NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|948283837|gb|KRH98102|]
View 

penicillin-binding protein [Cylindrospermopsis sp. CR12]

Protein Classification

FHA domain-containing protein; DUF3662 and FHA domain-containing protein( domain architecture ID 11507878)

FHA (forkhead-associated) domain-containing protein participates in signal transduction pathways via protein-protein interactions involving recognition of pThr and pTyr phosphopeptides| DUF3662 and FHA domain-containing protein may participate in signal transduction pathways via protein-protein interactions involving recognition of pThr and pTyr phosphopeptides through its FHA domain

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
MrcB COG0744
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ...
151-752 0e+00

Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440507 [Multi-domain]  Cd Length: 630  Bit Score: 644.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 151 KFLTWGMYGISGITALFALAIVWEWTKFDVNPLP-------TATSGPVVIYARDAyTPL--REPRNISHVDLKEIAdfgP 221
Cdd:COG0744    9 RLLRRLLGLLLLLLAVLVLAALAGLVALYVADLPdpeeledLALPQTSTIYDRDG-TLIatLGDENREWVPLDQIP---P 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 222 YIPGAVVASEDSRYYWHFGVDPLGILRAVFINTQSGDVQQGASTVTQQLARSLFrdyVGRQDSLGRKIREAIVSLKLETF 301
Cdd:COG0744   85 HLKDAVVAIEDRRFYEHGGVDPKGIARALVANLTAGGVVQGGSTITQQLVKNLF---LSNERTLSRKLKEALLALKLERK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 302 YSKDEILLTYLNRVFLGADTSGFEDAAKYYFEKSAKELTLSEAATLVGILPAPNGFDfcgdgPRK--LAAADYRNRVIRR 379
Cdd:COG0744  162 YSKDEILELYLNTVYFGRGAYGIEAAAQYYFGKSASDLTLAEAALLAGLVKAPSYYD-----PYRnpEAAKERRNLVLDR 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 380 MLDMGTINSTQANRARRSPVQVSPKVcERQAKTIAPYFYNYVFQELESILGAGAAREGNYIIETKLDPVIQAKAESALQN 459
Cdd:COG0744  237 MVEQGYITQAEADAAKAEPLTLVPPP-NGAAAGKYPYFVDYVRRELEELLGEDDLYRGGLKIYTTLDPKLQKAAEKAVKN 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 460 SVNKvgSNLRFSQGAIVTLDAKTGSILAMVGGKNYKESQFNRAIQAQRQPGSTFKVFAYAAAIEAGIPTYKSYSCNSFPW 539
Cdd:COG0744  316 VLPE--GKPGGLQAALVVVDPKTGEVLAMVGGRDYGKSQFNRATQAKRQPGSTFKPFVYAAALEQGYTPATTVDDEPVTF 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 540 GGFTYRP---CRSGGGSLDVATGFALSENPIALRLAREVGLNKVVEMAQRLGIKSSLESVPGLVLGQSVVNVLEMTGAFA 616
Cdd:COG0744  394 PGGGWSPknyDGRYRGPVTLREALANSLNTPAVRLAQEVGLDKVVDTARRLGITSPLDPNPSLALGTSEVSPLEMASAYA 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 617 AIGNRGVWNPPHAITRILDSSdcedrnnlktCREIYSFTQNPKAnqtVLKKNVANTMTDMMQAVVARGTGRAASIGMGEE 696
Cdd:COG0744  474 TFANGGVYVEPHAITKVTDAD----------GKVLYEAKPKCEQ---VISPEVAYLMTDMLQDVVTSGTGRAARLPGRPV 540
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 948283837 697 AGKTGTTDKNVDLWFIGFIPsrQLVTGIWLGNDNNSPT--LGSSGQAAQLWGNYMRQI 752
Cdd:COG0744  541 AGKTGTTNDNRDAWFVGYTP--QLVTAVWVGNDDNSPMgyVTGGSLPAPIWRDFMEAA 596
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
42-134 8.38e-20

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


:

Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 84.62  E-value: 8.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  42 PELWVQNGEES-QTYPLLGERYILGRSSrSCDIIVPNPVVSQVHLSLTRDSSQnnpvFTIKDENSTNGIYLGKRRVK-SL 119
Cdd:COG1716    2 ARLVVLEGPLAgRRFPLDGGPLTIGRAP-DNDIVLDDPTVSRRHARIRRDGGG----WVLEDLGSTNGTFVNGQRVTePA 76
                         90
                 ....*....|....*
gi 948283837 120 KLRHGDIVTLGPPEL 134
Cdd:COG1716   77 PLRDGDVIRLGKTEL 91
 
Name Accession Description Interval E-value
MrcB COG0744
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ...
151-752 0e+00

Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440507 [Multi-domain]  Cd Length: 630  Bit Score: 644.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 151 KFLTWGMYGISGITALFALAIVWEWTKFDVNPLP-------TATSGPVVIYARDAyTPL--REPRNISHVDLKEIAdfgP 221
Cdd:COG0744    9 RLLRRLLGLLLLLLAVLVLAALAGLVALYVADLPdpeeledLALPQTSTIYDRDG-TLIatLGDENREWVPLDQIP---P 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 222 YIPGAVVASEDSRYYWHFGVDPLGILRAVFINTQSGDVQQGASTVTQQLARSLFrdyVGRQDSLGRKIREAIVSLKLETF 301
Cdd:COG0744   85 HLKDAVVAIEDRRFYEHGGVDPKGIARALVANLTAGGVVQGGSTITQQLVKNLF---LSNERTLSRKLKEALLALKLERK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 302 YSKDEILLTYLNRVFLGADTSGFEDAAKYYFEKSAKELTLSEAATLVGILPAPNGFDfcgdgPRK--LAAADYRNRVIRR 379
Cdd:COG0744  162 YSKDEILELYLNTVYFGRGAYGIEAAAQYYFGKSASDLTLAEAALLAGLVKAPSYYD-----PYRnpEAAKERRNLVLDR 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 380 MLDMGTINSTQANRARRSPVQVSPKVcERQAKTIAPYFYNYVFQELESILGAGAAREGNYIIETKLDPVIQAKAESALQN 459
Cdd:COG0744  237 MVEQGYITQAEADAAKAEPLTLVPPP-NGAAAGKYPYFVDYVRRELEELLGEDDLYRGGLKIYTTLDPKLQKAAEKAVKN 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 460 SVNKvgSNLRFSQGAIVTLDAKTGSILAMVGGKNYKESQFNRAIQAQRQPGSTFKVFAYAAAIEAGIPTYKSYSCNSFPW 539
Cdd:COG0744  316 VLPE--GKPGGLQAALVVVDPKTGEVLAMVGGRDYGKSQFNRATQAKRQPGSTFKPFVYAAALEQGYTPATTVDDEPVTF 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 540 GGFTYRP---CRSGGGSLDVATGFALSENPIALRLAREVGLNKVVEMAQRLGIKSSLESVPGLVLGQSVVNVLEMTGAFA 616
Cdd:COG0744  394 PGGGWSPknyDGRYRGPVTLREALANSLNTPAVRLAQEVGLDKVVDTARRLGITSPLDPNPSLALGTSEVSPLEMASAYA 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 617 AIGNRGVWNPPHAITRILDSSdcedrnnlktCREIYSFTQNPKAnqtVLKKNVANTMTDMMQAVVARGTGRAASIGMGEE 696
Cdd:COG0744  474 TFANGGVYVEPHAITKVTDAD----------GKVLYEAKPKCEQ---VISPEVAYLMTDMLQDVVTSGTGRAARLPGRPV 540
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 948283837 697 AGKTGTTDKNVDLWFIGFIPsrQLVTGIWLGNDNNSPT--LGSSGQAAQLWGNYMRQI 752
Cdd:COG0744  541 AGKTGTTNDNRDAWFVGYTP--QLVTAVWVGNDDNSPMgyVTGGSLPAPIWRDFMEAA 596
PBP_1a_fam TIGR02074
penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan ...
215-752 2.20e-177

penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of bifunctional transglycosylase/transpeptidase penicillin-binding proteins (PBP). In the Proteobacteria, this family includes PBP 1A but not the paralogous PBP 1B (TIGR02071). This family also includes related proteins, often designated PBP 1A, from other bacterial lineages. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273955 [Multi-domain]  Cd Length: 531  Bit Score: 518.35  E-value: 2.20e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  215 EIADFGPYIPGAVVASEDSRYYWHFGVDPLGILRAVFINTQSGDVQQGASTVTQQLARSLFRDyvgrQD-SLGRKIREAI 293
Cdd:TIGR02074   6 PIDDIPENLINAFLAIEDRRFYDHFGIDLKGIGRAAVANITSGRVLEGGSTITQQLAKNLYLT----NErTITRKIQEAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  294 VSLKLETFYSKDEILLTYLNRVFLGADTSGFEDAAKYYFEKSAKELTLSEAATLVGILPAPNGFDfcgdgPRK--LAAAD 371
Cdd:TIGR02074  82 LALKLEQKLSKDEILELYLNRIYFGNGAYGIEAAAQFYFGKSVNDLTLAEAAMLAGLPKAPSAYN-----PFKnpERAKD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  372 YRNRVIRRMLDMGTINSTQANRARRSPVQVSPKVCERqAKTIAPYFYNYVFQELESILGAGAAREGnYIIETKLDPVIQA 451
Cdd:TIGR02074 157 RRNLVLSNMVENGYITAEEAEEAINEPIQLYLQTKKS-EQYKAPYFVDYVIQELEEEYGEELYTGG-LKIYTTLDLDAQK 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  452 KAESAL-QNSVNKVGSNLRFSQGAIVTLDAKTGSILAMVGGKNYKESQFNRAIQAQRQPGSTFKVFAYAAAIEAGIPTYK 530
Cdd:TIGR02074 235 AAEKVLnTGLRVAGRRDGDDLQAALVAIDPDTGAVRALVGGRDYGKSQFNRATQAKRQPGSTFKPFVYAAALEKGLTPAT 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  531 SYSCNSFPWGGFT-YRPCRSGG---GSLDVATGFALSENPIALRLAREVGLNKVVEMAQRLGIKSSLESVPGLVLGQSVV 606
Cdd:TIGR02074 315 IVNDEPITYNGNGpWSPKNYGGgyrGNVTLRQALAQSRNIPAVRLLQEVGLDKVVALAKRFGITSPLDPVLSLALGTVEV 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  607 NVLEMTGAFAAIGNRGVWNPPHAITRILDSSDcedrnnlktcREIYSFTQNPKAnqtVLKKNVANTMTDMMQAVVARGTG 686
Cdd:TIGR02074 395 SPLEMASAYAVFANGGKYVEPHGIRKIVDRDG----------KVIYENKPKTTQ---VISPATAYIMTDMLKGVVESGTG 461
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 948283837  687 RAASIGMGEEAGKTGTTDKNVDLWFIGFIPsrQLVTGIWLGNDNNSP---TLGSSGQAAQLWGNYMRQI 752
Cdd:TIGR02074 462 RSARLPGRPVAGKTGTTQNWRDAWFVGYTP--YYVTAVWVGYDDKKTlgkSGTGGGLAAPIWRDFMAEA 528
Transgly pfam00912
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ...
200-381 2.60e-67

Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of transglycosylase and transpeptidase in the N- and C-terminus respectively. The transglycosylase domain catalyzes the polymerization of murein glycan chains.


