|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
3-130 |
3.82e-81 |
|
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and similar proteins; SLMAP, also called sarcolemmal-associated protein (SLAP), is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. It is a cardiac membrane protein that plays an important role in E-C coupling and the adrenergic response of the heart. Overexpression of the SLMAP gene has been associated with diabetes and endothelial dysfunction of macro- and micro-blood vessels. SLMAP contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438731 [Multi-domain] Cd Length: 126 Bit Score: 255.66 E-value: 3.82e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 3 SALAVFSCRPNSHPFQERHVYLDEPVKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINS 82
Cdd:cd22679 1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 528494940 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 |
5.98e-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: 5.98e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528494940 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLASTQEASESSWQALIDEDRLLSRLEVMGNQLQ 225
Cdd:cd21911 1 QELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQLS 63
|
|
| FHA_DMA-like |
cd22692 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest ... |
27-108 |
1.11e-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: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 27 PVKIGRSVARCRPAQNNAT-FDCKVLSRNHALVWfdHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCEVLSGDIIQF 105
Cdd:cd22692 38 QIHIGRYTERVRQAIYHPVvFKSKVVSRTHGCIK--VDEGNWYIKDVKSSSGTFLNHQRLSPASRTSKPYPLRDGDILQL 115
|
...
gi 528494940 106 GVD 108
Cdd:cd22692 116 GMD 118
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
163-763 |
3.00e-17 |
|
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: 87.03 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLASTQEASESSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGirKELVA 242
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL--EELEA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 243 LTEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELA--------NKYNGAVNEI 314
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLkkleeaelKELQAELEEL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 315 KDLTEKIKLAEDKHEELTQKGLNEKKELQMRIEEMEEKEQALQARIEALQA---DNDFTNERLTALQAVRQLKEAVDSSI 391
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERlqeNLEGFSEGVKALLKNQSGLSGILGVL 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 392 NKLSNFDE--------VIDAHLQNNQTTVDNS-----------------LPSPDRLKENQIDAKECDMSDTLSPSKEKSS 446
Cdd:TIGR02168 526 SELISVDEgyeaaieaALGGRLQAVVVENLNAakkaiaflkqnelgrvtFLPLDSIKGTEIQGNDREILKNIEGFLGVAK 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 447 D----------------------DTSDGQMEEQELNEPQNR-VSLLKEMDR-----SLEAGDTEQVIPHIHRELQEAQEL 498
Cdd:TIGR02168 606 DlvkfdpklrkalsyllggvlvvDDLDNALELAKKLRPGYRiVTLDGDLVRpggviTGGSAKTNSSILERRREIEELEEK 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 499 ANTGKQKCLELQ---AMLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALR---EQRENTITTTREELYSAQEEILV 572
Cdd:TIGR02168 686 IEELEEKIAELEkalAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEaevEQLEERIAQLSKELTELEAEIEE 765
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 573 L---RHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQlqsqhqerasQLQGEVEKLQADCSG 649
Cdd:TIGR02168 766 LeerLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA----------NLRERLESLERRIAA 835
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 650 LQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKiqlaQAESRTR 729
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR----ELESKRS 911
|
650 660 670
....*....|....*....|....*....|....
gi 528494940 730 DLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDEL 763
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
172-776 |
2.30e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 80.87 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 172 LQEALHREQMLEQKLATLQRLLASTQEASESSWQALIDEDRllsrlevmgnqlqaySKNQTEDGIRKELVALTEDKHNYE 251
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS---------------ELEEEIEELQKELYALANEISRLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 252 ttakeslrrvlQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEEL 331
Cdd:TIGR02168 302 -----------QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 332 TQKGLNEKKELQM---RIEEMEEKEQALQARIEALQADNDFTNERLTALQAVR--QLKEAVDSSINKLSNFDEVIDAHLQ 406
Cdd:TIGR02168 371 ESRLEELEEQLETlrsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIeeLLKKLEEAELKELQAELEELEEELE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 407 NNQTTVDNSLPSPDRLKEnQIDAKECDMSDTLSPSKEKSSDDTSDGQMEEQELNEPQNRVSLLKEmdRSLEAGDTEQVIP 486
Cdd:TIGR02168 451 ELQEELERLEEALEELRE-ELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN--QSGLSGILGVLSE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 487 HIH----------------------------RELQEAQELANTGKQKCLEL----------------------------- 509
Cdd:TIGR02168 528 LISvdegyeaaieaalggrlqavvvenlnaaKKAIAFLKQNELGRVTFLPLdsikgteiqgndreilkniegflgvakdl 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 510 ------------------------QAMLEEERKTNRQQT-------------------EESAKQIRFLQTQLAKLQTDME 546
Cdd:TIGR02168 608 vkfdpklrkalsyllggvlvvddlDNALELAKKLRPGYRivtldgdlvrpggvitggsAKTNSSILERRREIEELEEKIE 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 547 ALrEQRENTITTTREELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQ 626
Cdd:TIGR02168 688 EL-EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 627 SQH----QERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENK 702
Cdd:TIGR02168 767 EERleeaEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528494940 703 LGSIQDQHQQDA---SKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLKLLQDK 776
Cdd:TIGR02168 847 IEELSEDIESLAaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
468-775 |
7.22e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 78.95 E-value: 7.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 468 LLKEMDRSLEagdteqvipHIHRELQEAQ---ELANTGKQKCLELQAMLEEERKTNRQQTEESAKQirfLQTQLAKLQTD 544
Cdd:TIGR02168 194 ILNELERQLK---------SLERQAEKAErykELKAELRELELALLVLRLEELREELEELQEELKE---AEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 545 MEALREQrentITTTREELYSAQEEILVLRHAMEAATAErereITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQ 624
Cdd:TIGR02168 262 LQELEEK----LEELRLEVSELEEEIEELQKELYALANE----ISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 625 LQsqhQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLG 704
Cdd:TIGR02168 334 EL---AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 705 SIQDQHQQ---------------DASKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVN 769
Cdd:TIGR02168 411 RLEDRRERlqqeieellkkleeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
....*.
gi 528494940 770 LKLLQD 775
Cdd:TIGR02168 491 LDSLER 496
|
|
| FHA_VPS64-like |
cd22695 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ... |
6-126 |
9.97e-15 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 64 (VPS64) and similar proteins; This subfamily includes VPS64 (also called factor arrest protein 9 or FAR9) and factor arrest protein 10 (FAR10), which participate in the control of the re-entry into the cell cycle following pheromone treatment. VPS64 is also involved in vacuolar protein sorting. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438747 [Multi-domain] Cd Length: 133 Bit Score: 71.56 E-value: 9.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 6 AVFSCRPNSHPFQERHV---YLDEPVKIGRSVARCRPAQN---------------NATFDCKVLSRNHALVWFDHKTGKF 67
Cdd:cd22695 2 HILVLKSLNATFETKFLvvpFKPDGLKLGRPVTNSVNKNNsgskrdlfsqqvrpdNGNFDSRVLSRNHACLSCDPTTGKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 528494940 68 YLQDTKSSNGTFINSQRLSRGSeesppCEVLSGDIIQFGVDVTEntrKVTHGCIVSTIK 126
Cdd:cd22695 82 YIRDLKSSNGTFVNGQKIRQND-----VELKVGDEVDLGTDIDS---KIEHRKISAYVE 132
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
13-106 |
1.43e-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: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 13 NSHPFQERHVYLDEPVKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINSQRLsrgseeS 92
Cdd:cd00060 6 DGDGGGREFPLTKGVVTIGRS------PDCDIVLDDPSVSRRHARIEVDG--GGVYLEDLGSTNGTFVNGKRI------T 71
|
90
....*....|....
gi 528494940 93 PPCEVLSGDIIQFG 106
Cdd:cd00060 72 PPVPLQDGDVIRLG 85
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
28-105 |
2.68e-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: 2.68e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528494940 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 ... |
457-766 |
3.67e-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: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 457 QELNEPQNRVSLLKEmdrslEAGDTEQVIPHIHRELQEAQELANTGKQKCLELQA---MLEEERKTNRQQTEESAKQIRF 533
Cdd:TIGR02169 695 SELRRIENRLDELSQ-----ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEdlsSLEQEIENVKSELKELEARIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 534 LQTQLAKLQTDMEALREQRENTITTTREELYSAQEEILVlrhAMEAATAEREREITALQGDLSIvtaeLDKWRQTAAKYE 613
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVS---RIEARLREIEQKLNRLTLEKEY----LEKEIQELQEQR 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 614 VEISNLQASFQ-----LQSQHQERASQL---QGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATL 685
Cdd:TIGR02169 843 IDLKEQIKSIEkeienLNGKKEELEEELeelEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 686 SSNLNALEKSQGDLENKLGSIQDQHQQDAS--KLKIQLAQAESRTRDLQ-------KEYDDTQSLLSDLRQRYEQTEQEK 756
Cdd:TIGR02169 923 KAKLEALEEELSEIEDPKGEDEEIPEEELSleDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEER 1002
|
330
....*....|
gi 528494940 757 RSINDELEQC 766
Cdd:TIGR02169 1003 KAILERIEEY 1012
|
|
| CC1_SLMAP-like |
cd21868 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ... |
167-204 |
3.88e-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: 64.04 E-value: 3.88e-13
10 20 30
....*....|....*....|....*....|....*...
gi 528494940 167 QLSQYLQEALHREQMLEQKLATLQRLLASTQEASESSW 204
Cdd:cd21868 1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
489-765 |
1.29e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 489 HRELQEAQELantgkqkcLELQAMLEEERKTNRQQtEESAKQIRFLQTQLAKLQTD---MEALREQRENTITTTREELYS 565
Cdd:COG1196 215 YRELKEELKE--------LEAELLLLKLRELEAEL-EELEAELEELEAELEELEAElaeLEAELEELRLELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 566 AQEEILVLRHAMEAATAERERE---ITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQ-LQSQHQERASQLQGEVE 641
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLeerRRELEERLEELEEELAELEEELEELEEELEELEEELEeAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 642 KLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKsqgdLENKLGSIQDQHQQDASKLKIQL 721
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER----LEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 528494940 722 AQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQ 765
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
14-106 |
1.02e-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: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 14 SHPFQERHVYLDE-PVKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716 8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
|
90
....*....|....
gi 528494940 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 |
1.23e-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: 1.23e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 528494940 52 SRNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCEVLSGDIIQFG 106
Cdd:cd22686 48 SKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPYPLTHGDELKIG 102
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
275-765 |
2.54e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.37 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 275 VERSLSNTEDECTHLREMNERTQEelRELANKYNGAVNEIKDLTEKIKLAEDKHEELTQKglneKKELQMRIEEMEEKEQ 354
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEE--KDLHERLNGLESELAELDEEIERYEEQREQARET----RDEADEVLEEHEERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 355 ALQ---ARIEALQADNDFT-NERLTALQAVRQLKEAVDSsinklsnfdevIDAHLQNNQTTVDNSLPSPDRLKENQ--ID 428
Cdd:PRK02224 252 ELEtleAEIEDLRETIAETeREREELAEEVRDLRERLEE-----------LEEERDDLLAEAGLDDADAEAVEARReeLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 429 AKECDMSDTLSPSKEKSSDDTSDGQMEEQELNEPQNRVSLLKEMDRSLEAgdteqviphihrELQEAQELANTGKQKcle 508
Cdd:PRK02224 321 DRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELES------------ELEEAREAVEDRREE--- 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 509 lQAMLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREqRENTITTTREELYSAQEEILVLRHAME---------- 578
Cdd:PRK02224 386 -IEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE-REAELEATLRTARERVEEAEALLEAGKcpecgqpveg 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 579 ----AATAEREREITALQGDLSIVTAELDKWRQ------TAAKYEVEISNL----QASFQLQSQHQERASQLQGEVEKLQ 644
Cdd:PRK02224 464 sphvETIEEDRERVEELEAELEDLEEEVEEVEErleraeDLVEAEDRIERLeerrEDLEELIAERRETIEEKRERAEELR 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 645 ADCSGLQNECDSLRAEKSTLMQ----------KLNRLEEELDSSRERSATLSSNLNALEksqgDLENKLGSIQDQHQQDA 714
Cdd:PRK02224 544 ERAAELEAEAEEKREAAAEAEEeaeeareevaELNSKLAELKERIESLERIRTLLAAIA----DAEDEIERLREKREALA 619
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 528494940 715 SK---LKIQLAQAESRTRDLQKEYDDTQslLSDLRQRYEQTEQEKRSINDELEQ 765
Cdd:PRK02224 620 ELndeRRERLAEKRERKRELEAEFDEAR--IEEAREDKERAEEYLEQVEEKLDE 671
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
164-757 |
3.25e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLAStQEASESSWQALIDEDRL-LSRLEVMGNQLQA--YSKNQTEDGIRKEL 240
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEE-LEAELAELEAELEELRLeLEELELELEEAQAeeYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 241 VALTEDKHNYETT---AKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDL 317
Cdd:COG1196 305 ARLEERRRELEERleeLEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 318 TEKIKLAEDKHEELTQKGLNEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQAVRQLKEAVDSSINKLSNF 397
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 398 DEVIDAHLQNNQTTVDNSLPSPDRLKENQIDAKECDMSDTLSPSKEKSSDDTSDGQMEEQELNEpqnRVSLLKEMDRSLE 477
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV---LIGVEAAYEAALE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 478 AGDTEQVIPHIHRELQEAQELANTGKQKclelqamlEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQREntit 557
Cdd:COG1196 542 AALAAALQNIVVEDDEVAAAAIEYLKAA--------KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLR---- 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 558 tTREELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQ 637
Cdd:COG1196 610 -EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERL 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 638 GEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKS----QGDLENKLGSIQDQHQQD 713
Cdd:COG1196 689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEElleeEALEELPEPPDLEELERE 768
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 528494940 714 ASKLKIQL--------------AQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKR 757
Cdd:COG1196 769 LERLEREIealgpvnllaieeyEELEERYDFLSEQREDLEEARETLEEAIEEIDRETR 826
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
493-758 |
3.25e-11 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 66.96 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 493 QEAQELANTgkqkcLeLQAMLEEERKTNRQQTEESakqIRFLQTQLAKLQTDMEALRE-----QRENTITTTREELYSAQ 567
Cdd:COG3206 148 ELAAAVANA-----L-AEAYLEQNLELRREEARKA---LEFLEEQLPELRKELEEAEAaleefRQKNGLVDLSEEAKLLL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 568 EEIlvlrhameaatAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERAsQLQGEVEKLQADc 647
Cdd:COG3206 219 QQL-----------SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLA-ELEAELAELSAR- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 648 sgLQNECDSLRAekstLMQKLNRLEEELDSSRERS-ATLSSNLNALEKSQGDLENKLGSIQDQHQQdasklkiqLAQAES 726
Cdd:COG3206 286 --YTPNHPDVIA----LRAQIAALRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAE--------LPELEA 351
|
250 260 270
....*....|....*....|....*....|..
