LQKQRDYL-TARIQRLEhqlqlLQEAINSK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 534 RktnRQQTEESAKQIRFLQtQLAKLQTDMEALREQRENT------ITTTREELYSAQEEILVlRHAMEAAT-AER--ERE 604
Cdd:PRK11281 254 R---LTLSEKTVQEAQSQD-EAARIQANPLVAQELEINLqlsqrlLKATEKLNTLTQQNLRV-KNWLDRLTqSERniKEQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 605 ITALQGDLsIVTAELDKWRQT--AAKYEVEISNLQASFQLQ----SQHQERASQLQGEVEKLQADCSG-----LQNECDS 673
Cdd:PRK11281 329 ISVLKGSL-LLSRILYQQQQAlpSADLIEGLADRIADLRLEqfeiNQQRDALFQPDAYIDKLEAGHKSevtdeVRDALLQ 407
|
410
....*....|....
gi 528494938 674 LRAEKSTLMQKLNR 687
Cdd:PRK11281 408 LLDERRELLDQLNK 421
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
712-787 |
3.63e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 712 SQGDLENKLGSIQ--DQHQQDASKLKIQLAQAESRTRDLQKEYDD-TQSLLSDLRQRYE-----QTEQEKRSINDELEQC 783
Cdd:PRK11281 61 VQQDLEQTLALLDkiDRQKEETEQLKQQLAQAPAKLRQAQAELEAlKDDNDEETRETLStlslrQLESRLAQTLDQLQNA 140
|
....
gi 528494938 784 KVNL 787
Cdd:PRK11281 141 QNDL 144
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
182-414 |
3.77e-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: 40.52 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 182 LEQKLATLQRLLASTQEASESSWQALIDEDRLLSRLEvmgNQLQAYSKNQTEdgIRKELVALTEDkhnyETTAKESLRRV 261
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALA---RRIRALEQELAA--LEAELAELEKE----IAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 262 LQEKIEVVRKLSEVERS-----LSNTEDECTHLR--EMNERTQEELRELANKYNGAVNEIKDLTEKIKlaedkheeltqk 334
Cdd:COG4942 103 KEELAELLRALYRLGRQpplalLLSPEDFLDAVRrlQYLKYLAPARREQAEELRADLAELAALRAELE------------ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 335 glNEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLEQLQEKSIKENNSFAVRQLKEAVDSSINKLSNF 414
Cdd:COG4942 171 --AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
531-638 |
4.46e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 531 EEERKTNRQQTEESAKQIRFLQTQLAKLQ---TDMEALREQRENTITTTREELYSAQEEilvlrhamEAATAEREREITA 607
Cdd:COG2433 398 EREKEHEERELTEEEEEIRRLEEQVERLEaevEELEAELEEKDERIERLERELSEARSE--------ERREIRKDREISR 469
|
90 100 110
....*....|....*....|....*....|.
gi 528494938 608 LQGDLSIVTAELDKWRQTAAKYEVEISNLQA 638
Cdd:COG2433 470 LDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
646-776 |
4.60e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 646 HQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNL---NALEKSQGDLENKlgS 722
Cdd:PRK04863 284 HLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALrqqEKIERYQADLEEL--E 361
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 528494938 723 IQDQHQQDASKL-KIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEqtEQEKRSI 776
Cdd:PRK04863 362 ERLEEQNEVVEEaDEQQEENEARAEAAEEEVDELKSQLADYQQALD--VQQTRAI 414
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
473-791 |
4.73e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 473 EQELNEPQNRVSLLKEMDRSLEagDTEQVIPHIHRELQEAQELANtgkQKCLELQAMLEEERKTNRQQTEESAKQIRFLQ 552
Cdd:COG4717 138 EAELAELPERLEELEERLEELR--ELEEELEELEAELAELQEELE---ELLEQLSLATEEELQDLAEELEELQQRLAELE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 553 TQLAKLQTDMEALREQRENTITTTREE-----------LYSAQEEILVLRHAMEAATAERERE---ITALQGDLSIVTAE 618
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENELEAAaleerlkearlLLLIAAALLALLGLGGSLLSLILTIagvLFLVLGLLALLFLL 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 619 LDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQADcsGLQNECDSLRaEKSTLMQKLNRLEEELDssRER 698
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE--ELLELLDRIE-ELQELLREAEELEEELQ--LEE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 699 SATLSSNLnaLEKSQGDLENKLGSIQDQHQQdASKLKIQLAQAESRTRDLQKEYDDTQSLLS--DLRQRYEQTEQEKRSI 776
Cdd:COG4717 368 LEQEIAAL--LAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEELEEL 444
|
330
....*....|....*
gi 528494938 777 NDELEQCKVNLKLLQ 791
Cdd:COG4717 445 EEELEELREELAELE 459