Pssm-ID: 459993 [Multi-domain]  Cd Length: 177  Bit Score: 219.70  E-value: 2.60e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  200 TPLREPRNISHVDLKeIADFGPYIPGAVVASEDSRYYWHFGVDPLGILRAVFINTQSGDVQQGASTVTQQLARSLFRDyv 279
Cdd:pfam00912   3 TLLAELGEENREYVP-LDDIPPALKNAVLAIEDRRFYEHGGVDPKGIARALLSNLRSGRIVQGGSTITQQLAKNLFLT-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  280 gRQDSLGRKIREAIVSLKLETFYSKDEILLTYLNRVFLGADTSGFEDAAKYYFEKSAKELTLSEAATLVGILPAPNGFDF 359
Cdd:pfam00912  80 -PERTLTRKLKEAVLALKLERRYSKDEILEAYLNTVYFGRGAYGIEAAARAYFGKDASDLTLAEAALLAGLPQAPSRYNP 158
                         170       180
                  ....*....|....*....|..
gi 948283837  360 CGDGPRklaAADYRNRVIRRML 381
Cdd:pfam00912 159 LRNPER---AKRRRNLVLDRMV 177
mrcB PRK09506
bifunctional glycosyl transferase/transpeptidase; Reviewed
228-749 4.26e-65

bifunctional glycosyl transferase/transpeptidase; Reviewed


Pssm-ID: 236544 [Multi-domain]  Cd Length: 830  Bit Score: 231.97  E-value: 4.26e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 228 VASEDSRYYWHFGVDPLGILRAVFINTQSGDVQQGASTVTQQLARSLFrdyVGRQDSLGRKIREAIVSLKLETFYSKDEI 307
Cdd:PRK09506 228 LATEDRHFYEHDGISLYSIGRAVLANLTAGRTVQGGSTLTQQLVKNLF---LSNERSLWRKANEAYMALIMDARYSKDRI 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 308 LLTYLNRVFLGADTS----GFEDAAKYYFEKSAKELTLSEAATLVGIL-------PAPNgfdfcgdgPRKlaAADYRNRV 376
Cdd:PRK09506 305 LELYLNEVYLGQSGDdqirGFPLASLYYFGRPVEELSLDQQALLVGMVkgaslynPWRN--------PKL--ALERRNLV 374
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 377 IRRMLDMGTINSTQANRARRSPVQVSPK--VCERQaktiaPYFYNYVFQELESILGAGAAREGNYIIETKLDPVIQAKAE 454
Cdd:PRK09506 375 LRLLQQQQIIDQELYDMLSARPLGVQPKggVISPQ-----PAFMQMVRQELQAKLGDKVKDLSGVKIFTTLDPVSQDAAE 449
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 455 SALQNSVN--KVGSNLRFSQGAIVTLDAKTGSILAMVGGKNYKESQFNRAIQAQRQPGSTFKVFAYAAAIEAgiPtyKSY 532
Cdd:PRK09506 450 KAVEEGIPalKKQRKLSDLETAMVVVDRFSGEVRAMVGGSEPQFAGYNRAMQARRSIGSLAKPATYLTALSQ--P--DKY 525
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 533 SCNSfpW-----------GGFTYRP---CRSGGGSLDVATGFALSENPIALRLAREVGLNKVVEMAQRLGI-KSSLESVP 597
Cdd:PRK09506 526 RLNT--WiadapislrqpNGQVWSPqndDRRFSGRVMLVDALTRSMNVPTVNLGMALGLPAVTDTWIKLGVpKDQLNPVP 603
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 598 GLVLGQSVVNVLEMTGAFAAI---GNRgvwnpphAITRILDSSDCEDRNNLKTcreiySFtqnPKANQTVLKKNVANTMT 674
Cdd:PRK09506 604 AMLLGALNLTPIEVAQAFQTIasgGNR-------APLSALRSVIAEDGKVLYQ-----SF---PQAERAVPAQAAYLTLY 668
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 948283837 675 DMMQaVVARGTGRAASIGMGEE--AGKTGTTDKNVDLWFIGfIPSRQlVTGIWLGNDNNSPT--LGSSGqAAQLWGNYM 749
Cdd:PRK09506 669 TMQQ-VVQRGTGRQLGAKYPNLhlAGKTGTTNDLVDSWFAG-IDGKE-VTITWVGRDNNQPTklYGASG-AMTIYQRYL 743
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
42-134 8.38e-20

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 84.62  E-value: 8.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  42 PELWVQNGEES-QTYPLLGERYILGRSSrSCDIIVPNPVVSQVHLSLTRDSSQnnpvFTIKDENSTNGIYLGKRRVK-SL 119
Cdd:COG1716    2 ARLVVLEGPLAgRRFPLDGGPLTIGRAP-DNDIVLDDPTVSRRHARIRRDGGG----WVLEDLGSTNGTFVNGQRVTePA 76
                         90
                 ....*....|....*
gi 948283837 120 KLRHGDIVTLGPPEL 134
Cdd:COG1716   77 PLRDGDVIRLGKTEL 91
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
44-134 9.23e-19

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: 81.55  E-value: 9.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  44 LWVQNGEESQTYPLLGERYILGRSSrSCDIIVPNPVVSQVHLSLTRDSSQnnpvFTIKDENSTNGIYLGKRRV-KSLKLR 122
Cdd:cd00060    3 IVLDGDGGGREFPLTKGVVTIGRSP-DCDIVLDDPSVSRRHARIEVDGGG----VYLEDLGSTNGTFVNGKRItPPVPLQ 77
                         90
                 ....*....|..
gi 948283837 123 HGDIVTLGPPEL 134
Cdd:cd00060   78 DGDVIRLGDTTF 89
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
62-129 5.60e-15

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 69.91  E-value: 5.60e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837   62 YILGRSSrSCDIIVPNPVVSQVHLSLTRDssqNNPVFTIKDENSTNGIYLGKRRVKSLK--LRHGDIVTL 129
Cdd:pfam00498   1 VTIGRSP-DCDIVLDDPSVSRRHAEIRYD---GGGRFYLEDLGSTNGTFVNGQRLGPEPvrLKDGDVIRL 66
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
62-116 2.95e-11

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 59.11  E-value: 2.95e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 948283837    62 YILGRSSRSCDIIVPNPVVSQVHLSLTRDSsqnNPVFTIKDENSTNGIYLGKRRV 116
Cdd:smart00240   1 VTIGRSSEDCDIQLDGPSISRRHAVIVYDG---GGRFYLIDLGSTNGTFVNGKRI 52
 
Name Accession Description Interval E-value
MrcB COG0744
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ...
151-752 0e+00

Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440507 [Multi-domain]  Cd Length: 630  Bit Score: 644.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 151 KFLTWGMYGISGITALFALAIVWEWTKFDVNPLP-------TATSGPVVIYARDAyTPL--REPRNISHVDLKEIAdfgP 221
Cdd:COG0744    9 RLLRRLLGLLLLLLAVLVLAALAGLVALYVADLPdpeeledLALPQTSTIYDRDG-TLIatLGDENREWVPLDQIP---P 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 222 YIPGAVVASEDSRYYWHFGVDPLGILRAVFINTQSGDVQQGASTVTQQLARSLFrdyVGRQDSLGRKIREAIVSLKLETF 301
Cdd:COG0744   85 HLKDAVVAIEDRRFYEHGGVDPKGIARALVANLTAGGVVQGGSTITQQLVKNLF---LSNERTLSRKLKEALLALKLERK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 302 YSKDEILLTYLNRVFLGADTSGFEDAAKYYFEKSAKELTLSEAATLVGILPAPNGFDfcgdgPRK--LAAADYRNRVIRR 379
Cdd:COG0744  162 YSKDEILELYLNTVYFGRGAYGIEAAAQYYFGKSASDLTLAEAALLAGLVKAPSYYD-----PYRnpEAAKERRNLVLDR 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 380 MLDMGTINSTQANRARRSPVQVSPKVcERQAKTIAPYFYNYVFQELESILGAGAAREGNYIIETKLDPVIQAKAESALQN 459
Cdd:COG0744  237 MVEQGYITQAEADAAKAEPLTLVPPP-NGAAAGKYPYFVDYVRRELEELLGEDDLYRGGLKIYTTLDPKLQKAAEKAVKN 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 460 SVNKvgSNLRFSQGAIVTLDAKTGSILAMVGGKNYKESQFNRAIQAQRQPGSTFKVFAYAAAIEAGIPTYKSYSCNSFPW 539
Cdd:COG0744  316 VLPE--GKPGGLQAALVVVDPKTGEVLAMVGGRDYGKSQFNRATQAKRQPGSTFKPFVYAAALEQGYTPATTVDDEPVTF 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 540 GGFTYRP---CRSGGGSLDVATGFALSENPIALRLAREVGLNKVVEMAQRLGIKSSLESVPGLVLGQSVVNVLEMTGAFA 616
Cdd:COG0744  394 PGGGWSPknyDGRYRGPVTLREALANSLNTPAVRLAQEVGLDKVVDTARRLGITSPLDPNPSLALGTSEVSPLEMASAYA 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 617 AIGNRGVWNPPHAITRILDSSdcedrnnlktCREIYSFTQNPKAnqtVLKKNVANTMTDMMQAVVARGTGRAASIGMGEE 696
Cdd:COG0744  474 TFANGGVYVEPHAITKVTDAD----------GKVLYEAKPKCEQ---VISPEVAYLMTDMLQDVVTSGTGRAARLPGRPV 540
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 948283837 697 AGKTGTTDKNVDLWFIGFIPsrQLVTGIWLGNDNNSPT--LGSSGQAAQLWGNYMRQI 752
Cdd:COG0744  541 AGKTGTTNDNRDAWFVGYTP--QLVTAVWVGNDDNSPMgyVTGGSLPAPIWRDFMEAA 596
PBP_1a_fam TIGR02074
penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan ...
215-752 2.20e-177

penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of bifunctional transglycosylase/transpeptidase penicillin-binding proteins (PBP). In the Proteobacteria, this family includes PBP 1A but not the paralogous PBP 1B (TIGR02071). This family also includes related proteins, often designated PBP 1A, from other bacterial lineages. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273955 [Multi-domain]  Cd Length: 531  Bit Score: 518.35  E-value: 2.20e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  215 EIADFGPYIPGAVVASEDSRYYWHFGVDPLGILRAVFINTQSGDVQQGASTVTQQLARSLFRDyvgrQD-SLGRKIREAI 293
Cdd:TIGR02074   6 PIDDIPENLINAFLAIEDRRFYDHFGIDLKGIGRAAVANITSGRVLEGGSTITQQLAKNLYLT----NErTITRKIQEAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  294 VSLKLETFYSKDEILLTYLNRVFLGADTSGFEDAAKYYFEKSAKELTLSEAATLVGILPAPNGFDfcgdgPRK--LAAAD 371
Cdd:TIGR02074  82 LALKLEQKLSKDEILELYLNRIYFGNGAYGIEAAAQFYFGKSVNDLTLAEAAMLAGLPKAPSAYN-----PFKnpERAKD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  372 YRNRVIRRMLDMGTINSTQANRARRSPVQVSPKVCERqAKTIAPYFYNYVFQELESILGAGAAREGnYIIETKLDPVIQA 451
Cdd:TIGR02074 157 RRNLVLSNMVENGYITAEEAEEAINEPIQLYLQTKKS-EQYKAPYFVDYVIQELEEEYGEELYTGG-LKIYTTLDLDAQK 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  452 KAESAL-QNSVNKVGSNLRFSQGAIVTLDAKTGSILAMVGGKNYKESQFNRAIQAQRQPGSTFKVFAYAAAIEAGIPTYK 530
Cdd:TIGR02074 235 AAEKVLnTGLRVAGRRDGDDLQAALVAIDPDTGAVRALVGGRDYGKSQFNRATQAKRQPGSTFKPFVYAAALEKGLTPAT 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  531 SYSCNSFPWGGFT-YRPCRSGG---GSLDVATGFALSENPIALRLAREVGLNKVVEMAQRLGIKSSLESVPGLVLGQSVV 606
Cdd:TIGR02074 315 IVNDEPITYNGNGpWSPKNYGGgyrGNVTLRQALAQSRNIPAVRLLQEVGLDKVVALAKRFGITSPLDPVLSLALGTVEV 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  607 NVLEMTGAFAAIGNRGVWNPPHAITRILDSSDcedrnnlktcREIYSFTQNPKAnqtVLKKNVANTMTDMMQAVVARGTG 686
Cdd:TIGR02074 395 SPLEMASAYAVFANGGKYVEPHGIRKIVDRDG----------KVIYENKPKTTQ---VISPATAYIMTDMLKGVVESGTG 461
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 948283837  687 RAASIGMGEEAGKTGTTDKNVDLWFIGFIPsrQLVTGIWLGNDNNSP---TLGSSGQAAQLWGNYMRQI 752
Cdd:TIGR02074 462 RSARLPGRPVAGKTGTTQNWRDAWFVGYTP--YYVTAVWVGYDDKKTlgkSGTGGGLAAPIWRDFMAEA 528
MrcA COG5009
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis];
151-752 2.07e-149

Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 444033 [Multi-domain]  Cd Length: 785  Bit Score: 455.39  E-value: 2.07e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 151 KFLTWGMYGISGITALFALAIVWEWTKF-----DVNPL-----PTATsgpvVIYARDAytplreprnishvdlKEIADFG 220
Cdd:COG5009    2 RLLKILLILLLLLLLLGALAVAGLYLYLspdlpDVETLkdyqpPTPS----RVYSADG---------------KLIAEFG 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 221 -------PY--IP----GAVVASEDSRYYWHFGVDPLGILRAVFINTQSGDVQQGASTVTQQLARSLFrdyVGRQDSLGR 287
Cdd:COG5009   63 eerripvPIeeIPplliNAFLAAEDKRFYEHPGVDPIGIARAAVVNLRTGRRVQGGSTITQQVAKNFL---LSPERTLTR 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 288 KIREAIVSLKLETFYSKDEILLTYLNRVFLGADTSGFEDAAKYYFEKSAKELTLSEAATLVGILPAPNGFDfcgdgPRK- 366
Cdd:COG5009  140 KIKEAILALRIEQELSKDEILELYLNKIYLGHRAYGVAAAAQTYFGKSLDELTLAEAAMLAGLPKAPSRYN-----PIRn 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 367 -LAAADYRNRVIRRMLDMGTINSTQANRARRSPVQVSPKvcERQAKTIAPYFYNYVFQELESILGAGAAREGNYIIETKL 445
Cdd:COG5009  215 pERALERRNYVLGRMLELGYITQAEYEAAKAEPLTARYH--GASAEVDAPYFAEMVRRELVERYGEDALYTGGLKVYTTL 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 446 DPVIQAKAESALQN--------------------------------------------SVNKVGSNLRFS---------- 471
Cdd:COG5009  293 DPRLQEAAEKALRDgllaydrrhgyrgpeahldlaeedwdealaevpdvgdlrpavvlEVDDKSARVGLRdgetgtlple 372
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 472 -------------------------------------------------QGAIVTLDAKTGSILAMVGGKNYKESQFNRA 502
Cdd:COG5009  373 glkwarpyindnrrgpapksasdvlkpgdvirvrpvadggwrlrqipevQGALVALDPHTGAVLALVGGFDFEQSKFNRA 452
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 503 IQAQRQPGSTFKVFAYAAAIEAGiptyksYSCNSF----------PWGGFTYRPCRSGG---GSLDVATGFALSENPIAL 569
Cdd:COG5009  453 TQAKRQPGSSFKPFVYAAALDNG------YTPATIindapivfddGGGGGVWRPKNYSGkfyGPTTLREALEKSRNLVTV 526
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 570 RLAREVGLNKVVEMAQRLGIKSSLESVPGLVLGQSVVNVLEMTGAFAAIGNRGVWNPPHAITRILDSS-----------D 638
Cdd:COG5009  527 RLLQDVGIDYVIDYAERFGIYSKLPPNLSLALGSGEVTPLEMARAYAVFANGGYRVEPYLIDRIEDRNgkviyradparA 606
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 639 CEDRNNLKTCREIYSFTQNPKanqTVLKKNVANTMTDMMQAVVARGTGRAA-SIGMgEEAGKTGTTDKNVDLWFIGFipS 717
Cdd:COG5009  607 CEDCDAAEWDGAEPRLPDPAE---QVIDPRTAYQMTSMLRGVVQRGTGRRArALGR-DIAGKTGTTNDSKDAWFVGF--T 680
                        730       740       750
                 ....*....|....*....|....*....|....*....
gi 948283837 718 RQLVTGIWLGNDNNSPtLGSSGQ----AAQLWGNYMRQI 752
Cdd:COG5009  681 PDLVAGVWVGFDDPRS-LGRGETggraALPIWIDFMKAA 718
PbpC COG4953
Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope ...
165-745 1.92e-81

Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443980 [Multi-domain]  Cd Length: 773  Bit Score: 275.94  E-value: 1.92e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 165 ALFALAIVWEWTKFdvnPLPTATSGP--VVIYARDAyTPLRE----------PrnishVDLKEIadfGPYIPGAVVASED 232
Cdd:COG4953   19 LLLALALWALDRLF---PLPLLFAVPysTVVLDRDG-TLLRAflaadgqwrlP-----VPLDEV---SPRYLQALLAYED 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 233 SRYYWHFGVDPLGILRAVFINTQSGDVQQGASTVTQQLARSLFrdyvGRQDSLGRKIREAIVSLKLETFYSKDEILLTYL 312
Cdd:COG4953   87 RRFYYHPGVNPLALLRAAWQNLRSGRIVSGGSTLTMQVARLLE----PRPRTLSGKLRQILRALQLERRYSKDEILELYL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 313 NRVFLGADTSGFEDAAKYYFEKSAKELTLSEAATLVgILP-APNGFDFcGDGPRKLAAAdyRNRVIRRMLDMGTINSTQA 391
Cdd:COG4953  163 NLAPYGGNIEGVEAASLAYFGKPPSRLSLAEAALLA-VLPqAPSRRRP-DRNPERARAA--RDRVLARLAEAGVIDAEEA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 392 NRARRSPVQVSPkvceRQAKTIAPYFYNYVFQELEsilgaGAARegnyiIETKLDPVIQAKAESALQNSVNKVGSNLRFS 471
Cdd:COG4953  239 ALALLEPVPARR----RPLPQLAPHLARRLLRQLP-----GGTR-----IRTTLDAGLQRRLERLVRRYVRRLKQNGIHN 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 472 qGAIVTLDAKTGSILAMVGGKNYkesqFNRA-------IQAQRQPGSTFKVFAYAAAIEAGI----------PTYksysc 534
Cdd:COG4953  305 -AAVLVVDNRTGEVLAYVGSADF----FDASrqgqvdmVRALRSPGSTLKPFLYGLALDQGLihpetlladvPTS----- 374
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 535 nsfpWGGftYRPCRSGGGSL-DVATGFAL--SENPIALRLAREVGLNKVVEMAQRLGIKSSL--ESVPGL--VLGQSVVN 607
Cdd:COG4953  375 ----FGG--YRPENFDGTFQgPVSAREALarSLNIPAVRLLEALGPARFYARLRRAGLRLLLppAEHYGLslILGGAEVT 448
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 608 VLEMTGAFAAIGNRGVWNPPHaitrildssdcedrnnlktcreiYSFTQNPKANQTVLKKNVANTMTDMMQAVVARG--T 685
Cdd:COG4953  449 LEELVGLYAALARGGEARPLR-----------------------LLAGEPASPGRRLLSPGAAWLVRDILSDVPRPDgaF 505
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 948283837 686 GRAASIGMGEEAGKTGTTDKNVDLWFIGFipSRQLVTGIWLGNDNNSPTLGSSGQ--AAQLW 745
Cdd:COG4953  506 GWRALDSPPPIAWKTGTSYGFRDAWAVGF--TGRYTVGVWVGNPDGTPVPGLTGAeaAAPLL 565
Transgly pfam00912
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ...
200-381 2.60e-67

Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of transglycosylase and transpeptidase in the N- and C-terminus respectively. The transglycosylase domain catalyzes the polymerization of murein glycan chains.


Pssm-ID: 459993 [Multi-domain]  Cd Length: 177  Bit Score: 219.70  E-value: 2.60e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  200 TPLREPRNISHVDLKeIADFGPYIPGAVVASEDSRYYWHFGVDPLGILRAVFINTQSGDVQQGASTVTQQLARSLFRDyv 279
Cdd:pfam00912   3 TLLAELGEENREYVP-LDDIPPALKNAVLAIEDRRFYEHGGVDPKGIARALLSNLRSGRIVQGGSTITQQLAKNLFLT-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  280 gRQDSLGRKIREAIVSLKLETFYSKDEILLTYLNRVFLGADTSGFEDAAKYYFEKSAKELTLSEAATLVGILPAPNGFDF 359
Cdd:pfam00912  80 -PERTLTRKLKEAVLALKLERRYSKDEILEAYLNTVYFGRGAYGIEAAARAYFGKDASDLTLAEAALLAGLPQAPSRYNP 158
                         170       180
                  ....*....|....*....|..
gi 948283837  360 CGDGPRklaAADYRNRVIRRML 381
Cdd:pfam00912 159 LRNPER---AKRRRNLVLDRMV 177
mrcB PRK09506
bifunctional glycosyl transferase/transpeptidase; Reviewed
228-749 4.26e-65

bifunctional glycosyl transferase/transpeptidase; Reviewed


Pssm-ID: 236544 [Multi-domain]  Cd Length: 830  Bit Score: 231.97  E-value: 4.26e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 228 VASEDSRYYWHFGVDPLGILRAVFINTQSGDVQQGASTVTQQLARSLFrdyVGRQDSLGRKIREAIVSLKLETFYSKDEI 307
Cdd:PRK09506 228 LATEDRHFYEHDGISLYSIGRAVLANLTAGRTVQGGSTLTQQLVKNLF---LSNERSLWRKANEAYMALIMDARYSKDRI 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 308 LLTYLNRVFLGADTS----GFEDAAKYYFEKSAKELTLSEAATLVGIL-------PAPNgfdfcgdgPRKlaAADYRNRV 376
Cdd:PRK09506 305 LELYLNEVYLGQSGDdqirGFPLASLYYFGRPVEELSLDQQALLVGMVkgaslynPWRN--------PKL--ALERRNLV 374
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 377 IRRMLDMGTINSTQANRARRSPVQVSPK--VCERQaktiaPYFYNYVFQELESILGAGAAREGNYIIETKLDPVIQAKAE 454
Cdd:PRK09506 375 LRLLQQQQIIDQELYDMLSARPLGVQPKggVISPQ-----PAFMQMVRQELQAKLGDKVKDLSGVKIFTTLDPVSQDAAE 449
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 455 SALQNSVN--KVGSNLRFSQGAIVTLDAKTGSILAMVGGKNYKESQFNRAIQAQRQPGSTFKVFAYAAAIEAgiPtyKSY 532
Cdd:PRK09506 450 KAVEEGIPalKKQRKLSDLETAMVVVDRFSGEVRAMVGGSEPQFAGYNRAMQARRSIGSLAKPATYLTALSQ--P--DKY 525
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 533 SCNSfpW-----------GGFTYRP---CRSGGGSLDVATGFALSENPIALRLAREVGLNKVVEMAQRLGI-KSSLESVP 597
Cdd:PRK09506 526 RLNT--WiadapislrqpNGQVWSPqndDRRFSGRVMLVDALTRSMNVPTVNLGMALGLPAVTDTWIKLGVpKDQLNPVP 603
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 598 GLVLGQSVVNVLEMTGAFAAI---GNRgvwnpphAITRILDSSDCEDRNNLKTcreiySFtqnPKANQTVLKKNVANTMT 674
Cdd:PRK09506 604 AMLLGALNLTPIEVAQAFQTIasgGNR-------APLSALRSVIAEDGKVLYQ-----SF---PQAERAVPAQAAYLTLY 668
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 948283837 675 DMMQaVVARGTGRAASIGMGEE--AGKTGTTDKNVDLWFIGfIPSRQlVTGIWLGNDNNSPT--LGSSGqAAQLWGNYM 749
Cdd:PRK09506 669 TMQQ-VVQRGTGRQLGAKYPNLhlAGKTGTTNDLVDSWFAG-IDGKE-VTITWVGRDNNQPTklYGASG-AMTIYQRYL 743
mrcA PRK11636
penicillin-binding protein 1a; Provisional
204-738 1.89e-59

penicillin-binding protein 1a; Provisional


Pssm-ID: 183248 [Multi-domain]  Cd Length: 850  Bit Score: 216.15  E-value: 1.89e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 204 EPRNIShVDLKEIAdfgPYIPGAVVASEDSRYYWHFGVDPLGILRAVFINTQSGDVQQGASTVTQQLARSLFrdyVGRQD 283
Cdd:PRK11636  63 EKRRIP-LTLDQIP---PEMVKAFIATEDSRFYEHHGVDPVGIFRAASVALFSGHASQGASTITQQLARNFF---LSPER 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 284 SLGRKIREAIVSLKLETFYSKDEILLTYLNRVFLGADTSGFEDAAKYYFEKSAKELTLSEAATLVGILPAPNGFDFCGDG 363
Cdd:PRK11636 136 TLMRKIKEAFLAIRIEQLLTKDEILELYLNKIYLGYRAYGVGAAAQVYFGKTVDQLTLSEMAVIAGLPKAPSTFNPLYSM 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 364 PRKLAAadyRNRVIRRMLDMGTINSTQANRARRSPVqvspkVCERQAKTI---APYFYNYVFQELESILGAGAAREGnYI 440
Cdd:PRK11636 216 DRAVAR---RNVVLSRMLDEGYITQAQYDQARSEPI-----VANYHAPEIafsAPYLSEMVRQEMYNRYGENAYEDG-YR 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 441 IETKLDPVIQAKAESALQNS------------------------------------------------------------ 460
Cdd:PRK11636 287 VYTTITRKVQQAAQQAVRNNvldydmrhgyrgpanvlwkvgesawdnkkitdtlkalptygpllpavvtsanpqeataml 366
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 461 -------------------------------------------VNKVGSNLRFSQ-----GAIVTLDAKTGSILAMVGGK 492
Cdd:PRK11636 367 adgssvalpmegvrwarpyrsdtqqgptprkvtdvvqtgqqiwVRQVDDAWWLAQvpdvnSALVSINPQNGAVMALVGGF 446
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 493 NYKESQFNRAIQAQRQPGSTFKVFAYAAAIEAGIpTYKSYsCNSFP---W---GGFTYRPCRSG---GGSLDVATGFALS 563
Cdd:PRK11636 447 DFNQSKFNRATQALRQVGSNIKPFLYTAAMDKGL-TLASM-LNDVPisrWdagAGSDWRPKNSPpqyAGPIRLRQGLGQS 524
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 564 ENPIALRLAREVGLNKVVEMAQRLGIKSS----LESvpgLVLGQSVVNVLEMTGAFAAIGNRGVWNPPHAITRILDssdc 639
Cdd:PRK11636 525 KNVVMVRAMRAMGVDYAAEYLQRFGFPAQnivhTES---LALGSASFTPMQVARGYAVMANGGFLVDPYFISKIEN---- 597
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 640 EDRNNLKT------CRE-----IYSFTQNPKANQTVLKKNVA------NTMTDMMQ------AVVAR------------- 683
Cdd:PRK11636 598 DQGGVIFEakpkvaCPEcdipvIYGDTQKSNVLENDDVENVAtsqeqqNSSVPMPQleqanqALVAQngaqeyaphvint 677
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 684 ---------------------GTG-RAA------SIGmgeeaGKTGTTDKNVDLWFIGFIPSrqLVTGIWLGNDNNSPTL 735
Cdd:PRK11636 678 plafliksalntnifgepgwmGTGwRAGrdlkrrDIG-----GKTGTTNSSKDAWFSGYGPG--VVTSVWIGFDDHRRDL 750