gi 528494940 727 RTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRS 758
Cdd:COG3206 352 ELRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
205-755 |
6.54e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 6.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 205 QALIDEDRLLsRLEVMGNQLQAYSKNQTEDGIRKELVALTEDKHNYETTAKESLRRVLQEKIEVVRK--------LSEVE 276
Cdd:COG1196 216 RELKEELKEL-EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELeleeaqaeEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 277 RSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEELTQKGLNEKKELQMRIEEMEEKEQAL 356
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 357 QARIEALQADNDFTNERLTALQAVRQLKEAVDSSINKLSNFDEVIDAHLQNNQTTVDNSLPSPDRLK---------ENQI 427
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEealeeaaeeEAEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 428 DAKECDMSDTLSPSKEKSSDDTSDGQMEEQELNEPQNRVSLLKEMDRSLEAGDT----EQVIPHIHRELQEAQELANTGK 503
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEgvkaALLLAGLRGLAGAVAVLIGVEA 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 504 QKCLELQAMLEEERKTNRQQTEESAKQ-IRFLQTQLAKLQTDMEALREQRENTITTTREELYSAQEEILVLRHAMEAATA 582
Cdd:COG1196 535 AYEAALEAALAAALQNIVVEDDEVAAAaIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADAR 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 583 EREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQAdcsglqnecdslRAEKS 662
Cdd:COG1196 615 YYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEA------------EAELE 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 663 TLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESRTRDLQKEYDDTQSLL 742
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
570
....*....|...
gi 528494940 743 SDLRQRYEQTEQE 755
Cdd:COG1196 763 EELERELERLERE 775
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
163-701 |
2.63e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLASTQEASESSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGIRKELVA 242
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 243 LTEDKHnyETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKIK 322
Cdd:COG1196 354 EEAEAE--LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 323 LAEDKHEELTQKGLNEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQAVRQLKEAVDSSINKLSNFDE-VI 401
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEgVK 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 402 DAHLQNNQTTVDNSLPSPDRLKENQIDAKECDMSDTLSPSKEKssDDTSDGQMEEQELNEPQNRVSLL---KEMDRSLEA 478
Cdd:COG1196 512 AALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE--DDEVAAAAIEYLKAAKAGRATFLpldKIRARAALA 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 479 GDTEQVIPHIHRELQEAQELANTGKQKCLELQAMLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQRENTITT 558
Cdd:COG1196 590 AALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 559 TREELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQG 638
Cdd:COG1196 670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE 749
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 639 EVEKLQADcsGLQNEcDSLRAEKSTLMQKLNRL-------EEELDSSRERSATLSSNLNALEKSQGDLEN 701
Cdd:COG1196 750 EEALEELP--EPPDL-EELERELERLEREIEALgpvnllaIEEYEELEERYDFLSEQREDLEEARETLEE 816
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
490-765 |
2.72e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 490 RELQEAQELAntgkQKCLELQAMLEEERKTNRQQTEesaKQIRFLQTQLAKLQTDMEALREqRENTITTTREELYSAQEE 569
Cdd:COG1196 235 RELEAELEEL----EAELEELEAELEELEAELAELE---AELEELRLELEELELELEEAQA-EEYELLAELARLEQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 570 ILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQADcsg 649
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE--- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 650 LQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESRTR 729
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270
....*....|....*....|....*....|....*.
gi 528494940 730 DLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQ 765
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| CC1_T3JAM |
cd21912 |
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ... |
164-204 |
3.55e-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: 55.82 E-value: 3.55e-10
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 528494940 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLASTQEASESSW 204
Cdd:cd21912 5 EILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
296-595 |
3.96e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.54 E-value: 3.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 296 TQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEELTQ---KGLNEKKELQMRIEEMEEKEQALQARIEALQADNDFTNE 372
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEeleQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 373 RLTALQAVRqlkEAVDSSINKLSNFDEVIDAHLQNNQTTVDNSLPSPDRLKEnQIDAKECDMSDT---LSPSKEKSSDDT 449
Cdd:TIGR02168 755 ELTELEAEI---EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE-ALDELRAELTLLneeAANLRERLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 450 SDGQMEEQELNEPQNRVSLLKEMDRSLEA--GDTEQVIPHIHRELQEAQELANTGKQKCLELQAMLEEERKTNR---QQT 524
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELReleSKR 910
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528494940 525 EESAKQIRFLQTQLAKLQTDMEALREQRENTITTTREELYSAQEEILVLRHAMEAATAEREREITALQGDL 595
Cdd:TIGR02168 911 SELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
135-720 |
5.14e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.21 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 135 ARRRSDVVPAPLPLaIDKVSANTPSMYSQELFQL----SQYLQEALHREQMLEQKLATLQR-LLASTQEASEsswqALID 209
Cdd:pfam15921 290 ARSQANSIQSQLEI-IQEQARNQNSMYMRQLSDLestvSQLRSELREAKRMYEDKIEELEKqLVLANSELTE----ARTE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 210 EDRLLSRLEVMGNQLQAY----SKNQTEDGIRKELVALTEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNtede 285
Cdd:pfam15921 365 RDQFSQESGNLDDQLQKLladlHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKS---- 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 286 cthlrEMNERTQEELRELANKyNGAVNEIKDLTEKIklaeDKHEELTQKGLNEKKELQMRIEEMEEKEQALQARIEALQA 365
Cdd:pfam15921 441 -----ECQGQMERQMAAIQGK-NESLEKVSSLTAQL----ESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKER 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 366 DNDFTNERLTalqavrQLKEAVDSSINKLSNFDEVIDaHLQNNQTtvdnslpspdrlkenqidakECDMSDTLSPSKEKs 445
Cdd:pfam15921 511 AIEATNAEIT------KLRSRVDLKLQELQHLKNEGD-HLRNVQT--------------------ECEALKLQMAEKDK- 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 446 sddtsdgqMEEQELNEPQNRVSLLKEMDRS-----LEAGDTEQVIPHIHRELQEAQELANTGKQKCLELQAMLEEERKTN 520
Cdd:pfam15921 563 --------VIEILRQQIENMTQLVGQHGRTagamqVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEK 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 521 RQQTEESAKQIRFLQtqlaklqtDMEALREQRENTITTTREELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTA 600
Cdd:pfam15921 635 VKLVNAGSERLRAVK--------DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQS 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 601 ELDKWRQTAAKYE-VEISNLQASFQLQSQHQERASQ---LQGEVEKLQADCSGLQNECDSLRAEKSTLMQKL-------N 669
Cdd:pfam15921 707 ELEQTRNTLKSMEgSDGHAMKVAMGMQKQITAKRGQidaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELstvatekN 786
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 528494940 670 RLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQD---QHQQDASKLKIQ 720
Cdd:pfam15921 787 KMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDiiqRQEQESVRLKLQ 840
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
121-772 |
9.81e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 62.44 E-value: 9.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 121 IVSTIKLFLPDGMEARRRSDVVPAPLPLAIDKVSANtpsmYSQELFQLSQYLQEA--LHREQ--MLEQKLATLQRLLAST 196
Cdd:pfam15921 47 TFTQIPIFPKYEVELDSPRKIIAYPGKEHIERVLEE----YSHQVKDLQRRLNESneLHEKQkfYLRQSVIDLQTKLQEM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 197 QEASEsswqALIDedrlLSRLEvmgNQLQAYSKNQTEDGIRKELVA--LTEDKHNYETTAKESLRR-------VLQEKIE 267
Cdd:pfam15921 123 QMERD----AMAD----IRRRE---SQSQEDLRNQLQNTVHELEAAkcLKEDMLEDSNTQIEQLRKmmlshegVLQEIRS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 268 VVRKLSEVERSLSNTEDECT--HLREMNERTQEELRELANkyngavnEIKDLTEKIKLAEDKHEELtqkglneKKELQMR 345
Cdd:pfam15921 192 ILVDFEEASGKKIYEHDSMStmHFRSLGSAISKILRELDT-------EISYLKGRIFPVEDQLEAL-------KSESQNK 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 346 IEEMEEKEQAlqaRIEALQADND-----FTNERLTALQAVRQLKEAVDSSINKLSNFDEVIDAHLQNNQTTVD---NSLP 417
Cdd:pfam15921 258 IELLLQQHQD---RIEQLISEHEveitgLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSqlrSELR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 418 SPDRLKENQIDAKECDM----SDTLSPSKEKSSDDTSDGQMEEQ------ELNEPQNRVSLLKEMDRSLEAGDTEQ--VI 485
Cdd:pfam15921 335 EAKRMYEDKIEELEKQLvlanSELTEARTERDQFSQESGNLDDQlqkllaDLHKREKELSLEKEQNKRLWDRDTGNsiTI 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 486 PHIHRELQ----EAQELANTGKQKCLELQAMLEEERKTNRQQTEESAKqirfLQTQLAKLQTDMEALREQRENtITTTRE 561
Cdd:pfam15921 415 DHLRRELDdrnmEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEK----VSSLTAQLESTKEMLRKVVEE-LTAKKM 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 562 ELYSAQEEIlvlrHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQ------ASFQLQSQHQERASQ 635
Cdd:pfam15921 490 TLESSERTV----SDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRnvqtecEALKLQMAEKDKVIE 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 636 -LQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLEnklgsIQDQHQQDA 714
Cdd:pfam15921 566 iLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE-----LEKVKLVNA 640
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 528494940 715 SKLKIQLAQAESRTRD-LQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLKL 772
Cdd:pfam15921 641 GSERLRAVKDIKQERDqLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKM 699
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
276-765 |
1.08e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 62.11 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 276 ERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKIKLAED---KHEELTQKGLNEKKEL-------QMR 345
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETElcaEAEEMRARLAARKQELeeilhelESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 346 IEEMEEKEQALQARIEALQADNDFTNERLTALQAVRQL----KEAVDSSINKLSnfDEVIDAHLQNNQTTVDNSLPSpDR 421
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKlqleKVTTEAKIKKLE--EDILLLEDQNSKLSKERKLLE-ER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 422 LKENQID-AKECDMSDTLSPSKEKSSDDTSDgqMEEQELNEPQNRVSLLKeMDRSLEaGDTEQVIPHIHRELQEAQELAN 500
Cdd:pfam01576 161 ISEFTSNlAEEEEKAKSLSKLKNKHEAMISD--LEERLKKEEKGRQELEK-AKRKLE-GESTDLQEQIAELQAQIAELRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 501 TGKQKCLELQAMLEEERKTNRQQTeESAKQIRFLQTQLAKLQTDMEALREQRENTITTTR------EELYSAQEEILVLR 574
Cdd:pfam01576 237 QLAKKEEELQAALARLEEETAQKN-NALKKIRELEAQISELQEDLESERAARNKAEKQRRdlgeelEALKTELEDTLDTT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 575 HAMEAATAEREREITALQGDLsivtaELDKWRQTAAKYEVEISNLQASFQLQSQhQERASQLQGEVEK----LQADCSGL 650
Cdd:pfam01576 316 AAQQELRSKREQEVTELKKAL-----EEETRSHEAQLQEMRQKHTQALEELTEQ-LEQAKRNKANLEKakqaLESENAEL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 651 QNECDSLRAEKSTLMQKLNRLEEELdssrersATLSSNLNALEKSQGDLENKLGSIQDQHQQDASklkiQLAQAESRTRD 730
Cdd:pfam01576 390 QAELRTLQQAKQDSEHKRKKLEGQL-------QELQARLSESERQRAELAEKLSKLQSELESVSS----LLNEAEGKNIK 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 528494940 731 LQKEYD-------DTQSLLSD-------LRQRYEQTEQEKRSINDELEQ 765
Cdd:pfam01576 459 LSKDVSslesqlqDTQELLQEetrqklnLSTRLRQLEDERNSLQEQLEE 507
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
488-692 |
1.17e-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: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 488 IHRELQEAQElantgKQKCLE-----LQAMLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQRENT---ITTT 559
Cdd:COG4913 240 AHEALEDARE-----QIELLEpirelAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLeaeLERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 560 REELYSAQEEILVLRHAMEAATAER----EREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQlqsqhqERASQ 635
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRleqlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA------ALRAE 388
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 528494940 636 LQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNAL 692
Cdd:COG4913 389 AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
469-712 |
1.87e-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: 61.62 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 469 LKEMDRSLEAGDTEqvIPHIHRELQEAQELANTGKQKCLELQAMLEEERKTNRQQTEESA----KQIRFLQTQLAKLQTD 544
Cdd:TIGR02169 232 KEALERQKEAIERQ--LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkEKIGELEAEIASLERS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 545 MEALREQRE-------------NTITTTREELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAK 611
Cdd:TIGR02169 310 IAEKERELEdaeerlakleaeiDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 612 YEVEISNLQ----ASFQLQSQHQERASQLQGEVEKLQADCSG-------LQNECDSLRAEKSTLMQKLNRLEEELDSSRE 680
Cdd:TIGR02169 390 YREKLEKLKreinELKRELDRLQEELQRLSEELADLNAAIAGieakineLEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
250 260 270
....*....|....*....|....*....|..
gi 528494940 681 RSATLSSNLNALEKSQGDLENKLGSIQDQHQQ 712
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARA 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
518-775 |
2.10e-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: 61.23 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 518 KTNRQQTEesaKQIRFLQTQLAKLQ-------TDMEALREQRENTIT--TTREELYSAQEEILVLR-HAMEAATAERERE 587
Cdd:TIGR02168 171 KERRKETE---RKLERTRENLDRLEdilneleRQLKSLERQAEKAERykELKAELRELELALLVLRlEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 588 ITALQGDLSIVTAELDKwrqtaakYEVEISNLQASFQlqsQHQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQK 667
Cdd:TIGR02168 248 LKEAEEELEELTAELQE-------LEEKLEELRLEVS---ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 668 LNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHqqdaSKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQ 747
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL----EELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
250 260
....*....|....*....|....*...
