|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
3-132 |
5.02e-80 |
|
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: 251.42 E-value: 5.02e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 3 SALAIFTCRPNSHPFQERHVYLDEPIKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINS 82
Cdd:cd22679 1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 767924277 83 QRLSRGSEESPPCEILSGDIIQFGVDVTENTRKgtVTHGCIVSTIKLFLP 132
Cdd:cd22679 79 QRLSKGSEESEPRELHSGDIVQFGVDVVENSRK--VTHGCIVATVTLFLP 126
|
|
| CC1_SLMAP |
cd21911 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal ... |
165-227 |
1.87e-26 |
|
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal membrane-associated protein (SLMAP), also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. SLMAP contains an N-terminal FHA domain followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409287 [Multi-domain] Cd Length: 63 Bit Score: 102.38 E-value: 1.87e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767924277 165 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQ 227
Cdd:cd21911 1 QELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQLS 63
|
|
| FHA_DMA-like |
cd22692 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest ... |
27-108 |
1.66e-18 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest protein 1 (DMA1), 2 (DMA2) and similar proteins; DMA1 (also known as checkpoint forkhead associated with RING domains-containing protein 1, or CHF1) and DMA2 (also known as checkpoint forkhead associated with RING domains-containing protein 2, or CHF2) are E3 ubiquitin-protein ligases which function in cell cycle retarding in conjunction with the UBC4 and UBC13/MMS2 complex, two E2 ubiquitin conjugating enzymes. They are involved in nutritional control of the cell cycle and required for proper spindle positioning, likely regulating septin ring deposition at the bud neck. DMA1 targets the degradation of G1 cyclin PCL1. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438744 [Multi-domain] Cd Length: 139 Bit Score: 82.62 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 27 PIKIGRSVARCRPAQNNAT-FDCKVLSRNHALVWfdHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQF 105
Cdd:cd22692 38 QIHIGRYTERVRQAIYHPVvFKSKVVSRTHGCIK--VDEGNWYIKDVKSSSGTFLNHQRLSPASRTSKPYPLRDGDILQL 115
|
...
gi 767924277 106 GVD 108
Cdd:cd22692 116 GMD 118
|
|
| FHA_VPS64-like |
cd22695 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ... |
6-109 |
7.33e-16 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 64 (VPS64) and similar proteins; This subfamily includes VPS64 (also called factor arrest protein 9 or FAR9) and factor arrest protein 10 (FAR10), which participate in the control of the re-entry into the cell cycle following pheromone treatment. VPS64 is also involved in vacuolar protein sorting. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438747 [Multi-domain] Cd Length: 133 Bit Score: 74.65 E-value: 7.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 6 AIFTCRPNSHPFQERHV---YLDEPIKIGRSVARCRPAQN---------------NATFDCKVLSRNHALVWFDHKTGKF 67
Cdd:cd22695 2 HILVLKSLNATFETKFLvvpFKPDGLKLGRPVTNSVNKNNsgskrdlfsqqvrpdNGNFDSRVLSRNHACLSCDPTTGKV 81
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 767924277 68 YLQDTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFGVDV 109
Cdd:cd22695 82 YIRDLKSSNGTFVNGQKIRQND-----VELKVGDEVDLGTDI 118
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
237-710 |
4.31e-14 |
|
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: 76.21 E-value: 4.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 237 SLRKELIALQEDKHNYETTAKE--SLRRVLQEKIEVVRKLSEVERSLsntEDECTHLKEMNERTQEELRELANKYNGAVN 314
Cdd:TIGR04523 170 ELENELNLLEKEKLNIQKNIDKikNKLLKLELLLSNLKKKIQKNKSL---ESQISELKKQNNQLKDNIEKKQQEINEKTT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 315 EIKDLSDKLKVAEGKQEEIQQKGQAEKKELQH---KIDEMEEKEQELQAKIEAL--QADNDFTNERLTALQEKlivEGHL 389
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLnnQKEQDWNKELKSELKNQ---EKKL 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 390 TKAveETKLSKENQtraKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKalleEERKAYRNQVEESTKQIQ 469
Cdd:TIGR04523 324 EEI--QNQISQNNK---IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK----KENQSYKQEIKNLESQIN 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 470 VLQAQLQrlhiDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERD---TDIASLQEELKKVRAELERWRKAA 546
Cdd:TIGR04523 395 DLESKIQ----NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKdltNQDSVKELIIKNLDNTRESLETQL 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 547 SEYEKEITSLQNSFQLRCQQCEDQQRE------EATRLQGEL--------------EKLRKEWNALETECHSLKRENVLL 606
Cdd:TIGR04523 471 KVLSRSINKIKQNLEQKQKELKSKEKElkklneEKKELEEKVkdltkkisslkekiEKLESEKKEKESKISDLEDELNKD 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 607 SSELQRQ--EKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHL---RDSADLKTLLSKAENQAKDVQKEYEKTQ 681
Cdd:TIGR04523 551 DFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKdliKEIEEKEKKISSLEKELEKAKKENEKLS 630
|
490 500
....*....|....*....|....*....
gi 767924277 682 TVLSELKLKFEMTEQEKQSITDELKQCKN 710
Cdd:TIGR04523 631 SIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
13-106 |
4.68e-14 |
|
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.
Pssm-ID: 438714 [Multi-domain] Cd Length: 92 Bit Score: 68.07 E-value: 4.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 13 NSHPFQERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINSQRLsrgseeS 92
Cdd:cd00060 6 DGDGGGREFPLTKGVVTIGRS------PDCDIVLDDPSVSRRHARIEVDG--GGVYLEDLGSTNGTFVNGKRI------T 71
|
90
....*....|....
gi 767924277 93 PPCEILSGDIIQFG 106
Cdd:cd00060 72 PPVPLQDGDVIRLG 85
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
241-704 |
5.19e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.33 E-value: 5.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 241 ELIALQEDKHNYETTAKESLRRV--LQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKD 318
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 319 LSDKLKVAEGKQEEIQQKGQAEKK--ELQHKIDEMEEKEQELQAKIEALQ--ADNDFTNERLTALQEKLIVEGHLTKAVE 394
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 395 ETKLSKENQTRAKESDFSDTLSPSKE---------KSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYR-NQVEES 464
Cdd:PTZ00121 1442 EAKKADEAKKKAEEAKKAEEAKKKAEeakkadeakKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEaKKAEEA 1521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 465 TKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSA---------------RDEILLLHQAAAKVASERDTDIASLQ 529
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAeekkkaeeakkaeedKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 530 EELKKVRAE----LERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVL 605
Cdd:PTZ00121 1602 EEEKKMKAEeakkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK 1681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 606 LSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYE---KTQT 682
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEekkKIAH 1761
|
490 500
....*....|....*....|..
gi 767924277 683 VLSELKLKFEMTEQEKQSITDE 704
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
165-707 |
7.50e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.48 E-value: 7.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 165 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSknqteDSLRKELIA 244
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL-----ESLEAELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 245 LQEDKHNYETTAKEsLRRVLQEKIEVVRKLSEVERSLSNT----EDECTHLKEMNERTQEELRELA--------NKYNGA 312
Cdd:TIGR02168 363 LEAELEELESRLEE-LEEQLETLRSKVAQLELQIASLNNEierlEARLERLEDRRERLQQEIEELLkkleeaelKELQAE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 313 VNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQAD----NDFTNERLTALQEKLIVEGH 388
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLqenlEGFSEGVKALLKNQSGLSGI 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 389 L-------------TKAVEET------KLSKENQTRAKesdfsDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKAL 449
Cdd:TIGR02168 522 LgvlselisvdegyEAAIEAAlggrlqAVVVENLNAAK-----KAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKN 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 450 LEEERKAYRNQVEESTKQIQVLQAQLQRLHIdTENLREEKDSEITSTRDELL-SARDEILLLHQAAAKVASERDTDIASL 528
Cdd:TIGR02168 597 IEGFLGVAKDLVKFDPKLRKALSYLLGGVLV-VDDLDNALELAKKLRPGYRIvTLDGDLVRPGGVITGGSAKTNSSILER 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 529 QEELKKVRAELERWRKAASEYEKEITSLQNSFQlrcqqcedQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSS 608
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELE--------ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 609 ELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTL---LSKAENQAKDVQKEYEKTQTVLS 685
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALreaLDELRAELTLLNEEAANLRERLE 827
|
570 580
....*....|....*....|..
gi 767924277 686 ELKLKFEMTEQEKQSITDELKQ 707
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEE 849
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
158-718 |
8.31e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.48 E-value: 8.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 158 NTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQA--CSKNQTE 235
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvAQLELQI 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 236 DSLRKELIAL------QEDKHNYETTAKESLRRVLQE--KIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELAN 307
Cdd:TIGR02168 396 ASLNNEIERLearlerLEDRRERLQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 308 KYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKID---------EMEEKEQELQAKIEA-----LQA------ 367
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlsELISVDEGYEAAIEAalggrLQAvvvenl 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 368 ---------------------------DNDFTNERLTALQEKLIVEGHLTKAVE----------------------ETKL 398
Cdd:TIGR02168 556 naakkaiaflkqnelgrvtflpldsikGTEIQGNDREILKNIEGFLGVAKDLVKfdpklrkalsyllggvlvvddlDNAL 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 399 SKENQTRAKESDFS---DTLSP--------SKEKSSDDTTDAQMDEqdLNEPLAKVSLLKALLEEERKAYRNQVEESTKQ 467
Cdd:TIGR02168 636 ELAKKLRPGYRIVTldgDLVRPggvitggsAKTNSSILERRREIEE--LEEKIEELEEKIAELEKALAELRKELEELEEE 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 468 IQVLQAQLQRLHIDTENLREEKD----------SEITSTRDELLSARDEILLLHQAAAKV---ASERDTDIASLQEELKK 534
Cdd:TIGR02168 714 LEQLRKELEELSRQISALRKDLArleaeveqleERIAQLSKELTELEAEIEELEERLEEAeeeLAEAEAEIEELEAQIEQ 793
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 535 VRAELERWRKAASEYEKEITSLQNSF---QLRCQQCEDQQREEATRL----------QGELEKLRKEWNALETECHSLKR 601
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATERRLedleeqieelSEDIESLAAEIEELEELIEELES 873
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 602 ENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHlrdsADLKTLLSKAENQAKDVQkeyektQ 681
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL----AQLELRLEGLEVRIDNLQ------E 943
|
650 660 670
....*....|....*....|....*....|....*..
gi 767924277 682 TVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 718
Cdd:TIGR02168 944 RLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
28-105 |
1.37e-13 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 66.06 E-value: 1.37e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767924277 28 IKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRLSRgseesPPCEILSGDIIQF 105
Cdd:pfam00498 1 VTIGRS------PDCDIVLDDPSVSRRHAEIRYD-GGGRFYLEDLGSTNGTFVNGQRLGP-----EPVRLKDGDVIRL 66
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
98-713 |
8.58e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 72.07 E-value: 8.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 98 LSGDIIQFGVDVTENTRKGTVTHGCIVSTIKLFLPDGMEARLRSDVIHAPLPSPVDKVAANTPSMYSQELFQLSQYLQEA 177
Cdd:pfam15921 160 LKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGR 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 178 LHR-EQMLEQKLATLQRLLAITQEASDTSWQALIDEdrllSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTa 256
Cdd:pfam15921 240 IFPvEDQLEALKSESQNKIELLLQQHQDRIEQLISE----HEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSM- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 257 keslrrvlqekieVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEiqqk 336
Cdd:pfam15921 315 -------------YMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDD---- 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 337 gqaekkELQHKIDEMEEKEQELQAKIEalqadndftnerltalQEKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLS 416
Cdd:pfam15921 378 ------QLQKLLADLHKREKELSLEKE----------------QNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALL 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 417 PSKEKSSDDTTDAQMDE-QDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQlQRLHIDTENLREEKDSEITS 495
Cdd:pfam15921 436 KAMKSECQGQMERQMAAiQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS-ERTVSDLTASLQEKERAIEA 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 496 TRDELLSARDEILLLHQAAAKVASERDtdiaslqeELKKVRAELERWRKAASEYEKEITSLQNSFQlRCQQCEDQQREEA 575
Cdd:pfam15921 515 TNAEITKLRSRVDLKLQELQHLKNEGD--------HLRNVQTECEALKLQMAEKDKVIEILRQQIE-NMTQLVGQHGRTA 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 576 TRLQGELEKLRKEWNALETECHSLK----------RENVLLSSELQRQEKELHNSQKQSLELTSDlsiLQMSRKELENQV 645
Cdd:pfam15921 586 GAMQVEKAQLEKEINDRRLELQEFKilkdkkdakiRELEARVSDLELEKVKLVNAGSERLRAVKD---IKQERDQLLNEV 662
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767924277 646 GSLKEqhlrdsaDLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFemteqekQSITDELKQCKNNLK 713
Cdd:pfam15921 663 KTSRN-------ELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQL-------KSAQSELEQTRNTLK 716
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
163-688 |
1.02e-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: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 163 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKEL 242
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 243 IALQEDkhnyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDK 322
Cdd:COG1196 298 ARLEQD-----------IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 323 LKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKEN 402
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 403 QTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQ--DLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHI 480
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAAlaELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAV 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 481 DTENLREEKDSEITSTR----------DELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVR------------AE 538
Cdd:COG1196 527 AVLIGVEAAYEAALEAAlaaalqnivvEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALargaigaavdlvAS 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 539 LERWRKAASEYEKEITSLQNSFQLRCQQCEDQQRE----------EATRLQGELEKLRKEWNALETECHSLKRENVLLSS 608
Cdd:COG1196 607 DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTlagrlrevtlEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 609 ELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELK 688
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
|
| CC1_SLMAP-like |
cd21868 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ... |
169-206 |
1.05e-12 |
|
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar proteins; The family includes Sarcolemmal membrane-associated protein (SLMAP), its paralog TRAF3-interacting JNK-activating modulator (T3JAM), and similar proteins. SLMAP, also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. T3JAM, also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. SLMAP contains an N-terminal FHA domain, followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409286 [Multi-domain] Cd Length: 38 Bit Score: 62.50 E-value: 1.05e-12
10 20 30
....*....|....*....|....*....|....*...
gi 767924277 169 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 206
Cdd:cd21868 1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
445-718 |
2.59e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.48 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 445 LLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLhidtENLREEKDSEITSTRDELLSARDeilLLHQAAAKVASERDTD 524
Cdd:TIGR02169 216 LLKEKREYEGYELLKEKEALERQKEAIERQLASL----EEELEKLTEEISELEKRLEEIEQ---LLEELNKKIKDLGEEE 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 525 IASLQEELKKVRAELERWRKAASEYEKEITSLQNsfQLRCQQCE-DQQREEATRLQGELEKLRKEWNALETECHSLKREN 603
Cdd:TIGR02169 289 QLRVKEKIGELEAEIASLERSIAEKERELEDAEE--RLAKLEAEiDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 604 VLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADlktlLSKAENQAKDVQKEYEKTQTV 683
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEE----LADLNAAIAGIEAKINELEEE 442
|
250 260 270
....*....|....*....|....*....|....*
gi 767924277 684 LSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 718
Cdd:TIGR02169 443 KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
174-718 |
4.41e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 4.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 174 LQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRllsrlevmgnqlqacSKNQTEDSLRKELIALQEDKHNYE 253
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS---------------ELEEEIEELQKELYALANEISRLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 254 ttakeslrrvlQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEI 333
Cdd:TIGR02168 302 -----------QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 334 QQKGQAEKKELQH---KIDEMEEKEQELQAKIEALQAD--------NDFTNERLTALQEKLIVEGHLTKAVEETKLSKEN 402
Cdd:TIGR02168 371 ESRLEELEEQLETlrsKVAQLELQIASLNNEIERLEARlerledrrERLQQEIEELLKKLEEAELKELQAELEELEEELE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 403 QTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQ------------- 469
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlselis 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 470 -----------VLQAQLQRLHIDTEN---------------------LREEKDSEITSTRDELLSARDEILLLHQAAAKV 517
Cdd:TIGR02168 531 vdegyeaaieaALGGRLQAVVVENLNaakkaiaflkqnelgrvtflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKF 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 518 ASERD-------------TDIASLQEELKKVRAEL-------ERWRKAASEY---EKEITSLQNSFQ--LRCQQCEDQQR 572
Cdd:TIGR02168 611 DPKLRkalsyllggvlvvDDLDNALELAKKLRPGYrivtldgDLVRPGGVITggsAKTNSSILERRReiEELEEKIEELE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 573 EEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQ- 651
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERl 770
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767924277 652 ---------HLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 718
Cdd:TIGR02168 771 eeaeeelaeAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
213-541 |
5.99e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 5.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 213 DRLLSRLEVMGNQLQACSKNQTEdsLRKELIALQEDkhnyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLK 292
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAE--LRKELEELEEE-----------LEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 293 EMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEgkqeeiqqkgqAEKKELQHKIDEMEEKEQELQAKIEALQADNDFT 372
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAE-----------AEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 373 NERLTALQEKLivEGHLTKAVEETKLSKENQTRAKEsdfsdtLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEE 452
Cdd:TIGR02168 816 NEEAANLRERL--ESLERRIAATERRLEDLEEQIEE------LSEDIESLAAEIEELEELIEELESELEALLNERASLEE 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 453 ERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREE------KDSEITSTRDELLSA-RDEILLLHQAAAKVASERDTDI 525
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELRRELEELREKlaqlelRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDE 967
|
330
....*....|....*.