                 ...
gi 948283837 736 GSS 738
Cdd:PRK11636 751 GRT 753
PRK14850 PRK14850
penicillin-binding protein 1b; Provisional
227-750 9.61e-56

penicillin-binding protein 1b; Provisional


Pssm-ID: 237835 [Multi-domain]  Cd Length: 764  Bit Score: 204.31  E-value: 9.61e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 227 VVASEDSRYYWHFGVDPLGILRAVFINTQSGDVQQGASTVTQQLARSLFrdyVGRQDSLGRKIREAIVSLKLETFYSKDE 306
Cdd:PRK14850 173 LLAIEDKYFYEHDGIHLSSIGRAFLVNLMSGHTIQGGSTLTQQLVKNLF---LTNTRSLWRKINEIYMALILDRFYSKDR 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 307 ILLTYLNRVFLGADTS----GFEDAAKYYFEKSAKELTLSEAATLVGILPAPNGFDfCGDGPRKlaAADYRNRVIRRMLD 382
Cdd:PRK14850 250 ILELYLNEVYLGQDGNeqirGFPLASIYYFGRPINELNLDQYALLVGMVKGASLYN-PWTNPNL--TLKRRNLVLFLLYK 326
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 383 MGTINSTQANRARRSPVQVSPKvcerqAKTIA--PYFYNYVFQELESILGAGAAREGNYIIETKLDPVIQAKAESALQNS 460
Cdd:PRK14850 327 QKVITRKLYKDLCSRPLNVQSK-----GNIISshPAFIQLVCEEFHKKIHYPFKNFSGTKIFTTLDYISQNAAEQAVKIG 401
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 461 VNKVGSNLRFS--QGAIVTLDAKTGSILAMVGGKNYKESQFNRAIQAQRQPGSTFKVFAYAAAIEAgiPTYksYSCNSfp 538
Cdd:PRK14850 402 IPILKRKKRLKdlEVAMVIIDRFSGEVRALIGSSKPEFNGYNRALKARRSIGSLSKPITYLTALSQ--PEK--YHLNT-- 475
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 539 W-----------GGFTYRP---CRSGGGSLDVATGFALSENPIALRLAREVGLNKVVEMAQRLGIKSS-LESVPGLVLGQ 603
Cdd:PRK14850 476 WisdtpisikldNGQYWTPknnNFSFSGKVMLIDALIHSINIPTVHLSINLGLKKLVDSWILLGISSNyITPLPSISLGA 555
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 604 SVVNVLEMTGAFAAIGNRGVWNPPHAITRILDssdceDRNNLktcreIYSFTqnPKANQTVLKKNVANTMTdMMQAVVAR 683
Cdd:PRK14850 556 INLTPMEVAQVFQIIGSGGYKSSLSSIRSIIS-----DDNKV-----LYQNF--PQSKHVESSQASYLTLY-AMQQVVKS 622
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 948283837 684 GTGRAASIGMGEE--AGKTGTTDKNVDLWFIGfIPSRQLVTgIWLGNDNNSPT--LGSSGqAAQLWGNYMR 750
Cdd:PRK14850 623 GTAKSLGTIFKEFslAGKTGTTNNLVDSWFVG-IDGKQVVI-TWIGRDNNHTTklYGSSG-AMKIYKRYLQ 690
FtsI COG0768
Cell division protein FtsI, peptidoglycan transpeptidase (Penicillin-binding protein 2) [Cell ...
445-716 2.41e-43

Cell division protein FtsI, peptidoglycan transpeptidase (Penicillin-binding protein 2) [Cell cycle control, cell division, chromosome partitioning, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440531 [Multi-domain]  Cd Length: 568  Bit Score: 165.38  E-value: 2.41e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 445 LDPVIQAKAESALQNSVNKVGSNlrfsQGAIVTLDAKTGSILAMVGGKNY---------KESQFNRAIQAQRQPGSTFKV 515
Cdd:COG0768  225 IDSDLQKIAEEALKKAVEEYKAK----SGAVVVMDPKTGEILAMASYPSFdpnlfvggpDEPLRNRAVQGTYEPGSTFKP 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 516 FAYAAAIEAG-IPTYKSYSCN-SFPWGGFTYRPCRSGG-GSLDVATGFALSENPIALRLAREVGLNKVVEMAQRLGI--K 590
Cdd:COG0768  301 FTAAAALEEGvITPDTTFDCPgYYRVGGRTIRDWDRGGhGTLTLTEALAKSSNVGFYKLALRLGIDKLYDYLKKFGLgqK 380
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 591 SSLE---SVPGLV---------------LGQSV-VNVLEMTGAFAAIGNRGVWNPPHAITRILDSSDCEDRnnlktcrei 651
Cdd:COG0768  381 TGIDlpgEASGLLpspkrwypgetatmsIGQGLsVTPLQLAQAYAAIANGGVLVKPHLVKEIVDPDGEVVK--------- 451
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 948283837 652 ysftQNPKANQTVLKKNVANTMTDMMQAVV--ARGTGRAASIGMGEEAGKTGTTDKnVDL------------WFIGFIP 716
Cdd:COG0768  452 ----EEPEVLRRVISPETAETVREGMEGVVnePGGTARRAAIPGYRVAGKTGTAQV-VDIgnggyykgrhiaSFVGFAP 525
Transpeptidase pfam00905
Penicillin binding protein transpeptidase domain; The active site serine (residue 337 in Swiss: ...
473-717 1.99e-38

Penicillin binding protein transpeptidase domain; The active site serine (residue 337 in Swiss:P14677) is conserved in all members of this family.


Pssm-ID: 425939 [Multi-domain]  Cd Length: 296  Bit Score: 144.87  E-value: 1.99e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  473 GAIVTLDAKTGSILAMVGGKNYKESQF-----NRAIQAQRQPGSTFKVFAYAAAIEAG-IPTYKSYSCNSFPWGGFTYRP 546
Cdd:pfam00905   1 GSAVVLDPKTGEVLAMVGKPSYDPNGFigplrNRAVTSRYEPGSTFKPFTALAALDNGvLKPDETIFDWPGKQQGGKSIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  547 C--RSGGGSLDVATGFALSENPIALRLAREVGLNKVVEMAQRLGIKSSL-----ESVPGLVLGQSV------------VN 607
Cdd:pfam00905  81 DwnQDQVGIGTLRQALEYSSNWYMQKLAQKLGADKLRSYLKKFGYGNKTgiglpGENAGYLTPYWLegatasfgigltIT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  608 VLEMTGAFAAIGNRGVWNPPHAITRILDSsdcedrnnlktcreiysfTQNPKANQTVLKKNVANTMTDMMQAVVARGTGR 687
Cdd:pfam00905 161 PLQQAQAYAAIANGGKLVPPHLVKSIEDK------------------VDPKVLNKLPISKSTAEKVKDMLRLVVNDGTGT 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 948283837  688 AASIGMGEE-AGKTGTT-----------DKNVDLWFIGFIPS 717
Cdd:pfam00905 223 GTAAVPGYKvAGKTGTAqvagpkgggyyDGAQIGWFVGYAPA 264
pbp2_mrdA TIGR03423
penicillin-binding protein 2; Members of this protein family are penicillin-binding protein 2 ...
433-716 2.06e-32

penicillin-binding protein 2; Members of this protein family are penicillin-binding protein 2 (PBP-2), a protein whose gene (designated pbpA or mrdA) generally is found next to the gene for RodA, a protein required for rod (bacillus) shape in many bacteria. PBP-2 acts as a transpeptidase for cell elongation (hence, rod-shape). [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 274573 [Multi-domain]  Cd Length: 592  Bit Score: 133.03  E-value: 2.06e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  433 AAREGNYIIETkLDPVIQAKAESALQNSvnkvgsnlrfsQGAIVTLDAKTGSILAMV--------------GGKNYKE-- 496
Cdd:TIGR03423 221 PPVPGKDLVLT-IDARLQQAAEKALGGR-----------RGAVVVMDPRTGEILAMVstpsfdpnlfvdgiSSKDYKAll 288
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  497 -----SQFNRAIQAQRQPGSTFKVFAYAAAIEAG-IPTYKSYSCN-SFPWGGFTYRpC--RSGGGSLDVATGFALSENPI 567
Cdd:TIGR03423 289 ndpdrPLLNRAIQGVYPPGSTFKPVVALAALEEGvITPETRIYCPgYFQLGGRRFR-CwkRGGHGRVDLRKAIEESCDVY 367
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  568 ALRLAREVGLNKVVEMAQRLGIKSSL-----ESVPGLV-----------------------LGQSVVNV--LEMTGAFAA 617
Cdd:TIGR03423 368 FYQLALRLGIDKIAEYAKRFGFGQKTgidlpGEKSGLVpsrewkrkrfgqpwypgdtlnvsIGQGYVLVtpLQLAVATAA 447
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  618 IGNRGVWNPPHAITRILDSSdcedrnnlktcREIYSFTQNPKANQTVLKKNVANTMTDMMQAVV--ARGTGRAASIGMGE 695
Cdd:TIGR03423 448 LANGGKLYKPHLVKSIEDPD-----------GGVVRRTEPEVLRPLPISPENLDVVREGMRDVVngPGGTARRARLGLPY 516
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 948283837  696 E-AGKTGT-------TDKNVDL-----------WFIGFIP 716
Cdd:TIGR03423 517 KmAGKTGTaqvvslkQGEKYDAeqiperlrdhaLFVAFAP 556
mono_pep_trsgly TIGR02070
monofunctional biosynthetic peptidoglycan transglycosylase; This family is one of the ...
165-379 8.57e-32