gi 528494940 748 RYEQTEQEKRSINDELEQCKVNLKLLQD 775
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQ 421
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
255-763 |
2.72e-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: 60.80 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 255 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEELTQK 334
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 335 GLNEK------KELQMRIEEMEEKEQALQARIEALQAD-NDFTNERLTALQAVRQLKEAVDSSINKLSNFDEvidaHLQN 407
Cdd:TIGR04523 203 LSNLKkkiqknKSLESQISELKKQNNQLKDNIEKKQQEiNEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQK----ELEQ 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 408 NQTTVDNSLPSPDRLKENQIDAKECDMSDTLSPSKEKSSDDTSDGQMEEQELNEPQNRVSLLKEMDRSL--EAGDTEQVI 485
Cdd:TIGR04523 279 NNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLkkELTNSESEN 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 486 PHIHRELQEAQ---ELANTGKQKCLELQAMLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQREN---TITTT 559
Cdd:TIGR04523 359 SEKQRELEEKQneiEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERlkeTIIKN 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 560 REELYSAQEEILVLRHA---MEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQ----ER 632
Cdd:TIGR04523 439 NSEIKDLTNQDSVKELIiknLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVkdltKK 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 633 ASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNR--LEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQH 710
Cdd:TIGR04523 519 ISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEK 598
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 528494940 711 QQDASKLKIQLAQAESRTRDL---QKEYDDTQSLLSDLRQRYEQTEQEKRSINDEL 763
Cdd:TIGR04523 599 KDLIKEIEEKEKKISSLEKELekaKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
264-748 |
7.38e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.28 E-value: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 264 EKIEVVRKLSEVERSLSNTEDECTHL---REMNERTQEELRELANKYNGAVNEIKDLTEKI-KLAEDKHEELTqkglnEK 339
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYeeqREQARETRDEADEVLEEHEERREELETLEAEIeDLRETIAETER-----ER 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 340 KELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQAVRQLKEAVDSSI-NKLSNFDEVIDAHLQNNQTTVDNSLPS 418
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELrDRLEECRVAAQAHNEEAESLREDADDL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 419 PDRLKENQIDAKECDmsDTLSPSKEKSSDDTSDGQMEEQELNEPQNRV---------------SLLKEMDRSLEA-GDTE 482
Cdd:PRK02224 355 EERAEELREEAAELE--SELEEAREAVEDRREEIEELEEEIEELRERFgdapvdlgnaedfleELREERDELREReAELE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 483 QVIPHIHRELQEAQELANTGK-----------------QKCLELQAMLEEERKTNRQQTE------ESAKQIRFLQTQLA 539
Cdd:PRK02224 433 ATLRTARERVEEAEALLEAGKcpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEeveerlERAEDLVEAEDRIE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 540 KLQT---DMEALREQRENTITTTREELYSAQEEILVLRHAME----AATAERER------EITALQGDLSIVTAELDKWR 606
Cdd:PRK02224 513 RLEErreDLEELIAERRETIEEKRERAEELRERAAELEAEAEekreAAAEAEEEaeeareEVAELNSKLAELKERIESLE 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 607 Q------TAAKYEVEISNLQASF-QLQSQHQERASQLQGEVEKLQADCSGLQNE-CDSLRAEKSTLMQKLNRLEEELDSS 678
Cdd:PRK02224 593 RirtllaAIADAEDEIERLREKReALAELNDERRERLAEKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEEKLDEL 672
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528494940 679 RERSATLSSNLNALEKSQGDLENklgsiqdqhqqdaskLKIQLAQAESRTRDLQKEYDDTQSLLS-------DLRQR 748
Cdd:PRK02224 673 REERDDLQAEIGAVENELEELEE---------------LRERREALENRVEALEALYDEAEELESmygdlraELRQR 734
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
527-760 |
1.10e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.85 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 527 SAKQIRFLQTQLAKLQTDMEALREQRENT---ITTTREELYSAQEEILVLR---HAMEAATAEREREITALQGDLSIVTA 600
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALkkeEKALLKQLAALERRIAALArriRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 601 ELDKWRQTAAKYeveisnLQASFQLQSQ-------HQERASQLQGEVEKLQADCSGLQNECDSLRAEKstlmQKLNRLEE 673
Cdd:COG4942 98 ELEAQKEELAEL------LRALYRLGRQpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADL----AELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 674 ELDSSRERsatlssnLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTE 753
Cdd:COG4942 168 ELEAERAE-------LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
....*..
gi 528494940 754 QEKRSIN 760
Cdd:COG4942 241 ERTPAAG 247
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
161-403 |
1.16e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 161 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLASTQEASESSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDgiRKEL 240
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER--IAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 241 VALTEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEK 320
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 321 IKLAEDKHEELTQkglnEKKELQMRIEEMEEKEQALQARIEALQAD-NDFTNERLTALQAVRQLKEAVDSSINKLSNFDE 399
Cdd:TIGR02168 833 IAATERRLEDLEE----QIEELSEDIESLAAEIEELEELIEELESElEALLNERASLEEALALLRSELEELSEELRELES 908
|
....
gi 528494940 400 VIDA 403
Cdd:TIGR02168 909 KRSE 912
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
512-770 |
1.20e-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: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 512 MLEEerktnrQQTEESAKQIRFLQTQLAKLQTDMEALREQRE--NTITTTREELYSAQEEILVLRHAMEAATAEREREit 589
Cdd:COG4913 217 MLEE------PDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAQR-- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 590 alqgdlsivtaELDKWRQTAAKYEVEISNLQASfqlQSQHQERASQLQGEVEKLQADCSGLQNEcdslraEKSTLMQKLN 669
Cdd:COG4913 289 -----------RLELLEAELEELRAELARLEAE---LERLEARLDALREELDELEAQIRGNGGD------RLEQLEREIE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 670 RLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQdasklkiQLAQAESRTRDLQKEYDDTQSLLSDLRQRY 749
Cdd:COG4913 349 RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA-------LLEALEEELEALEEALAEAEAALRDLRREL 421
|
250 260
....*....|....*....|.
gi 528494940 750 EQTEQEKRSindeLEQCKVNL 770
Cdd:COG4913 422 RELEAEIAS----LERRKSNI 438
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
28-85 |
2.39e-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: 2.39e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 528494940 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 |
2.55e-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: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 28 VKIGRSVARCRPAQNNATFDcKVLSRNHALVW---FDHKTGKFYLQDTkSSNGTFINSQRLSRGSEEsppcEVLSGDIIQ 104
Cdd:cd22685 30 YRIGRNPEVCDVFLCSSQHP-NLISREHAEIHaerDGNGNWKVLIEDR-STNGTYVNDVRLQDGQRR----ELSDGDTIT 103
|
90
....*....|....*..
gi 528494940 105 FG--VDVTENTRKVTHG 119
Cdd:cd22685 104 FGhkNGRRVKQWPYQKS 120
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
162-570 |
4.48e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 162 SQELFQLSQY--LQEALHREQMLEQKLATLQRLLASTQEASESSWQALIDEDRLLSRLEVMGNQLQAYSKNQTE--DGIR 237
Cdd:TIGR02169 664 GGILFSRSEPaeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKErlEELE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 238 KELVALTEDKHNYETTAKEsLRRVLQEKIEvvrKLSEVERSLSNTEDECTHlremnertqEELRELANKYNGAVNEIKDL 317
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKE-LEARIEELEE---DLHKLEEALNDLEARLSH---------SRIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 318 TEKIKLAEDKHEELTQKGL---NEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQ-AVRQLkeavDSSINK 393
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEyleKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEaALRDL----ESRLGD 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 394 LSNFDEVIDAHLQNNQTtvdnslpspdrlKENQIDAKECDMSDTLSPSKEKSsddtsdgQMEEQELNEpqnrvsLLKEMD 473
Cdd:TIGR02169 887 LKKERDELEAQLRELER------------KIEELEAQIEKKRKRLSELKAKL-------EALEEELSE------IEDPKG 941
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 474 RSLEAGDTEQVIPHIHRELQEAQElantgkqkclELQAmLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQRE 553
Cdd:TIGR02169 942 EDEEIPEEELSLEDVQAELQRVEE----------EIRA-LEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIE 1010
|
410
....*....|....*..
gi 528494940 554 NTITTTREELYSAQEEI 570
Cdd:TIGR02169 1011 EYEKKKREVFMEAFEAI 1027
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
578-765 |
4.81e-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: 4.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 578 EAATAEREREitaLQGDLSIVTAEL--DKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQADCSGLQNECD 655
Cdd:COG1196 208 QAEKAERYRE---LKEELKELEAELllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 656 SLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLgsiqDQHQQDASKLKIQLAQAESRTRDLQKEY 735
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL----EELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190
....*....|....*....|....*....|
gi 528494940 736 DDTQSLLSDLRQRYEQTEQEKRSINDELEQ 765
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLE 390
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
152-586 |
6.29e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 6.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 152 KVSANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLASTQEASEsswqaliDEDRLLSRLEVMGNQLQAYSKNQ 231
Cdd:COG4717 60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA-------ELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 232 TEDGIRKELVALTEdkhnyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDEC-THLREMNERTQEELRELANKYNGA 310
Cdd:COG4717 133 ELEALEAELAELPE--------RLEELEERLEELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 311 VNEIKDLTEKIKLAEDKHEELTQKGlnEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQAVRQLKEAVDSS 390
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEEL--EQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 391 INKLSNFDEVIDAHLQNNQTTVD--NSLPSPDRLKENQID--AKECDMSDTLSPSK-EKSSDDTSDGQMEEQELNEPQNR 465
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEelQALPALEELEEEELEelLAALGLPPDLSPEElLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 466 V---SLLKEMDRSLEAG--DTEQVIPHIHRELQEAQELANTGKQKCLELQA---------------MLEEERKTNRQQTE 525
Cdd:COG4717 363 LqleELEQEIAALLAEAgvEDEEELRAALEQAEEYQELKEELEELEEQLEEllgeleellealdeeELEEELEELEEELE 442
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528494940 526 ESAKQIRFLQTQLAKLQTDMEALREQRENT-----ITTTREELYSAQEEILVLRHAMEAATAERER 586
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLEEDGELAellqeLEELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
212-776 |
1.71e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 55.05 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 212 RLLSRLEVMGNQLQAYSKNQTEDGIRKELVALTEDKHNYETTAKESLRRVLQEKIEvvrkLSEVERSlSNTEDECTHLRE 291
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE----LDGFERG-PFSERQIKNFHT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 292 MNERTQEELRELANKyngavnEIKDLTEKIKLAEDKHEELTQKGLNEKKELQMRIEEMEEKEQALQARIEALQADNDFTN 371
Cdd:TIGR00606 398 LVIERQEDEAKTAAQ------LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 372 ERLTALQAVRQ-LKEAVDSSINKLSNFDEVIDAHLQNNQTTVDNSLPSPDRlKENQIDAKECDMSDTLSPSKEKSsddTS 450
Cdd:TIGR00606 472 RILELDQELRKaERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQ-EMEQLNHHTTTRTQMEMLTKDKM---DK 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 451 DGQMEEQELNEPQNRVSLLKEMDRSLEAGDTeqviphIHRELQEAQELANTGKQKCLELQAMLEEERKTNrqqteesaKQ 530
Cdd:TIGR00606 548 DEQIRKIKSRHSDELTSLLGYFPNKKQLEDW------LHSKSKEINQTRDRLAKLNKELASLEQNKNHIN--------NE 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 531 IRFLQTQLAKLQTDMEAL--REQRENTITTTREELYSAQEEilvlRHAMEAATAEREREITALQGDLSIVTAELDKWRQT 608
Cdd:TIGR00606 614 LESKEEQLSSYEDKLFDVcgSQDEESDLERLKEEIEKSSKQ----RAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQT 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 609 AAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQADCSGL----QNECDSLRAEKSTL---MQKLNRLEEELDSSRER 681
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLapgrQSIIDLKEKEIPELrnkLQKVNRDIQRLKNDIEE 769
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 682 SATLSSNLNALEKSQGDLENKLGSIQD-QHQQDASKLKIQLAQAESRTRDLQKEYddtqsllSDLRQRYEQTEQEKRSIN 760
Cdd:TIGR00606 770 QETLLGTIMPEEESAKVCLTDVTIMERfQMELKDVERKIAQQAAKLQGSDLDRTV-------QQVNQEKQEKQHELDTVV 842
|
570
....*....|....*.
gi 528494940 761 DELEQckvNLKLLQDK 776
Cdd:TIGR00606 843 SKIEL---NRKLIQDQ 855
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
14-110 |
2.28e-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: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 14 SHPFQERHV---YLDEPVKIGRSvARCRPAQNNATfdckvLSRNHALVW---FDHKTG-KFYLQDTkSSNGTFINSQRLS 86
Cdd:cd22670 7 SSPGSTDIVlpiYKNQVITIGRS-PSCDIVINDPF-----VSRTHCRIYsvqFDESSApLVYVEDL-SSNGTYLNGKLIG 79
|
90 100
....*....|....*....|....*
gi 528494940 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 |
2.40e-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: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 25 DEPVKIGRSVArcrpAQNNATFDC-KVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRLsrgsEESPPCEVLSGDII 103
Cdd:cd22663 20 GKEVTVGRGLG----VTYQLVSTCpLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERI----EPLKPYPLNEGDLI 90
|
90
....*....|.