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
516-773 |
4.98e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.06 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 516 ANTGKQKCLELQAMLEEERKTNRQQteesakqirflQTQLAKLQtdmEALREQrENTITTTREELYSAQeeilvlrhame 595
Cdd:PRK11637 42 ASDNRDQLKSIQQDIAAKEKSVRQQ-----------QQQRASLL---AQLKKQ-EEAISQASRKLRETQ----------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 596 aataereREITALQGDLSIVTAELDKWRQTAAKYEVEIS-NLQASFQlQSQHQERASQLQGE----VEKLQA-------- 662
Cdd:PRK11637 96 -------NTLNQLNKQIDELNASIAKLEQQQAAQERLLAaQLDAAFR-QGEHTGLQLILSGEesqrGERILAyfgylnqa 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 663 ---DCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGsiQDQHQ-----QDASKL 734
Cdd:PRK11637 168 rqeTIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQ--KDQQQlselrANESRL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 528494938 735 KIQLAQAE--------------SRTRDLQKEYDDTQSllsdlrqRYEQTEQEK 773
Cdd:PRK11637 246 RDSIARAEreakaraereareaARVRDKQKQAKRKGS-------TYKPTESER 291
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
216-792 |
5.14e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 216 RLEVMGNQLQAYSKNQTEDGIRKELVALTEDKHNYETTaKESLRRVLQEKIEVVRKLSEVERSLSNTEDECthlremnER 295
Cdd:PRK01156 151 RKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYL-EEKLKSSNLELENIKKQIADDEKSHSITLKEI-------ER 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 296 TQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEELtqkglnekKELQMRIEEMEEKEQALQARIEALqadNDFTNErlt 375
Cdd:PRK01156 223 LSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI--------KTAESDLSMELEKNNYYKELEERH---MKIIND--- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 376 ALQVRLEQLQEKSIKENNSFAVRQLKEAVDSSINKlsnFDEVID--AHLQNNQTTVDNSLPSPDRLKeNQIDAKECDMSD 453
Cdd:PRK01156 289 PVYKNRNYINDYFKYKNDIENKKQILSNIDAEINK---YHAIIKklSVLQKDYNDYIKKKSRYDDLN-NQILELEGYEMD 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 454 TLSPSK------------EKSSDDTSDGQMEEQELNE--PQNRVSLLKEMDRSL-----EAGDTEQVIPHIHRELQEAQE 514
Cdd:PRK01156 365 YNSYLKsieslkkkieeySKNIERMSAFISEILKIQEidPDAIKKELNEINVKLqdissKVSSLNQRIRALRENLDELSR 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 515 LAN--TGKQKCLELQAMLEEErKTNRQQTEESAKQIRfLQTQLAKLQTDMEALREQRENTItttREELYSAQEEILVLRh 592
Cdd:PRK01156 445 NMEmlNGQSVCPVCGTTLGEE-KSNHIINHYNEKKSR-LEEKIREIEIEVKDIDEKIVDLK---KRKEYLESEEINKSI- 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 593 AMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYE-VEISNLQASFQ----------------LQSQHQERASQLQG 655
Cdd:PRK01156 519 NEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKsLKLEDLDSKRTswlnalavislidietNRSRSNEIKKQLND 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 656 EVEKLQADCSGLQNEcdslraeKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLEN--KLGSIQDQHQQDASK 733
Cdd:PRK01156 599 LESRLQEIEIGFPDD-------KSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNykKQIAEIDSIIPDLKE 671
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528494938 734 LKIQLAQAESRTRDLQKEYDDTQSLLSD-------LRQRYEQTEQEKRSINDELEQCKVNLKLLQD 792
Cdd:PRK01156 672 ITSRINDIEDNLKKSRKALDDAKANRARlestieiLRTRINELSDRINDINETLESMKKIKKAIGD 737
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
173-366 |
6.37e-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: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 173 QEALHREQMLEQKLATLQRLLASTQEasesswqalidedrllsRLEVMGNQLQAYSKNQTEdgIRKELVALTEDKHNYET 252
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLKELPA-----------------ELAELEDELAALEARLEA--AKTELEDLEKEIKRLEL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 253 TAKESLRRV--LQEKIEVVRKlsevERSLSNTEDECTHLREMNERTQEELRELankyngaVNEIKDLTEKIKLAEDKHEE 330
Cdd:COG1579 67 EIEEVEARIkkYEEQLGNVRN----NKEYEALQKEIESLKRRISDLEDEILEL-------MERIEELEEELAELEAELAE 135
|
170 180 190
....*....|....*....|....*....|....*.