monofunctional biosynthetic peptidoglycan transglycosylase; This family is one of the transglycosylases involved in the late stages of peptidoglycan biosynthesis. Members tend to be small, about 240 amino acids in length, and consist almost entirely of a domain described by pfam00912 for transglycosylases. Species with this protein will have several other transglycosylases as well. All species with this protein are Proteobacteria that produce murein (peptidoglycan). [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273951 [Multi-domain]  Cd Length: 224  Bit Score: 123.34  E-value: 8.57e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  165 ALFALAIVWEWtkfdvnpLPTATSGPVVIYARDAYTPLREPRNISH--VDLKEIAdfgPYIPGAVVASEDSRYYWHFGVD 242
Cdd:TIGR02070  17 AVFAALASWRF-------VPPPSTAFMVAEKLALWGQGDPTCGIQHrwRPYDQIS---PNLKRAVIASEDAKFVEHHGFD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  243 PLGILRAVFINTQSGDVQQGASTVTQQLARSLFRdYVGRqdSLGRKIREAIVSLKLETFYSKDEILLTYLNRVFLGADTS 322
Cdd:TIGR02070  87 WEAIQDALEKNEKSGKVVRGGSTISQQLAKNLFL-WSGR--SYLRKGLEAWATWMLETWWSKQRILEVYLNSVEWGNGVF 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 948283837  323 GFEDAAKYYFEKSAKELTLSEAATLVGILPAPNGFDFCGDGPRklaaADYRNRVIRR 379
Cdd:TIGR02070 164 GAEAAARYYFKRSASNLTRGQAARLAAVLPNPKYYDENRPGPY----VRRKATWILK 216
PRK11240 PRK11240
penicillin-binding protein 1C; Provisional
166-526 5.68e-31

penicillin-binding protein 1C; Provisional


Pssm-ID: 183049 [Multi-domain]  Cd Length: 772  Bit Score: 129.82  E-value: 5.68e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 166 LFALAIVWEWTKFDVNPLPTATSGPVVIyARDAyTPL----------REPrnishVDLKEIAdfgPYIPGAVVASEDSRY 235
Cdd:PRK11240  17 LLLFLALWLADKLWPLPLHEVNPARVVV-AEDG-TPLwrfadadgiwRYP-----VTIEDVS---PRYLEALINYEDRWF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 236 YWHFGVDPLGILRAVFINTQSGDVQQGASTVTQQLARSLfrDYVGRqdSLGRKIREAIVSLKLETFYSKDEILLTYLNRV 315
Cdd:PRK11240  87 WKHPGVNPFSVARAAWQDLTSGRVISGGSTLTMQVARLL--DPHPR--TFGGKIRQLWRALQLEWHLSKREILTLYLNRA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 316 FLGADTSGFEDAAKYYFEKSAKELTLSEAAtLVGILP-APNGF--DfcgDGPRKLAAAdyRNRVIRRMLDMGTINSTQAN 392
Cdd:PRK11240 163 PFGGTLQGIGAASWAYLGKSPANLSYAEAA-LLAVLPqAPSRLrpD---RWPERAEAA--RNKVLERMAEQGVWSAEQVK 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 393 RARRSPVQVSPkvceRQAKTIAPYFynyvfqelESILGAGAAREgnyIIETKLDPVIQAKAESALQNSVNKVGSNlrfSQ 472
Cdd:PRK11240 237 ESREEPVWLAP----RQMPQLAPLF--------ARMMLGKSKSD---KIVTTLDAGLQRRLEDLALNWKGRLPPR---SS 298
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 948283837 473 GAIVTLDAKTGSILAMVGGKNYK-ESQFNRA--IQAQRQPGSTFKVFAYAAAIEAGI 526
Cdd:PRK11240 299 LAMIVVDHTDMAVRGWVGSVDLNdDSRFGHVdmVNAIRSPGSVLKPFVYGLALDDGL 355
PRK13481 PRK13481
glycosyltransferase; Provisional
222-394 3.08e-29

glycosyltransferase; Provisional


Pssm-ID: 184078 [Multi-domain]  Cd Length: 232  Bit Score: 116.44  E-value: 3.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 222 YIPGAVVASEDSRYYWHFGVDPLGILRAVFINTQSGDVQqGASTVTQQLARSLFRDyvgRQDSLGRKIREAIVSLKLETF 301
Cdd:PRK13481  56 YVKGAFISMEDERFYKHHGFDLKGTTRALFSTISDRDVQ-GGSTITQQVVKNYFYD---NERSFTRKVKELFVAHRVEKQ 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 302 YSKDEILLTYLNRVFLGADTSGFEDAAKYYF-------EKSAKELTLSEAATLVGILPAPNGFDFCGdgprklAAADYRN 374
Cdd:PRK13481 132 YSKNEILSFYLNNIYFGDNQYTLEGAANHYFgttvnknSTTMSHITVLQSAILASKVNAPSVYNIND------MSENFTQ 205
                        170       180
                 ....*....|....*....|...
gi 948283837 375 RV---IRRMLDMGTINSTQANRA 394
Cdd:PRK13481 206 RVstnLEKMKQQNYINETQYQQA 228
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
42-134 8.38e-20

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 84.62  E-value: 8.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  42 PELWVQNGEES-QTYPLLGERYILGRSSrSCDIIVPNPVVSQVHLSLTRDSSQnnpvFTIKDENSTNGIYLGKRRVK-SL 119
Cdd:COG1716    2 ARLVVLEGPLAgRRFPLDGGPLTIGRAP-DNDIVLDDPTVSRRHARIRRDGGG----WVLEDLGSTNGTFVNGQRVTePA 76
                         90
                 ....*....|....*
gi 948283837 120 KLRHGDIVTLGPPEL 134
Cdd:COG1716   77 PLRDGDVIRLGKTEL 91
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
44-134 9.23e-19

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: 81.55  E-value: 9.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  44 LWVQNGEESQTYPLLGERYILGRSSrSCDIIVPNPVVSQVHLSLTRDSSQnnpvFTIKDENSTNGIYLGKRRV-KSLKLR 122
Cdd:cd00060    3 IVLDGDGGGREFPLTKGVVTIGRSP-DCDIVLDDPSVSRRHARIEVDGGG----VYLEDLGSTNGTFVNGKRItPPVPLQ 77
                         90
                 ....*....|..
gi 948283837 123 HGDIVTLGPPEL 134
Cdd:cd00060   78 DGDVIRLGDTTF 89
FHA_Rv1747-like_rpt1 cd22694
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
44-141 3.59e-15

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: 71.59  E-value: 3.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  44 LWVQNGEESQTYPllGERYILGRSSRsCDIIVPNPVVSQVHLSLTRDSSQnnpvFTIKDENSTNGIYLGKRRVKSLKLRH 123
Cdd:cd22694    2 TIRIPGGELRFDP--GSSVRIGRDPD-ADVRLDDPRVSRRHALLEFDGDG----WVYTDLGSRNGTYLNGRRVQQVKLSD 74
                         90
                 ....*....|....*...
gi 948283837 124 GDIVTLGPPELAASVSLE 141
Cdd:cd22694   75 GTRVRLGDPTDGPALTVV 92
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
62-129 5.60e-15

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 69.91  E-value: 5.60e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837   62 YILGRSSrSCDIIVPNPVVSQVHLSLTRDssqNNPVFTIKDENSTNGIYLGKRRVKSLK--LRHGDIVTL 129
Cdd:pfam00498   1 VTIGRSP-DCDIVLDDPSVSRRHAEIRYD---GGGRFYLEDLGSTNGTFVNGQRLGPEPvrLKDGDVIRL 66
FHA_MEK1-like cd22670
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ...
48-143 4.17e-13

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: 66.10  E-value: 4.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  48 NGEESQTYPLL-GERYILGRSsRSCDIIVPNPVVSQVHLSL--TRDSSQNNPVFTIKDeNSTNGIYLGKRRVKSLK---L 121
Cdd:cd22670    9 PGSTDIVLPIYkNQVITIGRS-PSCDIVINDPFVSRTHCRIysVQFDESSAPLVYVED-LSSNGTYLNGKLIGRNNtvlL 86
                         90       100
                 ....*....|....*....|..
gi 948283837 122 RHGDIVTLGPpelaaSVSLEYL 143
Cdd:cd22670   87 SDGDVIEIAH-----SATFVYV 103
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
62-116 2.95e-11

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 59.11  E-value: 2.95e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 948283837    62 YILGRSSRSCDIIVPNPVVSQVHLSLTRDSsqnNPVFTIKDENSTNGIYLGKRRV 116
Cdd:smart00240   1 VTIGRSSEDCDIQLDGPSISRRHAVIVYDG---GGRFYLIDLGSTNGTFVNGKRI 52
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
50-135 1.54e-10

Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.


Pssm-ID: 465238 [Multi-domain]  Cd Length: 94  Bit Score: 58.42  E-value: 1.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837   50 EESQTYPLLGERYILGRSSRsCDIIVPNPVVSQVHLSLTRDSSqnnpVFTIKDENSTNGIYLGKRRVKSLK--LRHGDIV 127
Cdd:pfam16697   7 HAGAEFPLEGGRYRIGSDPD-CDIVLSDKEVSRVHLKLEVDDE----GWRLDDLGSGNGTLVNGQRVTELGiaLRPGDRI 81

                  ....*...
gi 948283837  128 TLGPPELA 135
Cdd:pfam16697  82 ELGQTEFC 89
FHA_ArnA-like cd22680
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ...
53-130 1.69e-10

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: 58.12  E-value: 1.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  53 QTYPLLGERYILGRSSrSCDIIVPNPVVSQVHLSLTRDSSQnnpvFTIKDENSTNGIYLG-KRRVK-SLKLRHGDIVTLG 130
Cdd:cd22680   14 KKFPFDFSSVSIGRDP-ENVIVIPDPFVSRNHARITVDSNE----IYIEDLGSTNGTFVNdFKRIKgPAKLHPNDIIKLG 88
FHA_NBN cd22667
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ...
44-130 9.16e-10

