|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
3-130 |
1.30e-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: 254.11 E-value: 1.30e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 3 SALAIFTCRPNSHPFQERHVYLDEPIKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHktSKFYLQDTKSSNGTFINS 82
Cdd:cd22679 1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 568989155 83 QRLSRGSEESPPCEILSGDIIQFGVDVTENTRKVTHGCIVSTIKLFLP 130
Cdd:cd22679 79 QRLSKGSEESEPRELHSGDIVQFGVDVVENSRKVTHGCIVATVTLFLP 126
|
|
| CC1_SLMAP |
cd21911 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal ... |
163-225 |
2.05e-26 |
|
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal membrane-associated protein (SLMAP), also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. SLMAP contains an N-terminal FHA domain followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409287 [Multi-domain] Cd Length: 63 Bit Score: 102.38 E-value: 2.05e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568989155 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQ 225
Cdd:cd21911 1 QELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQLS 63
|
|
| FHA_DMA-like |
cd22692 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest ... |
27-108 |
1.27e-17 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest protein 1 (DMA1), 2 (DMA2) and similar proteins; DMA1 (also known as checkpoint forkhead associated with RING domains-containing protein 1, or CHF1) and DMA2 (also known as checkpoint forkhead associated with RING domains-containing protein 2, or CHF2) are E3 ubiquitin-protein ligases which function in cell cycle retarding in conjunction with the UBC4 and UBC13/MMS2 complex, two E2 ubiquitin conjugating enzymes. They are involved in nutritional control of the cell cycle and required for proper spindle positioning, likely regulating septin ring deposition at the bud neck. DMA1 targets the degradation of G1 cyclin PCL1. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438744 [Multi-domain] Cd Length: 139 Bit Score: 79.92 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 27 PIKIGRSVARCRPAQNNAT-FDCKVLSRNHALVWfdHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQF 105
Cdd:cd22692 38 QIHIGRYTERVRQAIYHPVvFKSKVVSRTHGCIK--VDEGNWYIKDVKSSSGTFLNHQRLSPASRTSKPYPLRDGDILQL 115
|
...
gi 568989155 106 GVD 108
Cdd:cd22692 116 GMD 118
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
163-774 |
2.19e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 83.95 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSlrKELIA 242
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL--EELEA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 243 LQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKY-NGAVNEIKDLSDKL 321
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEEL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 322 KVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDDFLPKINGSTEKEKLMVQ 401
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVL 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 402 GHLTKVVEESKLSKE---------------NQAKA-----KESDLS-------DTLSPSKEKSSDDTTDAQMDEQ----- 449
Cdd:TIGR02168 526 SELISVDEGYEAAIEaalggrlqavvvenlNAAKKaiaflKQNELGrvtflplDSIKGTEIQGNDREILKNIEGFlgvak 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 450 DLNEPLAKVSLLKDDLQG--------------------------------------TQSETEAKQDIQHLRKELVEAQEL 491
Cdd:TIGR02168 606 DLVKFDPKLRKALSYLLGgvlvvddldnalelakklrpgyrivtldgdlvrpggviTGGSAKTNSSILERRREIEELEEK 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 492 ARTSKQKCFELQALL---EEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDT---EISSTRDKLLSAQDEILL 565
Cdd:TIGR02168 686 IEELEEKIAELEKALaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQleeRIAQLSKELTELEAEIEE 765
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 566 LRQA---AAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSF---QLRCQQCEDQQREEATRLQ---- 635
Cdd:TIGR02168 766 LEERleeAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATERRLEdlee 845
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 636 ------GELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHl 709
Cdd:TIGR02168 846 qieelsEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL- 924
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568989155 710 rdaADLKTLLSKAENQAKDVQkeyektQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 774
Cdd:TIGR02168 925 ---AQLELRLEGLEVRIDNLQ------ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| FHA_VPS64-like |
cd22695 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ... |
6-126 |
4.58e-15 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 64 (VPS64) and similar proteins; This subfamily includes VPS64 (also called factor arrest protein 9 or FAR9) and factor arrest protein 10 (FAR10), which participate in the control of the re-entry into the cell cycle following pheromone treatment. VPS64 is also involved in vacuolar protein sorting. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438747 [Multi-domain] Cd Length: 133 Bit Score: 72.72 E-value: 4.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 6 AIFTCRPNSHPFQERHV---YLDEPIKIGRSVARCRPAQN---------------NATFDCKVLSRNHALVWFDHKTSKF 67
Cdd:cd22695 2 HILVLKSLNATFETKFLvvpFKPDGLKLGRPVTNSVNKNNsgskrdlfsqqvrpdNGNFDSRVLSRNHACLSCDPTTGKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 568989155 68 YLQDTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFGVDVTEntrKVTHGCIVSTIK 126
Cdd:cd22695 82 YIRDLKSSNGTFVNGQKIRQND-----VELKVGDEVDLGTDIDS---KIEHRKISAYVE 132
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
13-106 |
2.24e-13 |
|
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.
Pssm-ID: 438714 [Multi-domain] Cd Length: 92 Bit Score: 66.53 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 13 NSHPFQERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKtsKFYLQDTKSSNGTFINSQRLsrgseeS 92
Cdd:cd00060 6 DGDGGGREFPLTKGVVTIGRS------PDCDIVLDDPSVSRRHARIEVDGG--GVYLEDLGSTNGTFVNGKRI------T 71
|
90
....*....|....
gi 568989155 93 PPCEILSGDIIQFG 106
Cdd:cd00060 72 PPVPLQDGDVIRLG 85
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
28-105 |
6.19e-13 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 64.13 E-value: 6.19e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568989155 28 IKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhKTSKFYLQDTKSSNGTFINSQRLSRgseesPPCEILSGDIIQF 105
Cdd:pfam00498 1 VTIGRS------PDCDIVLDDPSVSRRHAEIRYD-GGGRFYLEDLGSTNGTFVNGQRLGP-----EPVRLKDGDVIRL 66
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
228-766 |
7.32e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.87 E-value: 7.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 228 SKNQTEDSLRKELIALQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRElANKY 307
Cdd:PTZ00121 1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKK-ADEA 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 308 NGAVNEIKDLSDKLKvaeGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQA-KIEALQADNDFTNERLTALQGIQVDDFL 386
Cdd:PTZ00121 1321 KKKAEEAKKKADAAK---KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaEKKKEEAKKKADAAKKKAEEKKKADEAK 1397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 387 PKINGSTEKEKlmvqgHLTKVVEESKLSKENQAKAKESDLSDTL-SPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDL 465
Cdd:PTZ00121 1398 KKAEEDKKKAD-----ELKKAAAAKKKADEAKKKAEEKKKADEAkKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA 1472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 466 QGTQSETEAKQDIQHLRKELVEAQELARTSKQKCFELQAL-----LEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMEN 540
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAdeakkAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 541 LQEE--KDTEISSTRDKLLSAQDEILLLRQA--AAEAVSERDTDFVSLQEELKKVRAE----LEGWRKAASEYENEIRSL 612
Cdd:PTZ00121 1553 KAEElkKAEEKKKAEEAKKAEEDKNMALRKAeeAKKAEEARIEEVMKLYEEEKKMKAEeakkAEEAKIKAEELKKAEEEK 1632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 613 QSSFQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQM 692
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568989155 693 TRKELEKQVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYE---KTQTVLSELKLKFEMTEQEKQSITDELKQCKD 766
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEekkKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
|
|
| CC1_SLMAP-like |
cd21868 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ... |
167-204 |
1.07e-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: 62.89 E-value: 1.07e-12
10 20 30
....*....|....*....|....*....|....*...
gi 568989155 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21868 1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
190-774 |
1.26e-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: 72.01 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 190 QRLLAITQEASDTSWQALIDE--------DRLLSRLEVMGNQLQACSKNQTE-----DSLRKELIALQEDKHSYETT--- 253
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLRleelreelEELQEELKEAEEELEELTAELQEleeklEELRLEVSELEEEIEELQKElya 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 254 AKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQ 333
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 334 KGQAEKKELQT---KIDEMEEKEQELQAKI-------EALQADNDFTNERLTALQGIQVDDFLPKINGS---TEKEKLMV 400
Cdd:TIGR02168 373 RLEELEEQLETlrsKVAQLELQIASLNNEIerlearlERLEDRRERLQQEIEELLKKLEEAELKELQAEleeLEEELEEL 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 401 QGHLTKVVEESKlSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDE--QDLNEPLAKVSLLKDDLQG----------- 467
Cdd:TIGR02168 453 QEELERLEEALE-ELREELEEAEQALDAAERELAQLQARLDSLERLQEnlEGFSEGVKALLKNQSGLSGilgvlselisv 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 468 --------------------TQSETEAKQDIQHLRK-----------------ELVEAQELARTSKQKCFELQALLEEER 510
Cdd:TIGR02168 532 degyeaaieaalggrlqavvVENLNAAKKAIAFLKQnelgrvtflpldsikgtEIQGNDREILKNIEGFLGVAKDLVKFD 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 511 KAYRNQVE------------ESAKQIQVLQVQLQKL-----------------HMDMENLQEEKDTEISSTRDKLLSAQD 561
Cdd:TIGR02168 612 PKLRKALSyllggvlvvddlDNALELAKKLRPGYRIvtldgdlvrpggvitggSAKTNSSILERRREIEELEEKIEELEE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 562 EILLLRQAAAEAVSERDTdfvsLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQRE------------ 629
Cdd:TIGR02168 692 KIAELEKALAELRKELEE----LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKElteleaeieele 767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 630 ---------------EATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTR 694
Cdd:TIGR02168 768 erleeaeeelaeaeaEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 695 KELEKQVGSLKEQHlrdaADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 774
Cdd:TIGR02168 848 EELSEDIESLAAEI----EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
161-744 |
1.63e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 161 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKEL 240
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 241 IALQEDkhsyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDK 320
Cdd:COG1196 298 ARLEQD-----------IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 321 LKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDDflpkingsTEKEKLMV 400
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL--------AELEEEEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 401 QGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEAKQDIQH 480
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 481 LRKELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQ 560
Cdd:COG1196 519 LRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 561 DEILLLRQAAAEAvSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLqssfqlrcqqcedqqREEATRLQGELEK 640
Cdd:COG1196 599 AAVDLVASDLREA-DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV---------------TLEGEGGSAGGSL 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 641 LKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTLLS 720
Cdd:COG1196 663 TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL 742
|
570 580
....*....|....*....|....
gi 568989155 721 KAENQAKDVQKEYEKTQTVLSELK 744
Cdd:COG1196 743 EEEELLEEEALEELPEPPDLEELE 766
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
52-106 |
2.35e-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: 61.53 E-value: 2.35e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 568989155 52 SRNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQFG 106
Cdd:cd22686 48 SKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPYPLTHGDELKIG 102
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
14-106 |
7.29e-11 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 59.20 E-value: 7.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 14 SHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktSKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716 8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
|
90
....*....|....