gi 528494938 331 LTQKGLNEKKELQMRIEEMEEKEQALQARIEALQAD 366
Cdd:COG1579 136 LEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
314-488 |
8.60e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 40.03 E-value: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 314 IKDLTEKIKLAEDKHEELTQKG-----LNEKKELQMRIEEMEEKEQALQARIEALQadndfTNERLTALQVRLEQLQEKS 388
Cdd:PTZ00108 1104 VEKLNAELEKKEKELEKLKNTTpkdmwLEDLDKFEEALEEQEEVEEKEIAKEQRLK-----SKTKGKASKLRKPKLKKKE 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 389 IKENNSFAVRQLKEAVDSSINKLSNFDEVIDAHLQNNQTTVDNSLPSPDRLKENQIDAKECD-----MSDTLSPSKEKSS 463
Cdd:PTZ00108 1179 KKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVkrlksKKNNSSKSSEDND 1258
|
170 180
....*....|....*....|....*
gi 528494938 464 DDTSDGQMEEQELNEPQNRVSLLKE 488
Cdd:PTZ00108 1259 EFSSDDLSKEGKPKNAPKRVSAVQY 1283
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
229-771 |
8.64e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 229 KNQTEDGIRK---ELVALTEDKHNYettakeslRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELAn 305
Cdd:TIGR00606 586 INQTRDRLAKlnkELASLEQNKNHI--------NNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRA- 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 306 KYNGAVNEIKDLTEKIKLAEDKHEELTQKGLNEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQVRLE--- 382
Cdd:TIGR00606 657 MLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPgrq 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 383 ---QLQEKSIKEnnsfaVRQLKEAVDSSINKLSNfdevidaHLQNNQTTVDnslpspdrlkenqidakecdmsdTLSPSK 459
Cdd:TIGR00606 737 siiDLKEKEIPE-----LRNKLQKVNRDIQRLKN-------DIEEQETLLG-----------------------TIMPEE 781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 460 EKSSDDTSDGQMEEQELNEPQNRVSLLKEMDRSLEAGDTEQVIPHIHRELQEAQELANTGKQKcLELQAMLEEERKTNRQ 539
Cdd:TIGR00606 782 ESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSK-IELNRKLIQDQQEQIQ 860
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 540 QTEESAKQIRFLQTQLAKLQTDMEALREQRENTITTTRE---ELYSAQEEILVLRHAMEAATAEREREITA-------LQ 609
Cdd:TIGR00606 861 HLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSlirEIKDAKEQDSPLETFLEKDQQEKEELISSketsnkkAQ 940
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 610 GDLSIVTAELDK---WRQTAAKY------------EVEISNLQASFQLQSQHQERasqlqgevekLQADCSGLQNECDSL 674
Cdd:TIGR00606 941 DKVNDIKEKVKNihgYMKDIENKiqdgkddylkqkETELNTVNAQLEECEKHQEK----------INEDMRLMRQDIDTQ 1010
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 675 RAEKSTLMQKLNRL--EEELDSSRERSATLSSNLNALEKSQ-----GDLENKLGSIQDQH------QQDASKLKI----- 736
Cdd:TIGR00606 1011 KIQERWLQDNLTLRkrENELKEVEEELKQHLKEMGQMQVLQmkqehQKLEENIDLIKRNHvlalgrQKGYEKEIKhfkke 1090
|
570 580 590
....*....|....*....|....*....|....*....
gi 528494938 737 ----QLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQ 771
Cdd:TIGR00606 1091 lrepQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQ 1129
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
480-701 |
9.42e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 39.65 E-value: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 480 QNRVSLLKEMDRSLE-AGDTEQVI---PHIHRELQeaQELANTG---------------KQKCLELQA-MLEEERKTnrQ 539
Cdd:PRK10929 51 QSALNWLEERKGSLErAKQYQQVIdnfPKLSAELR--QQLNNERdeprsvppnmstdalEQEILQVSSqLLEKSRQA--Q 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 540 QTEESAKQIRFLQTQLAKLQTdmEALR-----EQRENTITTTREELYSAQeeiLVLRHAMEAATAER--EREITALQG-- 610
Cdd:PRK10929 127 QEQDRAREISDSLSQLPQQQT--EARRqlneiERRLQTLGTPNTPLAQAQ---LTALQAESAALKALvdELELAQLSAnn 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494938 611 --DLSIVTAELDKWRqtAAKYEVEISNLQAsfQLQSQHQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRL 688
Cdd:PRK10929 202 rqELARLRSELAKKR--SQQLDAYLQALRN--QLNSQRQREAERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQ 277
|
250
....*....|....*
gi 528494938 689 EEELD--SSRERSAT 701
Cdd:PRK10929 278 AQRMDliASQQRQAA 292
|
|
| |