gi 767924277 526 ASLQEELKKVRAELER 541
Cdd:TIGR02168 968 EEARRRLKRLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
192-722 |
1.03e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.54 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 192 QRLLAITQEASDTSWQALIDedrllsRLEVMGNQLQAcsKNQTEDSLRKELIALQEDKHNYET--TAKESLRRVLQEKIE 269
Cdd:TIGR02168 213 ERYKELKAELRELELALLVL------RLEELREELEE--LQEELKEAEEELEELTAELQELEEklEELRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 270 --------VVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEK 341
Cdd:TIGR02168 285 elqkelyaLANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 342 KELQhkidEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEG----HLTKAVEETKLSKENQTRAKESDFSDTLSP 417
Cdd:TIGR02168 365 AELE----ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEarleRLEDRRERLQQEIEELLKKLEEAELKELQA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 418 SKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKD------- 490
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKnqsglsg 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 491 -----SEITSTR--------------------DELLSARDEILLLHQAAAKVA------SERDTDIASLQEELKK----V 535
Cdd:TIGR02168 521 ilgvlSELISVDegyeaaieaalggrlqavvvENLNAAKKAIAFLKQNELGRVtflpldSIKGTEIQGNDREILKniegF 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 536 RAELERWRKAASEYEKEI----------TSLQNSFQLRCQQCEDQQ--------------------REEATRL--QGELE 583
Cdd:TIGR02168 601 LGVAKDLVKFDPKLRKALsyllggvlvvDDLDNALELAKKLRPGYRivtldgdlvrpggvitggsaKTNSSILerRREIE 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 584 KLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLL 663
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767924277 664 SKAENQAKDVQKEYEKTQTVLSE---LKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNNK 722
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEieeLEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
14-106 |
1.07e-11 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 61.51 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 14 SHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktGKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716 8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
|
90
....*....|....
gi 767924277 93 pPCEILSGDIIQFG 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 |
1.31e-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: 1.31e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 767924277 52 SRNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQFG 106
Cdd:cd22686 48 SKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPYPLTHGDELKIG 102
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
300-718 |
1.50e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.14 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 300 EELRELANKYNGAVNEIkdLSDKLKVAEGKQEEIQQKgqaEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTAL 379
Cdd:PRK02224 165 EEYRERASDARLGVERV--LSDQRGSLDQLKAQIEEK---EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 380 QEklIVEGH---------LTKAVEETKLSKENQTRAKEsDFSDTLSPSKEKSSD--DTTDAQMDEQDLNEPLAK-VSLLK 447
Cdd:PRK02224 240 DE--VLEEHeerreeletLEAEIEDLRETIAETERERE-ELAEEVRDLRERLEEleEERDDLLAEAGLDDADAEaVEARR 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 448 ALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEK----------DSEITSTRDELLSARDEILLLhQAAAKV 517
Cdd:PRK02224 317 EELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAeelreeaaelESELEEAREAVEDRREEIEEL-EEEIEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 518 ASER----DTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSF----QLR----CQQCE------------DQQRE 573
Cdd:PRK02224 396 LRERfgdaPVDLGNAEDFLEELREERDELREREAELEATLRTARERVeeaeALLeagkCPECGqpvegsphvetiEEDRE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 574 EATRLQGELEKLRKEWNALETECHSLKrenvllssELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQhl 653
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAE--------DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER-- 545
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767924277 654 rdSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS------ITDELKQCKNNLKLLREK 718
Cdd:PRK02224 546 --AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESlerirtLLAAIADAEDEIERLREK 614
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
214-717 |
1.63e-11 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 68.15 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 214 RLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTAKESLRRVLQEKIEvvrkLSEVERSlSNTEDECTHLKE 293
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE----LDGFERG-PFSERQIKNFHT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 294 MNERTQEELRELANKyngavnEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTN 373
Cdd:TIGR00606 398 LVIERQEDEAKTAAQ------LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 374 ERLTALQEKLIVEGHLTKAVE----ETKLSKENQTRAKESDFSDTL----SPSKEKSSDDTTDAQM-----DEQDLNEPL 440
Cdd:TIGR00606 472 RILELDQELRKAERELSKAEKnsltETLKKEVKSLQNEKADLDRKLrkldQEMEQLNHHTTTRTQMemltkDKMDKDEQI 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 441 AK---------VSLL-----KALLEEERKAYRNQVEESTKQIQVLQAQLQRLhidtENLREEKDSEITSTRDELLSARDE 506
Cdd:TIGR00606 552 RKiksrhsdelTSLLgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASL----EQNKNHINNELESKEEQLSSYEDK 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 507 ILllhqaAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQC------EDQQREEATRLQG 580
Cdd:TIGR00606 628 LF-----DVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCqrvfqtEAELQEFISDLQS 702
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 581 ELEKLRKEWNALETECHSLKRENVLL-------SSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSL--KEQ 651
Cdd:TIGR00606 703 KLRLAPDKLKSTESELKKKEKRRDEMlglapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTImpEEE 782
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767924277 652 HLRDSADLKTLLSKAENQAKDVQKEYEKTQTVL--SELKLKFEMTEQEKQSITDELKQCKNNLKLLRE 717
Cdd:TIGR00606 783 SAKVCLTDVTIMERFQMELKDVERKIAQQAAKLqgSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
163-627 |
4.53e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 163 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQeasdtswqalidedRLLSRLEVMGNQLQACSKNQTEdsLRKEL 242
Cdd:PRK03918 291 KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIE--------------ERIKELEEKEERLEELKKKLKE--LEKRL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 243 IALQEDKHNYETTakeslrRVLQEKIEVVRKlSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSD- 321
Cdd:PRK03918 355 EELEERHELYEEA------KAKKEELERLKK-RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKa 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 322 --KLKVAEGK------------QEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALqadndftnERLTALQEKLIVEG 387
Cdd:PRK03918 428 ieELKKAKGKcpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL--------EKVLKKESELIKLK 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 388 HLTKAVEET--KLSKENqtrakesdfsdtlspsKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEErKAYRNQVEEST 465
Cdd:PRK03918 500 ELAEQLKELeeKLKKYN----------------LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL-EELKKKLAELE 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 466 KQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDtDIASLQEELKKVRAELERWRKA 545
Cdd:PRK03918 563 KKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEK-ELKKLEEELDKAFEELAETEKR 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 546 ASEYEKEITSLQNSFqlrcqqcedqQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSL 625
Cdd:PRK03918 642 LEELRKELEELEKKY----------SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
..
gi 767924277 626 EL 627
Cdd:PRK03918 712 EL 713
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
165-651 |
5.54e-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: 5.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 165 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDtswQALIDEDRLLSRLEVMGNQLQAcsKNQTEDSLRKELIA 244
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRR---ELEERLEELEEELAELEEELEE--LEEELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 245 LQEDkhnyETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLK 324
Cdd:COG1196 349 AEEE----LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 325 VAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADndftnERLTALQEKLIVEGHLTKAVEETKLSKENQT 404
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL-----LEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 405 RAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQ----RLHI 480
Cdd:COG1196 500 EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratFLPL 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 481 DTENLREEKDSEITST---------------RDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKA 545
Cdd:COG1196 580 DKIRARAALAAALARGaigaavdlvasdlreADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 546 ASEYE-KEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQS 624
Cdd:COG1196 660 GSLTGgSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
490 500 510
....*....|....*....|....*....|....*.
gi 767924277 625 LELTSDLSILQ---------MSRKELENQVGSLKEQ 651
Cdd:COG1196 740 ELLEEEELLEEealeelpepPDLEELERELERLERE 775
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
231-593 |
2.29e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 231 KNQTEDSLRKELIALQ--EDKHNYETTAKESLRR---VLQEKIEVVRKLSEVERSLSntedecthLKEMNERtQEELREL 305
Cdd:TIGR02168 174 RKETERKLERTRENLDrlEDILNELERQLKSLERqaeKAERYKELKAELRELELALL--------VLRLEEL-REELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 306 ANKYNGAVNEIKDLSDKLKVAEGKQEEIQqkgqAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLI- 384
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELR----LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEe 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 385 VEGHLTKAVEETKLSKENQTRAKESdfSDTLSPSKEKSSDDTTDAQMDEQDLNEplaKVSLLKALLEEERKAY---RNQV 461
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEK--LEELKEELESLEAELEELEAELEELES---RLEELEEQLETLRSKVaqlELQI 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 462 EESTKQIQVLQAQLQRLhidtENLREEKDSEITSTRDELLSARdeillLHQAAAKVAsERDTDIASLQEELKKVRAELER 541
Cdd:TIGR02168 396 ASLNNEIERLEARLERL----EDRRERLQQEIEELLKKLEEAE-----LKELQAELE-ELEEELEELQEELERLEEALEE 465
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 767924277 542 WRKAASEYEKEITSLQNSF---QLRCQQCEDQQReeatRLQGELEKLRKEWNALE 593
Cdd:TIGR02168 466 LREELEEAEQALDAAERELaqlQARLDSLERLQE----NLEGFSEGVKALLKNQS 516
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
265-621 |
8.66e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 8.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 265 QEKIEVVRKLSEVERSLSNTEDEcthLKEMNERTQ--EELRELANKYNGAVNEIKDLS-----DKLKVAEGKQEEIQQkg 337
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDI---LNELERQLKslERQAEKAERYKELKAELRELElallvLRLEELREELEELQE-- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 338 qaEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKENQTRAkesdfsdtLSP 417
Cdd:TIGR02168 247 --ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN--------LER 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 418 SKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQrlhiDTENLREEKDSEITSTR 497
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE----ELEEQLETLRSKVAQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 498 DELLSARDEILLLhqaaakvaserDTDIASLQEELKKVRAELERWRKAASEYEKEitslqnsfqlrcqqcedQQREEATR 577
Cdd:TIGR02168 393 LQIASLNNEIERL-----------EARLERLEDRRERLQQEIEELLKKLEEAELK-----------------ELQAELEE 444
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 767924277 578 LQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQ 621
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
154-594 |
2.85e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 154 KVAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDtswqaliDEDRLLSRLEVMGNQLQACSKNQ 233
Cdd:COG4717 60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA-------ELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 234 TEDSLRKELIALQEdkhnyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKE-MNERTQEELRELANKYNGA 312
Cdd:COG4717 133 ELEALEAELAELPE--------RLEELEERLEELRELEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 313 VNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEA----LQADNDFTNERLTALQEKLIVEGH 388
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallaLLGLGGSLLSLILTIAGVLFLVLG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 389 LTkAVEETKLSKENQTRAKESDFSDTLsPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLE-EERKAYRNQVEESTKQ 467
Cdd:COG4717 285 LL-ALLFLLLAREKASLGKEAEELQAL-PALEELEEEELEELLAALGLPPDLSPEELLELLDRiEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 468 IQVLQAQ------LQRLHIDTEN---LREEKDSEITSTRDELLSARDEI-----LLLHQAAAKVASERDTDIASLQEELK 533
Cdd:COG4717 363 LQLEELEqeiaalLAEAGVEDEEelrAALEQAEEYQELKEELEELEEQLeellgELEELLEALDEEELEEELEELEEELE 442
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767924277 534 KVRAELERWRKAASEYEKEITSLQNSFQLrcqqceDQQREEATRLQGELEKLRKEWNALET 594
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLEEDGEL------AELLQELEELKAELRELAEEWAALKL 497
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
335-717 |
3.97e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 335 QKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDfTNERLTALQEKLI-VEGH-LTKAVEETKLSKEnQTRAKESDFS 412
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLERLRRERE-KAERYQALLKEKReYEGYeLLKEKEALERQKE-AIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 413 DTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVsllKALLEEERKAYRNQVEESTKQIQVLQAQLQrlhidtENLREEKDSE 492
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKI---KDLGEEEQLRVKEKIGELEAEIASLERSIA------EKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 493 itSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLqnsfqlrcqqcedqqR 572
Cdd:TIGR02169 322 --ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET---------------R 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 573 EEATRLQGELEKLRKEWNaletechSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQH 652
Cdd:TIGR02169 385 DELKDYREKLEKLKREIN-------ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767924277 653 LRDSADlktlLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLRE 717
Cdd:TIGR02169 458 EQLAAD----LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
230-718 |
4.52e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 4.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 230 SKNQTEDSLRKELIALQEDKHNYETTA------KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEmNERTQEELR 303
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKELEELKeeieelEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE-KVKELKELK 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 304 ELANKYNgavnEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKE---QELQAKIEALQADNDFTNERLTALQ 380
Cdd:PRK03918 290 EKAEEYI----KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELYE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 381 EKLIVEGHLTK--------AVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDE--QDLNEPLAKVSLLKALL 450
Cdd:PRK03918 366 EAKAKKEELERlkkrltglTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKaiEELKKAKGKCPVCGREL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 451 EEERKAyrNQVEESTKQIQVLQAQLQRLHIDTENLREEKdseitSTRDELLSARDEILLLHQAAAKVASERDTDIASLQE 530
Cdd:PRK03918 446 TEEHRK--ELLEEYTAELKRIEKELKEIEEKERKLRKEL-----RELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 531 ELKKVRAELERWRKAASEYEKEITSLQNSFqlrcqqcedqqrEEATRLQGELEKLRKEWNALETECHSLKRENVLLS--- 607
Cdd:PRK03918 519 ELEKKAEEYEKLKEKLIKLKGEIKSLKKEL------------EKLEELKKKLAELEKKLDELEEELAELLKELEELGfes 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 608 -SELQRQEKELHNSQKQSLELT---SDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSK--------AENQAKDVQK 675
Cdd:PRK03918 587 vEELEERLKELEPFYNEYLELKdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEleelekkySEEEYEELRE 666
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 767924277 676 EYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 718
Cdd:PRK03918 667 EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
269-718 |
4.85e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 59.65 E-value: 4.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 269 EVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKI 348
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 349 DEMEEKEQE---LQAKIEALQADNDFTNERLTALQEKLIVEGH----LTKAVEETKLSK---ENQTRAKESDFSDT---- 414
Cdd:TIGR04523 117 EQKNKLEVElnkLEKQKKENKKNIDKFLTEIKKKEKELEKLNNkyndLKKQKEELENELnllEKEKLNIQKNIDKIknkl 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 415 -----------------------LSPSKEKSSDDTTDAQMDEQDLNEPLAKVSL----LKALLEEERKAYR------NQV 461
Cdd:TIGR04523 197 lklelllsnlkkkiqknkslesqISELKKQNNQLKDNIEKKQQEINEKTTEISNtqtqLNQLKDEQNKIKKqlsekqKEL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 462 EESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILllhQAAAKVASERDTDIASLQEELKKVRAELER 541
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKL---EEIQNQISQNNKIISQLNEQISQLKKELTN 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 542 WRKAASEYEKEITSLQNsfqlrcqQCEDQQREEATRLQgELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQ 621
Cdd:TIGR04523 354 SESENSEKQRELEEKQN-------EIEKLKKENQSYKQ-EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 622 KQSLELTSDLSILQMSRKELENQVGSLKEQHlrdsADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSI 701
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELII----KNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL 501
|
490
....*....|....*..
gi 767924277 702 TDELKQCKNNLKLLREK 718
Cdd:TIGR04523 502 NEEKKELEEKVKDLTKK 518
|
|
| CC1_T3JAM |
cd21912 |
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ... |
166-206 |
7.11e-09 |
|
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; TRAF3-interacting JNK-activating modulator (T3JAM), also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. The model corresponds to a conserved region that shows high sequence similarity with the first CC (CC1) domain of Sarcolemmal membrane-associated protein (SLMAP), which is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409288 [Multi-domain] Cd Length: 45 Bit Score: 51.96 E-value: 7.11e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 767924277 166 ELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 206
Cdd:cd21912 5 EILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
273-692 |
7.46e-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: 59.42 E-value: 7.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 273 KLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAvneIKDLSDKLKvaegKQEEIQQKGQAEKKELQHKIDEME 352
Cdd:pfam01576 149 KLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAM---ISDLEERLK----KEEKGRQELEKAKRKLEGESTDLQ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 353 EKEQELQAKIEALQADNDFTNERLTALQEKLI---------------VEGHLTKAVEETKLSKENQTRAKES--DFSDTL 415
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAKKEEELQAALARLEeetaqknnalkkireLEAQISELQEDLESERAARNKAEKQrrDLGEEL 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 416 SPSKEKSSD--DTTDAQMDEQDLNEplAKVSLLKALLEEERKAYRNQVEEstkqiqvlqaqlqrlhidtenLREEKDSEI 493
Cdd:pfam01576 302 EALKTELEDtlDTTAAQQELRSKRE--QEVTELKKALEEETRSHEAQLQE---------------------MRQKHTQAL 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 494 TSTRDELLSARDEILLLHQAAAKVASERdtdiASLQEELKKVRAelerwRKAASEYEKEITSLQ-NSFQLRCQQCEDQQR 572
Cdd:pfam01576 359 EELTEQLEQAKRNKANLEKAKQALESEN----AELQAELRTLQQ-----AKQDSEHKRKKLEGQlQELQARLSESERQRA 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 573 EEA---TRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLsilqmsrKELENQVGSLK 649
Cdd:pfam01576 430 ELAeklSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRL-------RQLEDERNSLQ 502
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 767924277 650 EQhlrdsadlktlLSKAENQAKDVQKEYEKTQTVLSELKLKFE 692
Cdd:pfam01576 503 EQ-----------LEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
169-467 |
8.77e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 8.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 169 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTE-----DSLRKELI 243
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvkselKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 244 ALQEDKHNYETTAKESLRRVLQEKI-EVVRKLSEVERSLSNTEDECTHL-KEMNERTQE------ELRELANKYNGAVNE 315
Cdd:TIGR02169 769 ELEEDLHKLEEALNDLEARLSHSRIpEIQAELSKLEEEVSRIEARLREIeQKLNRLTLEkeylekEIQELQEQRIDLKEQ 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 316 IKDLSDKLKVAEGKQEEIQQKGQ----------AEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKL-I 384
Cdd:TIGR02169 849 IKSIEKEIENLNGKKEELEEELEeleaalrdleSRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLeA 928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 385 VEGHLTKAVEETKLSKE------------NQTRAKESDFSDtLSPSKEKSSDDTTDAQMDEQDLNEPLAKvsllkalLEE 452
Cdd:TIGR02169 929 LEEELSEIEDPKGEDEEipeeelsledvqAELQRVEEEIRA-LEPVNMLAIQEYEEVLKRLDELKEKRAK-------LEE 1000
|
330
....*....|....*
gi 767924277 453 ERKAYRNQVEESTKQ 467
Cdd:TIGR02169 1001 ERKAILERIEEYEKK 1015
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
240-718 |
1.64e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 240 KELIALQEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDL 319
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 320 SDKLKVAEGKQEEIQQ-KGQAEK-KELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETK 397
Cdd:PRK03918 272 KKEIEELEEKVKELKElKEKAEEyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 398 lSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQR 477
Cdd:PRK03918 352 -KRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 478 LhidtenlreEKDSEITSTRDELLSARDEILLLHQAAAKVASERDtDIASLQEELKKVRAELERWRKAASEYEKEITSLQ 557
Cdd:PRK03918 431 L---------KKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEK-ELKEIEEKERKLRKELRELEKVLKKESELIKLKE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 558 NSFQLRC--QQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRE---NVLLSSELQRQEKELHNSQKQSLELTSDLS 632
Cdd:PRK03918 501 LAEQLKEleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKElekLEELKKKLAELEKKLDELEEELAELLKELE 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 633 ILQM-SRKELENQVGSLKEQH-----LRDSA----DLKTLLSKAENQAKDVQKEYEKTQTVLSELK-----LKFEMTEQE 697
Cdd:PRK03918 581 ELGFeSVEELEERLKELEPFYneyleLKDAEkeleREEKELKKLEEELDKAFEELAETEKRLEELRkeleeLEKKYSEEE 660
|
490 500
....*....|....*....|.