gi 528494940 104 QFGVDVTENTR 114
Cdd:cd22663 91 QLGVPPENKEP 101
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
236-776 |
2.48e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 236 IRKELVALTEDKHNYETTAKEsLRRVLQEKIEVVRKLSEVERSlsntEDECTHLREMNERTQEELRELANKYNGAVNEIK 315
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEE-LKKEIEELEEKVKELKELKEK----AEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 316 DLTEKIKLAEDKHEELtQKGLNEKKELQMRIEEMEEKEQ------ALQARIEALQAD-NDFTNERLTA-LQAVRQLKEAV 387
Cdd:PRK03918 325 GIEERIKELEEKEERL-EELKKKLKELEKRLEELEERHElyeeakAKKEELERLKKRlTGLTPEKLEKeLEELEKAKEEI 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 388 DSSINKLsnfdevidahlqnnqttvdnslpspdRLKENQIDAKECDMSDTLSPSKEKSSDDTSDGQmeeqELNEpQNRVS 467
Cdd:PRK03918 404 EEEISKI--------------------------TARIGELKKEIKELKKAIEELKKAKGKCPVCGR----ELTE-EHRKE 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 468 LLKEMDRSLEagdteqvipHIHRELQEAQELANTGKQKCLELQAMLEEERKTNRQqtEESAKQIRFLQTQLAKLqtDMEA 547
Cdd:PRK03918 453 LLEEYTAELK---------RIEKELKEIEEKERKLRKELRELEKVLKKESELIKL--KELAEQLKELEEKLKKY--NLEE 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 548 LrEQRENTITTTREELYSAQEEILVLrhameaatAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQAsfqlqs 627
Cdd:PRK03918 520 L-EKKAEEYEKLKEKLIKLKGEIKSL--------KKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGF------ 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 628 qhqERASQLQGEVEKLQAdcsgLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQ 707
Cdd:PRK03918 585 ---ESVEELEERLKELEP----FYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS 657
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528494940 708 DQHQQDAS----KLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDeLEQCKVNLKLLQDK 776
Cdd:PRK03918 658 EEEYEELReeylELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK-LEKALERVEELREK 729
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
250-769 |
2.75e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 250 YETTAKES--LRRVLQEKIEVVRKL----SEVERSLSNTEDECTH-LREMNErTQEELRELANKYNGAVNEIKDLTE-KI 321
Cdd:PRK03918 160 YENAYKNLgeVIKEIKRRIERLEKFikrtENIEELIKEKEKELEEvLREINE-ISSELPELREELEKLEKEVKELEElKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 322 KLAEDKHEELTQKGlnEKKELQMRIEEMEEKEQALQARIEALQadndftnERLTALQAVRQLKEAVDssinKLSNFDEVI 401
Cdd:PRK03918 239 EIEELEKELESLEG--SKRKLEEKIRELEERIEELKKEIEELE-------EKVKELKELKEKAEEYI----KLSEFYEEY 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 402 DAHLQNNQTTVDNSlpspdrlkENQIDAKECDMSDTLSPSKEKssddtsdGQMEEqELNEPQNRVSLLKEMDRSLEagdt 481
Cdd:PRK03918 306 LDELREIEKRLSRL--------EEEINGIEERIKELEEKEERL-------EELKK-KLKELEKRLEELEERHELYE---- 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 482 eqvipHIHRELQEAQELANTGKQKCLE-LQAMLEEERKTNRQQTEESAK---QIRFLQTQLAKLQTDMEALREQRENTIT 557
Cdd:PRK03918 366 -----EAKAKKEELERLKKRLTGLTPEkLEKELEELEKAKEEIEEEISKitaRIGELKKEIKELKKAIEELKKAKGKCPV 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 558 TTREELYSAQEEILVLRHAMEAATAEREREITALQGDLSivtAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQ 637
Cdd:PRK03918 441 CGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLR---KELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNL 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 638 GEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEeldsSRERSATLSSNLNALEKSQGDLENKLGSIQ-DQHQQDASK 716
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGfESVEELEER 593
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528494940 717 LK---------IQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVN 769
Cdd:PRK03918 594 LKelepfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
595-762 |
3.35e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 595 LSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKL--QADCSGLQNECDSLRAEKSTLMQKLNRLE 672
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 673 EELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQT 752
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170
....*....|
gi 528494940 753 EQEKRSINDE 762
Cdd:COG4717 233 ENELEAAALE 242
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
27-106 |
3.49e-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: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 27 PVKIGRSVARcRPAQNNATFDC-----KVLSRNHALVWFDHKTGKFYLQdTKSSNGTFINSQRLSRGseeSPPCEVLSGD 101
Cdd:cd22701 18 EVVLGRNSKN-SSSTAADSVDIdlgpsKKISRRHARIFYDFTTQCFELS-VLGRNGVKVDGILVKPG---SPPVPLRSGS 92
|
....*
gi 528494940 102 IIQFG 106
Cdd:cd22701 93 LIQIG 97
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
289-758 |
3.65e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 289 LREMNERTQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEELTQKgLNEKKELQMRIEEMEEKEQALQARIEALqadnd 368
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKL----- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 369 ftnERLTALQAVRQLKEAVDSSINKLSNFDEVIDAHLQNNQTTVDNSlpspDRLKENQIDAKEcdmsdtlspskekssdd 448
Cdd:COG4717 122 ---EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEEL----EELEAELAELQE----------------- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 449 tsdgQMEEQELNEPQNRVSLLKEMDRSLEagDTEQVIPHIHRELQEAQELANTGKQKCLELQAMLEEERKTNRQQTEESA 528
Cdd:COG4717 178 ----ELEELLEQLSLATEEELQDLAEELE--ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 529 KQIRFLQTQLAKLQTDMEALREQRENTITTT--------------REELYSAQEEILVLRHAMEAATAEREREITALQGD 594
Cdd:COG4717 252 LLIAAALLALLGLGGSLLSLILTIAGVLFLVlgllallflllareKASLGKEAEELQALPALEELEEEELEELLAALGLP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 595 LSIVTAELDKWRQTAAKY---EVEISNLQASFQLQSQHQERASQLQG-----------------EVEKLQADCSGLQNEC 654
Cdd:COG4717 332 PDLSPEELLELLDRIEELqelLREAEELEEELQLEELEQEIAALLAEagvedeeelraaleqaeEYQELKEELEELEEQL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 655 DSLRAEKSTLMQKLN--RLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHqqDASKLKIQLAQAESRTRDLQ 732
Cdd:COG4717 412 EELLGELEELLEALDeeELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG--ELAELLQELEELKAELRELA 489
|
490 500
....*....|....*....|....*.
gi 528494940 733 KEYDDTQSLLSDLRQRYEQTEQEKRS 758
Cdd:COG4717 490 EEWAALKLALELLEEAREEYREERLP 515
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
256-677 |
5.33e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.37 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 256 ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERtQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEELTQKG 335
Cdd:PRK01156 315 SNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQ-ILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 336 LN--------------EKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQ------------AVRQLKEAVDS 389
Cdd:PRK01156 394 SEilkiqeidpdaikkELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNgqsvcpvcgttlGEEKSNHIINH 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 390 SINKLSNFDEVIDaHLQNNQTTVDNSLPSPDRLKEnQIDAKECDMSDTLSPSKEKSSDDTSDGQMEEQELNEPQNRVSLL 469
Cdd:PRK01156 474 YNEKKSRLEEKIR-EIEIEVKDIDEKIVDLKKRKE-YLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEI 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 470 KEMDRSLEAGDTEQviphihrelqeaqelANTGKQKCLELQAMLEEErkTNRQQTEESAKQIRFLQTQLAKLQTDMEALR 549
Cdd:PRK01156 552 KNRYKSLKLEDLDS---------------KRTSWLNALAVISLIDIE--TNRSRSNEIKKQLNDLESRLQEIEIGFPDDK 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 550 EQRENTITTTREELYSAQEEILVLRhameaataEREREITALQGDLSivtaelDKWRQTAAKYEVEISNLQASFQLqSQH 629
Cdd:PRK01156 615 SYIDKSIREIENEANNLNNKYNEIQ--------ENKILIEKLRGKID------NYKKQIAEIDSIIPDLKEITSRI-NDI 679
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 528494940 630 QERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDS 677
Cdd:PRK01156 680 EDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLES 727
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
301-641 |
1.27e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 301 RELANKYNGAVNEIKDLTEKIKLAEDKHEELTQKGLNEK-KELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQA 379
Cdd:COG1196 209 AEKAERYRELKEELKELEAELLLLKLRELEAELEELEAElEELEAELEELEAELAELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 380 VRQLKEAvdsSINKLSNFDEVIDAHLQNNQTTVdnslpspDRLKENQIDAKEcdmsdtlspskekssddtsDGQMEEQEL 459
Cdd:COG1196 289 EEYELLA---ELARLEQDIARLEERRRELEERL-------EELEEELAELEE-------------------ELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 460 NEPQNRVSLLKEMDRSLEAgdteqviphIHRELQEAQELANTGKQKCLELQAMLEEERKTNRQQTEESAKQIRFLQTQLA 539
Cdd:COG1196 340 EELEEELEEAEEELEEAEA---------ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 540 KLQTDMEALREQrentitttREELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNL 619
Cdd:COG1196 411 ALLERLERLEEE--------LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
330 340
....*....|....*....|..
gi 528494940 620 QASFQLQSQHQERASQLQGEVE 641
Cdd:COG1196 483 LEELAEAAARLLLLLEAEADYE 504
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
585-766 |
1.39e-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: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 585 EREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQgEVEKLQADCSGLQNECDSLRAEKSTL 664
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-DVASAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 665 M---QKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESRTRDLQKEYDDTQSL 741
Cdd:COG4913 688 AaleEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
|
170 180
....*....|....*....|....*
gi 528494940 742 LSDLRQRYEQTEQEKRSINDELEQC 766
Cdd:COG4913 768 RENLEERIDALRARLNRAEEELERA 792
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
488-686 |
1.61e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 488 IHRELQEAQELANTGKQKclelQAMLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQR---ENTITTTREEL- 563
Cdd:COG4942 32 LQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIaelRAELEAQKEELa 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 564 --------YSAQEEILVLRHA------------MEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQAS- 622
Cdd:COG4942 108 ellralyrLGRQPPLALLLSPedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEEr 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528494940 623 FQLQSQHQERASQLQgeveKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLS 686
Cdd:COG4942 188 AALEALKAERQKLLA----RLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
586-776 |
1.78e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 586 REITALQGDLSIVTAELDKWRQTAAKYEVEISNLQasfqlqsqhqERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLM 665
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDAS----------RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 666 QKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLG-SIQDQHQQDASKLKIQLAQAESRTRDLQKEyddtqslLSD 744
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShSRIPEIQAELSKLEEEVSRIEARLREIEQK-------LNR 823
|
170 180 190
....*....|....*....|....*....|..
gi 528494940 745 LRQRYEQTEQEKRSINDELEQCKVNLKLLQDK 776
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE 855
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
267-771 |
2.57e-06 |
|
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: 51.17 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 267 EVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEELTQKGLNEKKELQMRI 346
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 347 EEMEEKEQ---ALQARIEALQADNDFTNERLTALQAVRQLKEAVDSSINK----LSNFDEVIDAHLQNNQTTVDNSlpSP 419
Cdd:TIGR04523 117 EQKNKLEVelnKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKqkeeLENELNLLEKEKLNIQKNIDKI--KN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 420 DRLKENQI-------DAKECDMSDTLSPSKEKSSDDTSDGQMEEQELNEPQNRVSLLKEmdrslEAGDTEQVIPHIHREL 492
Cdd:TIGR04523 195 KLLKLELLlsnlkkkIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQT-----QLNQLKDEQNKIKKQL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 493 QEAQELANTGKQKCLELQAMLEE-ERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQ---RENTITTTREELYSAQE 568
Cdd:TIGR04523 270 SEKQKELEQNNKKIKELEKQLNQlKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQisqNNKIISQLNEQISQLKK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 569 EILVLrhamEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQsqhQERASQLQGEVEKLQADCS 648
Cdd:TIGR04523 350 ELTNS----ESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQ---EKLNQQKDEQIKKLQQEKE 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 649 GLQNECDSLRAEKSTLMQKLNRLEEE----------LDSSRErsaTLSSNLNALEKSQGDLENKLGSIQ---DQHQQDAS 715
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTNQdsvkeliiknLDNTRE---SLETQLKVLSRSINKIKQNLEQKQkelKSKEKELK 499
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 528494940 716 KLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLK 771
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK 555
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
55-108 |
3.22e-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: 3.22e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 528494940 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 |
3.45e-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: 3.45e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528494940 30 IGRSVArcrpaqNNATFDCKVLSRNHALVwfDHKTGKFYLQDTKSSNGTFINSQRLSRGseesppcEVLSGDIIQFG 106
Cdd:cd22698 25 IGRSSN------NDIRLNDHSVSRHHARI--VRQGDKCNLTDLGSTNGTFLNGIRVGTH-------ELKHGDRIQLG 86
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
172-587 |
3.48e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 172 LQEALHreQMLEQKL-ATLQRLLASTQEASESSWQALideDRLLSRLEVMGNQLQAYSKNQTE-DGIRKELVALTEDKHn 249
Cdd:COG4717 39 LLAFIR--AMLLERLeKEADELFKPQGRKPELNLKEL---KELEEELKEAEEKEEEYAELQEElEELEEELEELEAELE- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 250 yETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLremnERTQEELRELANKYNGAVNEIKDLTEKIKLAEDKHE 329
Cdd:COG4717 113 -ELREELEKLEKLLQLLPLYQELEALEAELAELPERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQLS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 330 ELTQKGLN----EKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQAVRQLKEA----------------VDS 389
Cdd:COG4717 188 LATEEELQdlaeELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllliaaallallglGGS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 390 SINKLSNFDEVI----------------DAHLQNNQTTVDNSLPSPDRLKENQID--AKECDMSDTLSPSK-EKSSDDTS 450
Cdd:COG4717 268 LLSLILTIAGVLflvlgllallflllarEKASLGKEAEELQALPALEELEEEELEelLAALGLPPDLSPEElLELLDRIE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 451 DGQMEEQELNEPQNRV---SLLKEMDRSLEAG--DTEQVIPHIHRELQEAQELantgKQKCLELQAMLEEERKTNRQQTE 525
Cdd:COG4717 348 ELQELLREAEELEEELqleELEQEIAALLAEAgvEDEEELRAALEQAEEYQEL----KEELEELEEQLEELLGELEELLE 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528494940 526 ESAKQirFLQTQLAKLQTDMEALREQRENtittTREELYSAQEEILVLRHAMEAATAERERE 587
Cdd:COG4717 424 ALDEE--ELEEELEELEEELEELEEELEE----LREELAELEAELEQLEEDGELAELLQELE 479
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
164-774 |
5.51e-06 |
|
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: 50.22 E-value: 5.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLASTQEASESSWQALIDEDRL------------LSRLEVMGNQLQAYSKNQ 231
Cdd:pfam12128 259 RLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGelsaadaavakdRSELEALEDQHGAFLDAD 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 232 TE---------DGIRKEL------VALTEDKHNYETTAKEslRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERT 296
Cdd:pfam12128 339 IEtaaadqeqlPSWQSELenleerLKALTGKHQDVTAKYN--RRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDD 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 297 QEEL-RELANKYNGAVNEIKDLTEKIKLA--EDK---------HEELTQKGLNekkelQMRIEEMEEKEQALQARIEALQ 364
Cdd:pfam12128 417 LQALeSELREQLEAGKLEFNEEEYRLKSRlgELKlrlnqatatPELLLQLENF-----DERIERAREEQEAANAEVERLQ 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 365 AD------------------NDFTNERLTALQAVRQL-------------KEAVD--SSINKL--------SNFDEVIDA 403
Cdd:pfam12128 492 SElrqarkrrdqasealrqaSRRLEERQSALDELELQlfpqagtllhflrKEAPDweQSIGKVispellhrTDLDPEVWD 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 404 H------------LQNNQTTVDNSLPSPDRLKEnQIDAKECDMSDTLSPSKEKSSD-DTSDGQMEEQELNEP-------Q 463
Cdd:pfam12128 572 GsvggelnlygvkLDLKRIDVPEWAASEEELRE-RLDKAEEALQSAREKQAAAEEQlVQANGELEKASREETfartalkN 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 464 NRVSL--LKEMDRSLEAGDTEQVIPHIHRELQEAQELANTGKQKCLELQAMLEEERKTNRQQTEESAKQIRFLQ----TQ 537
Cdd:pfam12128 651 ARLDLrrLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEgaldAQ 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 538 LAKLQTDMEALREQRENTITTTREELYSAqeeiLVLRHAMEAATAEREREITALQGDLSivtaELDKWRQTAAKYEVeis 617
Cdd:pfam12128 731 LALLKAAIAARRSGAKAELKALETWYKRD----LASLGVDPDVIAKLKREIRTLERKIE----RIAVRRQEVLRYFD--- 799
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 618 nlqasfQLQSQHQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRleeELDSSRERSATLSSNLNALEKSQG 697
Cdd:pfam12128 800 ------WYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEM---ERKASEKQQVRLSENLRGLRCEMS 870
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 698 DL-ENKLGSIQDQHQQDASKLKIQLAQ----AESRTRDLQKEYDDTQSLLSDLR-----QRYEQTEQEKRSINDELEQCK 767
Cdd:pfam12128 871 KLaTLKEDANSEQAQGSIGERLAQLEDlklkRDYLSESVKKYVEHFKNVIADHSgsglaETWESLREEDHYQNDKGIRLL 950
|
....*..