gi 568989155 93 pPCEILSGDIIQFG 106
Cdd:COG1716 75 -PAPLRDGDVIRLG 87
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
235-766 |
1.10e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.96 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 235 SLRKELIALQEDKHSYETTAKE--SLRRVLQEKIEVVRKLSEVERSLsntEDECTHLKEMNERTQEELRELANKYNGAVN 312
Cdd:TIGR04523 170 ELENELNLLEKEKLNIQKNIDKikNKLLKLELLLSNLKKKIQKNKSL---ESQISELKKQNNQLKDNIEKKQQEINEKTT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 313 EIKDLSDKLKVAEGKQEEIQQKGQAEKKELQT---KIDEMEEKEQELQAKIEAL--QADNDFTNERLTALQGIQVDdflp 387
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLnnQKEQDWNKELKSELKNQEKK---- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 388 kingstekeklmvqghltKVVEESKLSKENQakaKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQG 467
Cdd:TIGR04523 323 ------------------LEEIQNQISQNNK---IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 468 TQSETEA-KQDIQHLRKELVEAQELARTSKQKCFELQA---LLEEERKAYRNQVEESAKQIQvlqvqlqklhmDMENLQE 543
Cdd:TIGR04523 382 YKQEIKNlESQINDLESKIQNQEKLNQQKDEQIKKLQQekeLLEKEIERLKETIIKNNSEIK-----------DLTNQDS 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 544 EKDTEISSTRDKLLSAQDEILLLRQAaaeaVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSL---QSSFQLRC 620
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVLSRS----INKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLtkkISSLKEKI 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 621 QQCEdqqrEEATRLQGELEKLKKEWDVLETECHSLKKENVLLssELQRQEKELHNSQKqsfELTSDLSILQMTRKELEKQ 700
Cdd:TIGR04523 527 EKLE----SEKKEKESKISDLEDELNKDDFELKKENLEKEID--EKNKEIEELKQTQK---SLKKKQEEKQELIDQKEKE 597
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568989155 701 VGSLKEQhlrdAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKD 766
Cdd:TIGR04523 598 KKDLIKE----IEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
478-774 |
1.36e-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: 62.01 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 478 IQHLRKELVEAQELARTSKQKCFELQALLEEERKAyrnQVEESAKQIQVLQVQLQKLHMDMENLQEEKDtEISSTRDKLL 557
Cdd:TIGR02169 189 LDLIIDEKRQQLERLRREREKAERYQALLKEKREY---EGYELLKEKEALERQKEAIERQLASLEEELE-KLTEEISELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 558 SAQDEIL-LLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSsfQLRCQQCE-DQQREEATRLQ 635
Cdd:TIGR02169 265 KRLEEIEqLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE--RLAKLEAEiDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 636 GELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLR----- 710
Cdd:TIGR02169 343 REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRlseel 422
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568989155 711 -----DAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 774
Cdd:TIGR02169 423 adlnaAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
255-774 |
6.42e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 6.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 255 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNgAVNEIKDLSDKLKVAEGKQEEIQQK 334
Cdd:PRK03918 178 IERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 335 GQAEKKELQTKIDEMEEKEQELQAKIEALQ----------ADNDFTNERLTALQGIQvddflpKINGSTEKEKLMVQGHL 404
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKELKelkekaeeyiKLSEFYEEYLDELREIE------KRLSRLEEEINGIEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 405 TKVveESKLSKENQAKAKESDLSDTLSPSKEKSSD-DTTDAQMDE-------------QDLNEPLAKVSLLKDDLQGTQS 470
Cdd:PRK03918 331 KEL--EEKEERLEELKKKLKELEKRLEELEERHELyEEAKAKKEElerlkkrltgltpEKLEKELEELEKAKEEIEEEIS 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 471 E-TEAKQDIQHLRKELVEAQELARTSKQKCFELQALLEEERKA-----YRNQVEESAKQIQVLQVQLQKLHMDMENLqee 544
Cdd:PRK03918 409 KiTARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKelleeYTAELKRIEKELKEIEEKERKLRKELREL--- 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 545 kdteisstrDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFqlrcqqce 624
Cdd:PRK03918 486 ---------EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL-------- 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 625 dqqrEEATRLQGELEKLKKEWDVLETECHSLKKENVLLS----SELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQ 700
Cdd:PRK03918 549 ----EKLEELKKKLAELEKKLDELEEELAELLKELEELGfesvEELEERLKELEPFYNEYLELKDAEKELEREEKELKKL 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 701 VGSLKEQhLRDAADLKTLLSKAENQAKDVQK------------EYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNL 768
Cdd:PRK03918 625 EEELDKA-FEELAETEKRLEELRKELEELEKkyseeeyeelreEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
....*.
gi 568989155 769 KLLREK 774
Cdd:PRK03918 704 EEREKA 709
|
|
| CC1_T3JAM |
cd21912 |
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ... |
164-204 |
9.76e-09 |
|
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; TRAF3-interacting JNK-activating modulator (T3JAM), also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. The model corresponds to a conserved region that shows high sequence similarity with the first CC (CC1) domain of Sarcolemmal membrane-associated protein (SLMAP), which is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409288 [Multi-domain] Cd Length: 45 Bit Score: 51.58 E-value: 9.76e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 568989155 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21912 5 EILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
267-769 |
1.09e-08 |
|
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: 58.88 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 267 EVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKI 346
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 347 DEMEEKEQE---LQAKIEALQADNDFTNERLTALQGIQVDdfLPKINGSTEKEKLMVQGHLTKVVEE--SKLSKENQAKA 421
Cdd:TIGR04523 117 EQKNKLEVElnkLEKQKKENKKNIDKFLTEIKKKEKELEK--LNNKYNDLKKQKEELENELNLLEKEklNIQKNIDKIKN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 422 KESDLSDTLSPSKEKSSDDTTDaqmdEQDLNEPLAKVSLLKDDLQgtqsetEAKQDIQHLRKELVEAQELARTSKQKCFE 501
Cdd:TIGR04523 195 KLLKLELLLSNLKKKIQKNKSL----ESQISELKKQNNQLKDNIE------KKQQEINEKTTEISNTQTQLNQLKDEQNK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 502 LQALLEEERKayrnQVEESAKQIQVLQVQLQKLHMDMENLQEEKD--------TEISSTRDKLLSAQDEILLLRQAAAE- 572
Cdd:TIGR04523 265 IKKQLSEKQK----ELEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwnkelkSELKNQEKKLEEIQNQISQNNKIISQl 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 573 ---------AVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQrEEATRLQGELEKLKK 643
Cdd:TIGR04523 341 neqisqlkkELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE-KLNQQKDEQIKKLQQ 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 644 EWDVLETECHSLKKENVLLSSE------------------------------------------LQRQEKELHNSQKQSF 681
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEikdltnqdsvkeliiknldntresletqlkvlsrsinkikqnLEQKQKELKSKEKELK 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 682 ELTSDLSILQMTRKELEKQVGSLKEQhlrdAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMteQEKQSITDEL 761
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEK----IEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEI--DEKNKEIEEL 573
|
....*...
gi 568989155 762 KQCKDNLK 769
Cdd:TIGR04523 574 KQTQKSLK 581
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
163-641 |
1.62e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDtswQALIDEDRLLSRLEVMGNQLQAcsKNQTEDSLRKELIA 242
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRR---ELEERLEELEEELAELEEELEE--LEEELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 243 LQEDKHSYETTAKESLRRVL----------QEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVN 312
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLeaeaelaeaeEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 313 EIKDLSDKLKVAEGKQEEIQQK---GQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQvDDFLPKI 389
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEeaeLEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE-ADYEGFL 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 390 NGSTEKEKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKssDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQ 469
Cdd:COG1196 508 EGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE--DDEVAAAAIEYLKAAKAGRATFLPLDKIRAR 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 470 SETEAKQDIQHLRKELVEAQELARTSKQKCFELQALLEEER--KAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDT 547
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTlvAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 548 EISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQCE--- 624
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLeee 745
|
490 500 510
....*....|....*....|....*....|....
gi 568989155 625 -----------------DQQREEATRLQGELEKL 641
Cdd:COG1196 746 elleeealeelpeppdlEELERELERLEREIEAL 779
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
14-110 |
1.71e-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: 53.00 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 14 SHPFQERHV---YLDEPIKIGRSvARCRPAQNNATfdckvLSRNHALVW---FDHKT-SKFYLQDTkSSNGTFINSQRLS 86
Cdd:cd22670 7 SSPGSTDIVlpiYKNQVITIGRS-PSCDIVINDPF-----VSRTHCRIYsvqFDESSaPLVYVEDL-SSNGTYLNGKLIG 79
|
90 100
....*....|....*....|....*
gi 568989155 87 RGseespPCEILS-GDIIQFGVDVT 110
Cdd:cd22670 80 RN-----NTVLLSdGDVIEIAHSAT 99
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
298-774 |
1.73e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 298 EELRELANKYNGAVNEIkdLSDKLKVAEGKQEEIQQKgqaEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTAL 377
Cdd:PRK02224 165 EEYRERASDARLGVERV--LSDQRGSLDQLKAQIEEK---EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 378 QGIQvddflpkingSTEKEKLMVQGHLTKVVEESKLSKENQAKAKEsDLSDTLSPSKEKSSD--DTTDAQMDEQDLNEPL 455
Cdd:PRK02224 240 DEVL----------EEHEERREELETLEAEIEDLRETIAETERERE-ELAEEVRDLRERLEEleEERDDLLAEAGLDDAD 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 456 AK-VSLLKDDLQGTQSET-----EAKQDIQHLRKELVEAQELARTskqkcfelqalLEEERKAYRNQVEESakqiqvlqv 529
Cdd:PRK02224 309 AEaVEARREELEDRDEELrdrleECRVAAQAHNEEAESLREDADD-----------LEERAEELREEAAEL--------- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 530 qlqklhmdmenlqeekDTEISSTRDKLLSAQDEILLLR---QAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYE 606
Cdd:PRK02224 369 ----------------ESELEEAREAVEDRREEIEELEeeiEELRERFGDAPVDLGNAEDFLEELREERDELREREAELE 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 607 NEIRSLQSSF----QLR----CQQCE------------DQQREEATRLQGELEKLKKEWDVLETECHSLKkenvllssEL 666
Cdd:PRK02224 433 ATLRTARERVeeaeALLeagkCPECGqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAE--------DL 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 667 QRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQhlrdAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLK 746
Cdd:PRK02224 505 VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER----AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSK 580
|
490 500 510
....*....|....*....|....*....|....
gi 568989155 747 FEMTEQEKQS------ITDELKQCKDNLKLLREK 774
Cdd:PRK02224 581 LAELKERIESlerirtLLAAIADAEDEIERLREK 614
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
542-774 |
1.84e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 542 QEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDtdfvSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQL--- 618
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELE----ELEAELAELEAELEELRLELEELELELEEAQAEEYElla 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 619 ---RCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRK 695
Cdd:COG1196 296 elaRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 696 ELEKQVGSLKEQHL---RDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLR 772
Cdd:COG1196 376 EAEEELEELAEELLealRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
..
gi 568989155 773 EK 774
Cdd:COG1196 456 EE 457
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
250-756 |
3.99e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 3.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 250 YETTAKES--LRRVLQEKIEVVRKL----SEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLsDKLKV 323
Cdd:PRK03918 160 YENAYKNLgeVIKEIKRRIERLEKFikrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-EELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 324 AEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQadndftnerltalqgiQVDDFLPKINGSTEKEKLMVQGH 403
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE----------------EKVKELKELKEKAEEYIKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 404 LTKVVEESKLSKEnqakakESDLSDTLSPSKEKSSddttDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEAKQDIQHLRK 483
Cdd:PRK03918 303 EEYLDELREIEKR------LSRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 484 ELVE-AQELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTeiSSTRDKLLSAQDE 562
Cdd:PRK03918 373 ELERlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGK--CPVCGRELTEEHR 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 563 ILLLRQAAAE------AVSERDTDFVSLQEELKKVRAELEGWRKAASEYE--NEIRSLQSSFQLRCQQCEDQQREEATRL 634
Cdd:PRK03918 451 KELLEEYTAElkriekELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAEEYEKL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 635 QGELEKLKKEWDVLETECHS---LKKENVLLSSELQRQEKELHNSQKQSFELT-SDLSILQMTRKELE---------KQV 701
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKleeLKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEpfyneylelKDA 610
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 568989155 702 GSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 756
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR 665
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
212-773 |
4.44e-08 |
|
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: 56.98 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 212 RLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHSYETTAKESLRRVLQEKIEvvrkLSEVERSlSNTEDECTHLKE 291
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE----LDGFERG-PFSERQIKNFHT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 292 MNERTQEELRELANKyngavnEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQadndftn 371
Cdd:TIGR00606 398 LVIERQEDEAKTAAQ------LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ------- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 372 erltalqgiqvddflpKINGSTEKeklmvqghLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDL 451
Cdd:TIGR00606 465 ----------------QLEGSSDR--------ILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKL 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 452 NEPLAKVSLLKDDLQGTQSETEAKQDIQHLRKELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQL 531
Cdd:TIGR00606 521 DQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKEL 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 532 QKLhmdmENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEavserDTDFVSLQEELKKVRAELEGWRKAASEYENEIRS 611
Cdd:TIGR00606 601 ASL----EQNKNHINNELESKEEQLSSYEDKLFDVCGSQDE-----ESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQ 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 612 LQSSFQLRCQQC------EDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLL-------SSELQRQEKELHNSQK 678
Cdd:TIGR00606 672 LTDENQSCCPVCqrvfqtEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglapgrQSIIDLKEKEIPELRN 751
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 679 QSFELTSDLSILQMTRKELEKQVGSL--KEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVL--SELKLKFEMTEQEK 754
Cdd:TIGR00606 752 KLQKVNRDIQRLKNDIEEQETLLGTImpEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLqgSDLDRTVQQVNQEK 831
|
570
....*....|....*....
gi 568989155 755 QSITDELKQCKDNLKLLRE 773
Cdd:TIGR00606 832 QEKQHELDTVVSKIELNRK 850
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
28-85 |
4.88e-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: 4.88e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568989155 28 IKIGRSvarcrPAQNNATFDCKVLSRNHALVWFDhKTSKFYLQDTKSSNGTFINSQRL 85
Cdd:smart00240 1 VTIGRS-----SEDCDIQLDGPSISRRHAVIVYD-GGGRFYLIDLGSTNGTFVNGKRI 52
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
466-769 |
5.16e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 466 QGTQSETEAKQDIQHLRKELVEAQELARTSKQKCFELQA---LLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQ 542
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEdlsSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 543 EEKDTEISSTRDKLLSAQDEIlllrqaaaeaVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQ 622
Cdd:TIGR02169 786 ARLSHSRIPEIQAELSKLEEE----------VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 623 CEDQQREEAtRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVG 702
Cdd:TIGR02169 856 IENLNGKKE-ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 703 SLKEQHLRDAADLKTLLS----KAENQAKDVQ------------KEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCkD 766
Cdd:TIGR02169 935 EIEDPKGEDEEIPEEELSledvQAELQRVEEEiralepvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY-E 1013
|
...
gi 568989155 767 NLK 769
Cdd:TIGR02169 1014 KKK 1016
|
|
| FHA_TCF19 |
cd22685 |
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ... |
29-119 |
5.90e-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: 52.03 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 29 KIGRSVARCRPAQNNATFDcKVLSRNHALVWFDHKTS---KFYLQDTkSSNGTFINSQRLSRGSEEsppcEILSGDIIQF 105
Cdd:cd22685 31 RIGRNPEVCDVFLCSSQHP-NLISREHAEIHAERDGNgnwKVLIEDR-STNGTYVNDVRLQDGQRR----ELSDGDTITF 104
|
90
....*....|....*.
gi 568989155 106 G--VDVTENTRKVTHG 119
Cdd:cd22685 105 GhkNGRRVKQWPYQKS 120
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
233-763 |
7.03e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 7.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 233 EDSLRKELIALQEDKhsyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVN 312
Cdd:COG1196 222 LKELEAELLLLKLRE------LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 313 EIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQvddflpkingS 392
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE----------E 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 393 TEKEKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSET 472
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 473 EAKQDIQHLRKELVEAQELARTSKQKCFELQALL-----EEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDT 547
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALaelleELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 548 EISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAE-----LEGWRKAASEYENEIRSLQSSFQLRCQQ 622
Cdd:COG1196 526 VAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGratflPLDKIRARAALAAALARGAIGAAVDLVA 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 623 CEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVG 702
Cdd:COG1196 606 SDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568989155 703 SLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 763
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
162-596 |
1.05e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 162 SQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgNQLQAcsKNQTEDSLRKELI 241
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE---AELAE--AEEELEELAEELL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 242 ALQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKL 321
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 322 KVAEGKQEEIQQ-KGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDDFLPKINGSTEKEKLMV 400
Cdd:COG1196 470 EEAALLEAALAElLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 401 QGH------LTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMD--EQDLNEPLAKVSLLKDDLQGTQSET 472
Cdd:COG1196 550 NIVveddevAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDlvASDLREADARYYVLGDTLLGRTLVA 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 473 EAKQDIQHLRKELVE----------------AQELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLH- 535
Cdd:COG1196 630 ARLEAALRRAVTLAGrlrevtlegeggsaggSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREl 709
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568989155 536 -------MDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELE 596
Cdd:COG1196 710 aeaeeerLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
239-755 |
2.33e-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: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 239 ELIALQEDKHSYETTAK--ESLRRVLQEKIE-----VVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAV 311
Cdd:pfam15921 279 EITGLTEKASSARSQANsiQSQLEIIQEQARnqnsmYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 312 NEIKDLSDKLKVAEGKQEEIQQKGQAE--KKE--------------------------LQTKIDEMEEKEQELQAKIEAL 363
Cdd:pfam15921 359 TEARTERDQFSQESGNLDDQLQKLLADlhKREkelslekeqnkrlwdrdtgnsitidhLRRELDDRNMEVQRLEALLKAM 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 364 QADNDFTNER-LTALQGiqVDDFLPKINGST---EKEKLMvqghLTKVVEESKlSKENQAKAKESDLSDTLSPSKEKS-S 438
Cdd:pfam15921 439 KSECQGQMERqMAAIQG--KNESLEKVSSLTaqlESTKEM----LRKVVEELT-AKKMTLESSERTVSDLTASLQEKErA 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 439 DDTTDAQMDE--QDLNEPLAKVSLLK---DDLQGTQSETEA---------------KQDI--------QHLRKE---LVE 487
Cdd:pfam15921 512 IEATNAEITKlrSRVDLKLQELQHLKnegDHLRNVQTECEAlklqmaekdkvieilRQQIenmtqlvgQHGRTAgamQVE 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 488 AQELARTSKQKCFELQAL--LEEERKAYRNQVEesAKQIQVLQVQLQKLHMDMENLQEEKD---------TEISSTRDKL 556
Cdd:pfam15921 592 KAQLEKEINDRRLELQEFkiLKDKKDAKIRELE--ARVSDLELEKVKLVNAGSERLRAVKDikqerdqllNEVKTSRNEL 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 557 LSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRkaaseyeNEIRSLQSSFQLRCQQCEDQQReEATRLQG 636
Cdd:pfam15921 670 NSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTR-------NTLKSMEGSDGHAMKVAMGMQK-QITAKRG 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 637 ELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVgslkeqhlrdaADLK 716
Cdd:pfam15921 742 QIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKV-----------ANME 810
|
570 580 590
....*....|....*....|....*....|....*....
gi 568989155 717 TLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQ 755
Cdd:pfam15921 811 VALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
246-773 |
2.52e-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: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 246 DKHSYETTAKESLRRVLQEKIEvvrklsEVERSLSNTEDectHLKEMNERTqEELRELANKYNGAVNEIKDLSDKLKVAE 325
Cdd:pfam15921 131 DIRRRESQSQEDLRNQLQNTVH------ELEAAKCLKED---MLEDSNTQI-EQLRKMMLSHEGVLQEIRSILVDFEEAS 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 326 GKQ---------EEIQQKGQAEKK---ELQTKI-----------DEMEEKEQELQAKIEALQADNDFTNERLTALQGIQV 382
Cdd:pfam15921 201 GKKiyehdsmstMHFRSLGSAISKilrELDTEIsylkgrifpveDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEI 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 383 DDFLPKINgSTEKEKLMVQGHLTKVVEESKlskeNQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLK 462
Cdd:pfam15921 281 TGLTEKAS-SARSQANSIQSQLEIIQEQAR----NQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLAN 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 463 DDLqgTQSETEAKQDIQHLRKELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKlHMDMENLQ 542
Cdd:pfam15921 356 SEL--TEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDR-NMEVQRLE 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 543 EEKDTEISSTRDKLlSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRcQQ 622
Cdd:pfam15921 433 ALLKAMKSECQGQM-ERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK-ER 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 623 CEDQQREEATRLQG-------ELEKLKKEWDVL---ETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQM 692
Cdd:pfam15921 511 AIEATNAEITKLRSrvdlklqELQHLKNEGDHLrnvQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQV 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 693 TRKELEKQVG----SLKE-QHLRDAADLKtlLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDN 767
Cdd:pfam15921 591 EKAQLEKEINdrrlELQEfKILKDKKDAK--IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNE 668
|
....*.
gi 568989155 768 LKLLRE 773
Cdd:pfam15921 669 LNSLSE 674
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
237-710 |
4.69e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 237 RKELIALQEDKHSYETTaKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTqEELRELANKYNGAVNEIKD 316
Cdd:PRK03918 282 VKELKELKEKAEEYIKL-SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL-EELKKKLKELEKRLEELEE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 317 LSDKLKVAEGKQEEIQQ----KGQAEKKELQTKIDEMEEKEQELQAKIEALqadndftNERLTALQGIQVDDFLPKINGS 392
Cdd:PRK03918 360 RHELYEEAKAKKEELERlkkrLTGLTPEKLEKELEELEKAKEEIEEEISKI-------TARIGELKKEIKELKKAIEELK 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 393 TEKEKLMVQGHLtkVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEP--LAKVSLLKDDLQGTQS 470
Cdd:PRK03918 433 KAKGKCPVCGRE--LTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEseLIKLKELAEQLKELEE 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 471 ETEaKQDIQHLRKELVEAQELARTSKQKCFELQALLEE--ERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTE 548
Cdd:PRK03918 511 KLK-KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKEleKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEE 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 549 ISSTRDKLLSAQDEILLLRQAAAEaVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQlrcqqcedqqR 628
Cdd:PRK03918 590 LEERLKELEPFYNEYLELKDAEKE-LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS----------E 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 629 EEATRLQGELEKLKKEWDVLETECHSLKK---ENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLK 705
Cdd:PRK03918 659 EEYEELREEYLELSRELAGLRAELEELEKrreEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLK 738
|
....*
gi 568989155 706 EQHLR 710
Cdd:PRK03918 739 ERALS 743
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
336-641 |
4.92e-07 |
|
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: 53.52 E-value: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 336 QAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQgiqvddflpkingsTEKEKLMVQGHLTKVVEESKLSK 415
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLR--------------KELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 416 ENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEA-KQDIQHLRKELVEAQELART 494
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlREALDELRAELTLLNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 495 SKQKCFELQALLEEERKayrnQVEESAKQIQVLQVQLQKLHMDMENLQEEKDtEISSTRDKLLSAQDEILLLRQAAAEAV 574
Cdd:TIGR02168 822 LRERLESLERRIAATER----RLEDLEEQIEELSEDIESLAAEIEELEELIE-ELESELEALLNERASLEEALALLRSEL 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 575 SERDTDFVSLQEELKKVRAELEGWRKAASEY-------ENEIRSLQSSF--------------QLRCQQCEDQQREEATR 633
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLelrleglEVRIDNLQERLseeysltleeaealENKIEDDEEEARRRLKR 976
|
....*...
gi 568989155 634 LQGELEKL 641
Cdd:TIGR02168 977 LENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
256-596 |
6.46e-07 |
|
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: 53.14 E-value: 6.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 256 ESLRRVLQEKIEVVRK-LSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQK 334
Cdd:TIGR02168 683 EEKIEELEEKIAELEKaLAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 335 ---GQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGI---QVDDFLPKING--STEKEKLMVQGHLTK 406
Cdd:TIGR02168 763 ieeLEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEltlLNEEAANLRERleSLERRIAATERRLED 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 407 VVEESKLSKENQAKAKESdlSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEAKqdIQHLRKELV 486
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAE--IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK--RSELRRELE 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 487 EAQELARTSKQKCFELQALLEEERKAYRNQVEESAkqiqvlqvqlqklhMDMENLQEEKDTEISSTRDKLLSAQDEIL-- 564
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL--------------EEAEALENKIEDDEEEARRRLKRLENKIKel 984
|
330 340 350
....*....|....*....|....*....|....*.
gi 568989155 565 ----LLRQAAAEAVSERDTDFVSLQEELKKVRAELE 596
Cdd:TIGR02168 985 gpvnLAAIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
27-106 |
7.88e-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: 48.00 E-value: 7.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 27 PIKIGRSVARcRPAQNNATFDC-----KVLSRNHALVWFDHKTSKFYLQdTKSSNGTFINSQRLSRGseeSPPCEILSGD 101
Cdd:cd22701 18 EVVLGRNSKN-SSSTAADSVDIdlgpsKKISRRHARIFYDFTTQCFELS-VLGRNGVKVDGILVKPG---SPPVPLRSGS 92
|
....*
gi 568989155 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 ... |
245-748 |
9.24e-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: 52.87 E-value: 9.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 245 EDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTH-LKEMNERTQEE---LRELANKYNGAVNEIKDLSDK 320
Cdd:pfam01576 32 EKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEiLHELESRLEEEeerSQQLQNEKKKMQQHIQDLEEQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 321 LKvaegKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGiqvddflpkiNGSTEKEKLMV 400
Cdd:pfam01576 112 LD----EEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTS----------NLAEEEEKAKS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 401 QGHLtKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLA--KVSLLK--DDLQGTQS--ETEA 474
Cdd:pfam01576 178 LSKL-KNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAelRAQLAKkeEELQAALArlEEET 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 475 KQDIQHLRK---------ELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQ--- 542
Cdd:pfam01576 257 AQKNNALKKireleaqisELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKkal 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 543 -EEK---DTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSS--- 615
Cdd:pfam01576 337 eEETrshEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQlqe 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 616 FQLRCQQCEDQQREEA---TRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLsilqm 692
Cdd:pfam01576 417 LQARLSESERQRAELAeklSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRL----- 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 568989155 693 trKELEKQVGSLKEQhlrdaadlktlLSKAENQAKDVQKEYEKTQTVLSELKLKFE 748
Cdd:pfam01576 492 --RQLEDERNSLQEQ-----------LEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-763 |
1.41e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 197 QEASDTSWQALIDEDRLLSRLEVMGNQLQacsknqtedSLRKELIALQEDKHSYETTAKESLRRVLQEKI---EVVRKLS 273
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIE---------EERKRRDKLTEEYAELKEELEDLRAELEEVDKefaETRDELK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 274 EVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLK----VAEGKQEEIQQ-------------KGQ 336
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINeleeEKEDKALEIKKqewkleqlaadlsKYE 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 337 AEKKELQTKIDEMEEKEQELQAKIEAL--QADNDFTNERLTALQGIQVDDFLPKINGST-------EKEKLMVQ----GH 403
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLQRELAEAeaQARASEERVRGGRAVEEVLKASIQGVHGTVaqlgsvgERYATAIEvaagNR 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 404 LTKVVEES--------KLSKE-----------NQAKAKESDLS------------------------------DTLSpsk 434
Cdd:TIGR02169 549 LNNVVVEDdavakeaiELLKRrkagratflplNKMRDERRDLSilsedgvigfavdlvefdpkyepafkyvfgDTLV--- 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 435 eKSSDDTTDAQMD-------EQDLNEP--------LAKVSLLKDDLQGTQSETEAKQDIQHLRKELVEAQELARTSKQKC 499
Cdd:TIGR02169 626 -VEDIEAARRLMGkyrmvtlEGELFEKsgamtggsRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRL 704
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 500 FELQALLEEERKayrnQVEESAKQIQVLQVQLQKLHMDMENLQEekdtEISSTRDKLLSAQDEIlllrQAAAEAVSERDT 579
Cdd:TIGR02169 705 DELSQELSDASR----KIGEIEKEIEQLEQEEEKLKERLEELEE----DLSSLEQEIENVKSEL----KELEARIEELEE 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 580 DFVSLQEELKKVRAEL--EGWRKAASEYEnEIRSLQSSFQLRCQQCEdqqreeatrlqGELEKLKKEWDVLETECHSLKK 657
Cdd:TIGR02169 773 DLHKLEEALNDLEARLshSRIPEIQAELS-KLEEEVSRIEARLREIE-----------QKLNRLTLEKEYLEKEIQELQE 840
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 658 ENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKeqhlRDAADLKTLLSKAENQAKDVQKEYEKTQ 737
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK----KERDELEAQLRELERKIEELEAQIEKKR 916
|
650 660
....*....|....*....|....*.
gi 568989155 738 TVLSELKLKFEMTEQEKQSITDELKQ 763
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPKGE 942
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
26-106 |
1.84e-06 |
|
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438750 [Multi-domain] Cd Length: 93 Bit Score: 46.64 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 26 EPIKIGRSVArcrpaqNNATFDCKVLSRNHALVwfDHKTSKFYLQDTKSSNGTFINSQRLSRGseesppcEILSGDIIQF 105
Cdd:cd22698 21 DEFTIGRSSN------NDIRLNDHSVSRHHARI--VRQGDKCNLTDLGSTNGTFLNGIRVGTH-------ELKHGDRIQL 85
|
.
gi 568989155 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 |
1.88e-06 |
|
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: 47.35 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 25 DEPIKIGRSVArcrpAQNNATFDC-KVLSRNHALVWFDHKTSKFyLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDII 103
Cdd:cd22663 20 GKEVTVGRGLG----VTYQLVSTCpLMISRNHCVLKKNDEGQWT-IKDNKSLNGVWVNGERI----EPLKPYPLNEGDLI 90
|
90
....*....|.
gi 568989155 104 QFGVDVTENTR 114
Cdd:cd22663 91 QLGVPPENKEP 101
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
152-650 |
1.99e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 152 KVAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDtswqaliDEDRLLSRLEVMGNQLQACSKNQ 231
Cdd:COG4717 60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA-------ELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 232 TEDSLRKELIALQEdkhsyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKE-MNERTQEELRELANKYNGA 310
Cdd:COG4717 133 ELEALEAELAELPE--------RLEELEERLEELRELEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 311 VNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQAdndftnerLTALQGIQVDDFLPKIN 390
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALL--------ALLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 391 GSTekekLMVQGHLTKVVEESKLSKENQAKAKESDLsdtLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLkddlqgtqs 470
Cdd:COG4717 277 GVL----FLVLGLLALLFLLLAREKASLGKEAEELQ---ALPALEELEEEELEELLAALGLPPDLSPEELL--------- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 471 etEAKQDIQHLRKELVEAQELARTSKQKCF--ELQALLE----EERKAYRNQVEESAKqiqvlqvqlqklhmdmenlQEE 544
Cdd:COG4717 341 --ELLDRIEELQELLREAEELEEELQLEELeqEIAALLAeagvEDEEELRAALEQAEE-------------------YQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 545 KDTEISSTRDKLLSAQDEILLLRQAAAEAvsERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLrcqqce 624
Cdd:COG4717 400 LKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL------ 471
|
490 500
....*....|....*....|....*.
gi 568989155 625 DQQREEATRLQGELEKLKKEWDVLET 650
Cdd:COG4717 472 AELLQELEELKAELRELAEEWAALKL 497
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
27-117 |
2.08e-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: 46.97 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 27 PIKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLsrgSEESPPCEILSGDIIQFG 106
Cdd:cd22678 24 PLTIGRIQ------RGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESI---SPNGRPVVLSSGDVITLG 94
|
90
....*....|.
gi 568989155 107 vdvTENTRKVT 117
Cdd:cd22678 95 ---SETKILVR 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
501-763 |
3.11e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 501 ELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTd 580
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 581 fvsLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQcEDQQREEATRLQGELEKLKKEWDVLETEchslKKENV 660
Cdd:COG1196 300 ---LEQDIARLEERRRELEERLEELEEELAELEEELEELEEE-LEELEEELEEAEEELEEAEAELAEAEEA----LLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 661 LLSSELQRQE----KELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKT 736
Cdd:COG1196 372 AELAEAEEELeelaEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260
....*....|....*....|....*..
gi 568989155 737 QTVLSELKLKFEMTEQEKQSITDELKQ 763
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAA 478
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
55-108 |
3.37e-06 |
|
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) family; The Cep170 family includes Cep170 and Cep170B. Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438756 [Multi-domain] Cd Length: 102 Bit Score: 46.16 E-value: 3.37e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568989155 55 HALVWFDHKTSKFYLQDTKSSNGTFINSQRLSrgseESPPCEILSGDIIQFGVD 108
Cdd:cd22704 39 HAVITYDQIDNEFKIKDLGSLNGTFVNDSRIP----EQTYITLKLGDSIRFGYD 88
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
229-735 |
5.73e-06 |
|
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: 50.05 E-value: 5.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 229 KNQTEDSLRKeliaLQEDKHSYETTaKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELA---- 304
Cdd:TIGR00606 586 INQTRDRLAK----LNKELASLEQN-KNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAmlag 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 305 --NKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDftnERLTALQGIQv 382
Cdd:TIGR00606 661 atAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRD---EMLGLAPGRQ- 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 383 ddflpKINGSTEKEKLMVQGHLTKVVEEskLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQdLNEPLAKVSLLK 462
Cdd:TIGR00606 737 -----SIIDLKEKEIPELRNKLQKVNRD--IQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMER-FQMELKDVERKI 808
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 463 DDLQGTQSETEAKQDIQHLRKELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHM--DMEN 540
Cdd:TIGR00606 809 AQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRrqQFEE 888
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 541 LQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRC 620
Cdd:TIGR00606 889 QLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK 968
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 621 QQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKenvllSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQ 700
Cdd:TIGR00606 969 DDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQ-----DIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKE 1043
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 568989155 701 VG-----SLKEQHLRDAADLKtLLSKAENQAKDVQKEYEK 735
Cdd:TIGR00606 1044 MGqmqvlQMKQEHQKLEENID-LIKRNHVLALGRQKGYEK 1082
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
163-366 |
6.80e-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: 48.99 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQAcSKNQTEDSLRKELIA 242
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA-ELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 243 LQedKHSYETTAKESLR-RVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKL 321
Cdd:COG4942 113 LY--RLGRQPPLALLLSpEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568989155 322 KVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQAD 366
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
162-752 |
1.78e-05 |
|
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: 48.28 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 162 SQELFQLSQYLQEALHR----EQMLEQKLATLQRLLAITQEASDTSWQALIDEDRllsRLEVMGNQLQACSKNQTEDSLR 237
Cdd:pfam10174 129 AKELFLLRKTLEEMELRietqKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWER---TRRIAEAEMQLGHLEVLLDQKE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 238 KELIALQEDKHS-YETTAKESLRRVLQEKIEVV-RKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIK 315
Cdd:pfam10174 206 KENIHLREELHRrNQLQPDPAKTKALQTVIEMKdTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSK 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 316 DLsdKLKVAEGKQEeiQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQgIQVDDFLPKINgstEK 395
Cdd:pfam10174 286 FM--KNKIDQLKQE--LSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQ-TEVDALRLRLE---EK 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 396 EKLMVQghltKVVEESKLSKENQAKAKE-SDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEA 474
Cdd:pfam10174 358 ESFLNK----KTKQLQDLTEEKSTLAGEiRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSN 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 475 KQdiqhlrkELVEAQELARTSKQKCFE-LQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMenlqEEKDTEISSTR 553
Cdd:pfam10174 434 TD-------TALTTLEEALSEKERIIErLKEQREREDRERLEELESLKKENKDLKEKVSALQPEL----TEKESSLIDLK 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 554 DKLLSAQDEILLLRQAAAE---AVSERDTDFVSLQEELKKVRaELEGWRKAASEYENEIRSLQSSFQLRcqqcedqqREE 630
Cdd:pfam10174 503 EHASSLASSGLKKDSKLKSleiAVEQKKEECSKLENQLKKAH-NAEEAVRTNPEINDRIRLLEQEVARY--------KEE 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 631 ATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQsfeltsdlsiLQMTRKELEKQVGSLKEQHLR 710
Cdd:pfam10174 574 SGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVAN----------IKHGQQEMKKKGAQLLEEARR 643
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 568989155 711 DAADLKTllSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQ 752
Cdd:pfam10174 644 REDNLAD--NSQQLQLEELMGALEKTRQELDATKARLSSTQQ 683
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
52-106 |
2.15e-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: 44.18 E-value: 2.15e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568989155 52 SRNH-ALVWfdHK-TSKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22674 48 SRVHaALVY--HKhLNRVFLIDLGSTHGTFVGGIRL----EPHKPQQLPIDSTLRFG 98
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
584-768 |
2.42e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 584 LQEELKKVRAELEGWRKAASEY---ENEIRSLQSSFQL----RCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLK 656
Cdd:COG1196 194 ILGELERQLEPLERQAEKAERYrelKEELKELEAELLLlklrELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 657 KENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTL---LSKAENQAKDVQKEY 733
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELeeeLEELEEELEEAEEEL 353
|
170 180 190
....*....|....*....|....*....|....*
gi 568989155 734 EKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNL 768
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
51-106 |
2.46e-05 |
|
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also called human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP), is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438729 [Multi-domain] Cd Length: 106 Bit Score: 44.08 E-value: 2.46e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568989155 51 LSRNHALVWF----DHKTSKFYLQDTKSSNGTFINSQRLsrgseesPP---CEILSGDIIQFG 106
Cdd:cd22677 41 ISRYHAVLQYrgdaDDHDGGFYLYDLGSTHGTFLNKQRI-------PPkqyYRLRVGHVLKFG 96
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
289-760 |
2.76e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 289 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKgQAEKKELQTKIDEMEEKEQELQAKIEALQADND 368
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 369 F--TNERLTALQgIQVDDFLPKINGSTEKEKLMVQghltkvVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQM 446
Cdd:COG4717 127 LlpLYQELEALE-AELAELPERLEELEERLEELRE------LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 447 DEQDLNEplaKVSLLKDDLQGTQSETE-AKQDIQHLRKELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQ 525
Cdd:COG4717 200 ELEELQQ---RLAELEEELEEAQEELEeLEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 526 VLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEY 605
Cdd:COG4717 277 GVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 606 ENEIRslqssfQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSF--EL 683
Cdd:COG4717 357 EELEE------ELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeEL 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568989155 684 TSDLSILQMTRKELEKQVgslkEQHLRDAADLKTLLSKAENQAKdvqkeyektqtvLSELKLKFEMTEQEKQSITDE 760
Cdd:COG4717 431 EEELEELEEELEELEEEL----EELREELAELEAELEQLEEDGE------------LAELLQELEELKAELRELAEE 491
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
28-106 |
2.82e-05 |
|
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438732 [Multi-domain] Cd Length: 96 Bit Score: 43.48 E-value: 2.82e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568989155 28 IKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDhkTSKFYLQDTKSSNGTFINSQRlsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22680 23 VSIGRDP------ENVIVIPDPFVSRNHARITVD--SNEIYIEDLGSTNGTFVNDFK-----RIKGPAKLHPNDIIKLG 88
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
251-774 |
3.06e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 251 ETTAKESLRRVLQ-EKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELR-ELANKYNGA--VNEIKDLSDKLKVAE- 325
Cdd:PTZ00121 1114 ARKAEEAKKKAEDaRKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKaEEARKAEDAkkAEAARKAEEVRKAEEl 1193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 326 GKQEEIQQKGQAEKKELQTKIDEMEEKEQElqAKIEALQADNDFTNERLTALQGIQVDDFLPKINGSTEKEKLMVQGHLT 405
Cdd:PTZ00121 1194 RKAEDARKAEAARKAEEERKAEEARKAEDA--KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAA 1271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 406 KVVEESKLSKENQaKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKvsllkddlqgtqSETEAKQDIQHLRKEL 485
Cdd:PTZ00121 1272 IKAEEARKADELK-KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK------------KAEEAKKKADAAKKKA 1338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 486 VEAQELARTSKQKCFELQALL---EEERKAYRNQVEESAKQIQVLQVQLQKLHMDMEnlQEEKDTEISSTRDKLLSAQDE 562
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAeaaEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE--AKKKAEEDKKKADELKKAAAA 1416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 563 ILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQREEATRLQGELEKLK 642
Cdd:PTZ00121 1417 KKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAK 1496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 643 KEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSfeltsdlsilqmTRKELEKQVGSLKEQHLRDAADLKtllsKA 722
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK------------KADEAKKAEEKKKADELKKAEELK----KA 1560
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 568989155 723 ENQAKDVQKEYEKTQTVLSELKLKfEMTEQEKQSITDELKQCKDNLKLLREK 774
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAE-EAKKAEEARIEEVMKLYEEEKKMKAEE 1611
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
255-658 |
3.11e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 255 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQK 334
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 335 GQAEKKELQTKIDEMEEKEQ---ELQAKIEALQADNDftnerltalqgiqvDDFLPKINGSTEKeklmvqghltkvvees 411
Cdd:TIGR02169 753 IENVKSELKELEARIEELEEdlhKLEEALNDLEARLS--------------HSRIPEIQAELSK---------------- 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 412 klsKENQAKAKESDLSDTlspskekssddttdaqmdEQDLNEPLAKVSLLKDDLQGTQSETEakqDIQHLRKELVEAQEL 491
Cdd:TIGR02169 803 ---LEEEVSRIEARLREI------------------EQKLNRLTLEKEYLEKEIQELQEQRI---DLKEQIKSIEKEIEN 858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 492 ARTSKQKcfelqalLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDtEISSTRDKLLSAQDEILLLRQAAA 571
Cdd:TIGR02169 859 LNGKKEE-------LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE-ELEAQIEKKRKRLSELKAKLEALE 930
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 572 EAVSERDTDFVSLQEE------LKKVRAELEgwrkaasEYENEIRSLQSSFQLRCQQCEDQQREEaTRLQGELEKLKKEW 645
Cdd:TIGR02169 931 EELSEIEDPKGEDEEIpeeelsLEDVQAELQ-------RVEEEIRALEPVNMLAIQEYEEVLKRL-DELKEKRAKLEEER 1002
|
410
....*....|....*.
gi 568989155 646 DVLE---TECHSLKKE 658
Cdd:TIGR02169 1003 KAILeriEEYEKKKRE 1018
|
|
| FHA_RAD53-like_rpt2 |
cd22690 |
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
12-103 |
3.14e-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: 43.43 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 12 PNSHPfqerHVYL-DEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTSKF---YLQDTkSSNGTFINSQRLSR 87
Cdd:cd22690 8 NPSYP----DIELtQNTTFIGRS------KDCDEEITDPRISKHHCIITRKRSGKGLddvYVTDT-STNGTFINNNRLGK 76
|
90
....*....|....*.
gi 568989155 88 GSEesppCEILSGDII 103
Cdd:cd22690 77 GSQ----SLLQDGDEI 88
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
14-106 |
3.16e-05 |
|
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.
Pssm-ID: 438734 [Multi-domain] Cd Length: 96 Bit Score: 43.29 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 14 SHPFQERHvyldepIKIGRSVarcrpaQNNATFDCKVLSRNHALvwFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEesp 93
Cdd:cd22682 14 QFPITEST------IVIGRSV------ESQVQIDDDSVSRYHAK--LAVNPSAVSIIDLGSTNGTIVNGKKIPKLAS--- 76
|
90
....*....|...
gi 568989155 94 pCEILSGDIIQFG 106
Cdd:cd22682 77 -CDLQNGDQIKIG 88
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
13-110 |
6.80e-05 |
|
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also called nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438717 [Multi-domain] Cd Length: 97 Bit Score: 42.22 E-value: 6.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 13 NSHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTskFYLQDTKSSNGTFINSQRLSrgsee 91
Cdd:cd22665 7 SQAHGPEKDFPLYEgENVIGRD------PSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRL----- 73
|
90 100
....*....|....*....|.
gi 568989155 92 SPPC--EILSGDIIQFGvDVT 110
Cdd:cd22665 74 KPNVryELIDGDLLLFG-DVK 93
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
52-107 |
7.20e-05 |
|
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: 42.70 E-value: 7.20e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568989155 52 SRNHALVWFDH---------KTSKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQFGV 107
Cdd:cd22667 40 SRKHATLTVLHpeanlsdpdTRPELTLKDL-SKYGTFVNGEKLKGGSE----VTLKDGDVITFGV 99
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
289-521 |
8.18e-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: 8.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 289 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQkgqaEKKELQTKIDEMEEKEQELQAKIEALQADnd 368
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ----ELAALEAELAELEKEIAELRAELEAQKEE-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 369 fTNERLTALQGIQVDDFLPKINGSTEKEKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTlspskekssddTTDAQMDE 448
Cdd:COG4942 106 -LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL-----------RAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568989155 449 QDLNEPLAKVSLLKDDLQgtQSETEAKQDIQHLRKELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESA 521
Cdd:COG4942 174 AELEALLAELEEERAALE--ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
310-576 |
8.30e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 8.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 310 AVNEIKDLSDKLKVAEGKQEEIQqkgqAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQgiqvddflpki 389
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQ----AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE----------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 390 ngstekeklmvqghltkvveesklskeNQAKAKESDLSDTLSPSKEKSSD-DTTDAQMDEQDLNEPLAKVSLLKddlQGT 468
Cdd:COG3883 79 ---------------------------AEIEERREELGERARALYRSGGSvSYLDVLLGSESFSDFLDRLSALS---KIA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 469 QSETEAKQDIQHLRKELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTE 548
Cdd:COG3883 129 DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
250 260
....*....|....*....|....*...
gi 568989155 549 ISSTRDKLLSAQDEILLLRQAAAEAVSE 576
Cdd:COG3883 209 EAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
257-522 |
8.95e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.07 E-value: 8.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 257 SLRRVLQEKIEVVRKLSEVERslsnteDECTHLKEmNERTqEELRELANKYNGAVNEIKDLSDKLKVAEGKQ-------- 328
Cdd:PRK05771 13 TLKSYKDEVLEALHELGVVHI------EDLKEELS-NERL-RKLRSLLTKLSEALDKLRSYLPKLNPLREEKkkvsvksl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 329 EEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADndftNERLTALQGIQVDDflpkingstekeKLMVQGHLTKVV 408
Cdd:PRK05771 85 EELIKDVEEELEKIEKEIKELEEEISELENEIKELEQE----IERLEPWGNFDLDL------------SLLLGFKYVSVF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 409 eESKLSKEnqaKAKESDLSDTLSPSKEKSSDDTTD------AQMDEQDLNEPLAKVSLLKDDLQ--GTQSET--EAKQDI 478
Cdd:PRK05771 149 -VGTVPED---KLEELKLESDVENVEYISTDKGYVyvvvvvLKELSDEVEEELKKLGFERLELEeeGTPSELirEIKEEL 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 568989155 479 QHLRKELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESAK 522
Cdd:PRK05771 225 EEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAEALSK 268
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
229-777 |
1.14e-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: 45.87 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 229 KNQTEDSLRKELIALQEDKHSYETTAK---------ESLRRVLQEKIEVVRKLSEVERSlsnTEDECTHLKEMNERTQEE 299
Cdd:pfam05483 94 KVSIEAELKQKENKLQENRKIIEAQRKaiqelqfenEKVSLKLEEEIQENKDLIKENNA---TRHLCNLLKETCARSAEK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 300 LRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNdftnERLTALQG 379
Cdd:pfam05483 171 TKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDK----EKQVSLLL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 380 IQvddflpkingSTEKEKLMVQghLTKVVEESKlSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVS 459
Cdd:pfam05483 247 IQ----------ITEKENKMKD--LTFLLEESR-DKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 460 LLKDDLQgtqseteakqdiqhlrkelveaqelaRTSKQKCfelqaLLEEERKAyrnQVEESAKQIQVLQVQLQKLHMDME 539
Cdd:pfam05483 314 ALEEDLQ--------------------------IATKTIC-----QLTEEKEA---QMEELNKAKAAHSFVVTEFEATTC 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 540 NLQEEKDTEisstRDKLLSAQDEILLLRQAAAEAVSERD--TDFVSLQE----ELKKVRAELEGWRKAASEYENEIRSLQ 613
Cdd:pfam05483 360 SLEELLRTE----QQRLEKNEDQLKIITMELQKKSSELEemTKFKNNKEveleELKKILAEDEKLLDEKKQFEKIAEELK 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 614 SSFQlrcqqcedqqreeatRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMT 693
Cdd:pfam05483 436 GKEQ---------------ELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLE 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 694 RKELEKQVGSL--------------KEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITD 759
Cdd:pfam05483 501 NKELTQEASDMtlelkkhqediincKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEY 580
|
570
....*....|....*...
gi 568989155 760 ELKQCKDNLKLLREKGNN 777
Cdd:pfam05483 581 EVLKKEKQMKILENKCNN 598
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
339-756 |
1.24e-04 |
|
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: 45.50 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 339 KKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQgIQVDDFLPKINGSTEKEKLMVQGH-LTKVVEESKLSKEN 417
Cdd:pfam05557 15 QNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQ-KRIRLLEKREAEAEEALREQAELNrLKKKYLEALNKKLN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 418 QAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQgtqsETEAK-QDIQHLRKELVEAQELARTSK 496
Cdd:pfam05557 94 EKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLD----LLKAKaSEAEQLRQNLEKQQSSLAEAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 497 QKCFELQalleeerkaYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISstrdKLLSAQDEILLLR------QAA 570
Cdd:pfam05557 170 QRIKELE---------FEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNK----HLNENIENKLLLKeevedlKRK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 571 AEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRS--LQSSFQLRCQQCEDQQREEATRLQGELEKLKKEWDVL 648
Cdd:pfam05557 237 LEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSpeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARREL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 649 ETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDL----SILQMTRKEL-EKQVGSLKEQHLRDAADlktLLSKAE 723
Cdd:pfam05557 317 EQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgyrAILESYDKELtMSNYSPQLLERIEEAED---MTQKMQ 393
|
410 420 430
....*....|....*....|....*....|...
gi 568989155 724 NQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 756
Cdd:pfam05557 394 AHNEEMEAQLSVAEEELGGYKQQAQTLERELQA 426
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
547-779 |
1.32e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 547 TEISSTRDKLLSAQDEILLLRQAAAEAvserdTDFVSLQEELKKVRAELEGWR-----KAASEYENEIRSLQSSFQlrcq 621
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELA-----ERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEELRAELA---- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 622 qcedQQREEATRLQGELEKLKKEWDVLETECHSLKKENV-LLSSELQRQEKELHNsqkqsfeltsdlsiLQMTRKELEKQ 700
Cdd:COG4913 306 ----RLEAELERLEARLDALREELDELEAQIRGNGGDRLeQLEREIERLERELEE--------------RERRRARLEAL 367
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568989155 701 VGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQckdnlklLREKGNNKP 779
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS-------LERRKSNIP 439
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
18-86 |
1.39e-04 |
|
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: 41.54 E-value: 1.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568989155 18 QERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhkTSKFYLQDTKSSNGTFINSQRLS 86
Cdd:cd22694 8 GELRFDPGSSVRIGRD------PDADVRLDDPRVSRRHALLEFD--GDGWVYTDLGSRNGTYLNGRRVQ 68
|
|
| FHA_CHFR |
cd22672 |
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ... |
49-105 |
1.79e-04 |
|
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: 41.51 E-value: 1.79e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568989155 49 KVLSRNHALVWFDHKTsKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQF 105
Cdd:cd22672 39 KLVSGDHCKIIRDEKG-QVWLEDT-STNGTLVNKVKVVKGQK----VELKHGDVIYL 89
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
182-670 |
2.06e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 182 LEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgnqlqacSKNQTEDSLRKELIALQEDKHSYETTaKESLRRV 261
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHE---------ERREELETLEAEIEDLRETIAETERE-REELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 262 LQEKIEVVRKLSEVERSL-----------SNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEE 330
Cdd:PRK02224 281 VRDLRERLEELEEERDDLlaeaglddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 331 IQQKGQAEKKELQ---TKIDEMEEKEQELQAKIEALQADNDFTNERLTALQgiqvdDFLPKIngstEKEKLMVQGHLTKV 407
Cdd:PRK02224 361 LREEAAELESELEearEAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE-----DFLEEL----REERDELREREAEL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 408 VEESKLSKENQAKA----------------KESDLSDTLSPSKEKSSD---DTTDAQMDEQDLNEPLAKVSLLKDDLQGT 468
Cdd:PRK02224 432 EATLRTARERVEEAealleagkcpecgqpvEGSPHVETIEEDRERVEEleaELEDLEEEVEEVEERLERAEDLVEAEDRI 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 469 QSETEAKQDIQHL---RKELVEAQELARTSKQK-CFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQE- 543
Cdd:PRK02224 512 ERLEERREDLEELiaeRRETIEEKRERAEELRErAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESl 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 544 EKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGwrkAASEYENEIRSLQSSFQLRCQQC 623
Cdd:PRK02224 592 ERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDE---ARIEEAREDKERAEEYLEQVEEK 668
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 568989155 624 EDQQREEATRLQGELEKLKKEWDVLEtechSLKKENVLLSSELQRQE 670
Cdd:PRK02224 669 LDELREERDDLQAEIGAVENELEELE----ELRERREALENRVEALE 711
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
178-350 |
2.41e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 178 REQML--EQKLATLQRLLAITQEAsDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHSYE---T 252
Cdd:COG4913 241 HEALEdaREQIELLEPIRELAERY-AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEarlD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 253 TAKESLRRV--------------LQEKIE-VVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDL 317
Cdd:COG4913 320 ALREELDELeaqirgnggdrleqLEREIErLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEE 399
|
170 180 190
....*....|....*....|....*....|...
gi 568989155 318 SDKLKVAEGKQEEIQQKGQAEKKELQTKIDEME 350
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
463-673 |
2.47e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 463 DDLQGTQSETE-AKQDIQHLRkELVEAQELARTSKQKCFELQALLEEeRKAYRNQVEesakqiqvlqvqLQKLHMDMENL 541
Cdd:COG4913 235 DDLERAHEALEdAREQIELLE-PIRELAERYAAARERLAELEYLRAA-LRLWFAQRR------------LELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 542 QEEK---DTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDfvsLQEELKKVRAELEGWRKAASEYENEIRSLQSS--- 615
Cdd:COG4913 301 RAELarlEAELERLEARLDALREELDELEAQIRGNGGDRLEQ---LEREIERLERELEERERRRARLEALLAALGLPlpa 377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568989155 616 --------------FQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKEL 673
Cdd:COG4913 378 saeefaalraeaaaLLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
534-792 |
2.55e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 534 LHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAvSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQ 613
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEA-EEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 614 SSFQLRcqqcedQQREEATRLQGELEKLKKEWDvletechslkkenvllssELQRQEKELHNSQKQSFELTSDLSILQMT 693
Cdd:COG4717 123 KLLQLL------PLYQELEALEAELAELPERLE------------------ELEERLEELRELEEELEELEAELAELQEE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 694 RKELEKQVGSLKEQHLRDAAdlktllskaenqakdvqKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 773
Cdd:COG4717 179 LEELLEQLSLATEEELQDLA-----------------EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
250
....*....|....*....
gi 568989155 774 KGNNKPWPWMPMLAALVAV 792
Cdd:COG4717 242 EERLKEARLLLLIAAALLA 260
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
537-778 |
3.94e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 537 DMENLQEEKDTEISSTRDKLLSAQDEILLLRqAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSsf 616
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELR-EELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE-- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 617 QLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRK- 695
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKk 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 696 --ELEKQVGSLKEQHlRDAADLKTLLSKAENQAKdvqkeyEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 773
Cdd:PRK03918 347 lkELEKRLEELEERH-ELYEEAKAKKEELERLKK------RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
....*
gi 568989155 774 KGNNK 778
Cdd:PRK03918 420 EIKEL 424
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
251-774 |
4.35e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.19 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 251 ETTAKESLRRVLQEKIEVVRKLSEVERSLSNTE----DECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEG 326
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKeqakKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 327 KQEEIQQKGQ---AEKKELQTKIDEMEEKEQELQ--------AKIEALQADNDFTNERLTALQGIQVDDFLPKINGSTEK 395
Cdd:pfam02463 251 EEIESSKQEIekeEEKLAQVLKENKEEEKEKKLQeeelkllaKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 396 EKLMVQGHLTKVVEESKLSKENQAKAKESDLSD--------------TLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLL 461
Cdd:pfam02463 331 KKEKEEIEELEKELKELEIKREAEEEEEEELEKlqekleqleeellaKKKLESERLSSAAKLKEEELELKSEEEKEAQLL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 462 KDDLQGTQSETEAKQDIQhlrKELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENL 541
Cdd:pfam02463 411 LELARQLEDLLKEEKKEE---LEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLE 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 542 QEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQ 621
Cdd:pfam02463 488 LLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLV 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 622 QCEDQQREEATRLQGELEKLKKEWDvletecHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQV 701
Cdd:pfam02463 568 RALTELPLGARKLRLLIPKLKLPLK------SIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESA 641
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568989155 702 GSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 774
Cdd:pfam02463 642 KAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKK 714
|
|
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
53-106 |
4.82e-04 |
|
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 (FHAD1) and similar proteins; FHAD1, also called FHA domain-containing protein 1, is an uncharacterized FHA domain-containing protein. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438752 [Multi-domain] Cd Length: 96 Bit Score: 39.93 E-value: 4.82e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568989155 53 RNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPceilsGDIIQFG 106
Cdd:cd22700 36 EQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAP-----GDVLRFG 84
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
551-742 |
4.84e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 551 STRDKLLSAQDEILLLRQAAAEAVSERDTdfvsLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQcedQQREE 630
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEA----LEAELDALQERREALQRLAEYSWDEIDVASAEREIAELE---AELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 631 ATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQsfeltsdlsiLQMTRKELEkQVGSLKEQHLR 710
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE----------LDELQDRLE-AAEDLARLELR 748
|
170 180 190
....*....|....*....|....*....|..
gi 568989155 711 DAADLKTLLSKAENQAKDVQKEYEKTQTVLSE 742
Cdd:COG4913 749 ALLEERFAAALGDAVERELRENLEERIDALRA 780
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
25-108 |
5.00e-04 |
|
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: 40.49 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 25 DEPIKIGRsvarcRPAQNNAT----FDCKVLSRNHALVWFdhKTSKFYLQDTKSSNGTFINSQRLSR-GSEESPPCEILS 99
Cdd:cd22702 31 KQPCIIGS-----DPHQAISGisvvIPSPQVSELHARITC--KNGAFFLTDLGSEHGTWINDNEGRRyRAPPNFPVRLHP 103
|
....*....
gi 568989155 100 GDIIQFGVD 108
Cdd:cd22702 104 SDVIEFGSD 112
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
258-378 |
5.46e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 258 LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQ----- 332
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkey 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 568989155 333 QKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQ 378
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE 137
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
539-774 |
5.93e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 539 ENLQEEK--DTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSF 616
Cdd:PHA02562 178 ELNQQIQtlDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 617 QlrcqqcedQQREEATRLQGELEKLKKEWDVLE--TECHSLKkenvllsSELQRQEKELHNSQKQSFELTSDLSILQMTR 694
Cdd:PHA02562 258 N--------KLNTAAAKIKSKIEQFQKVIKMYEkgGVCPTCT-------QQISEGPDRITKIKDKLKELQHSLEKLDTAI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 695 KELEKQVGSLKEQHLR------DAADLKTLLSKAENQAKDVQKEYEKTQTvlselklkfemteqEKQSITDELKQCKDNL 768
Cdd:PHA02562 323 DELEEIMDEFNEQSKKllelknKISTNKQSLITLVDKAKKVKAAIEELQA--------------EFVDNAEELAKLQDEL 388
|
....*.
gi 568989155 769 KLLREK 774
Cdd:PHA02562 389 DKIVKT 394
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
16-111 |
6.26e-04 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaB and similar proteins; FhaB, also called FtsZ-interacting protein A (FipA), is a putative virulence factor involved in regulating cell shape. It can interact with polyketide-associated protein PapA5, a putative membrane protein involved in the biosynthesis of virulence enhancing lipids. FhaB regulates growth and cell division. It is probably required for divisomal protein assembly under oxidative stress. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438745 [Multi-domain] Cd Length: 91 Bit Score: 39.59 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 16 PFQERHVYLD-EPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFdhKTSKFYLQDTKSSNGTFINSQRLSRgseespP 94
Cdd:cd22693 7 TLQGQTFPIDkSGITIGRA------DDNDLVLSDDFVSSRHARIYL--QGSSWYLEDLGSTNGTFVNGNRVTQ------P 72
|
90
....*....|....*..
gi 568989155 95 CEILSGDIIQFGVDVTE 111
Cdd:cd22693 73 VVVQPGDTIRIGATVFE 89
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
587-773 |
6.35e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 587 ELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQCeDQQREEATRLQGELEKL---KKEWDVLETECHSLKKENVLLS 663
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREI-NEISSELPELREELEKLekeVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 664 SELQRQEKELHNSQKQSFELTSDLSILQMTRKELEK---------QVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYE 734
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190
....*....|....*....|....*....|....*....
gi 568989155 735 KtqtvLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 773
Cdd:PRK03918 332 E----LEEKEERLEELKKKLKELEKRLEELEERHELYEE 366
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
52-106 |
7.49e-04 |
|
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: 39.40 E-value: 7.49e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568989155 52 SRNHALVWFDHKTSKFYLQ-----------DTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFG 106
Cdd:cd22683 28 SRSCDLVLSDPSISRFHAElrleqnginviDNNSANGTFINGKRIKGKT-----YILKNGDIIVFG 88
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
327-721 |
8.40e-04 |
|
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: 42.74 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 327 KQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQA-DNDFTNER---LTALQGIQVDDFLPKINGSTEKEKLMVQG 402
Cdd:pfam13166 90 ESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKlEADFLDECwkkIKRKKNSALSEALNGFKYEANFKSRLLRE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 403 HLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDttDAQMDEqdlnepLAKVSLLKDDLQGTQSETEAKQDIQHLR 482
Cdd:pfam13166 170 IEKDNFNAGVLLSDEDRKAALATVFSDNKPEIAPLTFN--VIDFDA------LEKAEILIQKVIGKSSAIEELIKNPDLA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 483 KELVEAQELARTSKQKC-F---ELQALLEEERKAYRNQ-VEEsakqiqvlqvqlqklhmDMENLQEEKDTEISSTRDKL- 556
Cdd:pfam13166 242 DWVEQGLELHKAHLDTCpFcgqPLPAERKAALEAHFDDeFTE-----------------FQNRLQKLIEKVESAISSLLa 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 557 -LSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRK---AASEYE------NEIRSLQSS----------- 615
Cdd:pfam13166 305 qLPAVSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRALEAKRKdpfKSIELDsvdakiESINDLVASineliakhnei 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 616 ---FQLRCQQCEDQ-QREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELhnsqkqsfeltsdlsilq 691
Cdd:pfam13166 385 tdnFEEEKNKAKKKlRLHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEI------------------ 446
|
410 420 430
....*....|....*....|....*....|
gi 568989155 692 mtrKELEKQVGslkeQHLRDAADLKTLLSK 721
Cdd:pfam13166 447 ---KELEAQLR----DHKPGADEINKLLKA 469
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
328-588 |
1.07e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 328 QEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQgiqvddflpKINGSTEKEKLMVQGHLTKV 407
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA---------RRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 408 VEESKlSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEAkqdIQHLRKELVE 487
Cdd:COG4942 89 EKEIA-ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE---LRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 488 AQELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEisstrDKLLSAqdeilLLR 567
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL-----EALIAR-----LEA 234
|
250 260
....*....|....*....|.
gi 568989155 568 QAAAEAVSERDTDFVSLQEEL 588
Cdd:COG4942 235 EAAAAAERTPAAGFAALKGKL 255
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
490-746 |
1.17e-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: 42.19 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 490 ELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQA 569
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 570 AAEAVSERDTdfVSLQEELKKVR-AELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQREEatrlQGELEKLKKEWDVL 648
Cdd:pfam07888 110 SEELSEEKDA--LLAQRAAHEARiRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEE----EAERKQLQAKLQQT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 649 ETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELE---KQVGSLKEQ---HLRDAADLKTLLSKA 722
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEallEELRSLQERlnaSERKVEGLGEELSSM 263
|
250 260
....*....|....*....|....
gi 568989155 723 ENQAKDVQKEYEKTQTVLSELKLK 746
Cdd:pfam07888 264 AAQRDRTQAELHQARLQAAQLTLQ 287
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
489-691 |
1.18e-03 |
|
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: 42.42 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 489 QELARTSKQKcfelqaLLEEERKayRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQ 568
Cdd:pfam17380 396 QELEAARKVK------ILEEERQ--RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQ 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 569 AAAE-----AVSERDTDFVSLQEELKK--VRAELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQR----EEATRLQGE 637
Cdd:pfam17380 468 QEEErkrkkLELEKEKRDRKRAEEQRRkiLEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERrreaEEERRKQQE 547
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568989155 638 LEKLKK--EWDVLETECHSlKKENVLLSSELQRQEKELHNSQKQsFELTSDLSILQ 691
Cdd:pfam17380 548 MEERRRiqEQMRKATEERS-RLEAMEREREMMRQIVESEKARAE-YEATTPITTIK 601
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
294-521 |
1.24e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 294 ERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALqadndftNER 373
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL-------GER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 374 LTALQgiqvddflpkINGSTEK--EKLMVQGHLTKVVeeSKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDL 451
Cdd:COG3883 92 ARALY----------RSGGSVSylDVLLGSESFSDFL--DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568989155 452 NEPLAKVSLLKDDLQGTQSETEA-----KQDIQHLRKELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESA 521
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEAllaqlSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
468-707 |
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 568989155 468 TQSETEAKQDIQHLRKELVEAQELARTSKQKcfelQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEekdt 547
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 548 EISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQssfqlrcqqcedQQ 627
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR------------AD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 628 REEATRLQGELEKLKKEWDVLETEchsLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQ 707
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAE---LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
27-106 |
1.39e-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: 38.60 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 27 PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTSkfYLQDTKSSNGTFINSQRLsrgseeSPPCEILSGDIIQFG 106
Cdd:cd22668 19 SNIIGRG------SDADFRLPDTGVSRRHAEIRWDGQVA--HLTDLGSTNGTTVNNAPV------TPEWRLADGDVITLG 84
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
49-112 |
1.60e-03 |
|
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: 39.34 E-value: 1.60e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568989155 49 KVLSRNHALVWFDHKTS--KFYLQDTKSSNGTFINsqrlsrgSEESPPC---EILSGDIIQFGVDVTEN 112
Cdd:cd22681 64 ETCSKQHCVIQFRNVKGilKPYIMDLDSSNGTCLN-------DNVIPSSryvELRSGDVITFSKSNDYE 125
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
630-753 |
1.71e-03 |
|
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: 41.23 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 630 EATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNsQKQSFELTSDLSilqmtrkELEKQVGSLKeqhl 709
Cdd:pfam15294 134 EIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGA-KKDVKSNLKEIS-------DLEEKMAALK---- 201
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 568989155 710 rdaADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQE 753
Cdd:pfam15294 202 ---SDLEKTLNASTALQKSLEEDLASTKHELLKVQEQLEMAEKE 242
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
329-651 |
1.88e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 329 EEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQadndftnERLTALQGIqvddfLPKINgstekekLMVQGHLTKVV 408
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAK-------EGLSALNRL-----LPRLN-------LLADETLADRV 896
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 409 EESKlskenqakakesdlsdtlspskekssDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEakqDIQHLRKELVEA 488
Cdd:PRK04863 897 EEIR--------------------------EQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPE---QFEQLKQDYQQA 947
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 489 QELARTSKQKCFELQALLeeERKAYRNqVEESAKQIQVLQVQLQKLHMDMENLQEEKDTeissTRDKLLSAQDEILLLRQ 568
Cdd:PRK04863 948 QQTQRDAKQQAFALTEVV--QRRAHFS-YEDAAEMLAKNSDLNEKLRQRLEQAEQERTR----AREQLRQAQAQLAQYNQ 1020
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 569 AAAEAVSERDTDFVSLQE---ELKK--VRAElEGWRKAASEYENEIRSLQSSFQLRCQQCEDQ---QREEATRLQGELEK 640
Cdd:PRK04863 1021 VLASLKSSYDAKRQMLQElkqELQDlgVPAD-SGAEERARARRDELHARLSANRSRRNQLEKQltfCEAEMDNLTKKLRK 1099
|
330
....*....|.
gi 568989155 641 LKKEWDVLETE 651
Cdd:PRK04863 1100 LERDYHEMREQ 1110
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
563-782 |
1.99e-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: 41.29 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 563 ILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQcEDQQREEATRLQGELEKLK 642
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-IRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 643 KEWDVLETECHSLKKE-----------------NVLLSSE--------LQRQEKELHNSQKQSFELTSDLSILQMTRKEL 697
Cdd:COG4942 90 KEIAELRAELEAQKEElaellralyrlgrqpplALLLSPEdfldavrrLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 698 EKQVGSLKE---QHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 774
Cdd:COG4942 170 EAERAELEAllaELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
....*...
gi 568989155 775 GNNKPWPW 782
Cdd:COG4942 250 ALKGKLPW 257
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
163-348 |
2.61e-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: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWqALIDEDRLLSRLEVMGNQLQACSKNQTE-DSLRKELI 241
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-DEIDVASAEREIAELEAELERLDASSDDlAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 242 ALQEDkhsyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLK----EMNERTQEELRELANKYNGAVNEIKDL 317
Cdd:COG4913 696 ELEAE-----------LEELEEELDELKGEIGRLEKELEQAEEELDELQdrleAAEDLARLELRALLEERFAAALGDAVE 764
|
170 180 190
....*....|....*....|....*....|.
gi 568989155 318 SDKLKVAEGKQEEIQQKGQAEKKELQTKIDE 348
Cdd:COG4913 765 RELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
1-106 |
2.77e-03 |
|
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: 40.90 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 1 MPSALAIFTCRPNSHPFQERHVYLDEPIKIGRSvARC-----RPAQnnatfdckVLSRNHALVWFDHktSKFYLQDTkSS 75
Cdd:COG3456 1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRS-ADCdwvlpDPDR--------SVSRRHAEIRFRD--GAFCLTDL-ST 68
|
90 100 110
....*....|....*....|....*....|...
gi 568989155 76 NGTFIN--SQRLSRGSEEsppcEILSGDIIQFG 106
Cdd:COG3456 69 NGTFLNgsDHPLGPGRPV----RLRDGDRLRIG 97
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
501-732 |
3.42e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 501 ELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEkdteISSTRDKLLSAQDEILLLRQAAAEavserdtd 580
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAE-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 581 fvsLQEELKKVRAELEGWRKaasEYENEIRSLQSS-------FQLRCQQCEDQQREeATRLQGELEKLKKEWDVLETECH 653
Cdd:COG4942 88 ---LEKEIAELRAELEAQKE---ELAELLRALYRLgrqpplaLLLSPEDFLDAVRR-LQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 654 SLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQ---HLRDAADLKTLLSKAENQAKDVQ 730
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAElaeLQQEAEELEALIARLEAEAAAAA 240
|
..
gi 568989155 731 KE 732
Cdd:COG4942 241 ER 242
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
253-766 |
3.77e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.86 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 253 TAKESLR-RVLQEKIEVVRKLSEVERSLSNTEDEctHLKEMNERtQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEI 331
Cdd:pfam05483 197 LAFEELRvQAENARLEMHFKLKEDHEKIQHLEEE--YKKEINDK-EKQVSLLLIQITEKENKMKDLTFLLEESRDKANQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 332 QQKGQAEKKELQtkidEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDDFLPKINGSTEKEKLMVQGHLTKVVEES 411
Cdd:pfam05483 274 EEKTKLQDENLK----ELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSF 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 412 KLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKD----DLQGTQSETEAKQDIQHLRKELVE 487
Cdd:pfam05483 350 VVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNnkevELEELKKILAEDEKLLDEKKQFEK 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 488 -AQELARTSKQKCFELQALlEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENlQEEKDTEISSTRDKLLSAQDEILLL 566
Cdd:pfam05483 430 iAEELKGKEQELIFLLQAR-EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK-EKLKNIELTAHCDKLLLENKELTQE 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 567 RQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQCE---DQQREEATRLQGELEKLKK 643
Cdd:pfam05483 508 ASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKcklDKSEENARSIEYEVLKKEK 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 644 EWDVLETECHSLKKEnvllsselqrqekeLHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTLLSKAE 723
Cdd:pfam05483 588 QMKILENKCNNLKKQ--------------IENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFE 653
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 568989155 724 NQAKDVQKEYEKTQtvLSELKLkFEMTEQEKQSITDELKQCKD 766
Cdd:pfam05483 654 EIIDNYQKEIEDKK--ISEEKL-LEEVEKAKAIADEAVKLQKE 693
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
256-359 |
4.00e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 256 ESLRRVLQEKI-EVVRKLSEVERSLSNTEDEcthLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQK 334
Cdd:PRK00409 526 EELERELEQKAeEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYA 602
|
90 100
....*....|....*....|....*
gi 568989155 335 GQAEkKELQTKIDEMEEKEQELQAK 359
Cdd:PRK00409 603 SVKA-HELIEARKRLNKANEKKEKK 626
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
274-374 |
4.09e-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: 40.61 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 274 EVERSLSNTEDECTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEK----------K 340
Cdd:pfam06160 288 YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEvayselqeelE 367
|
90 100 110
....*....|....*....|....*....|....
gi 568989155 341 ELQTKIDEMEEKEQELQAKIEALQADNDFTNERL 374
Cdd:pfam06160 368 EILEQLEEIEEEQEEFKESLQSLRKDELEAREKL 401
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
555-732 |
4.48e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 555 KLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIrslqssfqlrcqqceDQQREEATRL 634
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI---------------EEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 635 QGELEKLK--KEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQmtrKELEKQVGSLKEQHLRDA 712
Cdd:COG1579 79 EEQLGNVRnnKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE---AELEEKKAELDEELAELE 155
|
170 180
....*....|....*....|
gi 568989155 713 ADLKTLLSKAENQAKDVQKE 732
Cdd:COG1579 156 AELEELEAEREELAAKIPPE 175
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
208-366 |
5.37e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 208 IDEDRLLSRLEVMGNQLQACSKNQTE---DSLRKELIALQED-KHSYETTAKEslrrvLQEKIEVVRKLSEVERSLsnte 283
Cdd:PRK04778 249 LDHLDIEKEIQDLKEQIDENLALLEEldlDEAEEKNEEIQERiDQLYDILERE-----VKARKYVEKNSDTLPDFL---- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 284 decTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKK---ELQTKIDEMEEKEQELQ 357
Cdd:PRK04778 320 ---EHAKEQNKELKEEIDRVKQSYtlnESELESVRQLEKQLESLEKQYDEITERIAEQEIaysELQEELEEILKQLEEIE 396
|
....*....
gi 568989155 358 AKIEALQAD 366
Cdd:PRK04778 397 KEQEKLSEM 405
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
236-366 |
5.56e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 236 LRKELIALQEDKHSYETTAKESLRRV--LQEKIEVVRKlsevERSLSNTEDECTHLKEMNERTQEELRELankyngaVNE 313
Cdd:COG1579 50 AKTELEDLEKEIKRLELEIEEVEARIkkYEEQLGNVRN----NKEYEALQKEIESLKRRISDLEDEILEL-------MER 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 568989155 314 IKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQAD 366
Cdd:COG1579 119 IEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
161-610 |
6.11e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 161 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQeasdtswqalidedRLLSRLEVMGNQLQACSKNQTEdsLRKEL 240
Cdd:PRK03918 291 KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIE--------------ERIKELEEKEERLEELKKKLKE--LEKRL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 241 IALQEDKHSYETTakeslrRVLQEKIEVVRKlSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSD- 319
Cdd:PRK03918 355 EELEERHELYEEA------KAKKEELERLKK-RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKa 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 320 --KLKVAEGK------------QEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIE----ALQADNDFTNERLTALQGIQ 381
Cdd:PRK03918 428 ieELKKAKGKcpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLRKELRelekVLKKESELIKLKELAEQLKE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 382 VDDFLPKIN------GSTEKEKLM-----VQGHLTKVVEESKLSK---------ENQAKAKESDLSDTLSPSKEKSSDDT 441
Cdd:PRK03918 508 LEEKLKKYNleelekKAEEYEKLKeklikLKGEIKSLKKELEKLEelkkklaelEKKLDELEEELAELLKELEELGFESV 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 442 TDAQMDEQDLNEPLAKVSLLKDdlqgTQSETEAKQD-IQHLRKELVEAQELARTSKQKCFELQALLEEERKAY-RNQVEE 519
Cdd:PRK03918 588 EELEERLKELEPFYNEYLELKD----AEKELEREEKeLKKLEEELDKAFEELAETEKRLEELRKELEELEKKYsEEEYEE 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 520 SAKQIQVLQVQLQKLHMDMENLQEEKDtEISSTRDKLLSAQDEIlllRQAAAEAvserdtdfvslqEELKKVRAELEGWR 599
Cdd:PRK03918 664 LREEYLELSRELAGLRAELEELEKRRE-EIKKTLEKLKEELEER---EKAKKEL------------EKLEKALERVEELR 727
|
490
....*....|.
gi 568989155 600 KAASEYENEIR 610
Cdd:PRK03918 728 EKVKKYKALLK 738
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
628-754 |
6.25e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 39.62 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 628 REEATRLQGELEKLKKEWDVLETECHSLKK----ENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGS 703
Cdd:smart00787 164 MKELELLNSIKPKLRDRKDALEEELRQLKQledeLEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIED 243
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 568989155 704 LKEQHLrdaaDLKTLLSKAENQAKDVQKeyeKTQTVLSELKLKFEMTEQEK 754
Cdd:smart00787 244 LTNKKS----ELNTEIAEAEKKLEQCRG---FTFKEIEKLKEQLKLLQSLT 287
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
236-519 |
6.58e-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: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 236 LRKELIALQEDKHSYETTAK--ESLRRVLQEKIEVVRKLSEVERSLSNTEDecthlkemnerTQEELRELANKYNgavnE 313
Cdd:COG4913 615 LEAELAELEEELAEAEERLEalEAELDALQERREALQRLAEYSWDEIDVAS-----------AEREIAELEAELE----R 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 314 IKDLSDKLKVAEGKQEEIQqkgqAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDDflPKINGST 393
Cdd:COG4913 680 LDASSDDLAALEEQLEELE----AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE--LRALLEE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 394 EKEKLMVQGHLTKVVE--ESKLSKENQAKAK-ESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAK-VSLLKDDLqgtq 469
Cdd:COG4913 754 RFAAALGDAVERELREnlEERIDALRARLNRaEEELERAMRAFNREWPAETADLDADLESLPEYLALlDRLEEDGL---- 829
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 568989155 470 seTEAKQDIQHLRKELVEaQELArtskqkcfELQALLEEERKAYRNQVEE 519
Cdd:COG4913 830 --PEYEERFKELLNENSI-EFVA--------DLLSKLRRAIREIKERIDP 868
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
172-361 |
6.97e-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: 38.35 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 172 LQEALHREQMLEQKLATLQRLLaitqeasdtswQALIDEDRLLSRLEVmgNQLQACSKNQTEDSLRKELIAlqedKHSYE 251
Cdd:pfam15619 6 LSARLHKIKELQNELAELQSKL-----------EELRKENRLLKRLQK--RQEKALGKYEGTESELPQLIA----RHNEE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 252 T-TAKESLRRvLQEKIEVV-RKLSEVERSLSNTEDECTHL------KEMNERT--QEELRELANKYNGAVNEIKDLSDKL 321
Cdd:pfam15619 69 VrVLRERLRR-LQEKERDLeRKLKEKEAELLRLRDQLKRLeklsedKNLAEREelQKKLEQLEAKLEDKDEKIQDLERKL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568989155 322 KVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIE 361
Cdd:pfam15619 148 ELENKSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLK 187
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
213-498 |
7.71e-03 |
|
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: 40.05 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 213 LLSRLEVMGNQLQACSKNQteDSLRKELIALQE--DKHSYETTAKESLRRVLQEKIE---------VVRKLSEVERSLSN 281
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQL--ASLEEELEKLTEeiSELEKRLEEIEQLLEELNKKIKdlgeeeqlrVKEKIGELEAEIAS 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 282 TEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLsdklkvaEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIE 361
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEEL-------EREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 362 ALQADNDFTNERLTALQGIQvddflpkingsteKEKLMVQGHLTKVVEESKLSKENQAKAKEsDLSDTLspSKEKSSDDT 441
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLK-------------REINELKRELDRLQEELQRLSEELADLNA-AIAGIE--AKINELEEE 442
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 568989155 442 TDAQMDEqdLNEPLAKVSLLKDDLQGTQSETEA-KQDIQHLRKELVEAQ-ELARTSKQK 498
Cdd:TIGR02169 443 KEDKALE--IKKQEWKLEQLAADLSKYEQELYDlKEEYDRVEKELSKLQrELAEAEAQA 499
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
256-487 |
7.92e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 40.03 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 256 ESLRRVLQEKIEVVRK--LSEVERSLSNTEDECTHLKEMN--ERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEI 331
Cdd:TIGR01612 1058 DEIEKEIGKNIELLNKeiLEEAEINITNFNEIKEKLKHYNfdDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEI 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 332 QQKGQAEKKELQTKI----------------DEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDDF-LPKING-ST 393
Cdd:TIGR01612 1138 KKKSENYIDEIKAQIndledvadkaisnddpEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTsLEEVKGiNL 1217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 394 EKEKLMVQGHLTKVVEESKLSkENQAKAKESDLSDtLSPSKEKSSDDTTDAQMdEQDLNEPLAKVSLLKDDLQG----TQ 469
Cdd:TIGR01612 1218 SYGKNLGKLFLEKIDEEKKKS-EHMIKAMEAYIED-LDEIKEKSPEIENEMGI-EMDIKAEMETFNISHDDDKDhhiiSK 1294
|
250
....*....|....*...
gi 568989155 470 SETEAKQDIQHLRKELVE 487
Cdd:TIGR01612 1295 KHDENISDIREKSLKIIE 1312
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
289-556 |
8.90e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.61 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 289 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALqadnd 368
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEEL----- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 369 ftNERLTALQgIQVDDFlpkingstekeklmvqghltkvveESKLSKENQAKAKESDLSDTLSpSKEKSSDDTTDAQMDE 448
Cdd:PHA02562 240 --TDELLNLV-MDIEDP------------------------SAALNKLNTAAAKIKSKIEQFQ-KVIKMYEKGGVCPTCT 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989155 449 QDLNEPLAKVSLLKDDL-QGTQSETEAKQDIQHLRKELVEAQELARTSKqkcfELQALLEEERKAYRNQVEEsAKQIQVL 527
Cdd:PHA02562 292 QQISEGPDRITKIKDKLkELQHSLEKLDTAIDELEEIMDEFNEQSKKLL----ELKNKISTNKQSLITLVDK-AKKVKAA 366
|
250 260 270
....*....|....*....|....*....|...
gi 568989155 528 QVQLQKLHMD----MENLQEEKDtEISSTRDKL 556
Cdd:PHA02562 367 IEELQAEFVDnaeeLAKLQDELD-KIVKTKSEL 398
|
|
| |