gi 767924277 698 KQSITDELKQCKNNLKLLREK 718
Cdd:PRK03918 661 YEELREEYLELSRELAGLRAE 681
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
291-718 |
1.75e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 291 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKgQAEKKELQHKIDEMEEKEQELQAKIEALQADND 370
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 371 F--TNERLTALQEKLIVEGHLTKAVEETKL---SKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSL 445
Cdd:COG4717 127 LlpLYQELEALEAELAELPERLEELEERLEelrELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 446 LKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHiDTENLREEKDS--------EITSTRDELLSARDEILLLHQAAAKV 517
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAA-LEERLKEARLLlliaaallALLGLGGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 518 ASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRcqqcEDQQREEATRLQGELEKLRKEWNALETECH 597
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLP----PDLSPEELLELLDRIEELQELLREAEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 598 SLKRE------NVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQ-HLRDSADLKTLLSKAENQA 670
Cdd:COG4717 362 ELQLEeleqeiAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELlEALDEEELEEELEELEEEL 441
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 767924277 671 KDVQKEYEKTQTVLSELKLKFEMTEQEK--QSITDELKQCKNNLKLLREK 718
Cdd:COG4717 442 EELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRELAEE 491
|
|
| FHA_TCF19 |
cd22685 |
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ... |
29-106 |
2.05e-08 |
|
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar proteins; TCF-19, also called transcription factor SC1, was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It also functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. TCF-19 contains an N-terminal fork head association domain (FHA), a proline rich region, and a C-terminal plant homeodomain (PHD) finger. The FHA domain may serve as a nuclear signaling domain or as a phosphoprotein binding domain. The proline rich region is a common characteristic of trans-activating factors. The PHD finger may allow TCF-19 to interact with chromatin via methylated histone H3.
Pssm-ID: 438737 [Multi-domain] Cd Length: 130 Bit Score: 53.19 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 29 KIGRSVARCRPAQNNATFDcKVLSRNHALVW---FDHKTGKFYLQDTkSSNGTFINSQRLSRGSEEsppcEILSGDIIQF 105
Cdd:cd22685 31 RIGRNPEVCDVFLCSSQHP-NLISREHAEIHaerDGNGNWKVLIEDR-STNGTYVNDVRLQDGQRR----ELSDGDTITF 104
|
.
gi 767924277 106 G 106
Cdd:cd22685 105 G 105
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
252-718 |
2.07e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 252 YETTAKES--LRRVLQEKIEVVRKL----SEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLsDKLKV 325
Cdd:PRK03918 160 YENAYKNLgeVIKEIKRRIERLEKFikrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-EELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 326 AEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQAdndfTNERLTALQEKLIVEGHLTKAVEETKlSKENQTR 405
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE----KVKELKELKEKAEEYIKLSEFYEEYL-DELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 406 AKESDFSDTLSPSKEKSSD---DTTDAQMDEQDLNEPLAKVSLLK--ALLEEERKAYRNQVEESTKQIQVLQAQ-LQRLH 479
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKEleeKEERLEELKKKLKELEKRLEELEerHELYEEAKAKKEELERLKKRLTGLTPEkLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 480 IDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVAS---------------ERDTDIASLQEELKKVRAELERWRK 544
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteeHRKELLEEYTAELKRIEKELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 545 AASEYEKEITSLQNSFQ-----LRCQQCEDQQREEATRLQG-ELEKLRKEWNALETechsLKRENVLLSSELQRQEKELH 618
Cdd:PRK03918 474 KERKLRKELRELEKVLKkeselIKLKELAEQLKELEEKLKKyNLEELEKKAEEYEK----LKEKLIKLKGEIKSLKKELE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 619 NSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAE------NQAKDVQKEYEKTQTVLSELKLKFE 692
Cdd:PRK03918 550 KLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEpfyneyLELKDAEKELEREEKELKKLEEELD 629
|
490 500
....*....|....*....|....*.
gi 767924277 693 MTEQEKQSITDELKQCKNNLKLLREK 718
Cdd:PRK03918 630 KAFEELAETEKRLEELRKELEELEKK 655
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
461-717 |
2.13e-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: 57.76 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 461 VEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDtdiaSLQEELKKVRAELE 540
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELE----ELTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 541 RWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEAtRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNS 620
Cdd:TIGR02168 271 ELRLEVSELEEEIEELQKELYALANEISRLEQQKQ-ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 621 QKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQK-EYEKTQTVLSELKLKFEMTEQEKQ 699
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERlEARLERLEDRRERLQQEIEELLKK 429
|
250
....*....|....*...
gi 767924277 700 SITDELKQCKNNLKLLRE 717
Cdd:TIGR02168 430 LEEAELKELQAELEELEE 447
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
14-110 |
2.50e-08 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine/threonine-protein kinase MEK1 and similar proteins; MEK1 (EC 2.7.11.1), also known as MRE4, is a meiosis-specific protein kinase required for chromosome synapsis and meiotic recombination. The recruitment and activation of MEK1 require the phosphorylation of the chromosome axis protein Hop1 at Thr318 (pT318), which is necessary for recognition by the MEK1 FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438722 [Multi-domain] Cd Length: 105 Bit Score: 52.23 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 14 SHPFQERHV---YLDEPIKIGRSvARCRPAQNNATfdckvLSRNHALVW---FDHKTG-KFYLQDTkSSNGTFINSQRLS 86
Cdd:cd22670 7 SSPGSTDIVlpiYKNQVITIGRS-PSCDIVINDPF-----VSRTHCRIYsvqFDESSApLVYVEDL-SSNGTYLNGKLIG 79
|
90 100
....*....|....*....|....*
gi 767924277 87 RGseespPCEILS-GDIIQFGVDVT 110
Cdd:cd22670 80 RN-----NTVLLSdGDVIEIAHSAT 99
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
28-85 |
4.11e-08 |
|
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.
Pssm-ID: 214578 [Multi-domain] Cd Length: 52 Bit Score: 49.87 E-value: 4.11e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 767924277 28 IKIGRSvarcrPAQNNATFDCKVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRL 85
Cdd:smart00240 1 VTIGRS-----SEDCDIQLDGPSISRRHAVIVYD-GGGRFYLIDLGSTNGTFVNGKRI 52
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
450-713 |
4.86e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 450 LEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLRE---EKDSEITSTRDELLSARDEI-----------LLLHQAAA 515
Cdd:TIGR02169 700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKErleELEEDLSSLEQEIENVKSELkelearieeleEDLHKLEE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 516 KV----ASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQ----------NSFQLRCQQCEDQQREEATR---- 577
Cdd:TIGR02169 780 ALndleARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTlekeylekeiQELQEQRIDLKEQIKSIEKEienl 859
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 578 ------LQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQ 651
Cdd:TIGR02169 860 ngkkeeLEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDP 939
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767924277 652 HLRDSADLKTLLS----KAENQAKDVQ------------KEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCkNNLK 713
Cdd:TIGR02169 940 KGEDEEIPEEELSledvQAELQRVEEEiralepvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY-EKKK 1016
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
239-683 |
5.99e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.45 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 239 RKELIALQEDKHNYETTAK--ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERtQEELRELANKYNGAVNEI 316
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQilSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQ-ILELEGYEMDYNSYLKSI 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 317 KDLSDKLKVAEGKQE-------EIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKL-IVEGH 388
Cdd:PRK01156 373 ESLKKKIEEYSKNIErmsafisEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMeMLNGQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 389 LTKAVEETKLSKENQTRAKEsDFSDTLSPSKEkssdDTTDAQMDEQDLNEplaKVSLLKALLEEERKAYRNQVEESTKQI 468
Cdd:PRK01156 453 SVCPVCGTTLGEEKSNHIIN-HYNEKKSRLEE----KIREIEIEVKDIDE---KIVDLKKRKEYLESEEINKSINEYNKI 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 469 QVLQAQLQRLHIDTENLR------EEKDSEITSTRDELLSARDEILLlhqaaaKVASERDT-DIASLQEELKKVRAELER 541
Cdd:PRK01156 525 ESARADLEDIKIKINELKdkhdkyEEIKNRYKSLKLEDLDSKRTSWL------NALAVISLiDIETNRSRSNEIKKQLND 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 542 WRKAASEYEKEITSLQNSFQLRCQQCEDQ------QREEATRLQGELEKLRKewnaletechslKRENvllsseLQRQEK 615
Cdd:PRK01156 599 LESRLQEIEIGFPDDKSYIDKSIREIENEannlnnKYNEIQENKILIEKLRG------------KIDN------YKKQIA 660
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767924277 616 ELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLS---KAENQAKDVQKEYEKTQTV 683
Cdd:PRK01156 661 EIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTrinELSDRINDINETLESMKKI 731
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
249-722 |
7.21e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 249 KHNYETTAKESLRRVLQEKIEVVRKLSEVERSlsntEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAE- 327
Cdd:PTZ00121 1207 KAEEERKAEEARKAEDAKKAEAVKKAEEAKKD----AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADe 1282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 328 -GKQEEIQQKGQAEKKELQHKIDEMEEKEQElQAKIEALQADNDFTNERLTALQEKliveghltkavEETKLSKENQTRA 406
Cdd:PTZ00121 1283 lKKAEEKKKADEAKKAEEKKKADEAKKKAEE-AKKADEAKKKAEEAKKKADAAKKK-----------AEEAKKAAEAAKA 1350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 407 KESDFSDTLSPSKEKssddttdAQMDEQDLNEPLAKVSLLKALLEEERKA--YRNQVEESTKQIQVL------QAQLQRL 478
Cdd:PTZ00121 1351 EAEAAADEAEAAEEK-------AEAAEKKKEEAKKKADAAKKKAEEKKKAdeAKKKAEEDKKKADELkkaaaaKKKADEA 1423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 479 HIDTENLRE----EKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAEL----ERWRKAASEYE 550
Cdd:PTZ00121 1424 KKKAEEKKKadeaKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAkkkaEEAKKKADEAK 1503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 551 KEITSLQNSFQLR----CQQCEDQQREEATRLQGELEKLRKEWNALEtechsLKRENVLLSSELQRQEKELHNSQKQSLE 626
Cdd:PTZ00121 1504 KAAEAKKKADEAKkaeeAKKADEAKKAEEAKKADEAKKAEEKKKADE-----LKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 627 LTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKlkfemTEQEKQSITDELK 706
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK-----KEAEEKKKAEELK 1653
|
490
....*....|....*.
gi 767924277 707 QCKNNLKLLREKGNNK 722
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKK 1669
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
164-593 |
7.93e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 7.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 164 SQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgNQLQAcsKNQTEDSLRKELI 243
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE---AELAE--AEEELEELAEELL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 244 ALQEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKL 323
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 324 KVAEGKQEEIQQ-KGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKE- 401
Cdd:COG1196 470 EEAALLEAALAElLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALq 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 402 NQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAK----------VSLLKALLEEERKAYRNQVEES------T 465
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAalargaigaaVDLVASDLREADARYYVLGDTLlgrtlvA 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 466 KQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKA 545
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767924277 546 ASEYEKEITSLQNSFQLRCQQCEDQQREEATR-----------------------LQGELEKLRKEWNALE 593
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELleeeelleeealeelpeppdleeLERELERLEREIEALG 780
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
257-602 |
1.03e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 257 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQK 336
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 337 GQAEKKELQHKIDEMEEKEQ---ELQAKIEALQADNDftNERLTALQEKLiveghltKAVEETKLSKENQTRAKESDFSD 413
Cdd:TIGR02169 753 IENVKSELKELEARIEELEEdlhKLEEALNDLEARLS--HSRIPEIQAEL-------SKLEEEVSRIEARLREIEQKLNR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 414 tLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKdSEI 493
Cdd:TIGR02169 824 -LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL-REL 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 494 TSTRDELLSARDEilllhqaAAKVASERDTDIASLQEELKkvraELERWRKAASEYEKEITSLQNsFQLRCQQCED---- 569
Cdd:TIGR02169 902 ERKIEELEAQIEK-------KRKRLSELKAKLEALEEELS----EIEDPKGEDEEIPEEELSLED-VQAELQRVEEeira 969
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 767924277 570 ---------QQREEATR----LQGELEKLRKEWNALE---TECHSLKRE 602
Cdd:TIGR02169 970 lepvnmlaiQEYEEVLKrldeLKEKRAKLEEERKAILeriEEYEKKKRE 1018
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
137-660 |
1.86e-07 |
|
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: 54.74 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 137 ARLRSDVIHAPLpSPVDKVAANTPSMYSQELFQL----SQYLQEALHREQMLEQKLATLQRLLAItqeASDTSWQALIDE 212
Cdd:pfam15921 290 ARSQANSIQSQL-EIIQEQARNQNSMYMRQLSDLestvSQLRSELREAKRMYEDKIEELEKQLVL---ANSELTEARTER 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 213 DRLLSRLEVMGNQLQAC----SKNQTEDSLRKELIALQEDKHNYETTAKESLRRVLQEKIEVVRKLS------------E 276
Cdd:pfam15921 366 DQFSQESGNLDDQLQKLladlHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEallkamksecqgQ 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 277 VERSLSNTEDECTHL-------------KEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQE-------EIQQK 336
Cdd:pfam15921 446 MERQMAAIQGKNESLekvssltaqlestKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEatnaeitKLRSR 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 337 GQAEKKELQHKIDEmEEKEQELQAKIEALQADNDFTNERLTALQEKL-----IVEGHLTKA----VEETKLSKE-NQTRA 406
Cdd:pfam15921 526 VDLKLQELQHLKNE-GDHLRNVQTECEALKLQMAEKDKVIEILRQQIenmtqLVGQHGRTAgamqVEKAQLEKEiNDRRL 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 407 KESDFsdtlspskeKSSDDTTDAQMDEQDlneplAKVSLLKalleeerkayrnqveesTKQIQVLQAQLQRLHIdTENLR 486
Cdd:pfam15921 605 ELQEF---------KILKDKKDAKIRELE-----ARVSDLE-----------------LEKVKLVNAGSERLRA-VKDIK 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 487 EEKD---SEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWR--------------KAASEY 549
Cdd:pfam15921 653 QERDqllNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRntlksmegsdghamKVAMGM 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 550 EKEITSLQNsfQLRCQQCEDQQREEATR--------LQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQ 621
Cdd:pfam15921 733 QKQITAKRG--QIDALQSKIQFLEEAMTnankekhfLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME 810
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 767924277 622 ----KQSLELTSDLSILQmsRKELENQvgSLKEQHLRDSADLK 660
Cdd:pfam15921 811 valdKASLQFAECQDIIQ--RQEQESV--RLKLQHTLDVKELQ 849
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
212-557 |
1.90e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 212 EDRLLSRLEVMGNQLQacsKNQTEDSLRKELIALQEDKHNYETTAK--------ESLRRVLQEKIEVVRKLSEVERSLSN 283
Cdd:TIGR02169 186 IERLDLIIDEKRQQLE---RLRREREKAERYQALLKEKREYEGYELlkekealeRQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 284 TEDECTH----LKEMNERtqeelrelankyngavneIKDLSdklkvaEGKQEEIQQK---GQAEKKELQHKIDEMEEKEQ 356
Cdd:TIGR02169 263 LEKRLEEieqlLEELNKK------------------IKDLG------EEEQLRVKEKigeLEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 357 ELQAKIEALQADNDFTNERLTALQEKLiveghLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQdl 436
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREI-----EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR-- 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 437 neplakvsllkalleEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREE---KDSEITSTRDELLSARDEIlllhqa 513
Cdd:TIGR02169 392 ---------------EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAiagIEAKINELEEEKEDKALEI------ 450
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 767924277 514 aakvaSERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQ 557
Cdd:TIGR02169 451 -----KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
225-652 |
2.06e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 54.67 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 225 QLQACSKNQTEDSLRKELIALQEDKHNYE--------TTAKESLRRVLQEKIEVVRK-----------LSEVERSLSNTE 285
Cdd:TIGR00606 597 NKELASLEQNKNHINNELESKEEQLSSYEdklfdvcgSQDEESDLERLKEEIEKSSKqramlagatavYSQFITQLTDEN 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 286 DECTHLKEMNERTQEELRE----LANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAK 361
Cdd:TIGR00606 677 QSCCPVCQRVFQTEAELQEfisdLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKV 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 362 IEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLA 441
Cdd:TIGR00606 757 NRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQH 836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 442 KVSLLKALLEEERKAyrnqVEESTKQIQVLQAQL-----QRLHIDT--------ENLREEKDSEITSTRDELLSARDEIL 508
Cdd:TIGR00606 837 ELDTVVSKIELNRKL----IQDQQEQIQHLKSKTnelksEKLQIGTnlqrrqqfEEQLVELSTEVQSLIREIKDAKEQDS 912
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 509 LLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGEL------ 582
Cdd:TIGR00606 913 PLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLeecekh 992
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767924277 583 -EKLRKEWNALETECHSLKRENVLLSSELQRQE-----KELHNSQKQSLELTSDLSILQMSR--KELENQVGSLKEQH 652
Cdd:TIGR00606 993 qEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKrenelKEVEEELKQHLKEMGQMQVLQMKQehQKLEENIDLIKRNH 1070
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
312-557 |
2.44e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 312 AVNEIKDLSDKLKVAEGKQEEIQqkgqAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLiveghlTK 391
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQ----AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI------EE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 392 AVEETKlskenqTRAKESdfsdtlspSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAyrnqveesTKQIQVL 471
Cdd:COG3883 84 RREELG------ERARAL--------YRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADL--------LEELKAD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 472 QAQLqrlhidtenlrEEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEK 551
Cdd:COG3883 142 KAEL-----------EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
....*.
gi 767924277 552 EITSLQ 557
Cdd:COG3883 211 AAAAAA 216
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
445-623 |
3.05e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 445 LLKALLEEERKAYR----------NQVEESTKQIQVLQAQLQRLHIDTENLrEEKDSEITSTRDELLSARDEILLLHQAA 514
Cdd:COG4717 47 LLERLEKEADELFKpqgrkpelnlKELKELEEELKEAEEKEEEYAELQEEL-EELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 515 AKVA-----SERDTDIASLQEELKKVRAELERWRKAASEY---EKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLR 586
Cdd:COG4717 126 QLLPlyqelEALEAELAELPERLEELEERLEELRELEEELeelEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190
....*....|....*....|....*....|....*..
gi 767924277 587 KEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQ 623
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
27-106 |
3.32e-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: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 27 PIKIGRSVARcRPAQNNATFDC-----KVLSRNHALVWFDHKTGKFYLQdTKSSNGTFINSQRLSRGseeSPPCEILSGD 101
Cdd:cd22701 18 EVVLGRNSKN-SSSTAADSVDIdlgpsKKISRRHARIFYDFTTQCFELS-VLGRNGVKVDGILVKPG---SPPVPLRSGS 92
|
....*
gi 767924277 102 IIQFG 106
Cdd:cd22701 93 LIQIG 97
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
265-712 |
3.51e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.03 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 265 QEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGA----------VNEIKDLSDKLKVAEGKQEEIQ 334
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAeemrarlaarKQELEEILHELESRLEEEEERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 335 QKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEK-LIVEGHLTKAVEETKLSKEnqtraKESDFSD 413
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDiLLLEDQNSKLSKERKLLEE-----RISEFTS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 414 TLSPSKEKSSDDTTDAQMDE---QDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTenlrEEKD 490
Cdd:pfam01576 167 NLAEEEEKAKSLSKLKNKHEamiSDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQL----AKKE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 491 SEITSTRDELlsarDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQ 570
Cdd:pfam01576 243 EELQAALARL----EEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 571 QREEATRLQgELEKLRKewnALETECHslkrenvllSSELQRQEKELHNSQkQSLELTSDLSILQMSRKELENQVGSLKE 650
Cdd:pfam01576 319 QELRSKREQ-EVTELKK---ALEEETR---------SHEAQLQEMRQKHTQ-ALEELTEQLEQAKRNKANLEKAKQALES 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767924277 651 QHLRDSADLKTLlskaeNQAK-DVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNL 712
Cdd:pfam01576 385 ENAELQAELRTL-----QQAKqDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSEL 442
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
199-707 |
3.57e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 199 QEASDTSWQALIDEDRLLSRLEVMGNQLQacsknqtedSLRKELIALQEDKHNYETTAKESLRRVLQEKI---EVVRKLS 275
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIE---------EERKRRDKLTEEYAELKEELEDLRAELEEVDKefaETRDELK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 276 EVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIqqkgQAEKKELQHKIDEMEEKE 355
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK----ALEIKKQEWKLEQLAADL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 356 QELQAKIEALQADNDFTNERLTALQEKLIV----------EGHLTKAVEETK---------------------------- 397
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELSKLQRELAEaeaqaraseeRVRGGRAVEEVLkasiqgvhgtvaqlgsvgeryataieva 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 398 ----------------------LSKENQTRA------KESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAK------- 442
Cdd:TIGR02169 545 agnrlnnvvveddavakeaielLKRRKAGRAtflplnKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKyvfgdtl 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 443 -----------------VSLLKALLE----------EERKAYRNQVEESTKqIQVLQAQLQRLHIDTENLREEKDsEITS 495
Cdd:TIGR02169 625 vvedieaarrlmgkyrmVTLEGELFEksgamtggsrAPRGGILFSRSEPAE-LQRLRERLEGLKRELSSLQSELR-RIEN 702
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 496 TRDELLSARD-----------EILLLHQAAAKVA----------SERDTDIASLQEELKKVRAELERWRKAASEYEKEIT 554
Cdd:TIGR02169 703 RLDELSQELSdasrkigeiekEIEQLEQEEEKLKerleeleedlSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN 782
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 555 SLQNSF----------QLRCQQCEDQQREEATR-LQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQ 623
Cdd:TIGR02169 783 DLEARLshsripeiqaELSKLEEEVSRIEARLReIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK 862
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 624 SLELTSDLSILQMSRKELENQVGSLKeqhlRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITD 703
Cdd:TIGR02169 863 KEELEEELEELEAALRDLESRLGDLK----KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED 938
|
....
gi 767924277 704 ELKQ 707
Cdd:TIGR02169 939 PKGE 942
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
268-712 |
5.98e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 268 IEVVRKLSEVERSLSNTEDECTHLKEMNERTQE--ELRELANKYNGAVNEIKDLSDKLKVAEGKQEeiQQKGQAEKKELQ 345
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELLEPIRELAERyaAARERLAELEYLRAALRLWFAQRRLELLEAE--LEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 346 HKIDEMEEKEQELQAKIEALQAD-NDFTNERLTALQEKLiveghltkaveETKLSKENQTRAKESDFSDTLSPSKEKSSD 424
Cdd:COG4913 309 AELERLEARLDALREELDELEAQiRGNGGDRLEQLEREI-----------ERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 425 DttdaqmdEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREeKDSEITStrdELLSAR 504
Cdd:COG4913 378 S-------AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER-RKSNIPA---RLLALR 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 505 DEIlllhqAAAKVASERDTDIASlqeELKKVRAELERWRKAA--------------SEYEKEIT----SLQNSFQLRCQQ 566
Cdd:COG4913 447 DAL-----AEALGLDEAELPFVG---ELIEVRPEEERWRGAIervlggfaltllvpPEHYAAALrwvnRLHLRGRLVYER 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 567 CEDQQREEATR---------------------LQGEL------------EKLRKEWNALETEC--------------HSL 599
Cdd:COG4913 519 VRTGLPDPERPrldpdslagkldfkphpfrawLEAELgrrfdyvcvdspEELRRHPRAITRAGqvkgngtrhekddrRRI 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 600 KRENVL----------LSSELQRQEKELHNSQKQSLELTSDLSILQMSR----------------KELENQVGSLKEQH- 652
Cdd:COG4913 599 RSRYVLgfdnraklaaLEAELAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidvASAEREIAELEAELe 678
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767924277 653 --LRDSADLKTLlskaENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNL 712
Cdd:COG4913 679 rlDASSDDLAAL----EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
184-623 |
6.03e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 6.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 184 LEQKLATLQRLLAI----TQEASDTSWQALIDEDRllSRLEVMGNQLQACSknQTEDSLRKELIALQEDKHNYETTAKES 259
Cdd:COG4913 267 ARERLAELEYLRAAlrlwFAQRRLELLEAELEELR--AELARLEAELERLE--ARLDALREELDELEAQIRGNGGDRLEQ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 260 LRRVLQEKievVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQA 339
Cdd:COG4913 343 LEREIERL---ERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 340 EKKELQHKIDEMEEK----EQELQAKIEALQADNDFTNERL-----------------TALqEK--------LIVEGH-- 388
Cdd:COG4913 420 ELRELEAEIASLERRksniPARLLALRDALAEALGLDEAELpfvgelievrpeeerwrGAI-ERvlggfaltLLVPPEhy 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 389 --LTKAVEETKL-------------SKENQTRA-----------KESDFSDTLSPSKEKSSD----DTTDA--------- 429
Cdd:COG4913 499 aaALRWVNRLHLrgrlvyervrtglPDPERPRLdpdslagkldfKPHPFRAWLEAELGRRFDyvcvDSPEElrrhprait 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 430 ---------QMDEQDLNEPLAKVSLL-------KALLEEERKAYRNQVEESTKQIQVLQAQLQRLhiDTENLREEKDSEI 493
Cdd:COG4913 579 ragqvkgngTRHEKDDRRRIRSRYVLgfdnrakLAALEAELAELEEELAEAEERLEALEAELDAL--QERREALQRLAEY 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 494 TSTRDELLSARDEILLLHQAAAKVaSERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFqlrcQQCEDQQRE 573
Cdd:COG4913 657 SWDEIDVASAEREIAELEAELERL-DASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL----EQAEEELDE 731
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 767924277 574 EATRLQGELEKLRKEWNA-LETECHSLKRENVL------LSSELQRQEKELHNSQKQ 623
Cdd:COG4913 732 LQDRLEAAEDLARLELRAlLEERFAAALGDAVErelrenLEERIDALRARLNRAEEE 788
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
259-506 |
6.26e-07 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 53.01 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 259 SLRRVLQEKIEVVRKLSEVERslsnteDECTHLKEmNERTqEELRELANKYNGAVNEIKDLSDKLKVAEGKQ-------- 330
Cdd:PRK05771 13 TLKSYKDEVLEALHELGVVHI------EDLKEELS-NERL-RKLRSLLTKLSEALDKLRSYLPKLNPLREEKkkvsvksl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 331 EEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQA---------DNDFTNERLTALQEKLIVEGHLTKAVEETKLSKE 401
Cdd:PRK05771 85 EELIKDVEEELEKIEKEIKELEEEISELENEIKELEQeierlepwgNFDLDLSLLLGFKYVSVFVGTVPEDKLEELKLES 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 402 NQTRAKESDFSDTLSP-----SKEkssddttdaqmDEQDLNEPLAKVSLLKALLEEERKAYRnQVEESTKQIQVLQAQLQ 476
Cdd:PRK05771 165 DVENVEYISTDKGYVYvvvvvLKE-----------LSDEVEEELKKLGFERLELEEEGTPSE-LIREIKEELEEIEKERE 232
|
250 260 270
....*....|....*....|....*....|
gi 767924277 477 RLHIDTENLREEKDSEITSTRDELLSARDE 506
Cdd:PRK05771 233 SLLEELKELAKKYLEELLALYEYLEIELER 262
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
26-106 |
6.96e-07 |
|
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438750 [Multi-domain] Cd Length: 93 Bit Score: 47.79 E-value: 6.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 26 EPIKIGRSVArcrpaqNNATFDCKVLSRNHALVwfDHKTGKFYLQDTKSSNGTFINSQRLSRGseesppcEILSGDIIQF 105
Cdd:cd22698 21 DEFTIGRSSN------NDIRLNDHSVSRHHARI--VRQGDKCNLTDLGSTNGTFLNGIRVGTH-------ELKHGDRIQL 85
|
.
gi 767924277 106 G 106
Cdd:cd22698 86 G 86
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
25-114 |
7.46e-07 |
|
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. Specially, RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438715 [Multi-domain] Cd Length: 110 Bit Score: 48.12 E-value: 7.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 25 DEPIKIGRSVArcrpAQNNATFDC-KVLSRNHALVWFDhKTGKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDII 103
Cdd:cd22663 20 GKEVTVGRGLG----VTYQLVSTCpLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERI----EPLKPYPLNEGDLI 90
|
90
....*....|.
gi 767924277 104 QFGVDVTENTR 114
Cdd:cd22663 91 QLGVPPENKEP 101
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
55-108 |
9.91e-07 |
|
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) family; The Cep170 family includes Cep170 and Cep170B. Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438756 [Multi-domain] Cd Length: 102 Bit Score: 47.70 E-value: 9.91e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 767924277 55 HALVWFDHKTGKFYLQDTKSSNGTFINSQRLSrgseESPPCEILSGDIIQFGVD 108
Cdd:cd22704 39 HAVITYDQIDNEFKIKDLGSLNGTFVNDSRIP----EQTYITLKLGDSIRFGYD 88
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
236-700 |
9.98e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 9.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 236 DSLRKELIALQEDKHNYETtAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNER--TQEELRELANKYNGAV 313
Cdd:COG4717 74 KELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELeaLEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 314 NEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLiveGHLTKAV 393
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL---EELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 394 EETKLSKENQTRAKESDFSDTLSPSkekssddttdaqmdeqdlnepLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQA 473
Cdd:COG4717 230 EQLENELEAAALEERLKEARLLLLI---------------------AAALLALLGLGGSLLSLILTIAGVLFLVLGLLAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 474 QLQRLHIDTENLREEKDSEITSTRDELLSAR--DEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAA--SEY 549
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELEEEelEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqlEEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 550 EKEITSLQNSFQLrcqQCEDQQREEATRLQgELEKLRKEWNALETECHSLKRENVLLSSELQRQ--EKELHNSQKQSLEL 627
Cdd:COG4717 369 EQEIAALLAEAGV---EDEEELRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEEL 444
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767924277 628 TSDLSILQMSRKELENQVGSLKEQHlrDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 700
Cdd:COG4717 445 EEELEELREELAELEAELEQLEEDG--ELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLP 515
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
231-721 |
1.54e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.65 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 231 KNQTEDSLRKELIALQEDKHNYETTAK---------ESLRRVLQEKIEVVRKLSEVERSlsnTEDECTHLKEMNERTQEE 301
Cdd:pfam05483 94 KVSIEAELKQKENKLQENRKIIEAQRKaiqelqfenEKVSLKLEEEIQENKDLIKENNA---TRHLCNLLKETCARSAEK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 302 LRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAkiEALQADNDFTNE---RLTA 378
Cdd:pfam05483 171 TKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEE--EYKKEINDKEKQvslLLIQ 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 379 LQEKLIVEGHLTKAVEETKlSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYR 458
Cdd:pfam05483 249 ITEKENKMKDLTFLLEESR-DKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTIC 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 459 NQVEESTKQIQVLQAQLQrlhidTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVR-- 536
Cdd:pfam05483 328 QLTEEKEAQMEELNKAKA-----AHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKnn 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 537 --AELERWRKAASEYEKEITSlQNSFQLRCQQCEDQQREeatrLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQE 614
Cdd:pfam05483 403 keVELEELKKILAEDEKLLDE-KKQFEKIAEELKGKEQE----LIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLK 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 615 KELHNSQKQSLELTSDLSILQMSRKELENQVGSL--------------KEQHLRDSADLKTLLSKAENQAKDVQKEYEKT 680
Cdd:pfam05483 478 TELEKEKLKNIELTAHCDKLLLENKELTQEASDMtlelkkhqediincKKQEERMLKQIENLEEKEMNLRDELESVREEF 557
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 767924277 681 QTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNN 721
Cdd:pfam05483 558 IQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN 598
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
184-682 |
1.99e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 184 LEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgnqlqacSKNQTEDSLRKELIALQEDKHNYETTaKESLRRV 263
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHE---------ERREELETLEAEIEDLRETIAETERE-REELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 264 LQEKIEVVRKLSEVERSL-----------SNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEE 332
Cdd:PRK02224 281 VRDLRERLEELEEERDDLlaeaglddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 333 IQQKGQAEKKELQH---KIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLiveghltkaveETKLSKENQTRAKES 409
Cdd:PRK02224 361 LREEAAELESELEEareAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL-----------EELREERDELREREA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 410 DFSDTLS------------------PSKEKSSDDTTDAQMDEQDlNEPLAKVSLLKALLEEERKAYRNQVE------EST 465
Cdd:PRK02224 430 ELEATLRtarerveeaealleagkcPECGQPVEGSPHVETIEED-RERVEELEAELEDLEEEVEEVEERLEraedlvEAE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 466 KQIQVLQAQLQRLhidtENLREEKDSEITSTRDELLSARDEilllhqaaakvASERDTDIASLQEELKKVRAELERWRKA 545
Cdd:PRK02224 509 DRIERLEERREDL----EELIAERRETIEEKRERAEELRER-----------AAELEAEAEEKREAAAEAEEEAEEAREE 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 546 ASEYEKEITSLQNSFQ-LRCQQCEDQQREEATRLQGELEKLRKEWNALETECH---SLKRENVL-LSSELQRQEKELHNS 620
Cdd:PRK02224 574 VAELNSKLAELKERIEsLERIRTLLAAIADAEDEIERLREKREALAELNDERRerlAEKRERKReLEAEFDEARIEEARE 653
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767924277 621 QKQSLE-----LTSDLSILQMSRKELENQVGSLKEQhLRDSADLKTLLSKAENQAKDVQKEYEKTQT 682
Cdd:PRK02224 654 DKERAEeyleqVEEKLDELREERDDLQAEIGAVENE-LEELEELRERREALENRVEALEALYDEAEE 719
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
446-700 |
2.26e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 446 LKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDseITSTRDELLSARDEIlllhqaaakvaSERDTDI 525
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG--LVDLSEEAKLLLQQL-----------SELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 526 ASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRcqqcedQQREEATRLQGELEKLRKEWnaleTECHSLKREnvl 605
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQ------QLRAQLAELEAELAELSARY----TPNHPDVIA--- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 606 LSSELQRQEKELHNSQKQSL-ELTSDLSILQMSRKELENQVGSLKEQHLRdsadlktlLSKAENQAKDVQKEYEKTQTVL 684
Cdd:COG3206 296 LRAQIAALRAQLQQEAQRILaSLEAELEALQAREASLQAQLAQLEARLAE--------LPELEAELRRLEREVEVARELY 367
|
250
....*....|....*.
gi 767924277 685 SELKLKFEMTEQEKQS 700
Cdd:COG3206 368 ESLLQRLEEARLAEAL 383
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
422-651 |
2.45e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 422 SSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREE---KDSEITSTRD 498
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaeLEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 499 ELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQnsfqlrcqqcedQQREEATRL 578
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR------------ADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767924277 579 QGELEKLRKEWNALETEchsLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQ 651
Cdd:COG4942 166 RAELEAERAELEALLAE---LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
291-553 |
2.88e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.78 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 291 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALqadnd 370
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEEL----- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 371 ftNERLTALQEKLI-VEGHLTK-AVEETKLSKENQTRAKESDF----------SDTLSPSKEKSSDDTTDAQMDEQDLNE 438
Cdd:PHA02562 240 --TDELLNLVMDIEdPSAALNKlNTAAAKIKSKIEQFQKVIKMyekggvcptcTQQISEGPDRITKIKDKLKELQHSLEK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 439 plakvsLLKALLEEERKAyrNQVEESTKQIQVLQAQLqrlhidtenlrEEKDSEITSTRDELLSARDEIlllHQAAAKVA 518
Cdd:PHA02562 318 ------LDTAIDELEEIM--DEFNEQSKKLLELKNKI-----------STNKQSLITLVDKAKKVKAAI---EELQAEFV 375
|
250 260 270
....*....|....*....|....*....|....*
gi 767924277 519 SErdtdiaslQEELKKVRAELERWRKAASEYEKEI 553
Cdd:PHA02562 376 DN--------AEELAKLQDELDKIVKTKSELVKEK 402
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
260-678 |
3.01e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 50.46 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 260 LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELAN----------KYNGAVNEIKDLSDKLKVAEGK 329
Cdd:pfam05622 2 LSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESgddsgtpggkKYLLLQKQLEQLQEENFRLETA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 330 QEEIQQKGQAEKK---ELQHKIDEMEEKEQELQA---KIEALQADNDftnerltalqekliveghltkaveetKLSKENQ 403
Cdd:pfam05622 82 RDDYRIKCEELEKevlELQHRNEELTSLAEEAQAlkdEMDILRESSD--------------------------KVKKLEA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 404 TrakesdfsdtlSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAY---RNQVEESTKQIQVLQAQLQRLHI 480
Cdd:pfam05622 136 T-----------VETYKKKLEDLGDLRRQVKLLEERNAEYMQRTLQLEEELKKAnalRGQLETYKRQVQELHGKLSEESK 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 481 DTENLR------EEKDSEITSTRDELLSARD------EILLLHQAAAKVASERDTDIASLQEELKKVRAELerwrkAASE 548
Cdd:pfam05622 205 KADKLEfeykklEEKLEALQKEKERLIIERDtlretnEELRCAQLQQAELSQADALLSPSSDPGDNLAAEI-----MPAE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 549 YEKEITSLQNSFQ-LRCQQcEDQQREEATRLQGELEKLRKEWNALETEcHSLKRENVLLSS----ELQRQEKELHNSQKQ 623
Cdd:pfam05622 280 IREKLIRLQHENKmLRLGQ-EGSYRERLTELQQLLEDANRRKNELETQ-NRLANQRILELQqqveELQKALQEQGSKAED 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 767924277 624 SLELTSDLSILQMSRKELENQVGSLKEQ--HLRDSADLKTLLSKAENQAKDVQKEYE 678
Cdd:pfam05622 358 SSLLKQKLEEHLEKLHEAQSELQKKKEQieELEPKQDSNLAQKIDELQEALRKKDED 414
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
255-653 |
3.06e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.59 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 255 TAKESLRRVLQEKIEVVR-KLSEVERSLSNTedecthlkemnertQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEI 333
Cdd:pfam10174 334 TAKEQRAAILQTEVDALRlRLEEKESFLNKK--------------TKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 334 QQKGQaekkELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKENQTRAKESDFSD 413
Cdd:pfam10174 400 QKKIE----NLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKK 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 414 TLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLK---ALLEEERKAYRNQVEESTKQIQVLQAQLQRLH--IDTENLREE 488
Cdd:pfam10174 476 ENKDLKEKVSALQPELTEKESSLIDLKEHASSLAssgLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHnaEEAVRTNPE 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 489 KDSEITSTRDELLSARDEilllhqaaakvASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCE 568
Cdd:pfam10174 556 INDRIRLLEQEVARYKEE-----------SGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIK 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 569 DQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQE----KELHNSQKQSL-ELTSDLSILQMSRKELEN 643
Cdd:pfam10174 625 HGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQEldatKARLSSTQQSLaEKDGHLTNLRAERRKQLE 704
|
410
....*....|
gi 767924277 644 QVGSLKEQHL 653
Cdd:pfam10174 705 EILEMKQEAL 714
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
27-106 |
6.12e-06 |
|
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 (AtPP2C70) and similar proteins; AtPP2C70, also called kinase-associated protein phosphatase, or protein ROOT ATTENUATED GROWTH 1, dephosphorylates the serine/threonine receptor-like kinase RLK5. It may function as a signaling component in a pathway involving RLK5. It acts as a negative regulator of the CLAVATA1 signaling in plant development by binding and dephosphorylating CLAVATA1. It is also a component of a signaling pathway which mediates adaptation to NaCl stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438730 [Multi-domain] Cd Length: 102 Bit Score: 45.43 E-value: 6.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 27 PIKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLsrgSEESPPCEILSGDIIQFG 106
Cdd:cd22678 24 PLTIGRIQ------RGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESI---SPNGRPVVLSSGDVITLG 94
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
324-650 |
7.56e-06 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 49.37 E-value: 7.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 324 KVAEGKQEEIQQKGQAeKKELQHKIDEMEEKEQELQAKIEALQADNDFT-NERLTALQEKLIVE-GHLTKAVEETKLSKE 401
Cdd:pfam09731 78 ESKEPKEEKKQVKIPR-QSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEkEKALEEVLKEAISKaESATAVAKEAKDDAI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 402 NQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRN---------------QVEESTK 466
Cdd:pfam09731 157 QAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLdaapetppklpehldNVEEKVE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 467 QIQVLQAQLQRLHIDTENLREEKDSEITSTRDEL----------LSARDEILLLH------QAAAKVASERDTDIASLQE 530
Cdd:pfam09731 237 KAQSLAKLVDQYKELVASERIVFQQELVSIFPDIipvlkednllSNDDLNSLIAHahreidQLSKKLAELKKREEKHIER 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 531 ELKKVRAELERWRkaaseyEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSEL 610
Cdd:pfam09731 317 ALEKQKEELDKLA------EELSARLEEVRAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEI 390
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 767924277 611 QRQEKELHNSQKQSLE----LTSDLSILQMSRKELENQVGSLKE 650
Cdd:pfam09731 391 ELQREFLQDIKEKVEEeragRLLKLNELLANLKGLEKATSSHSE 434
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
164-696 |
9.07e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.05 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 164 SQELFQLSQYLQEALHR----EQMLEQKLATLQRLLAITQEASDTSWQALIDEDRllsRLEVMGNQLQACSKNQTEDSLR 239
Cdd:pfam10174 129 AKELFLLRKTLEEMELRietqKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWER---TRRIAEAEMQLGHLEVLLDQKE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 240 KELIALQEDKH-NYETTAKESLRRVLQEKIEVV-RKLSEVERSLSNTEDECTHLKEMNERTQEELRElankyngavnEIK 317
Cdd:pfam10174 206 KENIHLREELHrRNQLQPDPAKTKALQTVIEMKdTKISSLERNIRDLEDEVQMLKTNGLLHTEDREE----------EIK 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 318 dlsdKLKVAEGKQEEIQQKGQAEKKELQHKIDEMeekeQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETK 397
Cdd:pfam10174 276 ----QMEVYKSHSKFMKNKIDQLKQELSKKESEL----LALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 398 LSKENQTRAKES---DFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEerkaYRNQVEESTKQIQVLQAQ 474
Cdd:pfam10174 348 DALRLRLEEKESflnKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIEN----LQEQLRDKDKQLAGLKER 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 475 LQRLHIDT---------------------ENLREEKDSEITSTRDELLSARDEILLLHQ---AAAKVASERDTDIASLQE 530
Cdd:pfam10174 424 VKSLQTDSsntdtalttleealsekeriiERLKEQREREDRERLEELESLKKENKDLKEkvsALQPELTEKESSLIDLKE 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 531 E--------------LKKVRAELERWRKAASEYEKEITSLQNS---------FQLRCQQCEDQ---QREEATRLQGELEK 584
Cdd:pfam10174 504 HasslassglkkdskLKSLEIAVEQKKEECSKLENQLKKAHNAeeavrtnpeINDRIRLLEQEvarYKEESGKAQAEVER 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 585 LRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQsleltsdlsiLQMSRKELENQVGSLKEQHLRDSADLKTllS 664
Cdd:pfam10174 584 LLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVAN----------IKHGQQEMKKKGAQLLEEARRREDNLAD--N 651
|
570 580 590
....*....|....*....|....*....|..
gi 767924277 665 KAENQAKDVQKEYEKTQTVLSELKLKFEMTEQ 696
Cdd:pfam10174 652 SQQLQLEELMGALEKTRQELDATKARLSSTQQ 683
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
51-106 |
9.78e-06 |
|
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also called human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP), is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438729 [Multi-domain] Cd Length: 106 Bit Score: 44.85 E-value: 9.78e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767924277 51 LSRNHALVWF----DHKTGKFYLQDTKSSNGTFINSQRLsrgseesPP---CEILSGDIIQFG 106
Cdd:cd22677 41 ISRYHAVLQYrgdaDDHDGGFYLYDLGSTHGTFLNKQRI-------PPkqyYRLRVGHVLKFG 96
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
52-106 |
1.14e-05 |
|
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 (PPP1R8) and similar proteins; PPP1R8, also called nuclear inhibitor of protein phosphatase 1 (NIPP-1), is an inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. It may also be involved in pre-mRNA splicing and binds DNA and might act as a transcriptional repressor. PPP1R8 seems to be required for cell proliferation. PPP1R8 contains an FHA domain that mediates interactions with threonine-phosphorylated maternal embryonic leucine zipper kinase (MELK). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438726 [Multi-domain] Cd Length: 108 Bit Score: 44.95 E-value: 1.14e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 767924277 52 SRNH-ALVWfdHK-TGKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22674 48 SRVHaALVY--HKhLNRVFLIDLGSTHGTFVGGIRL----EPHKPQQLPIDSTLRFG 98
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
28-106 |
1.44e-05 |
|
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438732 [Multi-domain] Cd Length: 96 Bit Score: 44.25 E-value: 1.44e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767924277 28 IKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDhkTGKFYLQDTKSSNGTFINSQRlsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22680 23 VSIGRDP------ENVIVIPDPFVSRNHARITVD--SNEIYIEDLGSTNGTFVNDFK-----RIKGPAKLHPNDIIKLG 88
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
273-721 |
1.83e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 273 KLSEVERSLSNTEDECTHLKEMNERTQEELRElankyngAVNEIKDLsdkLKVAEGKQEEIQQKgQAEKKELQHKIDEME 352
Cdd:TIGR04523 336 IISQLNEQISQLKKELTNSESENSEKQRELEE-------KQNEIEKL---KKENQSYKQEIKNL-ESQINDLESKIQNQE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 353 EKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKENQTrakesdfsdtlspskeKSSDDTTDAQmd 432
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELII----------------KNLDNTRESL-- 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 433 EQDLNEPLAKVSLLKALLEEERKayrnQVEESTKQIQVLQAQLQRLhidtenlrEEKDSEITSTRDELLSARDEIlllhq 512
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQK----ELKSKEKELKKLNEEKKEL--------EEKVKDLTKKISSLKEKIEKL----- 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 513 aaAKVASERDTDIASLQEELKKVRAELERwrkaaSEYEKEITSLQNSFqlrcqqceDQQREEATRLQGELEKLRKEWNAL 592
Cdd:TIGR04523 530 --ESEKKEKESKISDLEDELNKDDFELKK-----ENLEKEIDEKNKEI--------EELKQTQKSLKKKQEEKQELIDQK 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 593 ETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKD 672
Cdd:TIGR04523 595 EKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTK 674
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 767924277 673 VQKEYEKTQTVLSEL------KLKFEMTEQEKQSITDELKQCKNNLKLLREKGNN 721
Cdd:TIGR04523 675 IDDIIELMKDWLKELslhykkYITRMIRIKDLPKLEEKYKEIEKELKKLDEFSKE 729
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
257-633 |
1.95e-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: 48.43 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 257 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDlsDKLKVAEGKQEEIQQK 336
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYL--DYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 337 GQAEKKELQHKIDEMEekeqelqaKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLS 416
Cdd:pfam02463 246 LRDEQEEIESSKQEIE--------KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 417 PSKEKSsddttdAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEES-TKQIQVLQAQLQRLHIDTENLREEKDSEITS 495
Cdd:pfam02463 318 ESEKEK------KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEeLEKLQEKLEQLEEELLAKKKLESERLSSAAK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 496 TRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELerwrkaaseyEKEITSLQNSFQLRCQQCEDQqreEA 575
Cdd:pfam02463 392 LKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE----------EESIELKQGKLTEEKEELEKQ---EL 458
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 767924277 576 TRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSI 633
Cdd:pfam02463 459 KLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALI 516
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
14-106 |
2.43e-05 |
|
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.
Pssm-ID: 438734 [Multi-domain] Cd Length: 96 Bit Score: 43.67 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 14 SHPFQERHvyldepIKIGRSVarcrpaQNNATFDCKVLSRNHALvwFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEesp 93
Cdd:cd22682 14 QFPITEST------IVIGRSV------ESQVQIDDDSVSRYHAK--LAVNPSAVSIIDLGSTNGTIVNGKKIPKLAS--- 76
|
90
....*....|...
gi 767924277 94 pCEILSGDIIQFG 106
Cdd:cd22682 77 -CDLQNGDQIKIG 88
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
218-718 |
2.70e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.59 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 218 RLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTaKESLRRVLQEKIEVVRKLSEVERSLSNTEDECthlkemnER 297
Cdd:PRK01156 151 RKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYL-EEKLKSSNLELENIKKQIADDEKSHSITLKEI-------ER 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 298 TQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIqQKGQAEKKELQHKIDEMEEKEQELQAKI-EALQADNDFTNERL 376
Cdd:PRK01156 223 LSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI-KTAESDLSMELEKNNYYKELEERHMKIInDPVYKNRNYINDYF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 377 TALQEKLIVEGHLTKAVEETKLSKENQTRAK--ESDFSDTLSPSKEKSSDDT--TDAQMDEQDLNEPLAKVSLLKALLEE 452
Cdd:PRK01156 302 KYKNDIENKKQILSNIDAEINKYHAIIKKLSvlQKDYNDYIKKKSRYDDLNNqiLELEGYEMDYNSYLKSIESLKKKIEE 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 453 ERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLR---EEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQ 529
Cdd:PRK01156 382 YSKNIERMSAFISEILKIQEIDPDAIKKELNEINvklQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTT 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 530 EELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRenvLLSSE 609
Cdd:PRK01156 462 LGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLED---IKIKI 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 610 LQRQEKELHNSQKQSLELTSDLSILQMSRKELenqvgsLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKL 689
Cdd:PRK01156 539 NELKDKHDKYEEIKNRYKSLKLEDLDSKRTSW------LNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPD 612
|
490 500
....*....|....*....|....*....
gi 767924277 690 KFEMTEQEKQSITDELKQCKNNLKLLREK 718
Cdd:PRK01156 613 DKSYIDKSIREIENEANNLNNKYNEIQEN 641
|
|
| FHA_RAD53-like_rpt2 |
cd22690 |
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
12-103 |
2.79e-05 |
|
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine/threonine-protein kinase RAD53 and similar proteins; RAD53, also called CHEK2 homolog, or serine-protein kinase 1 (Spk1), is a nuclear protein kinase that phosphorylates proteins on serine, threonine, and tyrosine. It controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints and prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. It may be involved in the phosphorylation of RPH1. RAD53 contains two FHA domains. This model corresponds to the second one. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438742 [Multi-domain] Cd Length: 105 Bit Score: 43.82 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 12 PNSHPfqerHVYL-DEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFD-HKTGK--FYLQDTkSSNGTFINSQRLSR 87
Cdd:cd22690 8 NPSYP----DIELtQNTTFIGRS------KDCDEEITDPRISKHHCIITRKrSGKGLddVYVTDT-STNGTFINNNRLGK 76
|
90
....*....|....*.
gi 767924277 88 GSEesppCEILSGDII 103
Cdd:cd22690 77 GSQ----SLLQDGDEI 88
|
|
| FHA_CHFR |
cd22672 |
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ... |
49-105 |
2.88e-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: 43.82 E-value: 2.88e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 767924277 49 KVLSRNHALVWFDHKtGKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQF 105
Cdd:cd22672 39 KLVSGDHCKIIRDEK-GQVWLEDT-STNGTLVNKVKVVKGQK----VELKHGDVIYL 89
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
296-520 |
3.34e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 296 ERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQqkgqAEKKELQHKIDEMEEKEQELQAKIEALQADndfTNER 375
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQ----AELEALQAEIDKLQAEIAEAEAEIEERREE---LGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 376 LTALQEklivEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQM----DEQDLNEPLAKVSLLKALLE 451
Cdd:COG3883 92 ARALYR----SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAeleaKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767924277 452 EERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVASE 520
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
315-719 |
3.69e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 315 EIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHK---IDEMEEKEQELQAKIEALQA---DNDFTNERLTALQ-EKLIVEG 387
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVlreINEISSELPELREELEKLEKevkELEELKEEIEELEkELESLEG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 388 HLTKAVEETKLSKE--NQTRAKESDFSDTLSPSKEKSSDDTTDAQMDE--QDLNEPLAKVSLLKALLEEERKAYRNQ--- 460
Cdd:PRK03918 253 SKRKLEEKIRELEEriEELKKEIEELEEKVKELKELKEKAEEYIKLSEfyEEYLDELREIEKRLSRLEEEINGIEERike 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 461 -------VEESTKQIQVLQAQLQRLHIDTENLREEKDSEitsTRDELLSARDEILLLHQAAAKV--ASERDTDIaslQEE 531
Cdd:PRK03918 333 leekeerLEELKKKLKELEKRLEELEERHELYEEAKAKK---EELERLKKRLTGLTPEKLEKELeeLEKAKEEI---EEE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 532 LKKVRAELERWRKAASEYEKEITSLQnSFQLRCQQC-----EDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLL 606
Cdd:PRK03918 407 ISKITARIGELKKEIKELKKAIEELK-KAKGKCPVCgreltEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 607 SSELQRQEKELhnSQKQSLELTsdlsilqmsrKELENQVGSLK----EQHLRDSADLKTLLSKAENQAKDVQKEYEKtqt 682
Cdd:PRK03918 486 EKVLKKESELI--KLKELAEQL----------KELEEKLKKYNleelEKKAEEYEKLKEKLIKLKGEIKSLKKELEK--- 550
|
410 420 430
....*....|....*....|....*....|....*..
gi 767924277 683 vLSELKLKFEMTEQEKQSITDELkqcKNNLKLLREKG 719
Cdd:PRK03918 551 -LEELKKKLAELEKKLDELEEEL---AELLKELEELG 583
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
25-108 |
3.91e-05 |
|
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar proteins; ZEP, also called protein ABA DEFICIENT 1, ABA1, protein IMPAIRED IN BABA-INDUCED STERILITY 3, protein LOW EXPRESSION OF OSMOTIC STRESS-RESPONSIVE GENES 6, or protein NON-PHOTOCHEMICAL QUENCHING 2, plays an important role in the xanthophyll cycle and abscisic acid (ABA) biosynthesis. It converts zeaxanthin into antheraxanthin and subsequently violaxanthin. ZEP is required for resistance to osmotic and drought stresses, ABA-dependent stomatal closure, seed development and dormancy, modulation of defense gene expression, and disease resistance and non-photochemical quencing (NPQ). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438754 [Multi-domain] Cd Length: 123 Bit Score: 43.57 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 25 DEPIKIGRsvarcRPAQNNAT----FDCKVLSRNHALVWFdhKTGKFYLQDTKSSNGTFINSQRLSR-GSEESPPCEILS 99
Cdd:cd22702 31 KQPCIIGS-----DPHQAISGisvvIPSPQVSELHARITC--KNGAFFLTDLGSEHGTWINDNEGRRyRAPPNFPVRLHP 103
|
....*....
gi 767924277 100 GDIIQFGVD 108
Cdd:cd22702 104 SDVIEFGSD 112
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
18-86 |
4.72e-05 |
|
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the first FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438746 [Multi-domain] Cd Length: 93 Bit Score: 42.70 E-value: 4.72e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767924277 18 QERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhkTGKFYLQDTKSSNGTFINSQRLS 86
Cdd:cd22694 8 GELRFDPGSSVRIGRD------PDADVRLDDPRVSRRHALLEFD--GDGWVYTDLGSRNGTYLNGRRVQ 68
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
304-623 |
5.38e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.66 E-value: 5.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 304 ELANKYNG-AVNEIKDLSDKLKVAEGKQ--EEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNE-----R 375
Cdd:pfam17380 255 EYTVRYNGqTMTENEFLNQLLHIVQHQKavSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEmdrqaA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 376 LTALQEKLIVEghltKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSdDTTDAQMDEQDLNEPLAK---VSLLKALLEE 452
Cdd:pfam17380 335 IYAEQERMAME----RERELERIRQEERKRELERIRQEEIAMEISRMR-ELERLQMERQQKNERVRQeleAARKVKILEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 453 ERKayRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAAA-----KVASERDTDIAS 527
Cdd:pfam17380 410 ERQ--RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEerkrkKLELEKEKRDRK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 528 LQEELKK--VRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQR----EEATRLQGELEKLRKEWNALETECHSLKR 601
Cdd:pfam17380 488 RAEEQRRkiLEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERrreaEEERRKQQEMEERRRIQEQMRKATEERSR 567
|
330 340
....*....|....*....|...
gi 767924277 602 -ENVLLSSELQRQEKELHNSQKQ 623
Cdd:pfam17380 568 lEAMEREREMMRQIVESEKARAE 590
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
262-697 |
5.57e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.99 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 262 RVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEK 341
Cdd:COG5022 954 PELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASK 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 342 ------------KELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGhltkaveetklsKENQTRAKES 409
Cdd:COG5022 1034 iissestelsilKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTEN------------LLKTINVKDL 1101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 410 DFSDTLSpSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEK 489
Cdd:COG5022 1102 EVTNRNL-VKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEK 1180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 490 DSEITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAElERWRKAASEYEKEITSLQNSFQLRCQQCED 569
Cdd:COG5022 1181 RLYQSALYDEKSKLSSSEVNDLKNELIALFSKIFSGWPRGDKLKKLISE-GWVPTEYSTSLKGFNNLNKKFDTPASMSNE 1259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 570 QQREEATRLQGELEKLRKEWNALETECHSLKRE-NVLLSSELQRQEKELhnSQKQSLELTSDLSILQMSRKELENQVGSL 648
Cdd:COG5022 1260 KLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYiNVGLFNALRTKASSL--RWKSATEVNYNSEELDDWCREFEISDVDE 1337
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 767924277 649 KEQHLRDSADLKTLLSKAENQAKDV-QKEYEKTQTVLSELKLKFEMTEQE 697
Cdd:COG5022 1338 ELEELIQAVKVLQLLKDDLNKLDELlDACYSLNPAEIQNLKSRYDPADKE 1387
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
445-595 |
6.00e-05 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 46.59 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 445 LLKALLEEERK--AYRNQVEESTKQIQVLQAQLQRLHIDTENLREE--KDSEITSTRDELLSARDEILLLHQAAAKvASE 520
Cdd:pfam13166 305 QLPAVSDLASLlsAFELDVEDIESEAEVLNSQLDGLRRALEAKRKDpfKSIELDSVDAKIESINDLVASINELIAK-HNE 383
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767924277 521 RDTDIASLQEELKKvraelERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREeATRLQGELEKLRKEWNALETE 595
Cdd:pfam13166 384 ITDNFEEEKNKAKK-----KLRLHLVEEFKSEIDEYKDKYAGLEKAINSLEKE-IKNLEAEIKKLREEIKELEAQ 452
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
13-110 |
6.30e-05 |
|
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also called nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438717 [Multi-domain] Cd Length: 97 Bit Score: 42.22 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 13 NSHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTgkFYLQDTKSSNGTFINSQRLSrgsee 91
Cdd:cd22665 7 SQAHGPEKDFPLYEgENVIGRD------PSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRL----- 73
|
90 100
....*....|....*....|.
gi 767924277 92 SPPC--EILSGDIIQFGvDVT 110
Cdd:cd22665 74 KPNVryELIDGDLLLFG-DVK 93
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
507-726 |
7.09e-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: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 507 ILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQcEDQQREEATRLQGELEKLR 586
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-IRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 587 KEWNALETECHSLKRE-----------------NVLLSSE--------LQRQEKELHNSQKQSLELTSDLSILQMSRKEL 641
Cdd:COG4942 90 KEIAELRAELEAQKEElaellralyrlgrqpplALLLSPEdfldavrrLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 642 ENQVGSLKE---QHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 718
Cdd:COG4942 170 EAERAELEAllaELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
....*...
gi 767924277 719 GNNKPWPW 726
Cdd:COG4942 250 ALKGKLPW 257
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
245-717 |
1.97e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.04 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 245 LQEDKHNYETTAKeSLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMN--ERTQEELRELANKYNGAVNEIKDLSdk 322
Cdd:TIGR01612 1231 IDEEKKKSEHMIK-AMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNisHDDDKDHHIISKKHDENISDIREKS-- 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 323 LKVAEGKQEEiqQKGQAEKKELQHKIDEMEEKEQELQAKIEALQadNDFTNERLTALQEKLIVEGHLTKAVEETklskeN 402
Cdd:TIGR01612 1308 LKIIEDFSEE--SDINDIKKELQKNLLDAQKHNSDINLYLNEIA--NIYNILKLNKIKKIIDEVKEYTKEIEEN-----N 1378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 403 QTRAKESDFSDTLSPS-KEKSSDDT----TDAQMDEQDLNEPLAKVSLLKA-LLEEERK--AYRNQVEESTKQIQVLQAQ 474
Cdd:TIGR01612 1379 KNIKDELDKSEKLIKKiKDDINLEEckskIESTLDDKDIDECIKKIKELKNhILSEESNidTYFKNADENNENVLLLFKN 1458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 475 LQRLHIDTENLREEKDSEITSTRDELLSARDEilllHQAAAKvaserdtdiaSLQEELKKVRAELERWRKAASEYEKEIT 554
Cdd:TIGR01612 1459 IEMADNKSQHILKIKKDNATNDHDFNINELKE----HIDKSK----------GCKDEADKNAKAIEKNKELFEQYKKDVT 1524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 555 SLQNSF-QLRCQQCEDQQREEATRLQGELEKLRK----EWNALETECHSLKRENVLLSSELQRQEKE----------LHN 619
Cdd:TIGR01612 1525 ELLNKYsALAIKNKFAKTKKDSEIIIKEIKDAHKkfilEAEKSEQKIKEIKKEKFRIEDDAAKNDKSnkaaidiqlsLEN 1604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 620 SQKQSLELTSDLSILQMSRKE---LENQVGSL----KEQHLRDSAD----LKTLLSKAENQAKDVQKEYEKTQTVLSELK 688
Cdd:TIGR01612 1605 FENKFLKISDIKKKINDCLKEtesIEKKISSFsidsQDTELKENGDnlnsLQEFLESLKDQKKNIEDKKKELDELDSEIE 1684
|
490 500 510
....*....|....*....|....*....|....*..
gi 767924277 689 -LKFEMTEQEK-------QSITDELKQCKNNLKLLRE 717
Cdd:TIGR01612 1685 kIEIDVDQHKKnyeigiiEKIKEIAIANKEEIESIKE 1721
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
52-107 |
2.20e-04 |
|
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also called cell cycle regulatory protein p95, or Nijmegen breakage syndrome protein 1 (NBS1), is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. Nibrin modulates the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-dependent protein kinase catalytic subunit (DNA-PKcs) to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. Nibrin also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. Nibrin is a major player in the control of intra-S-phase checkpoint. This subfamily also includes Schizosaccharomyces pombe DNA repair and telomere maintenance protein Nbs1 and Arabidopsis thaliana AtNbs1. SpNbs1 is an FHA domain-containing protein required for DNA damage repair and S-phase DNA damage checkpoint. It is involved in telomere length maintenance and maintenance of chromatin structure. AtNbs1 is a component of MRN complex. It also functions in the very early stages of meiosis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438719 [Multi-domain] Cd Length: 108 Bit Score: 41.16 E-value: 2.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767924277 52 SRNHALVWFDHKTG---------KFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQFGV 107
Cdd:cd22667 40 SRKHATLTVLHPEAnlsdpdtrpELTLKDL-SKYGTFVNGEKLKGGSE----VTLKDGDVITFGV 99
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
155-383 |
2.86e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 155 VAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQAcSKNQT 234
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA-ELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 235 EDSLRKELIALQEDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEdectHLKEMNERTQEELRELANKyngaVN 314
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ----YLKYLAPARREQAEELRAD----LA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767924277 315 EIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKL 383
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
53-106 |
2.91e-04 |
|
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 (FHAD1) and similar proteins; FHAD1, also called FHA domain-containing protein 1, is an uncharacterized FHA domain-containing protein. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438752 [Multi-domain] Cd Length: 96 Bit Score: 40.32 E-value: 2.91e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 767924277 53 RNHALVWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPceilsGDIIQFG 106
Cdd:cd22700 36 EQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAP-----GDVLRFG 84
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
340-603 |
3.23e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 43.65 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 340 EKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLI-VEGHLTKAV-EETKLSKENQTRAKE-SDFSDTLS 416
Cdd:pfam15905 60 ELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEkVEAKLNAAVrEKTSLSASVASLEKQlLELTRVNE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 417 PSKEKSSDDTTDAQMdeqdlNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLRE---EKDSEI 493
Cdd:pfam15905 140 LLKAKFSEDGTQKKM-----SSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEklvSTEKEK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 494 TSTRDELLSARDEILLLHQAAAKVASERdTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQRE 573
Cdd:pfam15905 215 IEEKSETEKLLEYITELSCVSEQVEKYK-LDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEE 293
|
250 260 270
....*....|....*....|....*....|
gi 767924277 574 EATRLQGELEKLRKEWNALETECHSLKREN 603
Cdd:pfam15905 294 LLREYEEKEQTLNAELEELKEKLTLEEQEH 323
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
253-707 |
3.85e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 253 ETTAKESLRRVLQ-EKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELR-ELANKYNGA--VNEIKDLSDKLKVAE- 327
Cdd:PTZ00121 1114 ARKAEEAKKKAEDaRKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKaEEARKAEDAkkAEAARKAEEVRKAEEl 1193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 328 GKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKI------------EALQADNDFTNERLTALQEKLIVEGHLTKAVE- 394
Cdd:PTZ00121 1194 RKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAvkkaeeakkdaeEAKKAEEERNNEEIRKFEEARMAHFARRQAAIk 1273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 395 -ETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQdlneplAKVSLLKALLEEERK---AYRNQVEESTKQIQV 470
Cdd:PTZ00121 1274 aEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA------KKADEAKKKAEEAKKkadAAKKKAEEAKKAAEA 1347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 471 LQAQLQRLHIDTENLREE------KDSEITSTRDELLSARDEILLLHQAAAKvaSERDTDIAslqEELKKVRAElerwRK 544
Cdd:PTZ00121 1348 AKAEAEAAADEAEAAEEKaeaaekKKEEAKKKADAAKKKAEEKKKADEAKKK--AEEDKKKA---DELKKAAAA----KK 1418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 545 AASEYEKEITSLQNSFQLRCQQCEDQQREEATRlqgELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQS 624
Cdd:PTZ00121 1419 KADEAKKKAEEKKKADEAKKKAEEAKKADEAKK---KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEA 1495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 625 LELTSDLSILQMSRKELENqvgSLKEQHLRDSADLKtllsKAEN--QAKDVQKEYEKTQTvlSELKLKFEMTEQEKQSIT 702
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADE---AKKAEEAKKADEAK----KAEEakKADEAKKAEEKKKA--DELKKAEELKKAEEKKKA 1566
|
....*
gi 767924277 703 DELKQ 707
Cdd:PTZ00121 1567 EEAKK 1571
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
1-106 |
3.97e-04 |
|
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442679 [Multi-domain] Cd Length: 402 Bit Score: 43.60 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 1 MPSALAIFTCRPNSHPFQERHVYLDEPIKIGRSvARC-----RPAQnnatfdckVLSRNHALVWFDHktGKFYLQDTkSS 75
Cdd:COG3456 1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRS-ADCdwvlpDPDR--------SVSRRHAEIRFRD--GAFCLTDL-ST 68
|
90 100 110
....*....|....*....|....*....|...
gi 767924277 76 NGTFIN--SQRLSRGSEEsppcEILSGDIIQFG 106
Cdd:COG3456 69 NGTFLNgsDHPLGPGRPV----RLRDGDRLRIG 97
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
429-718 |
4.41e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 429 AQMDE------QDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHidTENLREEKD--SEITSTRDEL 500
Cdd:PHA02562 166 SEMDKlnkdkiRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKY--DELVEEAKTikAEIEELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 501 LSARDEIlllhqaaakvaSERDTDIASLQEELKKVRAELERWRKAASEYEKEITslqnsfqlrCQQCEDQQREEATRLQG 580
Cdd:PHA02562 244 LNLVMDI-----------EDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGV---------CPTCTQQISEGPDRITK 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 581 ELEKLrkewnaletechslkrenvllsSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQVGSLKEQhlrdsadlk 660
Cdd:PHA02562 304 IKDKL----------------------KELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQS--------- 352
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 767924277 661 tlLSKAENQAKDVQKEYEKTQTvlselklkfemteqEKQSITDELKQCKNNLKLLREK 718
Cdd:PHA02562 353 --LITLVDKAKKVKAAIEELQA--------------EFVDNAEELAKLQDELDKIVKT 394
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
247-631 |
4.43e-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: 43.80 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 247 EDKHNYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEmnertqeELRELANKYNGAVNEIKDLSDKLKVA 326
Cdd:TIGR00618 534 EQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDN-------RSKEDIPNLQNITVRLQDLTEKLSEA 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 327 EGKQEEIQQkgqAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKENQTRA 406
Cdd:TIGR00618 607 EDMLACEQH---ALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQ 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 407 KESDFSDTLSPSKEkssddttdaqmdeqDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLR 486
Cdd:TIGR00618 684 KMQSEKEQLTYWKE--------------MLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELM 749
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 487 EEkdseitstRDELLSARDEILLLHQAAAKVASERDTdiaslqeELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQ 566
Cdd:TIGR00618 750 HQ--------ARTVLKARTEAHFNNNEEVTAALQTGA-------ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPS 814
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767924277 567 CEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEkELHNSQKQSLELTSDL 631
Cdd:TIGR00618 815 DEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA-QLTQEQAKIIQLSDKL 878
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
183-718 |
4.49e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.56 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 183 MLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQT--EDSLR---KELIALQEDKHNY---ET 254
Cdd:pfam05483 262 LLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKalEEDLQiatKTICQLTEEKEAQmeeLN 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 255 TAKESLRRVLQEKIEVVRKLSEVERS----LSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLsdKLKVAEgkq 330
Cdd:pfam05483 342 KAKAAHSFVVTEFEATTCSLEELLRTeqqrLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEEL--KKILAE--- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 331 eeiQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKlivEGHLTKAVEE--TKLSKENQTRAKE 408
Cdd:pfam05483 417 ---DEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTS---EEHYLKEVEDlkTELEKEKLKNIEL 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 409 SDFSDTLSPSKEKSSDDTTDAQMdeqdlneplakvsllkalleeERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREE 488
Cdd:pfam05483 491 TAHCDKLLLENKELTQEASDMTL---------------------ELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 489 kdseITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLqnsfqlrcqqce 568
Cdd:pfam05483 550 ----LESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEEL------------ 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 569 dQQREEATRLQGELEKlrKEWNALETECHSLKREnvlLSSELQRQEKELHNSQKQ----SLELTSDLSILQMSRKELENQ 644
Cdd:pfam05483 614 -HQENKALKKKGSAEN--KQLNAYEIKVNKLELE---LASAKQKFEEIIDNYQKEiedkKISEEKLLEEVEKAKAIADEA 687
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767924277 645 VGSLKEQHLRDSADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 718
Cdd:pfam05483 688 VKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQ 761
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
574-720 |
4.72e-04 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 42.77 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 574 EATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNsQKQSLELTSDLSilqmsrkELENQVGSLKeqhl 653
Cdd:pfam15294 134 EIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGA-KKDVKSNLKEIS-------DLEEKMAALK---- 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767924277 654 rdsADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGN 720
Cdd:pfam15294 202 ---SDLEKTLNASTALQKSLEEDLASTKHELLKVQEQLEMAEKELEKKFQQTAAYRNMKEMLTKKNE 265
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
49-112 |
4.89e-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: 40.89 E-value: 4.89e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767924277 49 KVLSRNHALVWFDHKTG--KFYLQDTKSSNGTFINsqrlsrgSEESPPC---EILSGDIIQFGVDVTEN 112
Cdd:cd22681 64 ETCSKQHCVIQFRNVKGilKPYIMDLDSSNGTCLN-------DNVIPSSryvELRSGDVITFSKSNDYE 125
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
428-616 |
5.22e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 428 DAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEI--------TSTRDE 499
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLralyrlgrQPPLAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 500 LLSARD-----EILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFqlrcQQCEDQQREE 574
Cdd:COG4942 125 LLSPEDfldavRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL----EALKAERQKL 200
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767924277 575 ATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKE 616
Cdd:COG4942 201 LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
519-718 |
5.46e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 519 SERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQ--LRCQQCEDQQRE-EATRLQGELEKLRKEWNALETE 595
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREkaERYQALLKEKREyEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 596 CHSLKRENVLLSSELQRQEKELHNS----------------------QKQSLELTSDLSILQMSRKELENQVGSLKEQHL 653
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIeqlleelnkkikdlgeeeqlrvKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767924277 654 RDSADLKTLLSKAENQAKDV---QKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREK 718
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIeeeRKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
215-508 |
6.02e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.50 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 215 LLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHNYETTAKEslrrvlqeKIEVVRKLSEVERSlsntedecthlKEM 294
Cdd:TIGR01612 1455 LFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSKGC--------KDEADKNAKAIEKN-----------KEL 1515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 295 NERTQEELRELANKY----------------NGAVNEIKDLSDKLKVAEGKQEeiqQKGQAEKKElqhkidemeekeqel 358
Cdd:TIGR01612 1516 FEQYKKDVTELLNKYsalaiknkfaktkkdsEIIIKEIKDAHKKFILEAEKSE---QKIKEIKKE--------------- 1577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 359 QAKIEALQADNDFTNerltalqeKLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQmdEQDLNE 438
Cdd:TIGR01612 1578 KFRIEDDAAKNDKSN--------KAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQ--DTELKE 1647
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767924277 439 PLAKVSLLKALLEEERKAYRNqVEESTKQIQVLQAQLQRLHIDTENLRE-------EKDSEITSTRDELLSARDEIL 508
Cdd:TIGR01612 1648 NGDNLNSLQEFLESLKDQKKN-IEDKKKELDELDSEIEKIEIDVDQHKKnyeigiiEKIKEIAIANKEEIESIKELI 1723
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
16-111 |
6.40e-04 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaB and similar proteins; FhaB, also called FtsZ-interacting protein A (FipA), is a putative virulence factor involved in regulating cell shape. It can interact with polyketide-associated protein PapA5, a putative membrane protein involved in the biosynthesis of virulence enhancing lipids. FhaB regulates growth and cell division. It is probably required for divisomal protein assembly under oxidative stress. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438745 [Multi-domain] Cd Length: 91 Bit Score: 39.21 E-value: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 16 PFQERHVYLD-EPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFdhKTGKFYLQDTKSSNGTFINSQRLSRgseespP 94
Cdd:cd22693 7 TLQGQTFPIDkSGITIGRA------DDNDLVLSDDFVSSRHARIYL--QGSSWYLEDLGSTNGTFVNGNRVTQ------P 72
|
90
....*....|....*..
gi 767924277 95 CEILSGDIIQFGVDVTE 111
Cdd:cd22693 73 VVVQPGDTIRIGATVFE 89
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
421-687 |
7.10e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 421 KSSDDTTDAQMDEQDLNEPLAKVSLLKALlEEERKAYRNQVEESTKQIQVLQAQLQRLhidtenlreeKDSEITSTRDEL 500
Cdd:PRK11281 50 KQKLLEAEDKLVQQDLEQTLALLDKIDRQ-KEETEQLKQQLAQAPAKLRQAQAELEAL----------KDDNDEETRETL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 501 lsardeilllhqaaakvaseRDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQN----------SFQLRCQQCEDQ 570
Cdd:PRK11281 119 --------------------STLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTqperaqaalyANSQRLQQIRNL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 571 ----QREEATRLQGELEKLRKEWNALEtechslkrenvlLSSELQRQEKElHNSQKQSL-ELTSDLSILQMSRKELENQv 645
Cdd:PRK11281 179 lkggKVGGKALRPSQRVLLQAEQALLN------------AQNDLQRKSLE-GNTQLQDLlQKQRDYLTARIQRLEHQLQ- 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767924277 646 gslkeqhlrdsaDLKTL-----LSKAENQAKDVQKEYEKTQTVLSEL 687
Cdd:PRK11281 245 ------------LLQEAinskrLTLSEKTVQEAQSQDEAARIQANPL 279
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
258-722 |
8.09e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.12 E-value: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 258 ESLRRVLQEKIEVVRK--LSEVERSLSNTEDECTHLKEMN--ERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEI 333
Cdd:TIGR01612 1058 DEIEKEIGKNIELLNKeiLEEAEINITNFNEIKEKLKHYNfdDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEI 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 334 QQKGQAEKKELQHKIDEME---------EKEQELQAKIEALqadndftnerLTALQEKLIVEGHLTKAVEETKLSKENQT 404
Cdd:TIGR01612 1138 KKKSENYIDEIKAQINDLEdvadkaisnDDPEEIEKKIENI----------VTKIDKKKNIYDEIKKLLNEIAEIEKDKT 1207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 405 RAKEsdfSDTLSPSKEKSSDDTTDAQMDEQDlNEPLAKVSLLKALLE--EERKAYRNQVEESTKQIQVLQAQLQRLHIDT 482
Cdd:TIGR01612 1208 SLEE---VKGINLSYGKNLGKLFLEKIDEEK-KKSEHMIKAMEAYIEdlDEIKEKSPEIENEMGIEMDIKAEMETFNISH 1283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 483 EnlrEEKDSEITSTR-DELLS-ARDEILLLHQaaakvASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSF 560
Cdd:TIGR01612 1284 D---DDKDHHIISKKhDENISdIREKSLKIIE-----DFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNIL 1355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 561 QL-RCQQCEDQQREEATRLQGELEKLRKEWNALET------------ECHSlKRENVL--------------LSSELQRQ 613
Cdd:TIGR01612 1356 KLnKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKlikkikddinleECKS-KIESTLddkdidecikkikeLKNHILSE 1434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 614 EKELHNSQKQSLELTSDLSIL--------QMSRKELENQ-----------VGSLKEqHLRDSADLKTLLSKAENQA---K 671
Cdd:TIGR01612 1435 ESNIDTYFKNADENNENVLLLfkniemadNKSQHILKIKkdnatndhdfnINELKE-HIDKSKGCKDEADKNAKAIeknK 1513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 767924277 672 DVQKEYEKTQTVL------SELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNNK 722
Cdd:TIGR01612 1514 ELFEQYKKDVTELlnkysaLAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQK 1570
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
276-383 |
1.13e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.15 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 276 EVERSLSNTEDECTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEK----------K 342
Cdd:pfam06160 288 YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEvayselqeelE 367
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 767924277 343 ELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKL 383
Cdd:pfam06160 368 EILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLEL 408
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
165-364 |
1.35e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 165 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALID--------EDRLLSRLEVMGNQLQACSKNQTED 236
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekeiaelRAELEAQKEELAELLRALYRLGRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 237 SLrkELIALQEDKHNYETTAK--ESLRRVLQEKIEVVRK-LSEVERSLSNTEDECTHLKEMNERTQEELRELANkyngAV 313
Cdd:COG4942 121 PL--ALLLSPEDFLDAVRRLQylKYLAPARREQAEELRAdLAELAALRAELEAERAELEALLAELEEERAALEA----LK 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767924277 314 NEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEA 364
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
255-718 |
1.66e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.13 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 255 TAKESLRRVLQEKIEVVRKLSEVERSLSN--------TEDECTHLKEMNERTQEELRE-LANKYNGAVNEIKDLSDKLKV 325
Cdd:PTZ00440 894 SNKQLVEHLLNNKIDLKNKLEQHMKIINTdniiqkneKLNLLNNLNKEKEKIEKQLSDtKINNLKMQIEKTLEYYDKSKE 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 326 A-EGKQEEIQQKGQAEKKELQH---KIDEMEEKEQELQAKIealqadNDFTNER---LTALQEKLIvEGHLTKAVEETKL 398
Cdd:PTZ00440 974 NiNGNDGTHLEKLDKEKDEWEHfksEIDKLNVNYNILNKKI------DDLIKKQhddIIELIDKLI-KEKGKEIEEKVDQ 1046
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 399 SKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDE---------QDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQ 469
Cdd:PTZ00440 1047 YISLLEKMKTKLSSFHFNIDIKKYKNPKIKEEIKLleekveallKKIDENKNKLIEIKNKSHEHVVNADKEKNKQTEHYN 1126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 470 VLQAQLQRLHIDTENLREEKDS----EITSTRDELLSARDEILLLHQAAAKVASERdTDIASLQEELKKVRAELERWRKA 545
Cdd:PTZ00440 1127 KKKKSLEKIYKQMEKTLKELENmnleDITLNEVNEIEIEYERILIDHIVEQINNEA-KKSKTIMEEIESYKKDIDQVKKN 1205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 546 ASEYEKEITSLQNSfqlrcqqceDQQREEATRLQGELEKLRKEWNALETECHSLKRENvllssELQRQEKELHNSQKQSL 625
Cdd:PTZ00440 1206 MSKERNDHLTTFEY---------NAYYDKATASYENIEELTTEAKGLKGEANRSTNVD-----ELKEIKLQVFSYLQQVI 1271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 626 ELTSDLsilQMSRKELENQVGSLKEQHLRD-SADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQ--SIT 702
Cdd:PTZ00440 1272 KENNKM---ENALHEIKNMYEFLISIDSEKiLKEILNSTKKAEEFSNDAKKELEKTDNLIKQVEAKIEQAKEHKNkiYGS 1348
|
490
....*....|....*.
gi 767924277 703 DELKQCKNNLKLLREK 718
Cdd:PTZ00440 1349 LEDKQIDDEIKKIEQI 1364
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
233-718 |
1.70e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.13 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 233 QTEDSLRKELIALQEDKHNYETTAKEslRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEEL-RELANKYNG 311
Cdd:pfam12128 353 QSELENLEERLKALTGKHQDVTAKYN--RRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALeSELREQLEA 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 312 AVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKEL------QHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIV 385
Cdd:pfam12128 431 GKLEFNEEEYRLKSRLGELKLRLNQATATPELLlqlenfDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQ 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 386 EGHLTKAVEETKLSKENQTRAKESDFSDTLSpskekssddtTDAQMDEQDLNEPLAKVSLLKALLEEErkayrnQVEEST 465
Cdd:pfam12128 511 ASRRLEERQSALDELELQLFPQAGTLLHFLR----------KEAPDWEQSIGKVISPELLHRTDLDPE------VWDGSV 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 466 KQIQVLQAQlqRLHIDTENLREEKDSEitstrDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKA 545
Cdd:pfam12128 575 GGELNLYGV--KLDLKRIDVPEWAASE-----EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTA 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 546 aseyekeitsLQNSfQLRCQQCEDQQREEATRLQGELE----KLRKEWNALETECHSLKRENVLLSSELQRQEKEL---H 618
Cdd:pfam12128 648 ----------LKNA-RLDLRRLFDEKQSEKDKKNKALAerkdSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREArteK 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 619 NSQKQSLELTSDLSILQMS------RKELENQVGSLKEQHLRD--------------SADLKTLLSKAENQAKDVQK--E 676
Cdd:pfam12128 717 QAYWQVVEGALDAQLALLKaaiaarRSGAKAELKALETWYKRDlaslgvdpdviaklKREIRTLERKIERIAVRRQEvlR 796
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 767924277 677 YEKTQ--TVLSE---LKLKFEMTEQEKQSITDELKQCKNNLKLLREK 718
Cdd:pfam12128 797 YFDWYqeTWLQRrprLATQLSNIERAISELQQQLARLIADTKLRRAK 843
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
27-106 |
1.72e-03 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaA and similar proteins; FhaA regulates cell growth and peptidoglycan synthesis by binding to MviN. It may inhibit the late stages of peptidoglycan synthesis. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438720 [Multi-domain] Cd Length: 91 Bit Score: 38.22 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 27 PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTGkfYLQDTKSSNGTFINSQRLsrgseeSPPCEILSGDIIQFG 106
Cdd:cd22668 19 SNIIGRG------SDADFRLPDTGVSRRHAEIRWDGQVA--HLTDLGSTNGTTVNNAPV------TPEWRLADGDVITLG 84
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
324-700 |
1.81e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.65 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 324 KVAEGKQEEIQQKGQAEKKELQHK----------------IDEMEEKEQELQAKIEALQADNdftNERLTALQEKlIVEG 387
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKrarielekkasalkrqLDRESDRNQELQKRIRLLEKRE---AEAEEALREQ-AELN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 388 HLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRN---QVEES 464
Cdd:pfam05557 79 RLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEaeqLRQNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 465 TKQIQVLQAQLQRLH-IDTENLREEKDSEITST-RDELLS---------------------ARDEILL---LHQAAAKVA 518
Cdd:pfam05557 159 EKQQSSLAEAEQRIKeLEFEIQSQEQDSEIVKNsKSELARipelekelerlrehnkhlnenIENKLLLkeeVEDLKRKLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 519 SERDT--DIASLQEELKKVRAELERWRKAASEYEKEITS--LQNSFQLRCQQCEDQQREEATRLQGELEKLRKEWNALET 594
Cdd:pfam05557 239 REEKYreEAATLELEKEKLEQELQSWVKLAQDTGLNLRSpeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 595 ECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDL----SILQMSRKELENQVGSlkEQHLRDSADLKTLLSKAENQA 670
Cdd:pfam05557 319 ELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgyrAILESYDKELTMSNYS--PQLLERIEEAEDMTQKMQAHN 396
|
410 420 430
....*....|....*....|....*....|
gi 767924277 671 KDVQKEYEKTQTVLSELKLKFEMTEQEKQS 700
Cdd:pfam05557 397 EEMEAQLSVAEEELGGYKQQAQTLERELQA 426
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
265-593 |
1.89e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 265 QEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKgqaeKKEL 344
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEK----VKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 345 QHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEkliveghLTKAVEetKLSKENQTRakesdfsdTLSPSKEKssd 424
Cdd:COG1340 77 KEERDELNEKLNELREELDELRKELAELNKAGGSIDK-------LRKEIE--RLEWRQQTE--------VLSPEEEK--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 425 dttdaqmdeqdlnEPLAKVSLLKALLEEERKAyrnqvEESTKQIQVLQAQLQRLHIDTENLREekdsEITSTRDELLSAR 504
Cdd:COG1340 137 -------------ELVEKIKELEKELEKAKKA-----LEKNEKLKELRAELKELRKEAEEIHK----KIKELAEEAQELH 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 505 DEILLLHQAAAKVASERDT---DIASLQEELKKVRAELERWRKAASEYEKEITSLqnsfqlrcqqcedQQREEATRLQGE 581
Cdd:COG1340 195 EEMIELYKEADELRKEADElhkEIVEAQEKADELHEEIIELQKELRELRKELKKL-------------RKKQRALKREKE 261
|
330
....*....|..