gi 528494940 768 VNLKLLQ 774
Cdd:pfam12128 951 DYRKLVP 957
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
51-106 |
5.52e-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: 5.52e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528494940 51 LSRNHALVWF----DHKTGKFYLQDTKSSNGTFINSQRLsrgseesPP---CEVLSGDIIQFG 106
Cdd:cd22677 41 ISRYHAVLQYrgdaDDHDGGFYLYDLGSTHGTFLNKQRI-------PPkqyYRLRVGHVLKFG 96
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
565-735 |
5.65e-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: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 565 SAQEEILVLRHAMEAATAER---EREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERAS------- 634
Cdd:COG4913 607 DNRAKLAALEAELAELEEELaeaEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERldassdd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 635 --QLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGD-------LENKLGS 705
Cdd:COG4913 687 laALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEerfaaalGDAVERE 766
|
170 180 190
....*....|....*....|....*....|
gi 528494940 706 IQDQHQQDASKLKIQLAQAESRTRDLQKEY 735
Cdd:COG4913 767 LRENLEERIDALRARLNRAEEELERAMRAF 796
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
52-106 |
7.53e-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: 7.53e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 528494940 52 SRNH-ALVWfdHK-TGKFYLQDTKSSNGTFINSQRLsrgsEESPPCEVLSGDIIQFG 106
Cdd:cd22674 48 SRVHaALVY--HKhLNRVFLIDLGSTHGTFVGGIRL----EPHKPQQLPIDSTLRFG 98
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
633-776 |
1.22e-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: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 633 ASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGS-IQDQHQ 711
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErARALYR 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528494940 712 QDASKLKI-QLAQAES------RTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLKLLQDK 776
Cdd:COG3883 98 SGGSVSYLdVLLGSESfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
547-766 |
1.28e-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: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 547 ALREQRENTITTTREELYSAQEEILVLRHAMEAATAEREREIT-----ALQGDLSivtAELDKWRQTAAKYEVEISNLQA 621
Cdd:COG3096 781 AAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGghlavAFAPDPE---AELAALRQRRSELERELAQHRA 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 622 SFQlqsQHQERASQLQGEVEKLQadcsGLQNECDSLRAEksTLMQKLNRLEEELDSSRERSATLSSNLNALEKsqgdLEN 701
Cdd:COG3096 858 QEQ---QLRQQLDQLKEQLQLLN----KLLPQANLLADE--TLADRLEELREELDAAQEAQAFIQQHGKALAQ----LEP 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 702 KLGSIQDQHQQDASkLKIQLAQAESRTRDLQKE---------------YDDTQSLLSD-------LRQRYEQTEQEKRSI 759
Cdd:COG3096 925 LVAVLQSDPEQFEQ-LQADYLQAKEQQRRLKQQifalsevvqrrphfsYEDAVGLLGEnsdlnekLRARLEQAEEARREA 1003
|
....*..
gi 528494940 760 NDELEQC 766
Cdd:COG3096 1004 REQLRQA 1010
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
190-782 |
1.51e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.81 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 190 QRLLASTQEASESSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGIRKELVALTEDKHNYET----TAKESLRRVLQEK 265
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNeeriDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 266 IEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTE-KIKLAEDKHEELTQKGLNEKKELQM 344
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLErRKVDDEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 345 RIEEMEEKEQALQARIEALQADNDFTNERLTALQAVRQLKEAVDSSINKLSNFDEVIDAHLQNNQTTVDNSLPSPDRLKE 424
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLE 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 425 NQiDAKECDMSDTLSPSKEKSSDDTSDGQMEEQELNEPQNRVSLLKEMDRSLEAGDTEQViphihRELQEAQELANTGKQ 504
Cdd:pfam02463 413 LA-RQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE-----DLLKETQLVKLQEQL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 505 KcLELQAMLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQRENTITTTREELYSAQEEILVLRHAMEAATAER 584
Cdd:pfam02463 487 E-LLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQK 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 585 EREITALQGDLSIVTAELDKWRQTAAK---------------------YEVEISNLQASFQLQSQHQERASQLQGEVEKL 643
Cdd:pfam02463 566 LVRALTELPLGARKLRLLIPKLKLPLKsiavleidpilnlaqldkatlEADEDDKRAKVVEGILKDTELTKLKESAKAKE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 644 QADCSGLQNEcdSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQ 723
Cdd:pfam02463 646 SGLRKGVSLE--EGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELL 723
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528494940 724 AESRTRDLQK---EYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLKLLQDKGSNSGW 782
Cdd:pfam02463 724 ADRVQEAQDKineELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEK 785
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
575-776 |
1.96e-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: 47.84 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 575 HAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQAsfqlqsqhqeRASQLQGEVEKLQADCSGLQNEC 654
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER----------RIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 655 DSLRAEKSTLMQKLNRLEEELdSSRERSATLSSNLNALE--KSQGDLENK------LGSIQDQHQQDASKLKIQLAQAES 726
Cdd:COG4942 86 AELEKEIAELRAELEAQKEEL-AELLRALYRLGRQPPLAllLSPEDFLDAvrrlqyLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 528494940 727 RTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLKLLQDK 776
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
28-106 |
2.30e-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: 2.30e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528494940 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 |
2.37e-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: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 27 PVKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLsrgSEESPPCEVLSGDIIQFG 106
Cdd:cd22678 24 PLTIGRIQ------RGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESI---SPNGRPVVLSSGDVITLG 94
|
90
....*....|.
gi 528494940 107 vdvTENTRKVT 117
Cdd:cd22678 95 ---SETKILVR 102
|
|
| FHA_CHFR |
cd22672 |
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ... |
49-105 |
3.30e-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: 3.30e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 528494940 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 |
3.52e-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: 3.52e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528494940 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 |
4.28e-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: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 25 DEPVKIGRsvarcRPAQNNAT----FDCKVLSRNHALVWFdhKTGKFYLQDTKSSNGTFINSQRLSR-GSEESPPCEVLS 99
Cdd:cd22702 31 KQPCIIGS-----DPHQAISGisvvIPSPQVSELHARITC--KNGAFFLTDLGSEHGTWINDNEGRRyRAPPNFPVRLHP 103
|
....*....
gi 528494940 100 GDIIQFGVD 108
Cdd:cd22702 104 SDVIEFGSD 112
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
514-729 |
4.64e-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: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 514 EEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQRENT---ITTTREELYSAQEEILVLRHAMEAATAEREREITA 590
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELqaeLEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 591 LQ---GDLSIVTAELDkwrqtAAKYEVEISNLQASFQLQSQHQErasqlqgEVEKLQADCSGLQNECDSLRAEKSTLMQK 667
Cdd:COG3883 95 LYrsgGSVSYLDVLLG-----SESFSDFLDRLSALSKIADADAD-------LLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528494940 668 LNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESRTR 729
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
641-770 |
5.11e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 641 EKLQAdcsgLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLS--SNLNALEKSQGDLENKLGSIQDQHQQ-DASKl 717
Cdd:COG4913 610 AKLAA----LEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERlDASS- 684
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 528494940 718 kIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNL 770
Cdd:COG4913 685 -DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-692 |
5.67e-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: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 263 QEKIEVVRKLSEVERSLSNTEDEcthLREMNERTQ--EELRELANKYNGAVNEIKDLtEKIKLAEDKHEELtqkglNEKK 340
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDI---LNELERQLKslERQAEKAERYKELKAELREL-ELALLVLRLEELR-----EELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 341 ELQMRIEEMEEKEQALQARIEALQAD----NDFTNERLTALQAVRQLKEAVDSSINKLSNFDEVIDAHLQNnqttvdnsl 416
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKleelRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN--------- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 417 pspdrlKENQIDAKECDMSDTLSpSKEKSSDDTSDGQMEEQELNEpqNRVSLLKEMDRSleagdtEQVIPHIHRELQEAQ 496
Cdd:TIGR02168 314 ------LERQLEELEAQLEELES-KLDELAEELAELEEKLEELKE--ELESLEAELEEL------EAELEELESRLEELE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 497 ELANTGKQKCLELqamleeerktnRQQTEESAKQIRFLQTQLaklqtdmEALREQRENTITTTREELYSAQEeilVLRHA 576
Cdd:TIGR02168 379 EQLETLRSKVAQL-----------ELQIASLNNEIERLEARL-------ERLEDRRERLQQEIEELLKKLEE---AELKE 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 577 MEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEveisnlQASFQLQSQHQERASQLQGeVEKLQADCSGLQNECDS 656
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAE------QALDAAERELAQLQARLDS-LERLQENLEGFSEGVKA 510
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 528494940 657 LRAEKSTLMQKLNRLEE--ELDSSRER--SATLSSNLNAL 692
Cdd:TIGR02168 511 LLKNQSGLSGILGVLSEliSVDEGYEAaiEAALGGRLQAV 550
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
178-713 |
7.68e-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: 7.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 178 REQML--EQKLATLQRLLASTQEAsESSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGIRKELVALTEDKHNYE---T 252
Cdd:COG4913 241 HEALEdaREQIELLEPIRELAERY-AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEarlD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 253 TAKESLRRV--------------LQEKIE-VVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDL 317
Cdd:COG4913 320 ALREELDELeaqirgnggdrleqLEREIErLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 318 TEKIKLAEDKHEELTQKGLNEKKELQMRIEEME-------EKEQALQARI-EALQADND---FTNE-------------- 372
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLErrksnipARLLALRDALaEALGLDEAelpFVGElievrpeeerwrga 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 373 --------RLTAL---QAVRQLKEAVDSsiNKLS---NFDEV-IDAHLQNNQTTVDNSLPspdrlkeNQIDAKECDMSDT 437
Cdd:COG4913 480 iervlggfALTLLvppEHYAAALRWVNR--LHLRgrlVYERVrTGLPDPERPRLDPDSLA-------GKLDFKPHPFRAW 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 438 LspskekssddtsdgqmeEQELNEPQNRVSL-----LKEMDRSL-EAGDTEQviPHIHRELQEAQELA-------NTGKQ 504
Cdd:COG4913 551 L-----------------EAELGRRFDYVCVdspeeLRRHPRAItRAGQVKG--NGTRHEKDDRRRIRsryvlgfDNRAK 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 505 KclelqAMLEEERktnrqqtEESAKQIRFLQTQLAKLQTDMEALREQREntITTTREELYSAQEEILVLRHAMEAATAER 584
Cdd:COG4913 612 L-----AALEAEL-------AELEEELAEAEERLEALEAELDALQERRE--ALQRLAEYSWDEIDVASAEREIAELEAEL 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 585 EReITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQADCSGLQNECDSLRAEKstl 664
Cdd:COG4913 678 ER-LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE--- 753
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 528494940 665 mqklnRLEEELDSSRER--SATLSSNLNALEKSQGDLENKLGSIQDQHQQD 713
Cdd:COG4913 754 -----RFAAALGDAVERelRENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
456-646 |
7.93e-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: 45.91 E-value: 7.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 456 EQELNEPQNRVSLLKEMDRSLEAG--DTEQVIPHIHRELQEAQELANTGKQKCLELQAMLEEERKTNRQQTEESAKQIRF 533
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQlaALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 534 LQ-----------------TQLAKLQTDMEAL---REQRENTITTTREELYSAQEEILVLRHAMEAATAEREREITALQG 593
Cdd:COG4942 113 LYrlgrqpplalllspedfLDAVRRLQYLKYLapaRREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 528494940 594 DLSIVTAELDKWRQTAAKYEVEISNLQASfqlqsqhqerASQLQGEVEKLQAD 646
Cdd:COG4942 193 LKAERQKLLARLEKELAELAAELAELQQE----------AEELEALIARLEAE 235
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
30-106 |
8.32e-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: 8.32e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528494940 30 IGRSVarcrpaQNNATFDCKVLSRNHALvwFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEesppCEVLSGDIIQFG 106
Cdd:cd22682 24 IGRSV------ESQVQIDDDSVSRYHAK--LAVNPSAVSIIDLGSTNGTIVNGKKIPKLAS----CDLQNGDQIKIG 88
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
666-776 |
8.51e-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: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 666 QKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQ------------DQHQQDASKLKIQLAQAESRTRD--- 730
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlaeyswdeidvASAEREIAELEAELERLDASSDDlaa 689
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 528494940 731 LQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLKLLQDK 776
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
562-736 |
8.90e-05 |
|
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: 44.92 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 562 ELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQAsfqlqsqHQERASQLQGEVE 641
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA-------RIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 642 K---LQAdcsgLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLK 718
Cdd:COG1579 87 NnkeYEA----LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|....*....
gi 528494940 719 IQLAQAESRT-RDLQKEYD 736
Cdd:COG1579 163 AEREELAAKIpPELLALYE 181
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
600-765 |
9.79e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 9.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 600 AELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQADCSGLQNEcdslraeksTLMQKLNRLEEELDSSR 679
Cdd:PRK04863 837 AELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADE---------TLADRVEEIREQLDEAE 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 680 ERSATLSSNLNALEKsqgdLENKLGSIQdQHQQDASKLKIQLAQAESRTRDLQKE---------------YDDTQSLLSD 744
Cdd:PRK04863 908 EAKRFVQQHGNALAQ----LEPIVSVLQ-SDPEQFEQLKQDYQQAQQTQRDAKQQafaltevvqrrahfsYEDAAEMLAK 982
|
170 180
....*....|....*....|....*...
gi 528494940 745 -------LRQRYEQTEQEKRSINDELEQ 765
Cdd:PRK04863 983 nsdlnekLRQRLEQAEQERTRAREQLRQ 1010
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
163-395 |
9.85e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.84 E-value: 9.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 163 QELFQLSQYLQEALHREQMLEQKLATLQRLlastqEASESSWQALIDEDRLLSRLEVMGNQLQ-AYSK-NQTEDGI---- 236
Cdd:COG0497 172 KELEELRADEAERARELDLLRFQLEELEAA-----ALQPGEEEELEEERRRLSNAEKLREALQeALEAlSGGEGGAldll 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 237 ---RKELVALTEDKHNYETTAkESLRRVLQEKIEVVRklsEVERSLSNTEDECTHLREMNERtQEELRELANKYNGAVNE 313
Cdd:COG0497 247 gqaLRALERLAEYDPSLAELA-ERLESALIELEEAAS---ELRRYLDSLEFDPERLEEVEER-LALLRRLARKYGVTVEE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 314 IKDLTEKIKlaedkhEELTQkglnekkelqmrIEEMEEKEQALQARIEALQADNDFTNERLTAL--QAVRQLKEAVDSSI 391
Cdd:COG0497 322 LLAYAEELR------AELAE------------LENSDERLEELEAELAEAEAELLEAAEKLSAArkKAAKKLEKAVTAEL 383
|
....
gi 528494940 392 NKLS 395
Cdd:COG0497 384 ADLG 387
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
5-110 |
1.46e-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: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 5 LAVFSCRPnshpFQERHVYLDE-PVKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTgkFYLQDTKSSNGTFINSQ 83
Cdd:cd22665 3 LKVFSQAH----GPEKDFPLYEgENVIGRD------PSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNK 70
|
90 100
....*....|....*....|....*....
gi 528494940 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 ... |
433-765 |
1.46e-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: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 433 DMSDTLSPSKEKSSDDTSDGQMEEQELNEPQNRVSLLKEMDRSLEAGDteqviphihrELQEAQELANtgkqkclELQAM 512
Cdd:COG3096 310 EMARELEELSARESDLEQDYQAASDHLNLVQTALRQQEKIERYQEDLE----------ELTERLEEQE-------EVVEE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 513 LEEERKTNRQQTEESAKQIRFLQTQLAKLQTDME--------------ALREQR-------------ENTITTTREELYS 565
Cdd:COG3096 373 AAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDvqqtraiqyqqavqALEKARalcglpdltpenaEDYLAAFRAKEQQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 566 AQEEILVLRHAMEAATAEREREITALQGDLSIV--TAELDKW---RQTAAKYEVEISNLQASFQLQSQHQE--RASQLQG 638
Cdd:COG3096 453 ATEEVLELEQKLSVADAARRQFEKAYELVCKIAgeVERSQAWqtaRELLRRYRSQQALAQRLQQLRAQLAEleQRLRQQQ 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 639 EVEKLQADCSGLQNEC----DSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLEnKLGSIQDQHQQDA 714
Cdd:COG3096 533 NAERLLEEFCQRIGQQldaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELA-ARAPAWLAAQDAL 611
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 528494940 715 SKLKIQLAQAESRTRDLQkeyDDTQSLLSDLRQRY---EQTEQEKRSINDELEQ 765
Cdd:COG3096 612 ERLREQSGEALADSQEVT---AAMQQLLEREREATverDELAARKQALESQIER 662
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
313-764 |
1.51e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.34 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 313 EIKDLTEKIKLAEDKHEELTQ--KGLNEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQAVRQLKEAvdss 390
Cdd:TIGR00618 227 ELKHLREALQQTQQSHAYLTQkrEAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAV---- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 391 inklsnfdevidAHLQNNQTTVDNSLPSPDRLKENQIDAKECDMSDTLSPSKEKSSDDTsdgQMEEQELNEPQNRVSLLK 470
Cdd:TIGR00618 303 ------------TQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQT---LHSQEIHIRDAHEVATSI 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 471 EMDRSLEAGDTEqvipHIHRElqeaQELANTGKQKCLELQAMLEEERKTNRQQTEESAKQiRFLQTQLAKLQTDMEALRE 550
Cdd:TIGR00618 368 REISCQQHTLTQ----HIHTL----QQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF-RDLQGQLAHAKKQQELQQR 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 551 QRENTITTTREElysAQEEILVLRHAMEAATAEREREitALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQ 630
Cdd:TIGR00618 439 YAELCAAAITCT---AQCEKLEKIHLQESAQSLKERE--QQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHP 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 631 ERASQLQGEVEKLQADCSGLQNEC-------DSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKL 703
Cdd:TIGR00618 514 NPARQDIDNPGPLTRRMQRGEQTYaqletseEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNIT 593
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528494940 704 GSIQDQHQQDaSKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELE 764
Cdd:TIGR00618 594 VRLQDLTEKL-SEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQL 653
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
52-107 |
1.60e-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: 1.60e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528494940 52 SRNHALVWFDHKTG---------KFYLQDTkSSNGTFINSQRLSRGSEesppCEVLSGDIIQFGV 107
Cdd:cd22667 40 SRKHATLTVLHPEAnlsdpdtrpELTLKDL-SKYGTFVNGEKLKGGSE----VTLKDGDVITFGV 99
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
325-765 |
1.70e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 325 EDKHEELTQKGLNEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQAVRQLKEAVDSSINKLSNFDEVIDAH 404
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 405 LQNNQttVDNSL-PSPDRLKENQIDAKEcdmsdtLSPSKEKSSDDTSDGQMEEQELNEPQNRVSLLKEM---DRSLEAGD 480
Cdd:COG4717 132 QELEA--LEAELaELPERLEELEERLEE------LRELEEELEELEAELAELQEELEELLEQLSLATEEelqDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 481 TEQVIPHIHRELQEAQELANTGKQKCLELQAMLEEERKTNRQQteeSAKQIRFLQTQLAKLQTDMEALreqrENTITTTR 560
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK---EARLLLLIAAALLALLGLGGSL----LSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 561 EELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEV 640
Cdd:COG4717 277 GVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 641 EKLQAdcsglQNECDSLRAEKSTLMQKLN-RLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQ--------DQHQ 711
Cdd:COG4717 357 EELEE-----ELQLEELEQEIAALLAEAGvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEellealdeEELE 431
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 528494940 712 QDASKLKIQLAQAESRTRDLQKEYDDTQSLLSDLR--QRYEQTEQEKRSINDELEQ 765
Cdd:COG4717 432 EELEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAELRE 487
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
216-775 |
1.83e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 216 RLEVMGNQLQAYSKNQTEDGIRKELVALTEDKHNYETTaKESLRRVLQEKIEVVRKLSEVERSLSNTEDECthlremnER 295
Cdd:PRK01156 151 RKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYL-EEKLKSSNLELENIKKQIADDEKSHSITLKEI-------ER 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 296 TQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEELTQKGLNEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLT 375
Cdd:PRK01156 223 LSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFK 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 376 ALQAVRQLKEAVDSSINKLSNFDEVID--AHLQNNQTTVDNSLPSPDRLKeNQIDAKECDMSDTLSPSK----------- 442
Cdd:PRK01156 303 YKNDIENKKQILSNIDAEINKYHAIIKklSVLQKDYNDYIKKKSRYDDLN-NQILELEGYEMDYNSYLKsieslkkkiee 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 443 -EKSSDDTSDGQMEEQELNE--PQNRVSLLKEMDRSL-----EAGDTEQVIPHIHRELQEAQELAN--TGKQKCLELQAM 512
Cdd:PRK01156 382 ySKNIERMSAFISEILKIQEidPDAIKKELNEINVKLqdissKVSSLNQRIRALRENLDELSRNMEmlNGQSVCPVCGTT 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 513 LEEErKTNRQQTEESAKQIRfLQTQLAKLQTDMEALREQRENTItttREELYSAQEEILVLRhAMEAATAEREREITALQ 592
Cdd:PRK01156 462 LGEE-KSNHIINHYNEKKSR-LEEKIREIEIEVKDIDEKIVDLK---KRKEYLESEEINKSI-NEYNKIESARADLEDIK 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 593 GDLSIVTAELDKWRQTAAKYE-VEISNLQASFQ----------------LQSQHQERASQLQGEVEKLQADCSGLQNEcd 655
Cdd:PRK01156 536 IKINELKDKHDKYEEIKNRYKsLKLEDLDSKRTswlnalavislidietNRSRSNEIKKQLNDLESRLQEIEIGFPDD-- 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 656 slraeKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLEN--KLGSIQDQHQQDASKLKIQLAQAESRTRDLQK 733
Cdd:PRK01156 614 -----KSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNykKQIAEIDSIIPDLKEITSRINDIEDNLKKSRK 688
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 528494940 734 EYDDTQSLLSD-------LRQRYEQTEQEKRSINDELEQCKVNLKLLQD 775
Cdd:PRK01156 689 ALDDAKANRARlestieiLRTRINELSDRINDINETLESMKKIKKAIGD 737
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
209-660 |
2.60e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 209 DEDRLLSRLEVMGNQlqaysKNQTEDGIRKELVALTEDKHNYETtAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTH 288
Cdd:PRK02224 308 DAEAVEARREELEDR-----DEELRDRLEECRVAAQAHNEEAES-LREDADDLEERAEELREEAAELESELEEAREAVED 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 289 LREMNERTQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEELTQK-------------GLNEKKELQM----------- 344
Cdd:PRK02224 382 RREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREReaeleatlrtareRVEEAEALLEagkcpecgqpv 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 345 -------RIEEMEEKEQALQARIEALQADNDFTNERLTALQAVRQLKEAVDSSINKLSNFDEVIDAHlqnnqttvdnslp 417
Cdd:PRK02224 462 egsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAER------------- 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 418 spdrlkenqidakecdmsdtlspskekssddtsdgqmeEQELNEPQNRVSLLKEMDRSLEAGDTEQviphiHRELQEAQE 497
Cdd:PRK02224 529 --------------------------------------RETIEEKRERAEELRERAAELEAEAEEK-----REAAAEAEE 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 498 LAntgkQKCLELQAMLEEERKTNRQQTEESAKqIRFLQTQLAKLQTDMEALREQRENTI---TTTREELYSAQEEILVLR 574
Cdd:PRK02224 566 EA----EEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERLREKREALAelnDERRERLAEKRERKRELE 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 575 -----HAMEAATAEREREITALQGdlsiVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQLQGEVEKLQA---D 646
Cdd:PRK02224 641 aefdeARIEEAREDKERAEEYLEQ----VEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEALEAlydE 716
|
490
....*....|....
gi 528494940 647 CSGLQNECDSLRAE 660
Cdd:PRK02224 717 AEELESMYGDLRAE 730
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
561-771 |
2.72e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 561 EELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQtaakyevEISNLQASFQLQSQHQERASQLQGEV 640
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEK-------EVKELEELKEEIEELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 641 EKLQADCSGLQNECDSLRAEKSTLMQKLNRLeEELDSSRERSATLS-------SNLNALEKSQGDLENKLGSIQDQHQQD 713
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSefyeeylDELREIEKRLSRLEEEINGIEERIKEL 333
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 528494940 714 ASKlkiqlaqaESRTRDLQKEYDDTQSLLSDLRQRyEQTEQEKRSINDELEQCKVNLK 771
Cdd:PRK03918 334 EEK--------EERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLT 382
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
1-106 |
3.18e-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: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 1 MPSALAVFSCRPNSHPFQERHVYLDEPVKIGRSvARC-----RPAQnnatfdckVLSRNHALVWFDHktGKFYLQDTkSS 75
Cdd:COG3456 1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRS-ADCdwvlpDPDR--------SVSRRHAEIRFRD--GAFCLTDL-ST 68
|
90 100 110
....*....|....*....|....*....|....
gi 528494940 76 NGTFIN--SQRLSRGSEesppcEVLS-GDIIQFG 106
Cdd:COG3456 69 NGTFLNgsDHPLGPGRP-----VRLRdGDRLRIG 97
|
|
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
53-106 |
3.79e-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: 3.79e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 528494940 53 RNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPcevlsGDIIQFG 106
Cdd:cd22700 36 EQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAP-----GDVLRFG 84
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
628-765 |
4.87e-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: 42.60 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 628 QHQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALeKSQGDLENKLGSIQ 707
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNNKEYEALQKEIE 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 528494940 708 DQhQQDASKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQ 765
Cdd:COG1579 100 SL-KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
16-111 |
5.42e-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: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 16 PFQERHVYLD-EPVKIGRSvarcrpAQNNATFDCKVLSRNHALVWFdhKTGKFYLQDTKSSNGTFINSQRLSRgseespP 94
Cdd:cd22693 7 TLQGQTFPIDkSGITIGRA------DDNDLVLSDDFVSSRHARIYL--QGSSWYLEDLGSTNGTFVNGNRVTQ------P 72
|
90
....*....|....*..
gi 528494940 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 ... |
452-773 |
5.58e-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: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 452 GQMEEQELNEPQNRVSLLKEMDRSLEAGDTEQVIPHIHRELQEAQELANTGKQKCLELQAMLEEERKTNRQQtEESAKQI 531
Cdd:pfam02463 142 GKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYY-QLKEKLE 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 532 RFLQTQLAKLQTDMEALREQRENTITTTREELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTAELDKwrqtaaK 611
Cdd:pfam02463 221 LEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAK------E 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 612 YEVEISNLQASFQLQSQHQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNA 691
Cdd:pfam02463 295 EEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 692 LEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLK 771
Cdd:pfam02463 375 LLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELE 454
|
..
gi 528494940 772 LL 773
Cdd:pfam02463 455 KQ 456
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
258-394 |
5.73e-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: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 258 LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEEL-TQKGL 336
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrNNKEY 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528494940 337 N----EKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQA-VRQLKEAVDSSINKL 394
Cdd:COG1579 92 EalqkEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAeLEEKKAELDEELAEL 154
|
|
| FHA_RAD53-like_rpt2 |
cd22690 |
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
12-103 |
5.87e-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: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 12 PNSHPfqerHVYL-DEPVKIGRSvarcrpAQNNATFDCKVLSRNHALVWFD-HKTGK--FYLQDTkSSNGTFINSQRLSR 87
Cdd:cd22690 8 NPSYP----DIELtQNTTFIGRS------KDCDEEITDPRISKHHCIITRKrSGKGLddVYVTDT-STNGTFINNNRLGK 76
|
90
....*....|....*.
gi 528494940 88 GSEesppCEVLSGDII 103
Cdd:cd22690 77 GSQ----SLLQDGDEI 88
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
515-776 |
6.21e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 515 EERKTNRQQTEESAKQIRFLQTQLAKLQTDmealREQRENTITTTREELYSAQEEILVLRHAMEAATAEREREITALQGD 594
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 595 LSIVTAELDKWRQTAAKYEVEISNLQAsfQLQSQHQERASQLQGEVEKLQADcsglQNECDSLRAEKSTLMQKLNRLEEE 674
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELNK--KIKDLGEEEQLRVKEKIGELEAE----IASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 675 LDSSRErsatlssnlnaleKSQGDLENKLGSIQDQhqqdasklKIQLAQAESRTRDLQKEYDDtqsllsdLRQRYEQTEQ 754
Cdd:TIGR02169 327 LEAEID-------------KLLAEIEELEREIEEE--------RKRRDKLTEEYAELKEELED-------LRAELEEVDK 378
|
250 260
....*....|....*....|..
gi 528494940 755 EKRSINDELEQCKVNLKLLQDK 776
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKRE 400
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
49-112 |
6.37e-04 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 (PML1) and similar proteins; PML1 is an FHA domain-containing protein required for efficient splicing and pre-mRNA nuclear retention. It is a component of the pre-mRNA retention and splicing (RES) complex composed of at least BUD13, IST3, and PML1. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438733 [Multi-domain] Cd Length: 129 Bit Score: 40.50 E-value: 6.37e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528494940 49 KVLSRNHALVWFDHKTG--KFYLQDTKSSNGTFINsqrlsrgSEESPPC---EVLSGDIIQFGVDVTEN 112
Cdd:cd22681 64 ETCSKQHCVIQFRNVKGilKPYIMDLDSSNGTCLN-------DNVIPSSryvELRSGDVITFSKSNDYE 125
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
162-392 |
7.05e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 162 SQELFQLSQYLQEALHREQMLEQKLATLQRLLASTQEASESSWQALIDEDRLLSRLEVMGNQLQAySKNQTEDGIRKELV 241
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA-ELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 242 ALTEDKHNYETTAKESLRRVLQEKIEVV---RKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLT 318
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLlspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528494940 319 EKIKLAEDKHEELTQkglnEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQAVRQLKEAVDSSIN 392
Cdd:COG4942 178 ALLAELEEERAALEA----LKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
650-776 |
1.44e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 650 LQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLgsiqDQHQQDASKLKIQLAQAESrtr 729
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI----EEVEARIKKYEEQLGNVRN--- 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 528494940 730 dlQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLKLLQDK 776
Cdd:COG1579 88 --NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE 132
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
233-401 |
1.61e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 233 EDGIRKELVALTEDKHNYETTAKESLRRVLQEKI----EVVRKLSEVER------SLSNTEDECTHLREMNERTQEELRE 302
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEELAELLKELEELGFesveELEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDK 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 303 LANKYNGAVNEIKDLTEKIKLAEDKHEELTQKGLNEKK-ELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQAVR 381
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYlELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAK 710
|
170 180
....*....|....*....|
gi 528494940 382 QLKEAVDSSINKLSNFDEVI 401
Cdd:PRK03918 711 KELEKLEKALERVEELREKV 730
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
328-776 |
1.72e-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: 41.96 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 328 HEELTQKGLNEKKELQMRIEEMEEKEQALQARIEALQADNDF---TNERLTALQAVRQLKEAVDSSINKLSNFDEVIDAH 404
Cdd:TIGR00606 157 HQEDSNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQgqkVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESS 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 405 LQNNQTTVDNSLPSPDRLKE-NQIDAKECDMSDTLSPSKEKSSDDTSDGQMEEQELNEP-QNRVSLLKEM--DRSLEAGD 480
Cdd:TIGR00606 237 REIVKSYENELDPLKNRLKEiEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVfQGTDEQLNDLyhNHQRTVRE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 481 TEQVIPHIHREL----QEAQELaNTGKQKCLELQAMLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALRE-QRENT 555
Cdd:TIGR00606 317 KERELVDCQRELeklnKERRLL-NQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSErQIKNF 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 556 ITTTREELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQ 635
Cdd:TIGR00606 396 HTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 636 LQGEVEKLQADCSGLQN---------ECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLnALEKSQGDLENKLGSI 706
Cdd:TIGR00606 476 LDQELRKAERELSKAEKnsltetlkkEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQME-MLTKDKMDKDEQIRKI 554
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528494940 707 QDQHQQDASKLKIQL---AQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKVNLKLLQDK 776
Cdd:TIGR00606 555 KSRHSDELTSLLGYFpnkKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDK 627
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
573-765 |
1.74e-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: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 573 LRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEiSNLQASFQLQSQHQERASQLQGEVEKLQADCSGLQN 652
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQK-NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 653 ECDSLRAEKSTLMQKLNRLEE--ELDSSRERSATLSSNLNALEKSQGD-------LENKLGSIQDQHQQDASK----LKI 719
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPnhpdviaLRAQIAALRAQLQQEAQRilasLEA 320
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 528494940 720 QLAQAESRTRDLQKEYDDTQSLLSDL---RQRYEQTEQEKRSINDELEQ 765
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELYES 369
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
648-768 |
1.78e-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: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 648 SGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAESR 727
Cdd:smart00787 147 EGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKK 226
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 528494940 728 TRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKV 768
Cdd:smart00787 227 LEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
518-777 |
1.81e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 518 KTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQRENTITTTREELYSAQEEILvlrhAMEAATAEREREITALQGDLSI 597
Cdd:PHA02562 177 RELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAK----TIKAEIEELTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 598 VTAELDKWRQTAAKYEVEISNLQASFQLQSQHQER---ASQLQGEVEKLQadcsglqnecdSLRAEKSTLMQKLNRLEEE 674
Cdd:PHA02562 253 PSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGVCptcTQQISEGPDRIT-----------KIKDKLKELQHSLEKLDTA 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 675 LDSSRERSatlsSNLNALEKSQGDLENKLgsiqDQHQQDASKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQ 754
Cdd:PHA02562 322 IDELEEIM----DEFNEQSKKLLELKNKI----STNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVK 393
|
250 260
....*....|....*....|...
gi 528494940 755 EKRSINDELEQCKVNLKLLQDKG 777
Cdd:PHA02562 394 TKSELVKEKYHRGIVTDLLKDSG 416
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
229-554 |
1.89e-03 |
|
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: 41.93 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 229 KNQTEDGIRKELVALTEDKHNYETTAKESLRRVLQekievvrKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYN 308
Cdd:TIGR04523 301 NNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNK-------IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 309 GAVNEIKDLTEKIKLAEDKHEELTQKGLNEKK---ELQMRIEEMEEKEQALQARIEALQADNDFTNERL----------- 374
Cdd:TIGR04523 374 KLKKENQSYKQEIKNLESQINDLESKIQNQEKlnqQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIkdltnqdsvke 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 375 TALQAVRQLKEAVDSSINKLSNFDEVIDAHLQNNQTTVDNSLPSPDRLKEN--QIDAKECDMSDTLSPSKEKSSDDTSDG 452
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEkkELEEKVKDLTKKISSLKEKIEKLESEK 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 453 QMEEQELNEPQNRvslLKEMDRSLEAGDTEQVIPHIHRELQEAQELANTGKQKCLELQAML---EEERKTNRQQTEESAK 529
Cdd:TIGR04523 534 KEKESKISDLEDE---LNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIdqkEKEKKDLIKEIEEKEK 610
|
330 340
....*....|....*....|....*
gi 528494940 530 QIRFLQTQLAKLQTDMEALREQREN 554
Cdd:TIGR04523 611 KISSLEKELEKAKKENEKLSSIIKN 635
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
508-765 |
1.99e-03 |
|
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: 41.86 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 508 ELQAMLEEERKTNRQQtEESAKQIRFLQTQLAKLQTDMEALR-EQRENTITTTREELYSAQE-EILVLRHamEAATAERE 585
Cdd:COG3096 847 ELERELAQHRAQEQQL-RQQLDQLKEQLQLLNKLLPQANLLAdETLADRLEELREELDAAQEaQAFIQQH--GKALAQLE 923
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 586 REITALQGDlsivtaeldkwrqTAAKYEVEISNLQASfQLQSQHQERASQLQGEVEKLQ----ADCSGLQNECDSLrAEK 661
Cdd:COG3096 924 PLVAVLQSD-------------PEQFEQLQADYLQAK-EQQRRLKQQIFALSEVVQRRPhfsyEDAVGLLGENSDL-NEK 988
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 662 stLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQ---QDASKLKIQL-AQAESRTRDlqkEYDD 737
Cdd:COG3096 989 --LRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQeleQELEELGVQAdAEAEERARI---RRDE 1063
|
250 260
....*....|....*....|....*...
gi 528494940 738 TQSLLSDLRQRYEQTEQEKRSINDELEQ 765
Cdd:COG3096 1064 LHEELSQNRSRRSQLEKQLTRCEAEMDS 1091
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
490-770 |
2.09e-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: 41.70 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 490 RELQEAQELANTGKQKCL----ELQAMLEEERKTNRQQT------------------------EESAKQIRFLQTQLAKL 541
Cdd:pfam01576 731 RDLQARDEQGEEKRRQLVkqvrELEAELEDERKQRAQAVaakkkleldlkeleaqidaankgrEEAVKQLKKLQAQMKDL 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 542 QTDMEALREQRENTITTTRE----------ELYSAQEEILVLRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAK 611
Cdd:pfam01576 811 QRELEEARASRDEILAQSKEsekklknleaELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEAR 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 612 ---YEVEISNLQASFQLQSQHQERASQlqgEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELdssRERSATLSSN 688
Cdd:pfam01576 891 iaqLEEELEEEQSNTELLNDRLRKSTL---QVEQLTTELAAERSTSQKSESARQQLERQNKELKAKL---QEMEGTVKSK 964
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 689 LNAlekSQGDLENKLGSIQDQHQQDASklkiQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSINDELEQCKV 768
Cdd:pfam01576 965 FKS---SIAALEAKIAQLEEQLEQESR----ERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKR 1037
|
..
gi 528494940 769 NL 770
Cdd:pfam01576 1038 QL 1039
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
266-776 |
2.36e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 266 IEVVRKLSEVERSLSNTEDECTHLremnertqEELRELANKYNGAVNEIKDLTEKIKLAEDKHEELtqkglnEKKELQMR 345
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELL--------EPIRELAERYAAARERLAELEYLRAALRLWFAQR------RLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 346 IEEMEEKEQALQARIEALQADNDFTNERLTALQavRQLKEAVDSSINKLsnfdevidahlqnnqttvdnslpspdrlkEN 425
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELE--AQIRGNGGDRLEQL-----------------------------ER 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 426 QIDAKecdmsdtlspskekssddtsdgqmeEQELNEPQNRVSLLKEMDRSLEAGdteqvIPHIHRELQEAQELANtgkqk 505
Cdd:COG4913 346 EIERL-------------------------ERELEERERRRARLEALLAALGLP-----LPASAEEFAALRAEAA----- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 506 clELQAMLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALReQRENTITttreelysaqEEILVLRHAMEAATAERE 585
Cdd:COG4913 391 --ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE-RRKSNIP----------ARLLALRDALAEALGLDE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 586 REITALqGDLSIVTAELDKWRQTA--------------AKYEVE----ISNLQASFQLQSQH-QERASQLQGE------- 639
Cdd:COG4913 458 AELPFV-GELIEVRPEEERWRGAIervlggfaltllvpPEHYAAalrwVNRLHLRGRLVYERvRTGLPDPERPrldpdsl 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 640 VEKLQADCSGLQN-----------------------------------------ECDSLRAEKSTLM------QKLNRLE 672
Cdd:COG4913 537 AGKLDFKPHPFRAwleaelgrrfdyvcvdspeelrrhpraitragqvkgngtrhEKDDRRRIRSRYVlgfdnrAKLAALE 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 673 EELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKIQLAQAE-SRTRDLQKEYDDTQSLLSDLRQRYEQ 751
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiAELEAELERLDASSDDLAALEEQLEE 696
|
570 580
....*....|....*....|....*
gi 528494940 752 TEQEKRSINDELEQCKVNLKLLQDK 776
Cdd:COG4913 697 LEAELEELEEELDELKGEIGRLEKE 721
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
695-770 |
3.45e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 695 SQGDLENKLGSIQ--DQHQQDASKLKIQLAQAESRTRDLQKEYDD-TQSLLSDLRQRYE-----QTEQEKRSINDELEQC 766
Cdd:PRK11281 61 VQQDLEQTLALLDkiDRQKEETEQLKQQLAQAPAKLRQAQAELEAlKDDNDEETRETLStlslrQLESRLAQTLDQLQNA 140
|
....
gi 528494940 767 KVNL 770
Cdd:PRK11281 141 QNDL 144
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
629-759 |
4.12e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 629 HQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNL---NALEKSQGDLENKlgS 705
Cdd:PRK04863 284 HLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALrqqEKIERYQADLEEL--E 361
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 528494940 706 IQDQHQQDASKL-KIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEqtEQEKRSI 759
Cdd:PRK04863 362 ERLEEQNEVVEEaDEQQEENEARAEAAEEEVDELKSQLADYQQALD--VQQTRAI 414
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
310-670 |
4.23e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 310 AVNEIKDLTEKIKLA----EDKHEELTQKGLNEKK--ELQMRIEEMEEKEQALQARIEALQADNDF-TNERLTALqAVRQ 382
Cdd:PRK11281 47 ALNKQKLLEAEDKLVqqdlEQTLALLDKIDRQKEEteQLKQQLAQAPAKLRQAQAELEALKDDNDEeTRETLSTL-SLRQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 383 LKEAVDSSINKLSNfdevidahLQNNQTTVDNSLPS----PDR----LKENQIDAKEcdMSDTLSPSKEKSSDDTSDGQM 454
Cdd:PRK11281 126 LESRLAQTLDQLQN--------AQNDLAEYNSQLVSlqtqPERaqaaLYANSQRLQQ--IRNLLKGGKVGGKALRPSQRV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 455 E---EQELNEPQNrvSLLKemdRSLEAGDTEQVIphihreLQEAQELAnTGKQKCLE-----LQAMLEEERktnRQQTEE 526
Cdd:PRK11281 196 LlqaEQALLNAQN--DLQR---KSLEGNTQLQDL------LQKQRDYL-TARIQRLEhqlqlLQEAINSKR---LTLSEK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 527 SAKQIRFLQtQLAKLQTDMEALREQRENT------ITTTREELYSAQEEILVlRHAMEAAT-AER--EREITALQGDLsI 597
Cdd:PRK11281 261 TVQEAQSQD-EAARIQANPLVAQELEINLqlsqrlLKATEKLNTLTQQNLRV-KNWLDRLTqSERniKEQISVLKGSL-L 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 598 VTAELDKWRQT--AAKYEVEISNLQASFQLQ----SQHQERASQLQGEVEKLQADCSG-----LQNECDSLRAEKSTLMQ 666
Cdd:PRK11281 338 LSRILYQQQQAlpSADLIEGLADRIADLRLEqfeiNQQRDALFQPDAYIDKLEAGHKSevtdeVRDALLQLLDERRELLD 417
|
....
gi 528494940 667 KLNR 670
Cdd:PRK11281 418 QLNK 421
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
514-621 |
4.27e-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: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 514 EEERKTNRQQTEESAKQIRFLQTQLAKLQ---TDMEALREQRENTITTTREELYSAQEEilvlrhamEAATAEREREITA 590
Cdd:COG2433 398 EREKEHEERELTEEEEEIRRLEEQVERLEaevEELEAELEEKDERIERLERELSEARSE--------ERREIRKDREISR 469
|
90 100 110
....*....|....*....|....*....|.
gi 528494940 591 LQGDLSIVTAELDKWRQTAAKYEVEISNLQA 621
Cdd:COG2433 470 LDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
239-768 |
4.38e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 239 ELVALTEDKHNYETTAKESLRRV--LQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKD 316
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 317 LTEKIKLAEDKHEEltqkglnEKKELQMRIEEMEEKEQALQARIEAlQADNDFTNERLTALQAVRQLKEAVDSSinklsn 396
Cdd:PTZ00121 1362 AEEKAEAAEKKKEE-------AKKKADAAKKKAEEKKKADEAKKKA-EEDKKKADELKKAAAAKKKADEAKKKA------ 1427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 397 fDEVIDAhlqnnqttvdnslpspDRLKENQIDAKECDMSDTLSPSKEKSsddtsdgqmeeQELNEPQNRVSLLKEMDRSL 476
Cdd:PTZ00121 1428 -EEKKKA----------------DEAKKKAEEAKKADEAKKKAEEAKKA-----------EEAKKKAEEAKKADEAKKKA 1479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 477 EAGdteqviphihRELQEAQELANTGKQKCLELQAMLEEERKTNR-QQTEESAKQIRFLQTQLAKLQTDMEALREQRENT 555
Cdd:PTZ00121 1480 EEA----------KKADEAKKKAEEAKKKADEAKKAAEAKKKADEaKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD 1549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 556 ITTTREELYSAQEeilvlRHAMEAATAEREREITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERASQ 635
Cdd:PTZ00121 1550 ELKKAEELKKAEE-----KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 636 LQGEVEKLQADCSGLQNECDSLR-AEKSTLMQKLNRLE-EELDSSRERSATLSSNLNALEKSQGDLENKLGSiQDQHQQD 713
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKkAEELKKAEEENKIKaAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK-EAEEAKK 1703
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 528494940 714 ASKLKIQLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQTEQEKRSIN-DELEQCKV 768
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKkDEEEKKKI 1759
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
499-756 |
4.50e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.45 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 499 ANTGKQKCLELQAMLEEERKTNRQQteesakqirflQTQLAKLQtdmEALREQrENTITTTREELYSAQeeilvlrhame 578
Cdd:PRK11637 42 ASDNRDQLKSIQQDIAAKEKSVRQQ-----------QQQRASLL---AQLKKQ-EEAISQASRKLRETQ----------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 579 aataereREITALQGDLSIVTAELDKWRQTAAKYEVEIS-NLQASFQlQSQHQERASQLQGE----VEKLQA-------- 645
Cdd:PRK11637 96 -------NTLNQLNKQIDELNASIAKLEQQQAAQERLLAaQLDAAFR-QGEHTGLQLILSGEesqrGERILAyfgylnqa 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 646 ---DCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENKLGsiQDQHQ-----QDASKL 717
Cdd:PRK11637 168 rqeTIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQ--KDQQQlselrANESRL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 528494940 718 KIQLAQAE--------------SRTRDLQKEYDDTQSllsdlrqRYEQTEQEK 756
Cdd:PRK11637 246 RDSIARAEreakaraereareaARVRDKQKQAKRKGS-------TYKPTESER 291
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
172-379 |
4.55e-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: 39.63 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 172 LQEALHREQMLEQKLATLQRLLASTQEASESSwqalidEDRLLSRLEvmgNQLQAYSKNQTEDGIRKELvaltEDKHNYE 251
Cdd:pfam00261 24 LEEAEKRAEKAEAEVAALNRRIQLLEEELERT------EERLAEALE---KLEEAEKAADESERGRKVL----ENRALKD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 252 TTAKESLRRVLQEKIEVV----RKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDL---TEKIKLA 324
Cdd:pfam00261 91 EEKMEILEAQLKEAKEIAeeadRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLeasEEKASER 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 528494940 325 EDKHEElTQKGLNEK-KELQMRIEEMEEKEQALQARIEALQADNDFTNERLTALQA 379
Cdd:pfam00261 171 EDKYEE-QIRFLTEKlKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISE 225
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
256-358 |
4.72e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 256 ESLRRVLQEKI-EVVRKLSEVERSLSNTEDEcthLREMNERTQEELRELANKYNGAVNE--------IKDLTEKIKL--A 324
Cdd:PRK00409 526 EELERELEQKAeEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLEEAEKEAQQAIKEakkeadeiIKELRQLQKGgyA 602
|
90 100 110
....*....|....*....|....*....|....*..
gi 528494940 325 EDKHEELT--QKGLNEK-KELQMRIEEMEEKEQALQA 358
Cdd:PRK00409 603 SVKAHELIeaRKRLNKAnEKKEKKKKKQKEKQEELKV 639
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
173-366 |
5.05e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 173 QEALHREQMLEQKLATLQRLLASTQEasesswqalidedrllsRLEVMGNQLQAYSKNQTEdgIRKELVALTEDKHNYET 252
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLKELPA-----------------ELAELEDELAALEARLEA--AKTELEDLEKEIKRLEL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 253 TAKESLRRV--LQEKIEVVRKlsevERSLSNTEDECTHLREMNERTQEELRELankyngaVNEIKDLTEKIKLAEDKHEE 330
Cdd:COG1579 67 EIEEVEARIkkYEEQLGNVRN----NKEYEALQKEIESLKRRISDLEDEILEL-------MERIEELEEELAELEAELAE 135
|
170 180 190
....*....|....*....|....*....|....*.
gi 528494940 331 LTQKGLNEKKELQMRIEEMEEKEQALQARIEALQAD 366
Cdd:COG1579 136 LEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
223-754 |
5.80e-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: 40.42 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 223 QLQAYSKNQTEDGIRKELVALTEDKHNYE--------TTAKESLRRVLQEKIEVVRK-----------LSEVERSLSNTE 283
Cdd:TIGR00606 597 NKELASLEQNKNHINNELESKEEQLSSYEdklfdvcgSQDEESDLERLKEEIEKSSKqramlagatavYSQFITQLTDEN 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 284 DECTHLREMNERTQEELRE----LANKYNGAVNEIKDLTEKIKLAEDKHEELTQKGLNEKKELQMR---IEEMEEKEQAL 356
Cdd:TIGR00606 677 QSCCPVCQRVFQTEAELQEfisdLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKekeIPELRNKLQKV 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 357 QARIEALQADNDFTNERLTALQAVRQLKEAVDSSINKLSNFDEVIDAHLQNNQTTVDNSLPSPDRLKENQIDAKECDmsd 436
Cdd:TIGR00606 757 NRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQE--- 833
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 437 tlspSKEKSSDDTSDGQMEEQELNEPQNRVSLLKEMDRSLEagdTEQVipHIHRELQEAQELANTGKQKCLELQAMLEEe 516
Cdd:TIGR00606 834 ----KQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELK---SEKL--QIGTNLQRRQQFEEQLVELSTEVQSLIRE- 903
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 517 rktnrqqTEESAKQIRFLQTQLAKLQTDMEALREQRENTITTTREELYSAQEE---ILVLRHAMEAATAE-REREITALQ 592
Cdd:TIGR00606 904 -------IKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKvknIHGYMKDIENKIQDgKDDYLKQKE 976
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 593 GDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQhQERASQLQGEVEKLQadcsglqNECDSLRAEKSTLMQKLNrlE 672
Cdd:TIGR00606 977 TELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKI-QERWLQDNLTLRKRE-------NELKEVEEELKQHLKEMG--Q 1046
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 673 EELDSSRERSATLSSNLNALEKSQGDLENKLGSIQDQHQQDASKLKI-QLAQAESRTRDLQKEYDDTQSLLSDLRQRYEQ 751
Cdd:TIGR00606 1047 MQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREpQFRDAEEKYREMMIVMRTTELVNKDLDIYYKT 1126
|
...
gi 528494940 752 TEQ 754
Cdd:TIGR00606 1127 LDQ 1129
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
167-702 |
6.13e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.34 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 167 QLSQYLQEALHREQMLEQKLATLQRLLASTQEASESSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGIRKELVALTED 246
Cdd:TIGR00618 370 ISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITC 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 247 KHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELRELANKYNGAVNEIKDLTEKIKLaed 326
Cdd:TIGR00618 450 TAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPL--- 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 327 khEELTQKGLNEKKELQmriEEMEEKEQALQARIEALQADNDFTNERLTALQAVRQLKEAVDSSINKLSNFDEVIDAHLQ 406
Cdd:TIGR00618 527 --TRRMQRGEQTYAQLE---TSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTE 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 407 NNQTTVDNSLPSPDRLKEN-QIDAKECDMSDTLSPSKEKSSDDTSDGQMEEQELNEPQNRVSLLKEMDRSLEAGDTEQVI 485
Cdd:TIGR00618 602 KLSEAEDMLACEQHALLRKlQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLA 681
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 486 P----HIHRELQEAQELANTGKQKCLELQAMLEEERKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQRENtitttre 561
Cdd:TIGR00618 682 LqkmqSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQART------- 754
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 562 elysaqeeilVLRHAMEAATAEREREITALQGDlsivtaelDKWRQTAAKYEVEISNLQASF----QLQSQHQERASQLQ 637
Cdd:TIGR00618 755 ----------VLKARTEAHFNNNEEVTAALQTG--------AELSHLAAEIQFFNRLREEDThllkTLEAEIGQEIPSDE 816
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528494940 638 GEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLENK 702
Cdd:TIGR00618 817 DILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGI 881
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
258-676 |
7.41e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.88 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 258 LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLREMNERTQEELR----ELANKYNGAVNEIKDLTEKIKLAEDKHEELTQ 333
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELEsrvaELKEELRQSREKHEELEEKYKELSASSEELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 334 KG---LNEKKELQMRIEEMEEKEQALQARIEALQADNDFTNERltALQAVRQLKEavdssinklsnfDEVIDAHLQNnqt 410
Cdd:pfam07888 116 EKdalLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKER--AKKAGAQRKE------------EEAERKQLQA--- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 411 tvdnslpspdrlKENQIDAKECDMSDTLSPSKEKSSDDTSDGQMEEQELNEPQNRVSLLKEMDRSLEAgdteqviphIHR 490
Cdd:pfam07888 179 ------------KLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEA---------LLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 491 ELQEAQELANTGKQKCLELQAMLEEeRKTNRQQTEESAKQIRFLQTQLAKLQTDME-ALREQRENTitttreelysAQEE 569
Cdd:pfam07888 238 ELRSLQERLNASERKVEGLGEELSS-MAAQRDRTQAELHQARLQAAQLTLQLADASlALREGRARW----------AQER 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 570 ILVLRhameAATAEREReITALQGDLSIVTAELDKWRQTAAKYEVEISNLQASFQLQSQHQERasqlqgEVEKLQADCSG 649
Cdd:pfam07888 307 ETLQQ----SAEADKDR-IEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRR------ELQELKASLRV 375
|
410 420
....*....|....*....|....*..
gi 528494940 650 LQNECDSLRAEKSTLMQKLNRLEEELD 676
Cdd:pfam07888 376 AQKEKEQLQAEKQELLEYIRQLEQRLE 402
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
253-719 |
7.61e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 39.70 E-value: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 253 TAKESLR-RVLQEKIEVVRKLSEVERSLSNTEDEctHLREMNERtQEELRELANKYNGAVNEIKDLTEKIKLAEDKHEEL 331
Cdd:pfam05483 197 LAFEELRvQAENARLEMHFKLKEDHEKIQHLEEE--YKKEINDK-EKQVSLLLIQITEKENKMKDLTFLLEESRDKANQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 332 TQKGLNEKKELQMRIE-------EMEEKEQALQARIEALQADNDFTNERLTALQAVRQLKEAVDSSINKLSNFDEVIDAH 404
Cdd:pfam05483 274 EEKTKLQDENLKELIEkkdhltkELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 405 LQNNQTTVDNSLPSPD-RLKENQIDAKECDMS-DTLSPSKEKSSDDTSDGQMEEQELNepqnrvSLLKEMDRSL-EAGDT 481
Cdd:pfam05483 354 FEATTCSLEELLRTEQqRLEKNEDQLKIITMElQKKSSELEEMTKFKNNKEVELEELK------KILAEDEKLLdEKKQF 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 482 EQVIPHIHRELQEAQELANTGKQKCLELQAMLeeerKTNRQQTEESAKQIRFLQTQLAKLQTDMEALREQRENTITTTRE 561
Cdd:pfam05483 428 EKIAEELKGKEQELIFLLQAREKEIHDLEIQL----TAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 562 ELYSAQEEILVLRHAMEAATAEREREITALQgdlsivtaELDKWRQTAAKYEVEISNLQASFQLQ--------SQHQERA 633
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDIINCKKQEERMLK--------QIENLEEKEMNLRDELESVREEFIQKgdevkcklDKSEENA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 634 SQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRLEEELDSSRERSATLSSNLNALEKSQGDLE-------NKLGSI 706
Cdd:pfam05483 576 RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLElelasakQKFEEI 655
|
490
....*....|...
gi 528494940 707 QDQHQQDASKLKI 719
Cdd:pfam05483 656 IDNYQKEIEDKKI 668
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
463-684 |
8.30e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 39.65 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 463 QNRVSLLKEMDRSLE-AGDTEQVI---PHIHRELQeaQELANTG---------------KQKCLELQA-MLEEERKTnrQ 522
Cdd:PRK10929 51 QSALNWLEERKGSLErAKQYQQVIdnfPKLSAELR--QQLNNERdeprsvppnmstdalEQEILQVSSqLLEKSRQA--Q 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 523 QTEESAKQIRFLQTQLAKLQTdmEALR-----EQRENTITTTREELYSAQeeiLVLRHAMEAATAER--EREITALQG-- 593
Cdd:PRK10929 127 QEQDRAREISDSLSQLPQQQT--EARRqlneiERRLQTLGTPNTPLAQAQ---LTALQAESAALKALvdELELAQLSAnn 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 594 --DLSIVTAELDKWRqtAAKYEVEISNLQAsfQLQSQHQERASQLQGEVEKLQADCSGLQNECDSLRAEKSTLMQKLNRL 671
Cdd:PRK10929 202 rqELARLRSELAKKR--SQQLDAYLQALRN--QLNSQRQREAERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQ 277
|
250
....*....|....*
gi 528494940 672 EEELD--SSRERSAT 684
Cdd:PRK10929 278 AQRMDliASQQRQAA 292
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
439-586 |
8.45e-03 |
|
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: 39.73 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 439 SPSKEKSSDDTSDGQMEEQELNEPQNRVS---------LLKEMDRSLEAGDTE-----QVIPHIHRELQEAQE-LANTGK 503
Cdd:pfam07111 466 CPPPPPAPPVDADLSLELEQLREERNRLDaelqlsahlIQQEVGRAREQGEAErqqlsEVAQQLEQELQRAQEsLASVGQ 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528494940 504 QKCLELQAMLE--EERKTNRQQ-TEESAKQIRFLQTQLAKLQTdmeALREQRENTITTTREELYSAQEEILVLRHAMEAA 580
Cdd:pfam07111 546 QLEVARQGQQEstEEAASLRQElTQQQEIYGQALQEKVAEVET---RLREQLSDTKRRLNEARREQAKAVVSLRQIQHRA 622
|
....*.
gi 528494940 581 TAERER 586
Cdd:pfam07111 623 TQEKER 628
|
|
| |