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: 56.57  E-value: 9.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  44 LWVQNGEESQTYPLL-GERYILGRssRSCDIIVPN-PVVSQVHLSLTRDSSQNN-------PVFTIKDEnSTNGIYLGKR 114
Cdd:cd22667    3 LLSEQDGAGTSYYLLpGGEYTVGR--KDCDIIIVDdSSISRKHATLTVLHPEANlsdpdtrPELTLKDL-SKYGTFVNGE 79
                         90
                 ....*....|....*....
gi 948283837 115 RVKSLK---LRHGDIVTLG 130
Cdd:cd22667   80 KLKGGSevtLKDGDVITFG 98
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
48-130 3.12e-09

forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438725 [Multi-domain]  Cd Length: 95  Bit Score: 54.53  E-value: 3.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  48 NGEESQTYPLLGERYILGRSSrSCDIIVPNPVVSQVHLSLTRDsSQNNPVFTIKdeNSTNGIYLGKRRV-KSLKLRHGDI 126
Cdd:cd22673    9 DGTDGSRFPLTKKSCTFGRDL-SCDIRIQLPGVSREHCRIEVD-ENGKAYLENL--STTNPTLVNGKAIeKSAELKDGDV 84

                 ....
gi 948283837 127 VTLG 130
Cdd:cd22673   85 ITIG 88
FHA_MDC1 cd22665
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ...
44-130 4.70e-09

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: 54.16  E-value: 4.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  44 LWVQNGEESQTYPLL-GERYIlGRSSrSCDIIVPNPVVSQVHLSLTRDSSQnnpvFTIKDENSTNGIYLG-KRRVK---S 118
Cdd:cd22665    5 VFSQAHGPEKDFPLYeGENVI-GRDP-SCSVVLPDKSVSKQHACIEVDGGT----HLIEDLGSTNGTRIGnKVRLKpnvR 78
                         90
                 ....*....|..
gi 948283837 119 LKLRHGDIVTLG 130
Cdd:cd22665   79 YELIDGDLLLFG 90
FHA_CHFR cd22672
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ...
43-129 1.44e-08

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: 53.06  E-value: 1.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  43 ELWVQNGEESQTYPLLGERYILGRSsRSCDIIVP-NPVVSQVHLSLTRDSSQnnpVFTIKDeNSTNGIYLGKRRV---KS 118
Cdd:cd22672    4 QLVRLTEESSPPILLRKDEFTIGRA-KDCDLSFPgNKLVSGDHCKIIRDEKG---QVWLED-TSTNGTLVNKVKVvkgQK 78
                         90
                 ....*....|.
gi 948283837 119 LKLRHGDIVTL 129
Cdd:cd22672   79 VELKHGDVIYL 89
FHA_EspA-like cd22698
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ...
50-130 4.81e-08

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: 51.26  E-value: 4.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  50 EESQTYPLLGERYILGRSSrSCDIIVPNPVVSQVHLSLTRDSSQnnpvFTIKDENSTNGIYLGKRRVKSLKLRHGDIVTL 129
Cdd:cd22698   11 EEGKDYELDQDEFTIGRSS-NNDIRLNDHSVSRHHARIVRQGDK----CNLTDLGSTNGTFLNGIRVGTHELKHGDRIQL 85

                 .
gi 948283837 130 G 130
Cdd:cd22698   86 G 86
FHA_FhaA-like cd22668
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
44-134 8.73e-08

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: 50.54  E-value: 8.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  44 LWVQNGEeSQTYPLLGERYILGRSSRScDIIVPNPVVSQVHLSLTRDSSqnnpVFTIKDENSTNGIYLGKRRVK-SLKLR 122
Cdd:cd22668    3 LQLDDGS-GRVYQLREGSNIIGRGSDA-DFRLPDTGVSRRHAEIRWDGQ----VAHLTDLGSTNGTTVNNAPVTpEWRLA 76
                         90
                 ....*....|..
gi 948283837 123 HGDIVTLGPPEL 134
Cdd:cd22668   77 DGDVITLGHSEI 88
COG3456 COG3456
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ...
64-141 1.78e-07

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: 54.00  E-value: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  64 LGRSSrSCDIIVPNP--VVSQVHLSLTRDSSQnnpvFTIKDeNSTNGIYLG--KRRV---KSLKLRHGDIVTLGPPELAA 136
Cdd:COG3456   30 IGRSA-DCDWVLPDPdrSVSRRHAEIRFRDGA----FCLTD-LSTNGTFLNgsDHPLgpgRPVRLRDGDRLRIGDYEIRV 103

                 ....*
gi 948283837 137 SVSLE 141
Cdd:COG3456  104 EISGE 108
FHA_Slr1951-like cd22697
forkhead associated (FHA) domain found in Synechocystis sp. Slr1951 protein and similar ...
62-142 1.78e-07

forkhead associated (FHA) domain found in Synechocystis sp. Slr1951 protein and similar proteins; This subfamily corresponds to a group of uncharacterized FHA domain-containing proteins which show high sequence similarity with Synechocystis sp. protein Slr1951 and protein Sll1895. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438749 [Multi-domain]  Cd Length: 102  Bit Score: 49.77  E-value: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  62 YILGRSSRScDIIVPNPVVSQVHLSLTRDSSQNNP--VFTIKDE----NSTNGIYLGKRRVKSLKLRHGDIVTLGPpela 135
Cdd:cd22697   20 YTIGRHPGN-DIQIPSQQISRRHATLRRKINPNLDisFWIIDGDlegaESLNGLWVNGERILQHELVNGDEIALGP---- 94

                 ....*..
gi 948283837 136 aSVSLEY 142
Cdd:cd22697   95 -KIVLRY 100
FHA_RAD53-like_rpt2 cd22690
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ...
53-136 5.72e-07

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: 48.44  E-value: 5.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  53 QTYPLLGERYILGRSsRSCDIIVPNPVVSQVHLSLTRDSSQNNPVFTIKDENSTNGIYLGKRRV---KSLKLRHGDIVTL 129
Cdd:cd22690   12 PDIELTQNTTFIGRS-KDCDEEITDPRISKHHCIITRKRSGKGLDDVYVTDTSTNGTFINNNRLgkgSQSLLQDGDEIVL 90

                 ....*..
gi 948283837 130 GPPELAA 136
Cdd:cd22690   91 IWDKNNK 97
FHA_Rv1747-like_rpt2 cd22737
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
64-136 5.81e-07

second 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 second FHA domain, which has a circularly permuted FHA domain fold with a conserved pThr-binding interface.


Pssm-ID: 439356 [Multi-domain]  Cd Length: 93  Bit Score: 48.26  E-value: 5.81e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 948283837  64 LGRSSRScDIIVPNPVVSQVHLSLTRDSSQnnpvFTIKDENSTNGIYLGKRRVKSLKLRHGDIVTLGPPELAA 136
Cdd:cd22737   25 IGRASDN-DIVIPEGSVSRHHATLVPTPGG----TQIRDLRSTNGTFVNGLRVDAALLHDGDVVTIGDIDFVF 92
FHA_DUN1-like cd22683
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ...
64-130 7.19e-07

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: 47.87  E-value: 7.19e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 948283837  64 LGRSsRSCDIIVPNPVVSQVHLSLTRdssQNNPVFTIkDENSTNGIYLGKRRVK--SLKLRHGDIVTLG 130
Cdd:cd22683   25 IGRS-RSCDLVLSDPSISRFHAELRL---EQNGINVI-DNNSANGTFINGKRIKgkTYILKNGDIIVFG 88
FHA_RNF8 cd22663
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ...
59-142 2.05e-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: 46.97  E-value: 2.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  59 GERYILGRS-SRSCDIIVPNPV-VSQVHLSLTRDssqNNPVFTIKDENSTNGIYLGKRRVKSLK---LRHGDIVTLGPPe 133
Cdd:cd22663   20 GKEVTVGRGlGVTYQLVSTCPLmISRNHCVLKKN---DEGQWTIKDNKSLNGVWVNGERIEPLKpypLNEGDLIQLGVP- 95

                 ....*....
gi 948283837 134 LAASVSLEY 142
Cdd:cd22663   96 PENKEPAEY 104
FHA_TCF19 cd22685
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ...
56-142 2.52e-06

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: 47.41  E-value: 2.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  56 PLLGErYILGRSSRSCDIIVPNP----VVSQVH--LSLTRDSSQNNPVfTIKDeNSTNGIYLGKRRV---KSLKLRHGDI 126
Cdd:cd22685   25 PDLCE-YRIGRNPEVCDVFLCSSqhpnLISREHaeIHAERDGNGNWKV-LIED-RSTNGTYVNDVRLqdgQRRELSDGDT 101
                         90
                 ....*....|....*.
gi 948283837 127 VTLGPPELAASVSLEY 142
Cdd:cd22685  102 ITFGHKNGRRVKQWPY 117
PRK15105 PRK15105
peptidoglycan synthase FtsI; Provisional
445-705 7.87e-06

peptidoglycan synthase FtsI; Provisional


Pssm-ID: 185060 [Multi-domain]  Cd Length: 578  Bit Score: 49.43  E-value: 7.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 445 LDPVIQAKAESALQNSV--NKVGSnlrfsqGAIVTLDAKTGSILAMVGGKNY---------KESQFNRAIQAQRQPGSTF 513
Cdd:PRK15105 235 IDERLQALVYRELNNAVafNKAES------GSAVLVDVNTGEVLAMANSPSYnpnnlsgtpKDAMRNRAITDVFEPGSTV 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 514 KVFAYAAAIEAGIPTYKSYsCNSFPwggftYRPcrSGGGSLDVA-------TG-FALSENPIALRLAREVGLNKVVEMAQ 585
Cdd:PRK15105 309 KPMVVMTALQRGVVKENSV-LNTVP-----YRI--NGHEIKDVAryseltlTGvLQKSSNVGVSKLALAMPSSALVDTYS 380
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837 586 RLGIKSSLESvpGLVlGQS------------------------VVNVLEMTGAFAAIGNRGVWNpPHAITRIldssdced 641
Cdd:PRK15105 381 RFGLGKATNL--GLV-GERsglypqkqrwsdieratfsfgyglMVTPLQLARVYATIGSYGIYR-PLSITKV-------- 448
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 948283837 642 rnnlktcreiysftQNPKANQTVLKKNVANTMTDMMQAVVARGTG--RAASIGMgEEAGKTGTTDK 705
Cdd:PRK15105 449 --------------DPPVPGERVFPESIVRTVVHMMESVALPGGGgvKAAIKGY-RIAIKTGTAKK 499
FHA_Ct664-like cd22696
forkhead associated (FHA) domain found in Chlamydia trachomatis Ct664 protein and similar ...
59-130 1.07e-05