gi 767924277 582 LEKLRKEWNALE 593
Cdd:COG1340 262 KEELEEKAEEIF 273
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
255-541 |
1.94e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 255 TAKESLRRVLQEKIEVVRKLSEvERSLSNTEDECTHLKEMNERTQ--------------EELRELANKYNGavnEIKDLS 320
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKLKkynleelekkaeeyEKLKEKLIKLKG---EIKSLK 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 321 DKLKvaegKQEEIQQKgqaeKKELQHKIDEMEEKEQELQAKIEALQ-ADNDFTNERLTALQEKLIVEGHLTKAVEETKLS 399
Cdd:PRK03918 546 KELE----KLEELKKK----LAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKELERE 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 400 KENQTRAKEsdfsdTLSPSKEKSSDDTTDAQMDEQDLNEplakvsLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLh 479
Cdd:PRK03918 618 EKELKKLEE-----ELDKAFEELAETEKRLEELRKELEE------LEKKYSEEEYEELREEYLELSRELAGLRAELEEL- 685
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767924277 480 idtENLREEKDS---EITSTRDELLSARDEILLLHQAAAKVaserdtdiASLQEELKKVRAELER 541
Cdd:PRK03918 686 ---EKRREEIKKtleKLKEELEEREKAKKELEKLEKALERV--------EELREKVKKYKALLKE 739
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
520-721 |
2.01e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 520 ERDT--DIASLQEELKkvraELERWRKAASEYEKEITSLQnsfQLRcqqcedQQREEATRLQGELEKLRKEWNALETECH 597
Cdd:COG4913 220 EPDTfeAADALVEHFD----DLERAHEALEDAREQIELLE---PIR------ELAERYAAARERLAELEYLRAALRLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 598 SLKREnvLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQvgsLKEQHLRDSADLKTLLSKAENQAKDVQKEY 677
Cdd:COG4913 287 QRRLE--LLEAELEELRAELARLEAELERLEARLDALREELDELEAQ---IRGNGGDRLEQLEREIERLERELEERERRR 361
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767924277 678 EKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLREKGNN 721
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
417-640 |
2.36e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 417 PSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREE-------- 488
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgeraral 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 489 -KDSEITSTRDELLSARDEILLLHQAAA-KVASERDTDIAslqEELKKVRAELERWRKAASEYEKEITSLQnsfqlrcqq 566
Cdd:COG3883 96 yRSGGSVSYLDVLLGSESFSDFLDRLSAlSKIADADADLL---EELKADKAELEAKKAELEAKLAELEALK--------- 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767924277 567 ceDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKE 640
Cdd:COG3883 164 --AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
450-609 |
2.48e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 450 LEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDseitstrdELlsaRDEILllhqaaakvasERDTDIASLQ 529
Cdd:COG2433 390 LPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE--------EL---EAELE-----------EKDERIERLE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 530 EELKKVRAElerwRKAASEYEKEITSLQNsfqlrcqqcedqqreEATRLQGELEKLRKEWNALETECHSLKRENVLLSSE 609
Cdd:COG2433 448 RELSEARSE----ERREIRKDREISRLDR---------------EIERLERELEEERERIEELKRKLERLKELWKLEHSG 508
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
345-602 |
2.73e-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: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 345 QHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETK--LSKENQTRAKESDFSDTlspskEKS 422
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERL-----DAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 423 SDDTTDAQMDEQDLNEPLAKvsllkalLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLS 502
Cdd:COG4913 684 SDDLAALEEQLEELEAELEE-------LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 503 ARDEILLLHQAAAKVASERD---TDIASLQEELKKVRAE-LERWRKAASEYEKEITSLqNSFQlrcQQCEDQQREEATRL 578
Cdd:COG4913 757 AALGDAVERELRENLEERIDalrARLNRAEEELERAMRAfNREWPAETADLDADLESL-PEYL---ALLDRLEEDGLPEY 832
|
250 260
....*....|....*....|....*.
gi 767924277 579 QGELEKLRKEW--NALETECHSLKRE 602
Cdd:COG4913 833 EERFKELLNENsiEFVADLLSKLRRA 858
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
265-658 |
2.83e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.04 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 265 QEKIEVVRKLSEVERS----LSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGkqEEIQQKGQAE 340
Cdd:PLN02939 45 QQKKKRGKNIAPKQRSsnskLQSNTDENGQLENTSLRTVMELPQKSTSSDDDHNRASMQRDEAIAAID--NEQQTNSKDG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 341 KKELQHKIDEMEEKEQELQAKIEALQADNDFTNERL-TALQEKLIVEGHLTkaVEETKLSkENQTRAKESdfsdtlspSK 419
Cdd:PLN02939 123 EQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLeKILTEKEALQGKIN--ILEMRLS-ETDARIKLA--------AQ 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 420 EKSSDDTTDAQMDEqdlneplakvslLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKdSEITSTRDE 499
Cdd:PLN02939 192 EKIHVEILEEQLEK------------LRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAEL-IEVAETEER 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 500 LlsardeilllhqaaAKVASERDTDIASLQE-ELKKVRAELERWRKAASEYE---KEITSLQNSFQlrcqqCEDQQREEA 575
Cdd:PLN02939 259 V--------------FKLEKERSLLDASLRElESKFIVAQEDVSKLSPLQYDcwwEKVENLQDLLD-----RATNQVEKA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 576 TRLQGELEKLRKEWNALETechSLKRENVL-LSSE----LQRQEKELHNS-QKQSLELTSDLSILQMSRKELENQVGSLK 649
Cdd:PLN02939 320 ALVLDQNQDLRDKVDKLEA---SLKEANVSkFSSYkvelLQQKLKLLEERlQASDHEIHSYIQLYQESIKEFQDTLSKLK 396
|
....*....
gi 767924277 650 EQHLRDSAD 658
Cdd:PLN02939 397 EESKKRSLE 405
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
258-367 |
3.11e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 258 ESLRRVLQEKI-EVVRKLSEVERSLSNTEDEcthLKEMNERTQEELRELANKYNGAVNE--------IKDLSD--KLKVA 326
Cdd:PRK00409 526 EELERELEQKAeEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLEEAEKEAQQAIKEakkeadeiIKELRQlqKGGYA 602
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 767924277 327 EGKQEEIQQKgqaeKKELQHKIDEMEEKEQELQAKIEALQA 367
Cdd:PRK00409 603 SVKAHELIEA----RKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
255-562 |
3.13e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 255 TAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQ 334
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 335 ---QKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKENQTRAKESDF 411
Cdd:COG4372 115 eelEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 412 SDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDS 491
Cdd:COG4372 195 NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767924277 492 EITSTRDELLSARDEILLLHQAAAKVASERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNSFQL 562
Cdd:COG4372 275 EEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQL 345
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
260-622 |
3.28e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.65 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 260 LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRElankyngavnEIKDLSDKLKVAEGKQEEIQQKgqa 339
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELES----------RVAELKEELRQSREKHEELEEK--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 340 eKKELQHKIDEM-EEKEQELQAKIEALQADNDFTNERLTALQEKLIVEGHLTKAVEETKLSKeNQTRAKESDfsdtlsps 418
Cdd:pfam07888 103 -YKELSASSEELsEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAG-AQRKEEEAE-------- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 419 kekSSDDTTDAQMDEQDLNEPLAKVSLLKALLeEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREekdsEITSTRD 498
Cdd:pfam07888 173 ---RKQLQAKLQQTEEELRSLSKEFQELRNSL-AQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE----ELRSLQE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 499 ELLSARDEILLLHQAAAKVASERDTDIASL-QEELKKVRAELE------RWRKAASEYEKEITSLQNSFQLRCQQCEdQQ 571
Cdd:pfam07888 245 RLNASERKVEGLGEELSSMAAQRDRTQAELhQARLQAAQLTLQladaslALREGRARWAQERETLQQSAEADKDRIE-KL 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 767924277 572 REEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQK 622
Cdd:pfam07888 324 SAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLR 374
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
302-430 |
3.37e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 302 LRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQE 381
Cdd:COG3883 124 LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 767924277 382 KLIVEGHLTKAVEETKLSKENQTRAKESDFSDTLSPSKEKSSDDTTDAQ 430
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
165-395 |
3.39e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.83 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 165 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEasdtsWQALIDEDRLLSR----LEVMGNQLQACSKNQT--EDSL 238
Cdd:COG0497 172 KELEELRADEAERARELDLLRFQLEELEAAALQPGE-----EEELEEERRRLSNaeklREALQEALEALSGGEGgaLDLL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 239 RKELIALQEDKHnYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERtQEELRELANKYNGAVNEIKD 318
Cdd:COG0497 247 GQALRALERLAE-YDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEER-LALLRRLARKYGVTVEELLA 324
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767924277 319 LSDKLkvaegkqeeiqqkgQAEKKELQHKIDEMEEKEQELQAKIEALQAdndfTNERLTALQEKLIVEghLTKAVEE 395
Cdd:COG0497 325 YAEEL--------------RAELAELENSDERLEELEAELAEAEAELLE----AAEKLSAARKKAAKK--LEKAVTA 381
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
174-363 |
3.87e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 39.12 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 174 LQEALHREQMLEQKLATLQRLLaitqeasdtswQALIDEDRLLSRLEVmgNQLQACSKNQTEDSLRKELIAlqedKHNYE 253
Cdd:pfam15619 6 LSARLHKIKELQNELAELQSKL-----------EELRKENRLLKRLQK--RQEKALGKYEGTESELPQLIA----RHNEE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 254 T-TAKESLRRvLQEKIEVV-RKLSEVERSLSNTEDECTHL------KEMNERT--QEELRELANKYNGAVNEIKDLSDKL 323
Cdd:pfam15619 69 VrVLRERLRR-LQEKERDLeRKLKEKEAELLRLRDQLKRLeklsedKNLAEREelQKKLEQLEAKLEDKDEKIQDLERKL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767924277 324 KVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIE 363
Cdd:pfam15619 148 ELENKSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLK 187
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
210-383 |
3.93e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.59 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 210 IDEDRLLSRLEVMGNQLQACSKNQTE---DSLRKELIALQED-KHNYETTAKEslrrvLQEKIEVVRKLSEVERSLsnte 285
Cdd:PRK04778 249 LDHLDIEKEIQDLKEQIDENLALLEEldlDEAEEKNEEIQERiDQLYDILERE-----VKARKYVEKNSDTLPDFL---- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 286 decTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKG----------QAEKKELQHKIDEME 352
Cdd:PRK04778 320 ---EHAKEQNKELKEEIDRVKQSYtlnESELESVRQLEKQLESLEKQYDEITERIaeqeiayselQEELEEILKQLEEIE 396
|
170 180 190
....*....|....*....|....*....|.
gi 767924277 353 EKEQELQAKIEALQADNDFTNERLTALQEKL 383
Cdd:PRK04778 397 KEQEKLSEMLQGLRKDELEAREKLERYRNKL 427
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
481-722 |
4.64e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 481 DTENLREEKDSEITSTRDELLSARDEILLLHQAAAKVaSERDTDIASLQEELKKVRAELERWRKAASEYEKEITSLQNsf 560
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKL-EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE-- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 561 QLRCQQCEDQQREEATRLQGELEKLRKEWNALETECHSLKRENVLLSSELQRQEKELHNSQKQSLELTSD---LSILQMS 637
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKeerLEELKKK 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 638 RKELENQVGSLKEQHlRDSADLKTLLSKAENQAKdvqkeyEKTQTVLSELKLKFEMTEQEKQSITDELKQCKNNLKLLRE 717
Cdd:PRK03918 347 LKELEKRLEELEERH-ELYEEAKAKKEELERLKK------RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
....*
gi 767924277 718 KGNNK 722
Cdd:PRK03918 420 EIKEL 424
|
|
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
450-539 |
5.33e-03 |
|
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.
Pssm-ID: 462015 [Multi-domain] Cd Length: 198 Bit Score: 38.83 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 450 LEEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLRE---EKDSEITSTRDEL--LSARDEILLLHQAAAKVASERDTD 524
Cdd:pfam06818 50 KEEQIQELEDSLRSKTLELEVCENELQRKKNEAELLREkvgKLEEEVSGLREALsdVSPSGYESVYESDEAKEQRQEEAD 129
|
90
....*....|....*
gi 767924277 525 IASLQEELKKVRAEL 539
Cdd:pfam06818 130 LGSLRREVERLRAEL 144
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
329-684 |
5.46e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 329 KQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALqadndftNERLTALQEKLIVEGHLTKAVEETKLSKENQtrake 408
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQL-------CEEKNALQEQLQAETELCAEAEEMRARLAAR----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 409 sdfsdtlspskekssddttdaqmdEQDLNEPLAKvslLKALLEEERKAYRNQVEESTK---QIQVLQAQLQrlhiDTENL 485
Cdd:pfam01576 70 ------------------------KQELEEILHE---LESRLEEEEERSQQLQNEKKKmqqHIQDLEEQLD----EEEAA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 486 REEKDSEITSTRDELLSARDEILLLHQAAAKVASERDTdiasLQEELkkvrAELERWRKAASEYEKEITSLQNSFQLRCQ 565
Cdd:pfam01576 119 RQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKL----LEERI----SEFTSNLAEEEEKAKSLSKLKNKHEAMIS 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 566 QCEDQ-QREEATRLqgELEKLRKEWNALETECHS----LKRENVLLSSELQRQEKELHNSQKQSLELTSDLSILQMSRKE 640
Cdd:pfam01576 191 DLEERlKKEEKGRQ--ELEKAKRKLEGESTDLQEqiaeLQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRE 268
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 767924277 641 LENQVGSLKEqhlrDSADLKTLLSKAENQAKDVQKEYEKTQTVL 684
Cdd:pfam01576 269 LEAQISELQE----DLESERAARNKAEKQRRDLGEELEALKTEL 308
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
52-106 |
5.71e-03 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein kinase DUN1 and similar proteins; DUN1 is a protein kinase that controls the DNA damage response in yeast. It phosphorylates SML1 on serine residues and cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438735 [Multi-domain] Cd Length: 96 Bit Score: 36.70 E-value: 5.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767924277 52 SRNHALVWFDHKTGKFYLQ-----------DTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFG 106
Cdd:cd22683 28 SRSCDLVLSDPSISRFHAElrleqnginviDNNSANGTFINGKRIKGKT-----YILKNGDIIVFG 88
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
165-415 |
6.17e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 165 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWqALIDEDRLLSRLEVMGNQLQACSKNQTE-DSLRKELI 243
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-DEIDVASAEREIAELEAELERLDASSDDlAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 244 ALQEDkhnyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLK----EMNERTQEELRELANKYNGAVNEIkdl 319
Cdd:COG4913 696 ELEAE-----------LEELEEELDELKGEIGRLEKELEQAEEELDELQdrleAAEDLARLELRALLEERFAAALGD--- 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 320 sdklKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKL--IVEGHLTKAVEETK 397
Cdd:COG4913 762 ----AVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLdrLEEDGLPEYEERFK 837
|
250
....*....|....*...
gi 767924277 398 LSKENQTRAKESDFSDTL 415
Cdd:COG4913 838 ELLNENSIEFVADLLSKL 855
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
451-682 |
6.69e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 451 EEERKAYRNQVEESTKQIQVLQAQLQRLhidtenlreekDSEITSTRDELLSARDEILLLHQAAAKVASErdtdIASLQE 530
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDAL-----------QAELEELNEEYNELQAELEALQAEIDKLQAE----IAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 531 ELKKVRAELERWRKAASEYEKEITSLQ-----NSFQ------LRCQQCEDQQREE---ATRLQGELEKLRKEWNALETEC 596
Cdd:COG3883 80 EIEERREELGERARALYRSGGSVSYLDvllgsESFSdfldrlSALSKIADADADLleeLKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 597 HSLKRENVLLSSELQRQEKELhnsQKQSLELTSDLSILQMSRKELENQVGSLKEQHLRDSADLKTLLSKAENQAKDVQKE 676
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQ---EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
....*.
gi 767924277 677 YEKTQT 682
Cdd:COG3883 237 AAAAAA 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
236-383 |
6.88e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.75 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 236 DSLRKELIALQEDKhnyeTTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKE--MNERTQEELRELANKYNGAV 313
Cdd:COG1579 27 KELPAELAELEDEL----AALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNNKEYEALQKEIESLK 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 314 NEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQHKIDEMEEKEQELQAKIEALQADNDFTNERLTALQEKL 383
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
374-716 |
9.30e-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: 39.11 E-value: 9.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 374 ERLTALQEKLIVEGHLTKAVEETKLSK---ENQTRAKESDFSDtLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALL 450
Cdd:pfam07888 42 ERAELLQAQEAANRQREKEKERYKRDReqwERQRRELESRVAE-LKEELRQSREKHEELEEKYKELSASSEELSEEKDAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 451 EEERKAYRNQVEESTKQIQVLQAQLQRLHIDTENLREEKDSEITSTRDELLSARDEILLLHQAaakvaserdtdiaslQE 530
Cdd:pfam07888 121 LAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQT---------------EE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 531 ELKKVRAELERWRKAASEYEKEITSLQNSFQLRCQQCEDQQREEATR--LQGELEKLRKEWNALETECHSLKRENVLLSS 608
Cdd:pfam07888 186 ELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENeaLLEELRSLQERLNASERKVEGLGEELSSMAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924277 609 ELQRQEKELHNSQKQSLELTSDLSILQMSRKELENQvGSLKEQHLRDSADLKTllSKAENQAKDVQKEYEKTQTVLSE-L 687
Cdd:pfam07888 266 QRDRTQAELHQARLQAAQLTLQLADASLALREGRAR-WAQERETLQQSAEADK--DRIEKLSAELQRLEERLQEERMErE 342
|
330 340
....*....|....*....|....*....
gi 767924277 688 KLKFEMTeQEKQSITDELKQCKNNLKLLR 716
Cdd:pfam07888 343 KLEVELG-REKDCNRVQLSESRRELQELK 370
|
|
| VI_FHA |
TIGR03354 |
type VI secretion system FHA domain protein; Members of this protein family are FHA ... |
49-106 |
9.96e-03 |
|
type VI secretion system FHA domain protein; Members of this protein family are FHA (forkhead-associated) domain-containing proteins that are part of type VI secretion loci in a considerable number of bacteria, most of which are known pathogens. Species include Pseudomonas aeruginosa PAO1, Aeromonas hydrophila, Yersinia pestis, Burkholderia mallei, etc. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274537 [Multi-domain] Cd Length: 396 Bit Score: 38.89 E-value: 9.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767924277 49 KVLSRNHALV-WFDhktGKFYLQDTkSSNGTFINS--QRLSRGSEesppcEILS-GDIIQFG 106
Cdd:TIGR03354 43 RHVSGRHARIrYRD---GAYLLTDL-STNGVFLNGsgSPLGRGNP-----VRLEqGDRLRLG 95
|
|
| |