forkhead associated (FHA) domain found in Chlamydia trachomatis Ct664 protein and similar proteins; This subfamily corresponds to a group of uncharacterized FHA domain-containing proteins which show high sequence similarity with Chlamydia trachomatis Ct664 protein. Ct664 situates within the type III secretion system cluster that also encodes an STPK (CT673 in C. trachomatis), suggesting a role of CT664 in the chlamydial type III secretion system by mediating phosphorylation-dependent protein-protein interactions. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438748 [Multi-domain]  Cd Length: 97  Bit Score: 44.79  E-value: 1.07e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 948283837  59 GERYILGRSSRSCDIIVPNPVVSQVHLSLTRDssQNNPVFtIKDENSTNGIYLGKRRVKS-LKLRHGDIVTLG 130
Cdd:cd22696   20 GKTYFIGKDPTVCDIVLQDPSISRQHARLSID--QDNRVF-IEDLSSKNGVLVNGKPIEGkEEISGSDVISLG 89
FHA_Kanadaptin cd22677
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ...
48-130 1.66e-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: 44.47  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  48 NGEESQTYPLLGER-YILGRSSrSCDIIVPNPVVSQVH--LSLTRDSSQNNPVFTIKDENSTNGIYLGKRRVKS---LKL 121
Cdd:cd22677    9 NGVIVETLDLNGKSfYVFGRLP-GCDVVLEHPSISRYHavLQYRGDADDHDGGFYLYDLGSTHGTFLNKQRIPPkqyYRL 87

                 ....*....
gi 948283837 122 RHGDIVTLG 130
Cdd:cd22677   88 RVGHVLKFG 96
FHA_CHK2 cd22666
forkhead associated (FHA) domain found in checkpoint kinase 2 (Chk2) and similar proteins; ...
56-132 5.57e-05

forkhead associated (FHA) domain found in checkpoint kinase 2 (Chk2) and similar proteins; Chk2, also called Hucds1, Cds1 homolog, or serine/threonine-protein kinase Chk2, plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438718 [Multi-domain]  Cd Length: 112  Bit Score: 43.00  E-value: 5.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  56 PLLGERYILGRSSrSCDIIVPNPV---------VSQVHLSLTRD-SSQNNPVFTIKDeNSTNGIYLGKRRV---KSLKLR 122
Cdd:cd22666   15 DLVKDEYTFGRDK-SCDYCFDSPAlkktsyyrtYSKKHFRIFREkGSKNTYPVFLED-HSSNGTFVNGEKIgkgKKRPLN 92
                         90
                 ....*....|
gi 948283837 123 HGDIVTLGPP 132
Cdd:cd22666   93 NNDEIALSLP 102
FHA_SNIP1_DDL-like cd22676
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ...
62-130 1.69e-04

forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA domain-containing protein DDL, and similar proteins; SNIP1 is an FHA domain-containing protein required for pre-mRNA splicing as a component of the spliceosome. It inhibits NF-kappaB signaling by competing for its binding to the C/H1 domain of CBP/p300 transcriptional co-activators. It is involved in microRNA (miRNA) biogenesis. SNIP1 is a regulator of the cell cycle and cyclin D1 expression and may be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. This family also includes Arabidopsis thaliana FHA domain-containing protein DDL and similar proteins. DDL, also called protein DAWDLE, is involved in the microRNA (miRNA) and short interfering RNA (siRNA) biogenesis. It may facilitate DCL1 to access or recognize primary miRNAs. DDL binds RNA non-specifically. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438728 [Multi-domain]  Cd Length: 111  Bit Score: 41.51  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  62 YILGRSSRSCDIIVPNPVVSQVH----LSLTRDSSQNNPVFTIK----DENSTNGIYLGKRRVKSLK---LRHGDIVTLG 130
Cdd:cd22676   23 YLIGRDRRVADIPLDHPSCSKQHaviqFREVEKRNEGDVIENIRpyiiDLGSTNGTFLNGEKIEPRRyyeLREKDVLKFG 102
FHA_PPP1R8 cd22674
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ...
61-130 1.86e-04

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: 41.48  E-value: 1.86e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 948283837  61 RYILGRSSRSCDIIVPNPVVSQVHLSLTRdSSQNNPVFTIkDENSTNGIYLGKRRVKSLK---LRHGDIVTLG 130
Cdd:cd22674   28 YYLFGRNSDVCDFVLDHPSCSRVHAALVY-HKHLNRVFLI-DLGSTHGTFVGGIRLEPHKpqqLPIDSTLRFG 98
FHA_Cep170 cd22704
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ...
64-130 5.30e-04

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: 40.00  E-value: 5.30e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  64 LGRSSrsCDIIVPNPVVSQVHLSLTRDSSQNnpVFTIKDENSTNGIYLGKRRVKSL---KLRHGDIVTLG 130
Cdd:cd22704   21 VGRED--CDLILQSRSVDKQHAVITYDQIDN--EFKIKDLGSLNGTFVNDSRIPEQtyiTLKLGDSIRFG 86
FHA_RAD53-like_rpt1 cd22689
first forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ...
62-130 6.98e-04

first 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 first one. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438741 [Multi-domain]  Cd Length: 132  Bit Score: 40.34  E-value: 6.98e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 948283837  62 YILGRSsRSCDIIVPNPVVSQVHLSLTRDSSQNNPVFTIKDENSTNGIYLGKRRV--KSLK-LRHGDIVTLG 130
Cdd:cd22689   47 WTFGRH-PACDYHLGNSRLSNKHFQILLGESDPSDGNVLLNDISSNGTWLNGQRLekNSNQlLSQGDEITIG 117
FHA_YscD-like cd22710
forkhead associated (FHA) domain found in Yersinia enterocolitica Yop proteins translocation ...
56-131 1.17e-03

forkhead associated (FHA) domain found in Yersinia enterocolitica Yop proteins translocation protein D (YscD) and similar proteins; YscD protein is a single-pass inner membrane protein required for the export process of the Yop proteins. It is an essential component of the type III secretion system. YscD protein contains an N-terminal cytoplasmic domain, a transmembrane linker and a large periplasmic domain. The cytoplasmic domain consists of a forkhead-associated (FHA) fold. The FHA domain is a small phosphopeptide recognition module. Due to the lack of the conserved residues that are required for binding phosphothreonine, the cytoplasmic domain of YscD protein is therefore unlikely to function as a true FHA domain.


Pssm-ID: 438762 [Multi-domain]  Cd Length: 94  Bit Score: 38.92  E-value: 1.17e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 948283837  56 PLLGERYILGRSSRSCDIIVPNPVVSQVHLSLTRDSSQnnpvftIKDENSTNGIYL-GKRRVKSLKLRHGDIVTLGP 131
Cdd:cd22710   15 PLPPGRYVLGSDPLQCDLVLTDSGISPVHLVLEVDDGG------VRLLDSAEPLYQnGEPVVLGVLLNAFSIISVGF 85
FHA_Par42-like cd22675
forkhead associated (FHA) domain found in Trypanosoma brucei Parvulin 42 (TbPar42) and similar ...
62-117 1.75e-03

forkhead associated (FHA) domain found in Trypanosoma brucei Parvulin 42 (TbPar42) and similar proteins; TbPar42 is a nuclear protein that plays a key role in parasite cell proliferation. It exhibits an N-terminal forkhead associated (FHA)-domain and a peptidyl-prolyl-cis/trans-isomerase (PPIase) domain, both connected by a linker. Its PPIase domain adopts a parvulin fold and reflects structural elements of Pin1-type proteins but is catalytically inactive. Its FHA domain may be involved in the binding of phosphorylated target proteins. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438727 [Multi-domain]  Cd Length: 113  Bit Score: 38.69  E-value: 1.75e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 948283837  62 YILGRSsRSCDIIVPNPVVSQVHLSLTRDSSQNnpVFTIKDENSTNGIYLGKRRVK 117
Cdd:cd22675   31 YLFGRS-PVCDYVLEHPSISSVHAVLVFHGEQK--CFVLMDLGSTNGVKLNGKRIE 83
FHA_PS1-like cd22691
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ...
56-130 3.37e-03

forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) and similar proteins; PS1 is an FHA domain-containing protein required for normal spindle orientation at male meiosis II and normal formation of tetrad of microspores. It is not involved in female meiosis. Mutations in PS1 lead to the production of diploid pollen grains. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438743 [Multi-domain]  Cd Length: 113  Bit Score: 37.78  E-value: 3.37e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 948283837  56 PLLGERYILGRSSrSCDIIVPNPVVSQVHLSLTRDSSQNNpvFTIKDENSTNGIYLGKRRVKSLK---LRHGDIVTLG 130
Cdd:cd22691   25 SEEEDILVVGRHP-DCDIVLDHPSISRFHLEIRIIPSRRK--ITLTDLSSVHGTWVNGQRIEPGVpveLEEGDTVRLG 99
FHA_PP2C70-like cd22678
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ...
63-130 3.60e-03

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: 37.73  E-value: 3.60e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 948283837  63 ILGRSSRScDIIVPNPVVSQVHLSLTRDSSQNNpvFTIKDENSTNGIYLGKRRVK----SLKLRHGDIVTLG 130
Cdd:cd22678   26 TIGRIQRG-DIALKDDEVSGKHARIEWNSTGSK--WELVDLGSLNGTLVNGESISpngrPVVLSSGDVITLG 94
FHA_AGGF1 cd22686
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ...
63-134 7.38e-03

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: 37.26  E-value: 7.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283837  63 ILGR-SSRSCDIIVPNPVVSQVHLSLTRDSSQNNpvFTIKDENSTNGIYLGKRRVKSLK-------LRHGDIVTLGPPEL 134
Cdd:cd22686   29 TIGReKDHGHTIRIPELGVSKFHAEIYYDDDEQS--YTIVDLGSQNGTYLNGVRISQPKeksdpypLTHGDELKIGETTL 106
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH