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Conserved domains on  [gi|410355757|gb|JAA44482|]
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ubiquitin specific peptidase 8 [Pan troglodytes]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
777-1106 2.62e-111

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 348.66  E-value: 2.62e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   777 TGLRNLGNTCYMNSILQCLCNAPHLADYFNRNCYQDDINRSNLLGHkgeVAEEFGIIMKALWTG-QYRYISPKDFKITIG 855
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQKNsKSSSVSPKMFKKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   856 KINDQFAGYSQQDSQELLLFLMDGLHEDLNkadnrkrykeenndhlddfkaaehawQKHKQLNESIIVALFQGQFKSTVQ 935
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLN--------------------------GNHSTENESLITDLFRGQLKSRLK 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   936 CLTCHKKSRTFEAFMYLSLPLASTSKCT----LQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHL 1011
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIPGDSAELktasLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHL 211
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  1012 KRFSYDGRWKQKLQTSVDFPLEnLDLSQYVIGPK----NNLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDDHE 1087
Cdd:pfam00443  212 KRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELkpktNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEK 290
                          330       340
                   ....*....|....*....|
gi 410355757  1088 -VSDISVSSVKSSAAYILFY 1106
Cdd:pfam00443  291 vTEVDEETAVLSSSAYILFY 310
USP8_dimer pfam08969
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of ...
6-116 1.09e-36

USP8 dimerization domain; This domain is predominantly found in the amino terminal region of Ubiquitin carboxyl-terminal hydrolase 8 (USP8). It forms a five helical bundle that dimerizes.


:

Pssm-ID: 462647  Cd Length: 113  Bit Score: 133.96  E-value: 1.09e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757     6 SVPKELYLSSSLKDLNKKTEVKP--EKISTKSYVHSALKIFKTAEECRLDRDEERAYVLYMKYVTVYNLIKKRPDFKQQQ 83
Cdd:pfam08969    1 APLKPLHLSSSLEDLEKLTEKLEvdKNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVK 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 410355757    84 DYFHSILGPGNIKKAVEEAERLSESLKLRYEEA 116
Cdd:pfam08969   81 ATVRQMLGKTKINEVLDELEKLKTSLLERYEEE 113
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
375-547 2.27e-11

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


:

Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 66.79  E-value: 2.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   375 LNISTPVEPVAASKSDVSPIIQ-----PAPSIKNVPQIDRTKKPAvKLPEEHRIKSEstnhEQQSPQsgkVIPDRSTKPV 449
Cdd:TIGR02794   18 LILGSLYHSVKPEPGGGAEIIQavlvdPGAVAQQANRIQQQKKPA-AKKEQERQKKL----EQQAEE---AEKQRAAEQA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   450 VFSPTLMLTDEEKARIHAETAllmeknKQQKELRERQQEEQKEKlrkEEQEQKAKKKQEAEENEITEKQQKAREEMEKKE 529
Cdd:TIGR02794   90 RQKELEQRAAAEKAAKQAEQA------AKQAEEKQKQAEEAKAK---QAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKA 160
                          170
                   ....*....|....*...
gi 410355757   530 SEQAKKEDKETSAKRGKE 547
Cdd:TIGR02794  161 AAEAKKKAEEAKKKAEAE 178
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
192-304 1.89e-05

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


:

Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 44.40  E-value: 1.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   192 MTDKNISLIimDARRMQDYQDSCILHSLSVPEEAIspgvtasWIEAHLPDDSKDTWKKRGNVEYVVLLDWFSSAKDLqig 271
Cdd:pfam00581    1 LEDGKVVLI--DVRPPEEYAKGHIPGAVNVPLSSL-------SLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAA--- 68
                           90       100       110
                   ....*....|....*....|....*....|...
gi 410355757   272 tTLRSLKDALFKwesktvlrnEPLVLEGGYENW 304
Cdd:pfam00581   69 -AAALLKALGYK---------NVYVLDGGFEAW 91
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
459-665 2.35e-05

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 48.50  E-value: 2.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  459 DEEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRK--EEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKE 536
Cdd:COG3064    65 EQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKeaEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAA 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  537 DKETSAKRGKEITGVKRQSKSEHETSDAKK-SVEDRGKRCPTPEIQKKSTGDVPHTSVTGDSGSGKPFKIKGQPESGILR 615
Cdd:COG3064   145 EAEAAAKAEAEAARAAAAAAAAAAAAAARAaAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAAR 224
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 410355757  616 TGTFREDTDDTERNKAQREPLTRARSEEMGRIVPGLPSGWAKFLDPITGT 665
Cdd:COG3064   225 AAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAAL 274
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
777-1106 2.62e-111

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 348.66  E-value: 2.62e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   777 TGLRNLGNTCYMNSILQCLCNAPHLADYFNRNCYQDDINRSNLLGHkgeVAEEFGIIMKALWTG-QYRYISPKDFKITIG 855
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQKNsKSSSVSPKMFKKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   856 KINDQFAGYSQQDSQELLLFLMDGLHEDLNkadnrkrykeenndhlddfkaaehawQKHKQLNESIIVALFQGQFKSTVQ 935
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLN--------------------------GNHSTENESLITDLFRGQLKSRLK 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   936 CLTCHKKSRTFEAFMYLSLPLASTSKCT----LQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHL 1011
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIPGDSAELktasLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHL 211
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  1012 KRFSYDGRWKQKLQTSVDFPLEnLDLSQYVIGPK----NNLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDDHE 1087
Cdd:pfam00443  212 KRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELkpktNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEK 290
                          330       340
                   ....*....|....*....|
gi 410355757  1088 -VSDISVSSVKSSAAYILFY 1106
Cdd:pfam00443  291 vTEVDEETAVLSSSAYILFY 310
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
778-1107 5.23e-106

A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 331.56  E-value: 5.23e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  778 GLRNLGNTCYMNSILQCLCNaphladyfnrncyqddinrsnllghkgevaeefgiimkalwtgqyryispkdfkitigki 857
Cdd:cd02674     1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  858 ndqfagySQQDSQELLLFLMDGLHedlnkadnrkrykeenndhlddfkaaehawqkhkqlneSIIVALFQGQFKSTVQCL 937
Cdd:cd02674    21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  938 TCHKKSRTFEAFMYLSLPLASTS----KCTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKR 1013
Cdd:cd02674    56 TCGKTSTTFEPFTYLSLPIPSGSgdapKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR 135
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757 1014 FSYDGRWKQKLQTSVDFPLENLDLSQYVIGP-KNNLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDDHEVSDIS 1092
Cdd:cd02674   136 FSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRsFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVS 215
                         330
                  ....*....|....*
gi 410355757 1093 VSSVKSSAAYILFYT 1107
Cdd:cd02674   216 ESSVVSSSAYILFYE 230
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
700-1106 6.21e-55

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 206.27  E-value: 6.21e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  700 PQIPAERDREPSKLKRSYSSPDITQAIQEEEKRKPTVTPAVNRENKPTCYPKAEISRLSASQIRNLNPVFGgsgpaLTGL 779
Cdd:COG5560   194 PEIMGLRLGLDSFFRRYRVLASDGRVLHPLTRLELFEDRSVLLLSKITRNPDWLVDSIVDDHNRSINKEAG-----TCGL 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  780 RNLGNTCYMNSILQCLCNAPHLADYFNRNCYQDDINRSNLLGHKGEVAEEFGIIMKALWTGQYRYISPKDFKITIGKIND 859
Cdd:COG5560   269 RNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNE 348
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  860 QFAGYSQQDSQELLLFLMDGLHEDLNKAdNRKRYKEE----NNDHLDDFKAAEHAWQKHKQLNESIIVALFQGQFKSTVQ 935
Cdd:COG5560   349 EFSGYDQQDSQEFIAFLLDGLHEDLNRI-IKKPYTSKpdlsPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMYKSTLT 427
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  936 CLTCHKKSRTFEAFMYLSLPL---------------------------ASTSKCTLQD----------CLRLFS------ 972
Cdd:COG5560   428 CPGCGSVSITFDPFMDLTLPLpvsmvwkhtivvfpesgrrqplkieldASSTIRGLKKlvdaeygklgCFEIKVmciyyg 507
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  973 --------------KEEKLTDNNRFYCS----------HCRAR------------------------RDSL--------- 995
Cdd:COG5560   508 gnynmlepadkvllQDIPQTDFVYLYETndngievpvvHLRIEkgykskrlfgdpflqlnvlikasiYDKLvkefeellv 587
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  996 ----------------------KKIEIW--------------------KLPPVLLV---------HLKRFSYDGRW---- 1020
Cdd:COG5560   588 lvemkktdvdlvseqvrllreeSSPSSWlkleteidtkreeqveeegqMNFNDAVVisceweekrYLSLFSYDPLWtire 667
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757 1021 ----------------------------------KQKLQTS--------------------------------VDFPLEN 1034
Cdd:COG5560   668 igaaertitlqdclnefskpeqlglsdswycpgcKEFRQASkqmelwrlpmiliihlkrfssvrsfrdkiddlVEYPIDD 747
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 410355757 1035 LDLSQYVIGPKNNLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDDHEVSDISVSSVKSSAAYILFY 1106
Cdd:COG5560   748 LDLSGVEYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFY 819
USP8_dimer pfam08969
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of ...
6-116 1.09e-36

USP8 dimerization domain; This domain is predominantly found in the amino terminal region of Ubiquitin carboxyl-terminal hydrolase 8 (USP8). It forms a five helical bundle that dimerizes.


Pssm-ID: 462647  Cd Length: 113  Bit Score: 133.96  E-value: 1.09e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757     6 SVPKELYLSSSLKDLNKKTEVKP--EKISTKSYVHSALKIFKTAEECRLDRDEERAYVLYMKYVTVYNLIKKRPDFKQQQ 83
Cdd:pfam08969    1 APLKPLHLSSSLEDLEKLTEKLEvdKNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVK 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 410355757    84 DYFHSILGPGNIKKAVEEAERLSESLKLRYEEA 116
Cdd:pfam08969   81 ATVRQMLGKTKINEVLDELEKLKTSLLERYEEE 113
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
375-547 2.27e-11

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 66.79  E-value: 2.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   375 LNISTPVEPVAASKSDVSPIIQ-----PAPSIKNVPQIDRTKKPAvKLPEEHRIKSEstnhEQQSPQsgkVIPDRSTKPV 449
Cdd:TIGR02794   18 LILGSLYHSVKPEPGGGAEIIQavlvdPGAVAQQANRIQQQKKPA-AKKEQERQKKL----EQQAEE---AEKQRAAEQA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   450 VFSPTLMLTDEEKARIHAETAllmeknKQQKELRERQQEEQKEKlrkEEQEQKAKKKQEAEENEITEKQQKAREEMEKKE 529
Cdd:TIGR02794   90 RQKELEQRAAAEKAAKQAEQA------AKQAEEKQKQAEEAKAK---QAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKA 160
                          170
                   ....*....|....*...
gi 410355757   530 SEQAKKEDKETSAKRGKE 547
Cdd:TIGR02794  161 AAEAKKKAEEAKKKAEAE 178
PTZ00121 PTZ00121
MAEBL; Provisional
411-574 4.27e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.84  E-value: 4.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  411 KKPAVKLPEEHRIKSESTNHEQQSPQSGKVIPDRSTKPVvfsptlMLTDEEKARIHAETALLMEKNKQQKELRERQQEEQ 490
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV------MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  491 K--EKLRKEEQEQKAKKKQ---EAEENEITEKQQKAREEMEKKESEQAKKEDKEtsaKRGKEiTGVKRQSKSEHETSDAK 565
Cdd:PTZ00121 1633 KkvEQLKKKEAEEKKKAEElkkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED---EKKAA-EALKKEAEEAKKAEELK 1708

                  ....*....
gi 410355757  566 KSVEDRGKR 574
Cdd:PTZ00121 1709 KKEAEEKKK 1717
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
373-560 1.31e-07

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 55.93  E-value: 1.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   373 GPLNISTPVEPVAASKSDVSPIIQP---APSIK-NVPQIDRTKKPAVKLPEEHRIKSEstnhEQQSPQSgkviPDRSTKP 448
Cdd:pfam03154  471 GPPPITPPSGPPTSTSSAMPGIQPPssaSVSSSgPVPAAVSCPLPPVQIKEEALDEAE----EPESPPP----PPRSPSP 542
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   449 vvfSPTLMLTDEekariHAEtallmEKNKQQKELRERQQEEQKEKL--RKEEQEQKAKKKQEAEENEITEKQQKAREEme 526
Cdd:pfam03154  543 ---EPTVVNTPS-----HAS-----QSARFYKHLDRGYNSCARTDLyfMPLAGSKLAKKREEALEKAKREAEQKAREE-- 607
                          170       180       190
                   ....*....|....*....|....*....|....
gi 410355757   527 kKESEQAKKEDKETSAKRGKEITGVKRQSKSEHE 560
Cdd:pfam03154  608 -KEREKEKEKEREREREREREAERAAKASSSSHE 640
Agg_substance NF033875
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ...
309-614 1.92e-07

LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.


Pssm-ID: 411439 [Multi-domain]  Cd Length: 1306  Bit Score: 55.49  E-value: 1.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  309 PQYTTNAKVTPPPRRQN--------EEVSISLDFT-YPS-LEESIPSKPAAQTPPASIEVDENIELISDQNERmgplniS 378
Cdd:NF033875   50 PGTTTVQPDNPDPQSGSetpktavsEEATVQKDTTsQPTkVEEVASEKNGAEQSSATPNDTTNAQQPTVGAEK------S 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  379 TPVEPVAASKSDVSPIIQPApsiknvpqidrtkkpAVKLPEEHRIKSESTNHEQQSPQSGKVIPDRSTKP---VVFSPTl 455
Cdd:NF033875  124 AQEQPVVSPETTNEPLGQPT---------------EVAPAENEANKSTSIPKEFETPDVDKAVDEAKKDPnitVVEKPA- 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  456 mltdEEKARIHAETalLMEKNKQQKELrerqQEEQKEKLRKEEQEQKAKKKQEAEEN-EITEKQQKAREEMEKKESEQAK 534
Cdd:NF033875  188 ----EDLGNVSSKD--LAAKEKEVDQL----QKEQAKKIAQQAAELKAKNEKIAKENaEIAAKNKAEKERYEKEVAEYNK 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  535 KEDKETSAKRGKEITGVKRQSKSeheTSDAKKSVEDRGKRCPTPEIQKKSTGDVP----------HTSVTGDSGSGKPFK 604
Cdd:NF033875  258 HKNENGYVNEAISKNLVFDQSVV---TKDTKISSIKGGKFIKATDFNKVNAGDSKdiftklskdmGGKATGNFQNSFVKE 334
                         330
                  ....*....|
gi 410355757  605 IKGQPESGIL 614
Cdd:NF033875  335 ANLGSNGGYA 344
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
472-574 1.01e-06

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 52.73  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  472 LMEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKEDKETSAKrgkeitgV 551
Cdd:COG3064     4 ALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEA-------A 76
                          90       100
                  ....*....|....*....|...
gi 410355757  552 KRQSKSEHETSDAKKSVEDRGKR 574
Cdd:COG3064    77 KKLAEAEKAAAEAEKKAAAEKAK 99
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
192-304 1.89e-05

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 44.40  E-value: 1.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   192 MTDKNISLIimDARRMQDYQDSCILHSLSVPEEAIspgvtasWIEAHLPDDSKDTWKKRGNVEYVVLLDWFSSAKDLqig 271
Cdd:pfam00581    1 LEDGKVVLI--DVRPPEEYAKGHIPGAVNVPLSSL-------SLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAA--- 68
                           90       100       110
                   ....*....|....*....|....*....|...
gi 410355757   272 tTLRSLKDALFKwesktvlrnEPLVLEGGYENW 304
Cdd:pfam00581   69 -AAALLKALGYK---------NVYVLDGGFEAW 91
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
459-665 2.35e-05

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 48.50  E-value: 2.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  459 DEEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRK--EEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKE 536
Cdd:COG3064    65 EQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKeaEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAA 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  537 DKETSAKRGKEITGVKRQSKSEHETSDAKK-SVEDRGKRCPTPEIQKKSTGDVPHTSVTGDSGSGKPFKIKGQPESGILR 615
Cdd:COG3064   145 EAEAAAKAEAEAARAAAAAAAAAAAAAARAaAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAAR 224
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 410355757  616 TGTFREDTDDTERNKAQREPLTRARSEEMGRIVPGLPSGWAKFLDPITGT 665
Cdd:COG3064   225 AAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAAL 274
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
457-552 7.69e-05

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 46.03  E-value: 7.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  457 LTDEEKAriHAETALLMEKNKQQKELRERQQEEQKEKLRK-----EEQEQKAKKKQEAEENEITEKQQKAREEMEKKESE 531
Cdd:cd16269   193 LTEKEKE--IEAERAKAEAAEQERKLLEEQQRELEQKLEDqersyEEHLRQLKEKMEEERENLLKEQERALESKLKEQEA 270
                          90       100
                  ....*....|....*....|.
gi 410355757  532 QAKKEDKETSAKRGKEITGVK 552
Cdd:cd16269   271 LLEEGFKEQAELLQEEIRSLK 291
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
463-531 2.95e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 42.19  E-value: 2.95e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 410355757    463 ARIHAETALLMEKNKQQKELRERQQEEQK--EKLRKEE----QEQKAKKKQE--AEENEITEKQQKAREEMEKKESE 531
Cdd:smart00935   15 AGKAAQKQLEKEFKKRQAELEKLEKELQKlkEKLQKDAatlsEAAREKKEKElqKKVQEFQRKQQKLQQDLQKRQQE 91
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
458-643 9.28e-04

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 43.45  E-value: 9.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   458 TDEEkarihAETALLMEKNKQQKELRERQQEEQKEKLRKEEQE---QKAKKKQEAEENEITEKQQKAREEMEKKESEQAK 534
Cdd:TIGR00927  645 TGEE-----GERPTEAEGENGEESGGEAEQEGETETKGENESEgeiPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEG 719
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   535 KEDKETSAKRGKEITGVKRQSKSEHETSD--AKKSVEDRGKRCPTpEIQKKSTGDVPHTSVTGDSGSGKPFKIKGqpESG 612
Cdd:TIGR00927  720 ETEAEGTEDEGEIETGEEGEEVEDEGEGEaeGKHEVETEGDRKET-EHEGETEAEGKEDEDEGEIQAGEDGEMKG--DEG 796
                          170       180       190
                   ....*....|....*....|....*....|.
gi 410355757   613 ILRTGTFREDTDDTERNKAQREPLTRARSEE 643
Cdd:TIGR00927  797 AEGKVEHEGETEAGEKDEHEGQSETQADDTE 827
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
199-310 3.58e-03

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 38.21  E-value: 3.58e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757    199 LIIMDARRMQDYQDSCILHSLSVPEEAISPGVTASWieaHLPDDSKDTWKKRGNVEYVVLLDwfssakdlqiGTTLRSlk 278
Cdd:smart00450    5 VVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELD---ILEFEELLKRLGLDKDKPVVVYC----------RSGNRS-- 69
                            90       100       110
                    ....*....|....*....|....*....|..
gi 410355757    279 dALFKWESKTVLRNEPLVLEGGYENWLLCYPQ 310
Cdd:smart00450   70 -AKAAWLLRELGFKNVYLLDGGYKEWSAAGPP 100
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
777-1106 2.62e-111

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 348.66  E-value: 2.62e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   777 TGLRNLGNTCYMNSILQCLCNAPHLADYFNRNCYQDDINRSNLLGHkgeVAEEFGIIMKALWTG-QYRYISPKDFKITIG 855
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQKNsKSSSVSPKMFKKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   856 KINDQFAGYSQQDSQELLLFLMDGLHEDLNkadnrkrykeenndhlddfkaaehawQKHKQLNESIIVALFQGQFKSTVQ 935
Cdd:pfam00443   78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLN--------------------------GNHSTENESLITDLFRGQLKSRLK 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   936 CLTCHKKSRTFEAFMYLSLPLASTSKCT----LQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHL 1011
Cdd:pfam00443  132 CLSCGEVSETFEPFSDLSLPIPGDSAELktasLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHL 211
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  1012 KRFSYDGRWKQKLQTSVDFPLEnLDLSQYVIGPK----NNLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDDHE 1087
Cdd:pfam00443  212 KRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELkpktNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEK 290
                          330       340
                   ....*....|....*....|
gi 410355757  1088 -VSDISVSSVKSSAAYILFY 1106
Cdd:pfam00443  291 vTEVDEETAVLSSSAYILFY 310
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
778-1107 5.23e-106

A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 331.56  E-value: 5.23e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  778 GLRNLGNTCYMNSILQCLCNaphladyfnrncyqddinrsnllghkgevaeefgiimkalwtgqyryispkdfkitigki 857
Cdd:cd02674     1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  858 ndqfagySQQDSQELLLFLMDGLHedlnkadnrkrykeenndhlddfkaaehawqkhkqlneSIIVALFQGQFKSTVQCL 937
Cdd:cd02674    21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  938 TCHKKSRTFEAFMYLSLPLASTS----KCTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKR 1013
Cdd:cd02674    56 TCGKTSTTFEPFTYLSLPIPSGSgdapKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR 135
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757 1014 FSYDGRWKQKLQTSVDFPLENLDLSQYVIGP-KNNLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDDHEVSDIS 1092
Cdd:cd02674   136 FSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRsFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVS 215
                         330
                  ....*....|....*
gi 410355757 1093 VSSVKSSAAYILFYT 1107
Cdd:cd02674   216 ESSVVSSSAYILFYE 230
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
778-1106 4.00e-72

Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239072 [Multi-domain]  Cd Length: 255  Bit Score: 240.46  E-value: 4.00e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  778 GLRNLGNTCYMNSILQCLCNaphladyfnrncyqddinrsnllghkgevaeefgiimkalwtgqyryispkdfkitigki 857
Cdd:cd02257     1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  858 ndqfagySQQDSQELLLFLMDGLHEDLNKADNRKRYKEENndhlddfkaaehawqkhkqlnESIIVALFQGQFKSTVQCL 937
Cdd:cd02257    21 -------EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSL---------------------KSLIHDLFGGKLESTIVCL 72
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  938 TCHKKSRTFEAFMYLSLPL--ASTSKCTLQDCLRLFSKEEKLTDNNRFYCSHCRaRRDSLKKIEIWKLPPVLLVHLKRFS 1015
Cdd:cd02257    73 ECGHESVSTEPELFLSLPLpvKGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFS 151
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757 1016 YDGRW-KQKLQTSVDFPLEnLDLSQYV------IGPKNNLKKYNLFSVSNHYGGL-DGGHYTAYCKNAARQRWFKFDD-- 1085
Cdd:cd02257   152 FNEDGtKEKLNTKVSFPLE-LDLSPYLsegekdSDSDNGSYKYELVAVVVHSGTSaDSGHYVAYVKDPSDGKWYKFNDdk 230
                         330       340
                  ....*....|....*....|....
gi 410355757 1086 ---HEVSDISVSSVKSSAAYILFY 1106
Cdd:cd02257   231 vteVSEEEVLEFGSLSSSAYILFY 254
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
778-1107 4.31e-67

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 229.18  E-value: 4.31e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  778 GLRNLGNTCYMNSILQCLCNAPHLADYF--NRNCYQDDINRSN--LLGHKGEVAEEFGIIMKalwTGQYryiSPKDFKIT 853
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFlsDRHSCTCLSCSPNscLSCAMDEIFQEFYYSGD---RSPY---GPINLLYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  854 IGKINDQFAGYSQQDSQELLLFLMDGLHEDLnkadnrKRYKEENNDhlddfkaaehawqkHKQLNeSIIVALFQGQFKST 933
Cdd:cd02660    76 SWKHSRNLAGYSQQDAHEFFQFLLDQLHTHY------GGDKNEAND--------------ESHCN-CIIHQTFSGSLQSS 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  934 VQCLTCHKKSRTFEAFMYLSLPLASTSKC-------------TLQDCLRLFSKEEKLTDNNrFYCSHCRARRDSLKKIEI 1000
Cdd:cd02660   135 VTCQRCGGVSTTVDPFLDLSLDIPNKSTPswalgesgvsgtpTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSI 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757 1001 WKLPPVLLVHLKRFSYD-GRWKQKLQTSVDFPLEnLDLSQYVIG---------PKNNLKKYNLFSVSNHYGGLDGGHYTA 1070
Cdd:cd02660   214 KKLPPVLCFQLKRFEHSlNKTSRKIDTYVQFPLE-LNMTPYTSSsigdtqdsnSLDPDYTYDLFAVVVHKGTLDTGHYTA 292
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 410355757 1071 YCKNAARQrWFKFDDHEVSDISVSSVKSSAAYILFYT 1107
Cdd:cd02660   293 YCRQGDGQ-WFKFDDAMITRVSEEEVLKSQAYLLFYH 328
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
777-1106 7.61e-61

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 210.59  E-value: 7.61e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  777 TGLRNLGNTCYMNSILQCLCNAPHLADYFNRNCYQDDINRsnllghkgevaEEFGI-------IMKALWTGQYrYISPKD 849
Cdd:cd02661     2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCN-----------EGFCMmcaleahVERALASSGP-GSAPRI 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  850 FKITIGKINDQFAGYSQQDSQELLLFLMDGLHedlnKADNRKRYKEENNDHLddfkaaehawQKHKqlneSIIVALFQGQ 929
Cdd:cd02661    70 FSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQ----KACLDRFKKLKAVDPS----------SQET----TLVQQIFGGY 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  930 FKSTVQCLTCHKKSRTFEAFMYLSLPLASTSkcTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLV 1009
Cdd:cd02661   132 LRSQVKCLNCKHVSNTYDPFLDLSLDIKGAD--SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTI 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757 1010 HLKRFSYDGRwkQKLQTSVDFPlENLDLSQYVIGPKNNLKKYNLFSVSNHYGG-LDGGHYTAYCKnAARQRWFKFDDHEV 1088
Cdd:cd02661   210 HLKRFSNFRG--GKINKQISFP-ETLDLSPYMSQPNDGPLKYKLYAVLVHSGFsPHSGHYYCYVK-SSNGKWYNMDDSKV 285
                         330
                  ....*....|....*...
gi 410355757 1089 SDISVSSVKSSAAYILFY 1106
Cdd:cd02661   286 SPVSIETVLSQKAYILFY 303
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
700-1106 6.21e-55

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 206.27  E-value: 6.21e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  700 PQIPAERDREPSKLKRSYSSPDITQAIQEEEKRKPTVTPAVNRENKPTCYPKAEISRLSASQIRNLNPVFGgsgpaLTGL 779
Cdd:COG5560   194 PEIMGLRLGLDSFFRRYRVLASDGRVLHPLTRLELFEDRSVLLLSKITRNPDWLVDSIVDDHNRSINKEAG-----TCGL 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  780 RNLGNTCYMNSILQCLCNAPHLADYFNRNCYQDDINRSNLLGHKGEVAEEFGIIMKALWTGQYRYISPKDFKITIGKIND 859
Cdd:COG5560   269 RNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNE 348
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  860 QFAGYSQQDSQELLLFLMDGLHEDLNKAdNRKRYKEE----NNDHLDDFKAAEHAWQKHKQLNESIIVALFQGQFKSTVQ 935
Cdd:COG5560   349 EFSGYDQQDSQEFIAFLLDGLHEDLNRI-IKKPYTSKpdlsPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMYKSTLT 427
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  936 CLTCHKKSRTFEAFMYLSLPL---------------------------ASTSKCTLQD----------CLRLFS------ 972
Cdd:COG5560   428 CPGCGSVSITFDPFMDLTLPLpvsmvwkhtivvfpesgrrqplkieldASSTIRGLKKlvdaeygklgCFEIKVmciyyg 507
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  973 --------------KEEKLTDNNRFYCS----------HCRAR------------------------RDSL--------- 995
Cdd:COG5560   508 gnynmlepadkvllQDIPQTDFVYLYETndngievpvvHLRIEkgykskrlfgdpflqlnvlikasiYDKLvkefeellv 587
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  996 ----------------------KKIEIW--------------------KLPPVLLV---------HLKRFSYDGRW---- 1020
Cdd:COG5560   588 lvemkktdvdlvseqvrllreeSSPSSWlkleteidtkreeqveeegqMNFNDAVVisceweekrYLSLFSYDPLWtire 667
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757 1021 ----------------------------------KQKLQTS--------------------------------VDFPLEN 1034
Cdd:COG5560   668 igaaertitlqdclnefskpeqlglsdswycpgcKEFRQASkqmelwrlpmiliihlkrfssvrsfrdkiddlVEYPIDD 747
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 410355757 1035 LDLSQYVIGPKNNLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDDHEVSDISVSSVKSSAAYILFY 1106
Cdd:COG5560   748 LDLSGVEYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFY 819
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
778-1106 2.51e-49

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 176.42  E-value: 2.51e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  778 GLRNLGNTCYMNSILQCLCNAPHLADYFNRNcyqddinRSNLLGhkgevaeefgiimkalwtgQYRYISPkdfkitigki 857
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET-------PKELFS-------------------QVCRKAP---------- 44
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  858 ndQFAGYSQQDSQELLLFLMDGLhedlnkadnrkrykeenndhlddfkaaehawqkhkqlnESIIVALFQGQFKSTVQCL 937
Cdd:cd02667    45 --QFKGYQQQDSHELLRYLLDGL--------------------------------------RTFIDSIFGGELTSTIMCE 84
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  938 TCHKKSRTFEAFMYLSLPLA--STSKCTLQDCLRLFSKEEKLTDNNRFYCSHC-RARRDSLkkieIWKLPPVLLVHLKRF 1014
Cdd:cd02667    85 SCGTVSLVYEPFLDLSLPRSdeIKSECSIESCLKQFTEVEILEGNNKFACENCtKAKKQYL----ISKLPPVLVIHLKRF 160
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757 1015 SYDGRWK-QKLQTSVDFPlENLDLSQYVIGPKNNLK-----KYNLFSVSNHYGGLDGGHYTAYCK--------------- 1073
Cdd:cd02667   161 QQPRSANlRKVSRHVSFP-EILDLAPFCDPKCNSSEdkssvLYRLYGVVEHSGTMRSGHYVAYVKvrppqqrlsdltksk 239
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 410355757 1074 ------NAARQRWFKFDDHEVSDISVSSVKSSAAYILFY 1106
Cdd:cd02667   240 paadeaGPGSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
778-1107 7.32e-48

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 172.88  E-value: 7.32e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  778 GLRNLGNTCYMNSILQCLcnaphladYFNR--NCYQDdinrsnllghkgevaeefgiIMKALWTGQYRY--ISPKDFKIT 853
Cdd:cd02663     1 GLENFGNTCYCNSVLQAL--------YFENllTCLKD--------------------LFESISEQKKRTgvISPKKFITR 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  854 IGKINDQFAGYSQQDSQELLLFLMDGLHEDLNKAdnRKRYKEENNDHLDDFKAAEHAWqkhkqlnesiIVALFQGQFKST 933
Cdd:cd02663    53 LKRENELFDNYMHQDAHEFLNFLLNEIAEILDAE--RKAEKANRKLNNNNNAEPQPTW----------VHEIFQGILTNE 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  934 VQCLTCHKKSRTFEAFMYLSLPLASTskCTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKR 1013
Cdd:cd02663   121 TRCLTCETVSSRDETFLDLSIDVEQN--TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKR 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757 1014 FSYDGRWKQ--KLQTSVDFPLEnLDLSQYVIGPKNNLKKYNLFSVSNHYG-GLDGGHYTAYCKNAArqRWFKFDD----- 1085
Cdd:cd02663   199 FKYDEQLNRyiKLFYRVVFPLE-LRLFNTTDDAENPDRLYELVAVVVHIGgGPNHGHYVSIVKSHG--GWLLFDDetvek 275
                         330       340
                  ....*....|....*....|....*
gi 410355757 1086 ---HEVSDISVSSVKSSAAYILFYT 1107
Cdd:cd02663   276 ideNAVEEFFGDSPNQATAYVLFYQ 300
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
778-1087 2.28e-47

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 172.61  E-value: 2.28e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  778 GLRNLGNTCYMNSILQCL-CNAPHLADYFNRNCYQDDINR---SNLLGHKGEVAEEFGIIMKALWTGQYRYISPKDFKIT 853
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWfMNLEFRKAVYECNSTEDAELKnmpPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  854 IGKINDQfagysQQDSQELLLFLMDGLHEDLNKADNRKrykeenndhlddfkaaehawqkhkqlNESIIVALFQGQFKST 933
Cdd:cd02668    81 LGLDTGQ-----QQDAQEFSKLFLSLLEAKLSKSKNPD--------------------------LKNIVQDLFRGEYSYV 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  934 VQCLTCHKKSRTFEAFMYLSLPLASTSkcTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKR 1013
Cdd:cd02668   130 TQCSKCGRESSLPSKFYELELQLKGHK--TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLR 207
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 410355757 1014 FSYD--GRWKQKLQTSVDFPlENLDLSQYVIGPKNNLKKYNLFSVSNHYG-GLDGGHYTAYCKNAARQRWFKFDDHE 1087
Cdd:cd02668   208 FVFDrkTGAKKKLNASISFP-EILDMGEYLAESDEGSYVYELSGVLIHQGvSAYSGHYIAHIKDEQTGEWYKFNDED 283
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
778-1085 1.85e-44

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 164.35  E-value: 1.85e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  778 GLRNLGNTCYMNSILQCLCNAPhladYFNRNCYQ--------DDINRSNLLghkgEVaeefgiIMKALWTGQYRYISPKD 849
Cdd:cd02659     4 GLKNQGATCYMNSLLQQLYMTP----EFRNAVYSipptedddDNKSVPLAL----QR------LFLFLQLSESPVKTTEL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  850 FKITIGKINDQFAGYSQQDSQELLLFLMDGLhedlnkadnrkrykeenndhlddfkaaEHAWQKHKQlnESIIVALFQGQ 929
Cdd:cd02659    70 TDKTRSFGWDSLNTFEQHDVQEFFRVLFDKL---------------------------EEKLKGTGQ--EGLIKNLFGGK 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  930 FKSTVQCLTCHKKSRTFEAFmyLSLPLASTSKCTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLV 1009
Cdd:cd02659   121 LVNYIICKECPHESEREEYF--LDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTL 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757 1010 HLKRFSYDGR--WKQKLQTSVDFPLEnLDLSQYVIGPKNNLK-----------KYNLFSVSNHYGGLDGGHYTAYCKNAA 1076
Cdd:cd02659   199 QLKRFEFDFEtmMRIKINDRFEFPLE-LDMEPYTEKGLAKKEgdsekkdsesyIYELHGVLVHSGDAHGGHYYSYIKDRD 277

                  ....*....
gi 410355757 1077 RQRWFKFDD 1085
Cdd:cd02659   278 DGKWYKFND 286
USP8_dimer pfam08969
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of ...
6-116 1.09e-36

USP8 dimerization domain; This domain is predominantly found in the amino terminal region of Ubiquitin carboxyl-terminal hydrolase 8 (USP8). It forms a five helical bundle that dimerizes.


Pssm-ID: 462647  Cd Length: 113  Bit Score: 133.96  E-value: 1.09e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757     6 SVPKELYLSSSLKDLNKKTEVKP--EKISTKSYVHSALKIFKTAEECRLDRDEERAYVLYMKYVTVYNLIKKRPDFKQQQ 83
Cdd:pfam08969    1 APLKPLHLSSSLEDLEKLTEKLEvdKNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVK 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 410355757    84 DYFHSILGPGNIKKAVEEAERLSESLKLRYEEA 116
Cdd:pfam08969   81 ATVRQMLGKTKINEVLDELEKLKTSLLERYEEE 113
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
778-1106 9.69e-33

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 129.92  E-value: 9.69e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  778 GLRNLGNTCYMNSILQCLcnapHLADYFNRncyqdDINRSNLLGHKGEVAEEFGIIM-KALWTGQYRYISPKDFKITIGK 856
Cdd:cd02664     1 GLINLGNTCYMNSVLQAL----FMAKDFRR-----QVLSLNLPRLGDSQSVMKKLQLlQAHLMHTQRRAEAPPDYFLEAS 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  857 INDQFAGYSQQDSQELLLFLMDGLHedlnkadnrkrykeenndhlddfkaaehawqkhkqlneSIIVALFQGQFKSTVQC 936
Cdd:cd02664    72 RPPWFTPGSQQDCSEYLRYLLDRLH--------------------------------------TLIEKMFGGKLSTTIRC 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  937 LTCHKKSRTFEAFMYLSLplastSKCTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKRFSY 1016
Cdd:cd02664   114 LNCNSTSARTERFRDLDL-----SFPSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSY 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757 1017 D--GRWKQKLQTSVDFPlENLDLSQYV----IGPKNNLKK---------------YNLFSVSNHYG-GLDGGHYTAYCKN 1074
Cdd:cd02664   189 DqkTHVREKIMDNVSIN-EVLSLPVRVesksSESPLEKKEeesgddgelvtrqvhYRLYAVVVHSGySSESGHYFTYARD 267
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 410355757 1075 AA--------------------RQRWFKFDDH-------EVSDISVSSVKSSAAYILFY 1106
Cdd:cd02664   268 QTdadstgqecpepkdaeendeSKNWYLFNDSrvtfssfESVQNVTSRFPKDTPYILFY 326
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
778-1085 3.45e-29

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239122 [Multi-domain]  Cd Length: 305  Bit Score: 118.97  E-value: 3.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  778 GLRNLGNTCYMNSILQCLCNAPHLAD---YFNRNCYQDDINRSNLLghkgevaEEFGIIMKALWTGQYRyISPKDFKITI 854
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRDalkNYNPARRGANQSSDNLT-------NALRDLFDTMDKKQEP-VPPIEFLQLL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  855 GKINDQFA------GYSQQDSQELLLFLMDGLHEDLNKADnrkrykeenndhlddfkaaehawqkhkqLNESIIVALFQG 928
Cdd:cd02657    73 RMAFPQFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAG----------------------------SKGSFIDQLFGI 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  929 QFKSTVQCL-TCHKKSRTFEAFMYLSLPLASTSKC-TLQDCLRLFSKEE--KLTDNnrfycshcrARRDSL--KKIEIWK 1002
Cdd:cd02657   125 ELETKMKCTeSPDEEEVSTESEYKLQCHISITTEVnYLQDGLKKGLEEEieKHSPT---------LGRDAIytKTSRISR 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757 1003 LPPVLLVHLKRFSydgrWKQKLQT------SVDFPLEnLDLSQYVigpkNNLKKYNLFSVSNHYG-GLDGGHYTAYCKNA 1075
Cdd:cd02657   196 LPKYLTVQFVRFF----WKRDIQKkakilrKVKFPFE-LDLYELC----TPSGYYELVAVITHQGrSADSGHYVAWVRRK 266
                         330
                  ....*....|
gi 410355757 1076 ARQRWFKFDD 1085
Cdd:cd02657   267 NDGKWIKFDD 276
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
774-1087 4.37e-29

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 119.61  E-value: 4.37e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  774 PALTGLRNLGNTCYMNSILQCLCNAPH----LADYFNRNCYQDDINRSNLLGHKgevaeefgiimkaLWTGQYRYISPKD 849
Cdd:cd02671    22 LPFVGLNNLGNTCYLNSVLQVLYFCPGfkhgLKHLVSLISSVEQLQSSFLLNPE-------------KYNDELANQAPRR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  850 FKITIGKINDQFAGYSQQDSQELLLFLMDGLHEDLNKadnrkrykeenndhlddfkaaehawqkhkqlnesiivaLFQGQ 929
Cdd:cd02671    89 LLNALREVNPMYEGYLQHDAQEVLQCILGNIQELVEK--------------------------------------DFQGQ 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  930 FKSTVQCLTCHKKSRTFEAFMYLSLPLAS-----------------TSKCTLQDCLRLFSKEEKLTDNNRFYCSHCRARR 992
Cdd:cd02671   131 LVLRTRCLECETFTERREDFQDISVPVQEselskseesseispdpkTEMKTLKWAISQFASVERIVGEDKYFCENCHHYT 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  993 DSLKKIEIWKLPPVLLVHLKRFSYDGRWK------QKLQTSVDFPLEnLDLSQYVIGPKNNLkkYNLFSVSNHYGG-LDG 1065
Cdd:cd02671   211 EAERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKVNTPLLTPLK-LSLEEWSTKPKNDV--YRLFAVVMHSGAtISS 287
                         330       340
                  ....*....|....*....|..
gi 410355757 1066 GHYTAYCknaarqRWFKFDDHE 1087
Cdd:cd02671   288 GHYTAYV------RWLLFDDSE 303
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
778-1106 1.73e-28

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 117.04  E-value: 1.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  778 GLRNLGNTCYMNSILQCLCNAPHLADYFN--RNCYQDDIN--RSNLLGHKGEVAeefgiimKALWTGQYRY--------- 844
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDdlENKFPSDVVdpANDLNCQLIKLA-------DGLLSGRYSKpaslksend 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  845 -----ISPKDFKITIGKINDQFAGYSQQDSQELLLFLMDglhedlnKADNRKRYKEENNdhlddfkaaehawqkhkqLNE 919
Cdd:cd02658    74 pyqvgIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLID-------KLDRESFKNLGLN------------------PND 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  920 siivaLFQGQFKSTVQCLTCHKKSRTFEAFMYLSLPL------------ASTSKCTLQDCLRLFSKEEKLTDnnrfYCSH 987
Cdd:cd02658   129 -----LFKFMIEDRLECLSCKKVKYTSELSEILSLPVpkdeatekeegeLVYEPVPLEDCLKAYFAPETIED----FCST 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  988 CRARRDSLKKIEIWKLPPVLLVHLKRFSYDGRWKQ-KLQTSVDFPlenldlsqYVIGPknnlKKYNLFSVSNHYG-GLDG 1065
Cdd:cd02658   200 CKEKTTATKTTGFKTFPDYLVINMKRFQLLENWVPkKLDVPIDVP--------EELGP----GKYELIAFISHKGtSVHS 267
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 410355757 1066 GHYTAYCK--NAARQRWFKFDDHEVSDISVSSVKSSAAYILFY 1106
Cdd:cd02658   268 GHYVAHIKkeIDGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
778-1085 7.32e-25

Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 112.27  E-value: 7.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  778 GLRNLGNTCYMNSILQCLcnapHLADYFNRNCYQ--DDINRSNllghkGEVAEEFGIIMKALWTGQYRyISPKDFkiTIG 855
Cdd:COG5077   195 GLRNQGATCYMNSLLQSL----FFIAKFRKDVYGipTDHPRGR-----DSVALALQRLFYNLQTGEEP-VDTTEL--TRS 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  856 KINDQFAGYSQQDSQELLLFLMDGLhedlnkadnrkrykeENNdhlddfkaaehawqKHKQLNESIIVALFQGQFKSTVQ 935
Cdd:COG5077   263 FGWDSDDSFMQHDIQEFNRVLQDNL---------------EKS--------------MRGTVVENALNGIFVGKMKSYIK 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  936 CLTCHKKSRTFEAFMYLSLPLASTSkcTLQDCLRLFSKEEKLTDNNRFYCSHcRARRDSLKKIEIWKLPPVLLVHLKRFS 1015
Cdd:COG5077   314 CVNVNYESARVEDFWDIQLNVKGMK--NLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFE 390
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 410355757 1016 YDGRWKQ--KLQTSVDFPLEnLDLSQYV----IGPKNNLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDD 1085
Cdd:COG5077   391 YDFERDMmvKINDRYEFPLE-IDLLPFLdrdaDKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDD 465
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
778-1106 4.71e-23

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 99.36  E-value: 4.71e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  778 GLRNLGNTCYMNSILQCLCNAPHLADYFNRNcyqddinrsnllghkgevaeefgiimkalwtgqyryispkdfkitigki 857
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEF------------------------------------------------- 31
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  858 ndqfagYSQQDSQELLLFLMDGLhedlnkadnrkrykeenndhlddfkaaehawqkhkqlnESIIVALFQGQFKSTVQCL 937
Cdd:cd02662    32 ------LEQQDAHELFQVLLETL--------------------------------------EQLLKFPFDGLLASRIVCL 67
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  938 TCHKKSR-TFEAFMYLSLPL---ASTSKCTLQDCLRLFSKEEKLTDnnrFYCSHCrarrdslkKIEIWKLPPVLLVHLKR 1013
Cdd:cd02662    68 QCGESSKvRYESFTMLSLPVpnqSSGSGTTLEHCLDDFLSTEIIDD---YKCDRC--------QTVIVRLPQILCIHLSR 136
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757 1014 FSYDGRWK-QKLQTSVDFPLEnldLSQYvigpknnlkKYNLFSVSNHYGGLDGGHYTAY--------------------C 1072
Cdd:cd02662   137 SVFDGRGTsTKNSCKVSFPER---LPKV---------LYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreG 204
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 410355757 1073 KNAARQRWFKF-DDHEVSDISVSSVKSSAAYILFY 1106
Cdd:cd02662   205 PSSTSHPWWRIsDTTVKEVSESEVLEQKSAYMLFY 239
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
774-1085 1.67e-22

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 102.01  E-value: 1.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  774 PALTGLRNLGNTCYMNSILQCLCNAPHLADYF-NRNCYQDDINRSNLLGHKgevaeeFGIIMKALWTGQY--RYISPKDF 850
Cdd:cd02669   117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFlLYENYENIKDRKSELVKR------LSELIRKIWNPRNfkGHVSPHEL 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  851 KITIGKINDQFAGYSQQ-DSQELLLFLMDGLHEDLNKAdnrkrykeenndhlddfkaaehawqkhKQLNESIIVALFQGQ 929
Cdd:cd02669   191 LQAVSKVSKKKFSITEQsDPVEFLSWLLNTLHKDLGGS---------------------------KKPNSSIIHDCFQGK 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  930 FKSTVQCLTCHK---------------KSRTFEAFMYLS--LPLASTSKCTLQD-CLRLFSKEEKLtdnNRFYCSHCRAR 991
Cdd:cd02669   244 VQIETQKIKPHAeeegskdkffkdsrvKKTSVSPFLLLTldLPPPPLFKDGNEEnIIPQVPLKQLL---KKYDGKTETEL 320
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  992 RDSLKKIEIWKLPPVLLVHLKRFSYDGRWKQKLQTSVDFPLENLDLSQYVIGPKNNLK---KYNLfsVSN--HYGG-LDG 1065
Cdd:cd02669   321 KDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNlstKYNL--VANivHEGTpQED 398
                         330       340
                  ....*....|....*....|
gi 410355757 1066 GHYTAYCKNAARQRWFKFDD 1085
Cdd:cd02669   399 GTWRVQLRHKSTNKWFEIQD 418
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
778-1106 2.79e-22

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 98.34  E-value: 2.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  778 GLRNLGNTCYMNSILQCLC-NAPHLADY-----FNRNCYQDDINRSnllgHKGEVAEEFGIIMKALWTGQyryispkdfK 851
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILAlYLPKLDELlddlsKELKVLKNVIRKP----EPDLNQEEALKLFTALWSSK---------E 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  852 ITIGKINDQfagYSQQDSQELLLFLMDGLHEDLNKADNRKRYK--EENNDHLDDfkaaehawqkhkQLNEsIIVALFQGQ 929
Cdd:COG5533    68 HKVGWIPPM---GSQEDAHELLGKLLDELKLDLVNSFTIRIFKttKDKKKTSTG------------DWFD-IIIELPDQT 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  930 F---KSTVQCltchkksrTFEAFMYLslplaSTSKCTLqdclrlfskeeKLTDNNRFycsHCRARRDSLKKIEiwKLPPV 1006
Cdd:COG5533   132 WvnnLKTLQE--------FIDNMEEL-----VDDETGV-----------KAKENEEL---EVQAKQEYEVSFV--KLPKI 182
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757 1007 LLVHLKRFSYDGRwKQKLQTSVDFPLEnLDLSQYVIGPKNNLKKYNLFSVSNHYGGLDGGHYTAYCKnaARQRWFKFDDH 1086
Cdd:COG5533   183 LTIQLKRFANLGG-NQKIDTEVDEKFE-LPVKHDQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVK--KGGKWEKANDS 258
                         330       340
                  ....*....|....*....|...
gi 410355757 1087 EVSDISVSSVKSSA---AYILFY 1106
Cdd:COG5533   259 DVTPVSEEEAINEKaknAYLYFY 281
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
375-547 2.27e-11

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 66.79  E-value: 2.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   375 LNISTPVEPVAASKSDVSPIIQ-----PAPSIKNVPQIDRTKKPAvKLPEEHRIKSEstnhEQQSPQsgkVIPDRSTKPV 449
Cdd:TIGR02794   18 LILGSLYHSVKPEPGGGAEIIQavlvdPGAVAQQANRIQQQKKPA-AKKEQERQKKL----EQQAEE---AEKQRAAEQA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   450 VFSPTLMLTDEEKARIHAETAllmeknKQQKELRERQQEEQKEKlrkEEQEQKAKKKQEAEENEITEKQQKAREEMEKKE 529
Cdd:TIGR02794   90 RQKELEQRAAAEKAAKQAEQA------AKQAEEKQKQAEEAKAK---QAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKA 160
                          170
                   ....*....|....*...
gi 410355757   530 SEQAKKEDKETSAKRGKE 547
Cdd:TIGR02794  161 AAEAKKKAEEAKKKAEAE 178
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
865-1085 1.22e-08

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 56.80  E-value: 1.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  865 SQQDSQELLLFLMDGLHedlnkadnrkrykeenndhlDDFKAAEHAWQKHKQlNESIIVALFQGQFkSTVQCLTcHKKSR 944
Cdd:cd02665    21 QQQDVSEFTHLLLDWLE--------------------DAFQAAAEAISPGEK-SKNPMVQLFYGTF-LTEGVLE-GKPFC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  945 TFEafMYLSLPLASTSKCTLQDCLR--LFSKEEKLTDNNRFYCSHCRARRDslkkieiwKLPPVLLVHLKRFSYDGRWKQ 1022
Cdd:cd02665    78 NCE--TFGQYPLQVNGYGNLHECLEaaMFEGEVELLPSDHSVKSGQERWFT--------ELPPVLTFELSRFEFNQGRPE 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 410355757 1023 KLQTSVDFPLEnldLSQYvigpknnlkKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDD 1085
Cdd:cd02665   148 KIHDKLEFPQI---IQQV---------PYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYND 198
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
779-1106 1.68e-08

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 56.77  E-value: 1.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  779 LRNLGNTCYMNSILQCLCnaphladyfnrncyqddinrsnllghkgevaeefgiimkalwtgqyryispkdfkiTIGKIN 858
Cdd:cd02673     2 LVNTGNSCYFNSTMQALS--------------------------------------------------------SIGKIN 25
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  859 DQFAGYSQQDSQELLLFL---MDGLHEdlNKADNRKRYKEENndhlddfkaaehawqkhKQLNEsiiVALFQGQFKSTVQ 935
Cdd:cd02673    26 TEFDNDDQQDAHEFLLTLleaIDDIMQ--VNRTNVPPSNIEI-----------------KRLNP---LEAFKYTIESSYV 83
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  936 CLTCHKKSRTFEAFMYLSLPLASTSKCTLQDclrLFSKEEKLTDNNRfYCSHCRARRDSLKKiEIWKLPPVLLVHLKRFs 1015
Cdd:cd02673    84 CIGCSFEENVSDVGNFLDVSMIDNKLDIDEL---LISNFKTWSPIEK-DCSSCKCESAISSE-RIMTFPECLSINLKRY- 157
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757 1016 ydgrwkqKLQTSVdfpLENLDLSQYVIGP-KNNLKKYNLFSVSNHYG-GLDGGHYTAYCKNAAR-QRWFKFDD---HEVS 1089
Cdd:cd02673   158 -------KLRIAT---SDYLKKNEEIMKKyCGTDAKYSLVAVICHLGeSPYDGHYIAYTKELYNgSSWLYCSDdeiRPVS 227
                         330
                  ....*....|....*..
gi 410355757 1090 DISVSSVKSSAAYILFY 1106
Cdd:cd02673   228 KNDVSTNARSSGYLIFY 244
PTZ00121 PTZ00121
MAEBL; Provisional
411-574 4.27e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.84  E-value: 4.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  411 KKPAVKLPEEHRIKSESTNHEQQSPQSGKVIPDRSTKPVvfsptlMLTDEEKARIHAETALLMEKNKQQKELRERQQEEQ 490
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV------MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  491 K--EKLRKEEQEQKAKKKQ---EAEENEITEKQQKAREEMEKKESEQAKKEDKEtsaKRGKEiTGVKRQSKSEHETSDAK 565
Cdd:PTZ00121 1633 KkvEQLKKKEAEEKKKAEElkkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED---EKKAA-EALKKEAEEAKKAEELK 1708

                  ....*....
gi 410355757  566 KSVEDRGKR 574
Cdd:PTZ00121 1709 KKEAEEKKK 1717
PTZ00121 PTZ00121
MAEBL; Provisional
401-587 1.25e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.30  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  401 IKNVPQIDRTKKPAVKLPEEHRIKSESTNHEQQSPQSGKVIPDRSTKPVVFSPTLMLTDEEKARIHAETALLMEKNKQQ- 479
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKa 1677
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  480 KELRERQQEEQK---------------EKLRKEEQEQKAKKKQ---EAEENEITEKQQKAREEMEKKESEQAKKEDKETS 541
Cdd:PTZ00121 1678 EEAKKAEEDEKKaaealkkeaeeakkaEELKKKEAEEKKKAEElkkAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 410355757  542 --AKRGKEITGVKRQSKSEHETSDAKKSVEDRGKRCPTPEIQKKSTGD 587
Cdd:PTZ00121 1758 kiAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFD 1805
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
373-560 1.31e-07

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 55.93  E-value: 1.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   373 GPLNISTPVEPVAASKSDVSPIIQP---APSIK-NVPQIDRTKKPAVKLPEEHRIKSEstnhEQQSPQSgkviPDRSTKP 448
Cdd:pfam03154  471 GPPPITPPSGPPTSTSSAMPGIQPPssaSVSSSgPVPAAVSCPLPPVQIKEEALDEAE----EPESPPP----PPRSPSP 542
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   449 vvfSPTLMLTDEekariHAEtallmEKNKQQKELRERQQEEQKEKL--RKEEQEQKAKKKQEAEENEITEKQQKAREEme 526
Cdd:pfam03154  543 ---EPTVVNTPS-----HAS-----QSARFYKHLDRGYNSCARTDLyfMPLAGSKLAKKREEALEKAKREAEQKAREE-- 607
                          170       180       190
                   ....*....|....*....|....*....|....
gi 410355757   527 kKESEQAKKEDKETSAKRGKEITGVKRQSKSEHE 560
Cdd:pfam03154  608 -KEREKEKEKEREREREREREAERAAKASSSSHE 640
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
462-573 1.51e-07

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 54.85  E-value: 1.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   462 KARIHAETAllmEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKEDKETS 541
Cdd:TIGR02794   72 KLEQQAEEA---EKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEA 148
                           90       100       110
                   ....*....|....*....|....*....|..
gi 410355757   542 AKRGKEITGVKRQSKSEHETSDAKKSVEDRGK 573
Cdd:TIGR02794  149 AKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAK 180
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
453-539 1.55e-07

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 51.97  E-value: 1.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   453 PTLMLTDEEKA-RIHAETALLMEKNKQQKELRERQQEEQkEKLRKEEQEQKA---KKKQEAEENEITEKQQKAREEMEKK 528
Cdd:pfam05672    2 PSAGTTDAEEAaRILAEKRRQAREQREREEQERLEKEEE-ERLRKEELRRRAeeeRARREEEARRLEEERRREEEERQRK 80
                           90
                   ....*....|.
gi 410355757   529 ESEQAKKEDKE 539
Cdd:pfam05672   81 AEEEAEEREQR 91
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
875-1085 1.84e-07

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 54.20  E-value: 1.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   875 FLMDGLHEDLNKAdnrkrykeenndhlddfkaaehawQKHKQLNESIIVALFQGQFKSTVQCLTC-HKKSRTFEAFMY-L 952
Cdd:pfam13423  105 FLLDQLSSEENST------------------------PPNPSPAESPLEQLFGIDAETTIRCSNCgHESVRESSTHVLdL 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   953 SLPLASTS------KCTLQDCLRLFSKEEKLTdnnRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKRFSYDgrWKQKLQT 1026
Cdd:pfam13423  161 IYPRKPSSnnkkppNQTFSSILKSSLERETTT---KAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE--WRQLWKT 235
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 410355757  1027 SVDFPLE-NLDLSQYVIGPkNNLKKYNLFS-VSNHYGGLDGGHYTAYCK-------NAARQRWFKFDD 1085
Cdd:pfam13423  236 PGWLPPEiGLTLSDDLQGD-NEIVKYELRGvVVHIGDSGTSGHLVSFVKvadseleDPTESQWYLFND 302
Agg_substance NF033875
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ...
309-614 1.92e-07

LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.


Pssm-ID: 411439 [Multi-domain]  Cd Length: 1306  Bit Score: 55.49  E-value: 1.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  309 PQYTTNAKVTPPPRRQN--------EEVSISLDFT-YPS-LEESIPSKPAAQTPPASIEVDENIELISDQNERmgplniS 378
Cdd:NF033875   50 PGTTTVQPDNPDPQSGSetpktavsEEATVQKDTTsQPTkVEEVASEKNGAEQSSATPNDTTNAQQPTVGAEK------S 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  379 TPVEPVAASKSDVSPIIQPApsiknvpqidrtkkpAVKLPEEHRIKSESTNHEQQSPQSGKVIPDRSTKP---VVFSPTl 455
Cdd:NF033875  124 AQEQPVVSPETTNEPLGQPT---------------EVAPAENEANKSTSIPKEFETPDVDKAVDEAKKDPnitVVEKPA- 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  456 mltdEEKARIHAETalLMEKNKQQKELrerqQEEQKEKLRKEEQEQKAKKKQEAEEN-EITEKQQKAREEMEKKESEQAK 534
Cdd:NF033875  188 ----EDLGNVSSKD--LAAKEKEVDQL----QKEQAKKIAQQAAELKAKNEKIAKENaEIAAKNKAEKERYEKEVAEYNK 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  535 KEDKETSAKRGKEITGVKRQSKSeheTSDAKKSVEDRGKRCPTPEIQKKSTGDVP----------HTSVTGDSGSGKPFK 604
Cdd:NF033875  258 HKNENGYVNEAISKNLVFDQSVV---TKDTKISSIKGGKFIKATDFNKVNAGDSKdiftklskdmGGKATGNFQNSFVKE 334
                         330
                  ....*....|
gi 410355757  605 IKGQPESGIL 614
Cdd:NF033875  335 ANLGSNGGYA 344
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
476-574 2.10e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 54.43  E-value: 2.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  476 NKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKEdkETSAKRGKEITGVKRQS 555
Cdd:PRK09510   74 AKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQA--EEAAAKAAAAAKAKAEA 151
                          90
                  ....*....|....*....
gi 410355757  556 KSEHETSDAKKSVEDRGKR 574
Cdd:PRK09510  152 EAKRAAAAAKKAAAEAKKK 170
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
460-587 5.84e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 53.27  E-value: 5.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  460 EEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRKEEQEQKA----------KKKQEAEENEITEKQQKAREEMEKKE 529
Cdd:PRK09510   62 EQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQlekerlaaqeQKKQAEEAAKQAALKQKQAEEAAAKA 141
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 410355757  530 SEQAKKEDK------ETSAKRGKEITGVKRQSKSEHET-SDAKKSVEDRGKRCPTPEIQKKSTGD 587
Cdd:PRK09510  142 AAAAKAKAEaeakraAAAAKKAAAEAKKKAEAEAAKKAaAEAKKKAEAEAAAKAAAEAKKKAEAE 206
PTZ00121 PTZ00121
MAEBL; Provisional
408-587 7.53e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 7.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  408 DRTKKPAVKLPEEHRIKSESTNHEQQSPQSGKVIPDRSTKPVVFSPTLMLTDEEKARiHAETALLMEKNKQQKELRERQQ 487
Cdd:PTZ00121 1222 DAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR-KADELKKAEEKKKADEAKKAEE 1300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  488 EEQKEKLRKEEQEQK----AKKKQEAEENEITEKQQKARE-----EMEKKESEQAKKEDKetsAKRGKEITGVKRQSKSE 558
Cdd:PTZ00121 1301 KKKADEAKKKAEEAKkadeAKKKAEEAKKKADAAKKKAEEakkaaEAAKAEAEAAADEAE---AAEEKAEAAEKKKEEAK 1377
                         170       180
                  ....*....|....*....|....*....
gi 410355757  559 HETSDAKKSVEDRGKrcpTPEIQKKSTGD 587
Cdd:PTZ00121 1378 KKADAAKKKAEEKKK---ADEAKKKAEED 1403
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
474-570 9.28e-07

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 50.42  E-value: 9.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   474 EKNKQQKELRERQQEEQKEklRKEEQEQKAKKKQEAEEneitEKQQKAREEMEKKESEQAKKEDKETsaKRGKEITGVKR 553
Cdd:pfam09756   15 EAKRQQREAEEEEREEREK--LEEKREEEYKEREEREE----EAEKEKEEEERKQEEEQERKEQEEY--EKLKSQFVVEE 86
                           90
                   ....*....|....*..
gi 410355757   554 QSKSEHETSDAKKSVED 570
Cdd:pfam09756   87 EGTDKLSAEDESQLLED 103
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
472-574 1.01e-06

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 52.73  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  472 LMEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKEDKETSAKrgkeitgV 551
Cdd:COG3064     4 ALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEA-------A 76
                          90       100
                  ....*....|....*....|...
gi 410355757  552 KRQSKSEHETSDAKKSVEDRGKR 574
Cdd:COG3064    77 KKLAEAEKAAAEAEKKAAAEKAK 99
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
474-606 1.35e-06

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 49.69  E-value: 1.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   474 EKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKED----KETSAKRGKEIT 549
Cdd:pfam11600   21 DKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEKERREKKEKDEKEKAEklrlKEEKRKEKQEAL 100
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   550 GVKRQSKSEHETSDAKKSVEDR---GKRCPTPEIQKKSTGDVPHTsVTGDSGSGKPFKIK 606
Cdd:pfam11600  101 EAKLEEKRKKEEEKRLKEEEKRikaEKAEITRFLQKPKTQQAPKT-LAGSCGKFAPFEIK 159
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
474-574 1.94e-06

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 51.38  E-value: 1.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   474 EKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKEDKETSAKRGKEITGVKR 553
Cdd:TIGR02794   74 EQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAE 153
                           90       100
                   ....*....|....*....|.
gi 410355757   554 QSKSEHETSDAKKSVEDRGKR 574
Cdd:TIGR02794  154 EEAKAKAAAEAKKKAEEAKKK 174
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
459-594 2.55e-06

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 51.54  E-value: 2.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   459 DEEKARIHAETAllmEKN--KQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKareEMEKKESEQAK-K 535
Cdd:pfam05262  228 DADKAQQKADFA---QDNadKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQI---EIKKNDEEALKaK 301
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 410355757   536 EDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKRCPTPEIQKKSTGDVPHTSVT 594
Cdd:pfam05262  302 DHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDAIDSSN 360
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
477-584 2.55e-06

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 51.75  E-value: 2.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  477 KQQKELRERQQEEQK-EKLrKEEQEQKAKKKQEAEENEITEKQQKAREEME--KKESEQAKKEDKEtsaKRGKEITGVKr 553
Cdd:PRK00409  531 ELEQKAEEAEALLKEaEKL-KEELEEKKEKLQEEEDKLLEEAEKEAQQAIKeaKKEADEIIKELRQ---LQKGGYASVK- 605
                          90       100       110
                  ....*....|....*....|....*....|.
gi 410355757  554 qsksEHETSDAKKSVEDRGKrcPTPEIQKKS 584
Cdd:PRK00409  606 ----AHELIEARKRLNKANE--KKEKKKKKQ 630
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
473-583 3.11e-06

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 50.61  E-value: 3.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   473 MEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKEDKETSAKRGKEITGVK 552
Cdd:TIGR02794   62 AAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAE 141
                           90       100       110
                   ....*....|....*....|....*....|.
gi 410355757   553 RQSKSEhetsdAKKSVEDRGKRCPTPEIQKK 583
Cdd:TIGR02794  142 RKAKEE-----AAKQAEEEAKAKAAAEAKKK 167
PTZ00121 PTZ00121
MAEBL; Provisional
461-584 3.47e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 3.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  461 EKARIHAETALLMEKNKQQKELRERQQEEQK----EKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKE 536
Cdd:PTZ00121 1381 DAAKKKAEEKKKADEAKKKAEEDKKKADELKkaaaAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE 1460
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 410355757  537 DKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKRcpTPEIQKKS 584
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK--ADEAKKAA 1506
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
459-543 8.82e-06

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 49.49  E-value: 8.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  459 DEEKARIHAETAL-LMEKNKQQKELRERQQEEQKEKLRKEEQ------EQKAKKKQEAEEN-EITEKQQKAR-EEMEKKE 529
Cdd:COG2268   222 EAEEAELEQEREIeTARIAEAEAELAKKKAEERREAETARAEaeaayeIAEANAEREVQRQlEIAEREREIElQEKEAER 301
                          90
                  ....*....|....
gi 410355757  530 SEQAKKEDKETSAK 543
Cdd:COG2268   302 EEAELEADVRKPAE 315
PTZ00121 PTZ00121
MAEBL; Provisional
461-573 1.05e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  461 EKARIHAETALLMEKnKQQKELRERQQEEQKEKLRKEEQEQKA---KKKQE----AEE-NEITEKQQKAREEMEKKESEQ 532
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAE-AAADEAEAAEEKAEAAEKKKEEAKKKAdaaKKKAEekkkADEaKKKAEEDKKKADELKKAAAAK 1417
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 410355757  533 AKKEDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGK 573
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK 1458
PTZ00121 PTZ00121
MAEBL; Provisional
457-573 1.22e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  457 LTDEEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEE----NEITEKQQKAREEMEKKESEQ 532
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkkaEEKKKAEEAKKAEEDKNMALR 1581
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 410355757  533 AKKEDKETSAKRGKEITGVKRQSKsEHETSDAKKSVEDRGK 573
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEK-KMKAEEAKKAEEAKIK 1621
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
470-587 1.32e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 48.65  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  470 ALLMEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITE-KQQKAREEMEKKESEQAKK----EDKETSAKR 544
Cdd:PRK09510   59 AVVEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQlEKERLAAQEQKKQAEEAAKqaalKQKQAEEAA 138
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 410355757  545 GKEITGVKRQSKSEHE-TSDAKKSVEDRGKRCPTPEIQKKSTGD 587
Cdd:PRK09510  139 AKAAAAAKAKAEAEAKrAAAAAKKAAAEAKKKAEAEAAKKAAAE 182
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
457-574 1.34e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  457 LTDEEKARIHAETALL-MEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKK 535
Cdd:COG1196   297 LARLEQDIARLEERRReLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 410355757  536 EDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKR 574
Cdd:COG1196   377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
PTZ00121 PTZ00121
MAEBL; Provisional
474-584 1.34e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  474 EKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREemEKKESEQAKKEDKETSaKRGKEitgVKR 553
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE--EKKKADEAKKKAEEDK-KKADE---LKK 1412
                          90       100       110
                  ....*....|....*....|....*....|.
gi 410355757  554 QSKSEHETSDAKKSVEDRGKrcpTPEIQKKS 584
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKK---ADEAKKKA 1440
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
460-612 1.43e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 48.65  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  460 EEKARIHAETALLmEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKK-ESEQAKKEDK 538
Cdd:PRK09510  135 EEAAAKAAAAAKA-KAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKaEAEAKKKAAA 213
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 410355757  539 ETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKRCPtpeiQKKSTGDVPHTSVTGDSGSGKPFKIKGQPESG 612
Cdd:PRK09510  214 EAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAA----AAKAAAEVDDLFGGLDSGKNAPKTGGGAKGNG 283
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
485-539 1.67e-05

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 48.33  E-value: 1.67e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 410355757   485 RQQEEqkEKLRKEEQEQKAKKKQEAEEneitEKQQKAREEMEKKES--EQAKKEDKE 539
Cdd:pfam07946  266 REEEI--EKIKKAAEEERAEEAQEKKE----EAKKKEREEKLAKLSpeEQRKYEEKE 316
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
459-544 1.70e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 1.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  459 DEEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKEDK 538
Cdd:COG1196   284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363

                  ....*.
gi 410355757  539 ETSAKR 544
Cdd:COG1196   364 EEALLE 369
Caldesmon pfam02029
Caldesmon;
460-611 1.75e-05

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 48.71  E-value: 1.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   460 EEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKqeaeeneitEKQQKAREEMEKKESEQAKKEDKE 539
Cdd:pfam02029  102 ERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTE---------VRQAEEEGEEEEDKSEEAEEVPTE 172
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 410355757   540 TSAKrgKEITGVKrqSKSEHETSDAKKSVEDRGKRCPTPEIQKKSTGDVPHTSVTGDSGSGKPFKIKGQPES 611
Cdd:pfam02029  173 NFAK--EEVKDEK--IKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEA 240
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
192-304 1.89e-05

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 44.40  E-value: 1.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   192 MTDKNISLIimDARRMQDYQDSCILHSLSVPEEAIspgvtasWIEAHLPDDSKDTWKKRGNVEYVVLLDWFSSAKDLqig 271
Cdd:pfam00581    1 LEDGKVVLI--DVRPPEEYAKGHIPGAVNVPLSSL-------SLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAA--- 68
                           90       100       110
                   ....*....|....*....|....*....|...
gi 410355757   272 tTLRSLKDALFKwesktvlrnEPLVLEGGYENW 304
Cdd:pfam00581   69 -AAALLKALGYK---------NVYVLDGGFEAW 91
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
459-571 1.89e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 48.97  E-value: 1.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   459 DEEKARiHAETALLMEKNKQQKELRERQQE-EQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKED 537
Cdd:pfam17380  441 EEERAR-EMERVRLEEQERQQQVERLRQQEeERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLE 519
                           90       100       110
                   ....*....|....*....|....*....|....
gi 410355757   538 KETSaKRGKEITGVKRQSKSEHETSDAKKSVEDR 571
Cdd:pfam17380  520 KEME-ERQKAIYEEERRREAEEERRKQQEMEERR 552
PTZ00121 PTZ00121
MAEBL; Provisional
461-583 2.01e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  461 EKARIHAETALLMEKNKQQKELRERQQEEQK--EKLRKEEQEQK----AKKKQEAEENEITEKQQKAREEMEKKESEQAK 534
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEAKKADEAKKKAEEAKKkaDEAKKAAEAKKkadeAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK 1546
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 410355757  535 KEDKetsAKRGKEITGVKRQSKSEhetsDAKKSVEDRGKRCPTPEIQKK 583
Cdd:PTZ00121 1547 KADE---LKKAEELKKAEEKKKAE----EAKKAEEDKNMALRKAEEAKK 1588
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
455-574 2.01e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  455 LMLTDEEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAK 534
Cdd:COG1196   290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 410355757  535 KEdKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKR 574
Cdd:COG1196   370 AE-AELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
470-573 2.07e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.22  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  470 ALLMEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKEDKETSAKR-GKEI 548
Cdd:COG4942   150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEElEALI 229
                          90       100
                  ....*....|....*....|....*
gi 410355757  549 TGVKRQSKSEHETSDAKKSVEDRGK 573
Cdd:COG4942   230 ARLEAEAAAAAERTPAAGFAALKGK 254
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
459-665 2.35e-05

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 48.50  E-value: 2.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  459 DEEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRK--EEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKE 536
Cdd:COG3064    65 EQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKeaEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAA 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  537 DKETSAKRGKEITGVKRQSKSEHETSDAKK-SVEDRGKRCPTPEIQKKSTGDVPHTSVTGDSGSGKPFKIKGQPESGILR 615
Cdd:COG3064   145 EAEAAAKAEAEAARAAAAAAAAAAAAAARAaAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAAR 224
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 410355757  616 TGTFREDTDDTERNKAQREPLTRARSEEMGRIVPGLPSGWAKFLDPITGT 665
Cdd:COG3064   225 AAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAAL 274
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
343-509 3.02e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 48.22  E-value: 3.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   343 IPSKPAAQTPPASIEVDENIELISDQNERMGPLNISTPVepvAASKSDVSPIIQpapsIKNVPqIDRTKKPAVKLPEEHR 422
Cdd:pfam03154  468 VPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPV---PAAVSCPLPPVQ----IKEEA-LDEAEEPESPPPPPRS 539
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   423 IKSEST-----NHEQQSPQSGKVIpDR-----STKPVVFSPtLMLTDEEKARIHAETALLMEKNKQQKELRERQQEEQKE 492
Cdd:pfam03154  540 PSPEPTvvntpSHASQSARFYKHL-DRgynscARTDLYFMP-LAGSKLAKKREEALEKAKREAEQKAREEKEREKEKEKE 617
                          170
                   ....*....|....*..
gi 410355757   493 KLRKEEQEQKAKKKQEA 509
Cdd:pfam03154  618 REREREREREAERAAKA 634
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
459-573 3.02e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 47.88  E-value: 3.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  459 DEEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRKEEQEQK----AKKKQEAEENEITEKQQKAREEMEKKESEQAK 534
Cdd:PRK09510   97 AAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKaaaaAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAA 176
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 410355757  535 KEDKETSAKRGKEITGVKRQSKSEHE-TSDAKKSVEDRGK 573
Cdd:PRK09510  177 KKAAAEAKKKAEAEAAAKAAAEAKKKaEAEAKKKAAAEAK 216
PTZ00121 PTZ00121
MAEBL; Provisional
461-592 3.62e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 3.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  461 EKARIHAETALLMEKNKQQKELRE-----------RQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKArEEMEKKE 529
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIRKfeearmahfarRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKA-DEAKKKA 1311
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 410355757  530 SEQAKKEDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKRCPTPEIQKKSTGDVPHTS 592
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374
PTZ00121 PTZ00121
MAEBL; Provisional
461-584 3.71e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 3.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  461 EKARIHAETALLM--EKNKQQKELRERQQEEQK-EKLRK--EEQEQKAK--KKQEAEENEITEKQQKARE-----EMEKK 528
Cdd:PTZ00121 1360 EAAEEKAEAAEKKkeEAKKKADAAKKKAEEKKKaDEAKKkaEEDKKKADelKKAAAAKKKADEAKKKAEEkkkadEAKKK 1439
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 410355757  529 ESEQAKKEDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKrcpTPEIQKKS 584
Cdd:PTZ00121 1440 AEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK---ADEAKKKA 1492
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
462-531 4.23e-05

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 45.21  E-value: 4.23e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 410355757  462 KARIHAETALLMEKNKQQKELRERQQE--EQKEKLRKEE----QEQKAKKKQE--AEENEITEKQQKAREEMEKKESE 531
Cdd:COG2825    39 PEGKAAQKKLEKEFKKRQAELQKLEKElqALQEKLQKEAatlsEEERQKKERElqKKQQELQRKQQEAQQDLQKRQQE 116
DUF4355 pfam14265
Domain of unknown function (DUF4355); This family of proteins is found in bacteria and viruses. ...
459-535 4.99e-05

Domain of unknown function (DUF4355); This family of proteins is found in bacteria and viruses. Proteins in this family are typically between 180 and 214 amino acids in length.


Pssm-ID: 405026 [Multi-domain]  Cd Length: 119  Bit Score: 43.83  E-value: 4.99e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 410355757   459 DEEKARIHAEtALLMEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEiTEKQQKAREEMEKKESEQAKK 535
Cdd:pfam14265    1 DSEVDKIVAK-ALATKKNNLEKEIEDEIKEAKKLAKMNAEEKAKYELEKLQKELE-EEKAELARKELKAEARKMLSE 75
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
441-535 6.36e-05

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 46.41  E-value: 6.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   441 IPDRSTKPVVFSPtlmltdeeKARIHAETALLMEKNKQQKELRERQQEEqkeklRKEEQEQKAKKKQEAEENEITEKQQK 520
Cdd:pfam07946  244 LIDKLAKRAKLRP--------EALKKAKKTREEEIEKIKKAAEEERAEE-----AQEKKEEAKKKEREEKLAKLSPEEQR 310
                           90
                   ....*....|....*
gi 410355757   521 AREEMEKKesEQAKK 535
Cdd:pfam07946  311 KYEEKERK--KEQRK 323
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
459-573 6.59e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 6.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  459 DEEKARIHAETALLMEKNKQQKELR--ERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESE--QAK 534
Cdd:COG1196   379 EELEELAEELLEALRAAAELAAQLEelEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEleEEE 458
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 410355757  535 KEDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGK 573
Cdd:COG1196   459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
PTZ00121 PTZ00121
MAEBL; Provisional
461-571 6.59e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 6.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  461 EKARIHAETALLMEKNKQQKELRERQQEEQK---EKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKED 537
Cdd:PTZ00121 1421 DEAKKKAEEKKKADEAKKKAEEAKKADEAKKkaeEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAD 1500
                          90       100       110
                  ....*....|....*....|....*....|....
gi 410355757  538 KETSAKRGKEITGVKRQSKSEHETSDAKKSVEDR 571
Cdd:PTZ00121 1501 EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK 1534
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
460-569 7.34e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 47.13  E-value: 7.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  460 EEKARiHAEtALLMEKNKQQKELrerqqEEQKEKLrkEEQEQKAKKKQEAEENEITEkqqKAREEMEKKESEQAKKEDKE 539
Cdd:PRK00409  533 EQKAE-EAE-ALLKEAEKLKEEL-----EEKKEKL--QEEEDKLLEEAEKEAQQAIK---EAKKEADEIIKELRQLQKGG 600
                          90       100       110
                  ....*....|....*....|....*....|
gi 410355757  540 TSAKRGKEITGVKRQSKSEHETSDAKKSVE 569
Cdd:PRK00409  601 YASVKAHELIEARKRLNKANEKKEKKKKKQ 630
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
457-552 7.69e-05

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 46.03  E-value: 7.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  457 LTDEEKAriHAETALLMEKNKQQKELRERQQEEQKEKLRK-----EEQEQKAKKKQEAEENEITEKQQKAREEMEKKESE 531
Cdd:cd16269   193 LTEKEKE--IEAERAKAEAAEQERKLLEEQQRELEQKLEDqersyEEHLRQLKEKMEEERENLLKEQERALESKLKEQEA 270
                          90       100
                  ....*....|....*....|.
gi 410355757  532 QAKKEDKETSAKRGKEITGVK 552
Cdd:cd16269   271 LLEEGFKEQAELLQEEIRSLK 291
MAT1 pfam06391
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
457-552 8.09e-05

CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.


Pssm-ID: 461894 [Multi-domain]  Cd Length: 202  Bit Score: 44.92  E-value: 8.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   457 LTDEEKARIHAETALLmeknKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEE------------NEITEKQQKAREE 524
Cdd:pfam06391   80 LILKNKMKLSQEEEEL----EELLELEKREKEERRKEEKQEEEEEKEKKEKAKQElidelmtsnkdaEEIIAQHKKTAKK 155
                           90       100
                   ....*....|....*....|....*...
gi 410355757   525 MEKKESEQAKKEDKETSAKRGKEITGVK 552
Cdd:pfam06391  156 RKSERRRKLEELNRVLEQKPTQFSTGIK 183
PRK12704 PRK12704
phosphodiesterase; Provisional
461-539 1.02e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.31  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  461 EKARIHAETALLMEKNKQQKELRERQQE-EQKEK--LRKEEQEQKAKKKQEAEENEITEKQQKA---REEMEKKESEQAK 534
Cdd:PRK12704   56 KEALLEAKEEIHKLRNEFEKELRERRNElQKLEKrlLQKEENLDRKLELLEKREEELEKKEKELeqkQQELEKKEEELEE 135

                  ....*
gi 410355757  535 KEDKE 539
Cdd:PRK12704  136 LIEEQ 140
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
459-574 1.10e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  459 DEEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKEDK 538
Cdd:COG1196   263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 410355757  539 ETSAKRGKEitgvKRQSKSEHETSDAKKSVEDRGKR 574
Cdd:COG1196   343 EEELEEAEE----ELEEAEAELAEAEEALLEAEAEL 374
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
460-536 1.15e-04

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 46.02  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  460 EEKARIHAETALLMEKNKQQKEL--------RERQQE-EQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKkes 530
Cdd:COG2268   257 AETARAEAEAAYEIAEANAEREVqrqleiaeREREIElQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIR--- 333

                  ....*.
gi 410355757  531 EQAKKE 536
Cdd:COG2268   334 AKGLAE 339
PTZ00121 PTZ00121
MAEBL; Provisional
459-574 1.17e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  459 DEEKARIHAETALLMEKNKQQKELRERQQEEQKEKL----RKEEQEQKAKK-KQEAEENEITEKQQKAREEMEKKESEQA 533
Cdd:PTZ00121 1345 AEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAdaakKKAEEKKKADEaKKKAEEDKKKADELKKAAAAKKKADEAK 1424
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 410355757  534 KKEDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKR 574
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK 1465
PTZ00121 PTZ00121
MAEBL; Provisional
460-573 1.17e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  460 EEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKEDKE 539
Cdd:PTZ00121 1397 KKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAK 1476
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 410355757  540 TSAKRGKEITGVKRQSKSEHETSD-AKKSVEDRGK 573
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADeAKKAAEAKKK 1511
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
459-643 1.44e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 45.80  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  459 DEEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQ---------QKAREEMEKKE 529
Cdd:COG3064    54 EEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAaaaaekekaEEAKRKAEEEA 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  530 SEQAKKEDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKRCPTPEIQKKSTGDVPHTSVTGDSGSGKPFKIKGQP 609
Cdd:COG3064   134 KRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAAD 213
                         170       180       190
                  ....*....|....*....|....*....|....
gi 410355757  610 ESGILRTGTFREDTDDTERNKAQREPLTRARSEE 643
Cdd:COG3064   214 AALLALAVAARAAAASREAALAAVEATEEAALGG 247
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1002-1106 1.61e-04

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 44.44  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757 1002 KLPPVLLVHLKRFSYDGRWKQKLQTSVDFPLEnLDL----------------------SQYVIGPKNNLKKYNLFSVSNH 1059
Cdd:cd02670    97 KAPSCLIICLKRYGKTEGKAQKMFKKILIPDE-IDIpdfvaddpracskcqlecrvcyDDKDFSPTCGKFKLSLCSAVCH 175
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 410355757 1060 YG-GLDGGHYTAYCK-----------NAARQRWFKFDDHEVSDISVSSVKSSA------AYILFY 1106
Cdd:cd02670   176 RGtSLETGHYVAFVRygsysltetdnEAYNAQWVFFDDMADRDGVSNGFNIPAarlledPYMLFY 240
PTZ00121 PTZ00121
MAEBL; Provisional
461-584 1.80e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  461 EKARIHAETALLMEKNKQQKELRERQQEEQKEKLR-KEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKEDKE 539
Cdd:PTZ00121 1305 DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEeAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK 1384
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 410355757  540 TSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKRcpTPEIQKKS 584
Cdd:PTZ00121 1385 KKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKK--ADEAKKKA 1427
PTZ00121 PTZ00121
MAEBL; Provisional
460-569 1.88e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  460 EEKARIHAETALLMEKNKQQKELRERQQEEQK-EKLRKEEQEQKAKKKQEAEEneiTEKQQKAREEMEKKESEQAKKEDK 538
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKaDEAKKAEEAKKADEAKKAEE---AKKADEAKKAEEKKKADELKKAEE 1556
                          90       100       110
                  ....*....|....*....|....*....|.
gi 410355757  539 etsAKRGKEITGVKRQSKSEHETSDAKKSVE 569
Cdd:PTZ00121 1557 ---LKKAEEKKKAEEAKKAEEDKNMALRKAE 1584
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
459-559 1.88e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 44.88  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  459 DEEKARIHAETALLmEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEkKESEQAKKEDK 538
Cdd:cd16269   181 AEAEAILQADQALT-EKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKME-EERENLLKEQE 258
                          90       100
                  ....*....|....*....|.
gi 410355757  539 ETSAKRGKEITGVKRQSKSEH 559
Cdd:cd16269   259 RALESKLKEQEALLEEGFKEQ 279
PTZ00121 PTZ00121
MAEBL; Provisional
460-573 1.89e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  460 EEKARIHAETALLMEKNKQQKELRERQQEEQK---------EKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKES 530
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKadeakkkaeEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE 1480
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 410355757  531 EQAKKEDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGK 573
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK 1523
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
457-548 2.39e-04

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 44.59  E-value: 2.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   457 LTDEEKArIHAETALLMEKNKQQKELRERQQEEQK----EKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQ 532
Cdd:pfam02841  199 LTAKEKA-IEAERAKAEAAEAEQELLREKQKEEEQmmeaQERSYQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEEL 277
                           90
                   ....*....|....*.
gi 410355757   533 AKKEDKETSAKRGKEI 548
Cdd:pfam02841  278 LKEGFKTEAESLQKEI 293
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
457-571 2.40e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.52  E-value: 2.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   457 LTDEEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRKEE-------------QEQKAKKKQEAEENEITEKQ----- 518
Cdd:pfam13868   82 IEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEkqrqlreeidefnEEQAEWKELEKEEEREEDERileyl 161
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 410355757   519 -QKAREEMEKKESEQAKKEDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDR 571
Cdd:pfam13868  162 kEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQ 215
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
460-642 2.63e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 45.03  E-value: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  460 EEKARIHAEtallmeKNKQQKELRERQQEEQKEKLRKEEQE-------QKAKKKQEAEENEITEKQQKAREEME-KKESE 531
Cdd:COG3064    32 EQKAKEEAE------EERLAELEAKRQAEEEAREAKAEAEQraaelaaEAAKKLAEAEKAAAEAEKKAAAEKAKaAKEAE 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  532 QAKKEDKETSAKRGKEITGVKRQSKSEhetsdAKKSVEDRGKRCPTPEIQKKSTGDVPHTSVTGDSGSGKPFKIKGQPES 611
Cdd:COG3064   106 AAAAAEKAAAAAEKEKAEEAKRKAEEE-----AKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAA 180
                         170       180       190
                  ....*....|....*....|....*....|.
gi 410355757  612 GILRTGTFREDTDDTERNKAQREPLTRARSE 642
Cdd:COG3064   181 ALVAAAAAAVEAADTAAAAAAALAAAAAAAA 211
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
463-531 2.95e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 42.19  E-value: 2.95e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 410355757    463 ARIHAETALLMEKNKQQKELRERQQEEQK--EKLRKEE----QEQKAKKKQE--AEENEITEKQQKAREEMEKKESE 531
Cdd:smart00935   15 AGKAAQKQLEKEFKKRQAELEKLEKELQKlkEKLQKDAatlsEAAREKKEKElqKKVQEFQRKQQKLQQDLQKRQQE 91
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
456-613 3.51e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 3.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  456 MLTDEEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKK 535
Cdd:COG3883   126 KIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 410355757  536 EDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKRCPTPEIQKKSTGDVPHTSVTGDSGSGKPFKIKGQPESGI 613
Cdd:COG3883   206 AAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAG 283
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
467-563 3.78e-04

Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.


Pssm-ID: 434558 [Multi-domain]  Cd Length: 154  Bit Score: 42.09  E-value: 3.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   467 AETALLMEKNKQQK-ELRERQQEEQKEKLRKEEQEQKAKKKQEAEeneitEKQQKAREEMEKKESEQAKK--EDKETSAK 543
Cdd:pfam15236   60 AIKKQLEEKERQKKlEEERRRQEEQEEEERLRREREEEQKQFEEE-----RRKQKEKEEAMTRKTQALLQamQKAQELAQ 134
                           90       100
                   ....*....|....*....|
gi 410355757   544 RGKEITGVKRQSKSEHETSD 563
Cdd:pfam15236  135 RLKQEQRIRELAEKGHDTSQ 154
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
431-546 3.80e-04

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 43.15  E-value: 3.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   431 EQQSPQSGKVIPDRSTKPVVFSPTLMLT---DEEKARIHAETALlmEKNKQQKElRERQQEEQKEKLRKEEQEQKAKKKQ 507
Cdd:pfam13904   14 QPEEESSKHRVPSLSLDSSSQSSSLTYArklEGLKLERQPLEAY--ENWLAAKQ-RQRQKELQAQKEEREKEEQEAELRK 90
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 410355757   508 EAEENEITE-KQQKAREEMEKKESEQAKKEDKETSAKRGK 546
Cdd:pfam13904   91 RLAKEKYQEwLQRKARQQTKKREESHKQKAAESASKSLAK 130
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
459-570 3.81e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 3.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  459 DEEKARIHAETALL-MEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKED 537
Cdd:COG1196   238 EAELEELEAELEELeAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
                          90       100       110
                  ....*....|....*....|....*....|...
gi 410355757  538 KETSAKRGKEITGVKRQSKSEHETSDAKKSVED 570
Cdd:COG1196   318 LEELEEELAELEEELEELEEELEELEEELEEAE 350
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
430-539 3.83e-04

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 44.56  E-value: 3.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   430 HEQQSPQSGKVIPDRSTKPVVFSPTLMLTDEEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRKE------EQEQKA 503
Cdd:pfam15709  282 SKYDAEESQVSIDGRSSPTQTFVVTGNMESEEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRLEverkrrEQEEQR 361
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 410355757   504 KKKQEAEE------NEITEKQQKAREEM----EKKESEQAKKEDKE 539
Cdd:pfam15709  362 RLQQEQLEraekmrEELELEQQRRFEEIrlrkQRLEEERQRQEEEE 407
Nop53 pfam07767
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ...
459-547 4.48e-04

Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.


Pssm-ID: 462259 [Multi-domain]  Cd Length: 353  Bit Score: 43.82  E-value: 4.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   459 DEEKARIHAETAL-----LMEKNKQQKELRER----QQEEQKEKLRKE-EQEQKAKKKQEAEENEItEKQQKAREEMEKK 528
Cdd:pfam07767  206 EAEKKRLKEEEKLervleKIAESAATAEAREEkrktKAQRNKEKRRKEeEREAKEEKALKKKLAQL-ERLKEIAKEIAEK 284
                           90
                   ....*....|....*....
gi 410355757   529 ESEQAKKEDKETSAKRGKE 547
Cdd:pfam07767  285 EKEREEKAEARKREKRKKK 303
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
416-583 4.75e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 44.34  E-value: 4.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   416 KLPEEHRIKSESTNHEQQSPQSGKVIPDRSTKPVVFSPTLMltdeEKARIHAETALLMEKNKQQKElRERQQEeqkeKLR 495
Cdd:pfam17380  382 RLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEM----EQIRAEQEEARQREVRRLEEE-RAREME----RVR 452
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   496 KEEQE--QKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKE--DKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDR 571
Cdd:pfam17380  453 LEEQErqQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKilEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEE 532
                          170
                   ....*....|..
gi 410355757   572 GKRCPTPEIQKK 583
Cdd:pfam17380  533 ERRREAEEERRK 544
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
440-566 4.92e-04

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 43.87  E-value: 4.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   440 VIPDRSTKPVvfspTLMLTDEEKARIHAETAL-----------------LMEKNKQQKELR------ERQQEEQKEKLRK 496
Cdd:pfam15558    1 VVPERDRKIA----ALMLARHKEEQRMRELQQqaalaweelrrrdqkrqETLERERRLLLQqsqeqwQAEKEQRKARLGR 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   497 EEQEQKAKKKQEAEENE-----ITEKQQKAREE-MEK----------------KESEQAKKEDKETSAKRGKEITGVKRQ 554
Cdd:pfam15558   77 EERRRADRREKQVIEKEsrwreQAEDQENQRQEkLERarqeaeqrkqcqeqrlKEKEEELQALREQNSLQLQERLEEACH 156
                          170
                   ....*....|..
gi 410355757   555 SKSEHETSDAKK 566
Cdd:pfam15558  157 KRQLKEREEQKK 168
PTZ00121 PTZ00121
MAEBL; Provisional
461-571 5.04e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 5.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  461 EKARIHAETALLMEKNKQQKELRERQQEEQK---EKLRKEEQEQKAKKKQEAEE-NEITEKQQKAREEMEKKESEQAKKE 536
Cdd:PTZ00121 1434 DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKkaeEAKKADEAKKKAEEAKKADEaKKKAEEAKKKADEAKKAAEAKKKAD 1513
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 410355757  537 D--KETSAKRGKEITGVKRQSKSEhetsDAKKSVEDR 571
Cdd:PTZ00121 1514 EakKAEEAKKADEAKKAEEAKKAD----EAKKAEEKK 1546
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
459-573 5.14e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.19  E-value: 5.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   459 DEEKARIHAETALLMEKNKQQKE-LRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKqQKAREEMEKKESEQAKKED 537
Cdd:pfam02463  288 LKLLAKEEEELKSELLKLERRKVdDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEL-EIKREAEEEEEEELEKLQE 366
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 410355757   538 KETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGK 573
Cdd:pfam02463  367 KLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
459-571 5.53e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 5.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  459 DEEKARIHAETALL-MEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKED 537
Cdd:COG1196   259 EAELAELEAELEELrLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
                          90       100       110
                  ....*....|....*....|....*....|....
gi 410355757  538 KETSAKRGKEITGVKRQSKSEHETSDAKKSVEDR 571
Cdd:COG1196   339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
469-544 6.77e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 40.67  E-value: 6.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   469 TALLMEKNKQ----QKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKA---REEMEKKESEQAKKEDKETS 541
Cdd:pfam20492   36 AEELEEERRQaeeeAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEIarlEEEVERKEEEARRLQEELEE 115

                   ...
gi 410355757   542 AKR 544
Cdd:pfam20492  116 ARE 118
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
456-565 7.15e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.57  E-value: 7.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   456 MLTDEEKARihaETALLMEKNKQ---QKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREE------ME 526
Cdd:pfam17380  496 ILEKELEER---KQAMIEEERKRkllEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEErsrleaME 572
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 410355757   527 K--------KESEQAKKEDKETSakrgkEITGVK---RQSKSEHETSDAK 565
Cdd:pfam17380  573 ReremmrqiVESEKARAEYEATT-----PITTIKpiyRPRISEYQPPDVE 617
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
469-583 7.27e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 43.30  E-value: 7.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   469 TALLMEKNKQQKELRERQQEEQKEKlRKEEQEQKA--KKKQEAEENEITEKQQKAREEMEKKESEQAKKEDKETSAKRGK 546
Cdd:TIGR02794   39 QAVLVDPGAVAQQANRIQQQKKPAA-KKEQERQKKleQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEK 117
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 410355757   547 EITGVKRQSKSEHEtsdAKKSVEDRGKRCPTPEIQKK 583
Cdd:TIGR02794  118 QKQAEEAKAKQAAE---AKAKAEAEAERKAKEEAAKQ 151
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
473-539 7.31e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 40.67  E-value: 7.31e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 410355757   473 MEKNKQQKELRERQQEEQKEKLRKE--EQEQKA----KKKQEAEEN--EITEKQQKAREEMEKKEsEQAKKEDKE 539
Cdd:pfam20492    4 AEREKQELEERLKQYEEETKKAQEEleESEETAeeleEERRQAEEEaeRLEQKRQEAEEEKERLE-ESAEMEAEE 77
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
461-536 7.88e-04

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 41.31  E-value: 7.88e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 410355757  461 EKARIHAEtALLMEKNKQQKELRErQQEEQKEKLRKEEQEQKAKKKQEAEEnEITEKQQKAREEMEkKESEQAKKE 536
Cdd:COG0711    44 ERAKEEAE-AALAEYEEKLAEARA-EAAEIIAEARKEAEAIAEEAKAEAEA-EAERIIAQAEAEIE-QERAKALAE 115
PRK11637 PRK11637
AmiB activator; Provisional
467-544 8.46e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 43.14  E-value: 8.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  467 AETALLMEKNKQQKELRERQQEeQKEKLrkeEQEQKAKKKQ----------------EAEENEI--------TEKQQKAR 522
Cdd:PRK11637  184 AQKAELEEKQSQQKTLLYEQQA-QQQKL---EQARNERKKTltglesslqkdqqqlsELRANESrlrdsiarAEREAKAR 259
                          90       100
                  ....*....|....*....|..
gi 410355757  523 EEMEKKESEQAKkeDKETSAKR 544
Cdd:PRK11637  260 AEREAREAARVR--DKQKQAKR 279
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
459-547 8.46e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 8.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   459 DEEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKK---QEAEENEITEKQQKAREEMEKKESEQAKK 535
Cdd:TIGR02168  284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKldeLAEELAELEEKLEELKEELESLEAELEEL 363
                           90
                   ....*....|..
gi 410355757   536 EDKETSAKRGKE 547
Cdd:TIGR02168  364 EAELEELESRLE 375
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
461-560 9.01e-04

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 42.94  E-value: 9.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  461 EKARIHAETALLMEKNKQQKELRERQQEEQKEKLRKEEQeQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKEDKET 540
Cdd:COG2268   204 AEAEAERETEIAIAQANREAEEAELEQEREIETARIAEA-EAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQ 282
                          90       100
                  ....*....|....*....|..
gi 410355757  541 --SAKRGKEITgVKRQSKSEHE 560
Cdd:COG2268   283 leIAEREREIE-LQEKEAEREE 303
PTZ00399 PTZ00399
cysteinyl-tRNA-synthetase; Provisional
474-557 9.02e-04

cysteinyl-tRNA-synthetase; Provisional


Pssm-ID: 240402 [Multi-domain]  Cd Length: 651  Bit Score: 43.48  E-value: 9.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  474 EKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEaeeneitEKQQKAR---EEMEKKESEQAKKEDKE---TSAKRGKE 547
Cdd:PTZ00399  549 DKEELQREKEEKEALKEQKRLRKLKKQEEKKKKEL-------EKLEKAKippAEFFKRQEDKYSAFDETglpTHDADGEE 621
                          90
                  ....*....|
gi 410355757  548 ITgvKRQSKS 557
Cdd:PTZ00399  622 IS--KKERKK 629
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
458-643 9.28e-04

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 43.45  E-value: 9.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   458 TDEEkarihAETALLMEKNKQQKELRERQQEEQKEKLRKEEQE---QKAKKKQEAEENEITEKQQKAREEMEKKESEQAK 534
Cdd:TIGR00927  645 TGEE-----GERPTEAEGENGEESGGEAEQEGETETKGENESEgeiPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEG 719
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   535 KEDKETSAKRGKEITGVKRQSKSEHETSD--AKKSVEDRGKRCPTpEIQKKSTGDVPHTSVTGDSGSGKPFKIKGqpESG 612
Cdd:TIGR00927  720 ETEAEGTEDEGEIETGEEGEEVEDEGEGEaeGKHEVETEGDRKET-EHEGETEAEGKEDEDEGEIQAGEDGEMKG--DEG 796
                          170       180       190
                   ....*....|....*....|....*....|.
gi 410355757   613 ILRTGTFREDTDDTERNKAQREPLTRARSEE 643
Cdd:TIGR00927  797 AEGKVEHEGETEAGEKDEHEGQSETQADDTE 827
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
457-554 1.09e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  457 LTDEEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRK--------EEQEQKAKKKQEAEENEITEKQQKARE-EMEK 527
Cdd:COG1196   218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEEleaelaelEAELEELRLELEELELELEEAQAEEYElLAEL 297
                          90       100
                  ....*....|....*....|....*..
gi 410355757  528 KESEQAKKEDKETSAKRGKEITGVKRQ 554
Cdd:COG1196   298 ARLEQDIARLEERRRELEERLEELEEE 324
PRK12704 PRK12704
phosphodiesterase; Provisional
461-535 1.18e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  461 EKARIHAETALLMEKNK-QQKELRERQQEEQ----KEKLRKEEQE-QKAKKKQEAEENEITEKQqkarEEMEKKESEQAK 534
Cdd:PRK12704   67 HKLRNEFEKELRERRNElQKLEKRLLQKEENldrkLELLEKREEElEKKEKELEQKQQELEKKE----EELEELIEEQLQ 142

                  .
gi 410355757  535 K 535
Cdd:PRK12704  143 E 143
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
912-1085 1.22e-03

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239137 [Multi-domain]  Cd Length: 268  Bit Score: 42.11  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  912 QKHKQLNE-----SIIVALFQGQFKSTVQC-----LTCHKKSRTFEAFMY-LSLPLASTSKCTLQDCLRLFSKEEKLTDN 980
Cdd:cd02672    53 KESCLLCElgylfSTLIQNFTRFLLETISQdqlgtPFSCGTSRNSVSLLYtLSLPLGSTKTSKESTFLQLLKRSLDLEKV 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  981 NRFYCSHCRARRDSLKKIEIWKLPP----VLLVHLKRFSYDGRWKQ-------KLQTSVDFPLENLDLSQYVIGPKNNlK 1049
Cdd:cd02672   133 TKAWCDTCCKYQPLEQTTSIRHLPDilllVLVINLSVTNGEFDDINvvlpsgkVMQNKVSPKAIDHDKLVKNRGQESI-Y 211
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 410355757 1050 KYNLFS-VSNHYGGLDGGHYTA----YCKNAARQRWFKFDD 1085
Cdd:cd02672   212 KYELVGyVCEINDSSRGQHNVVfvikVNEESTHGRWYLFND 252
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
457-572 1.29e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 42.72  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  457 LTDEEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKA--REEMEKKESEQAK 534
Cdd:COG3064    79 LAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAaeAEAAAKAEAEAAR 158
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 410355757  535 KEDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRG 572
Cdd:COG3064   159 AAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTA 196
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
478-557 1.52e-03

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 42.36  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  478 QQKELRERQQE---EQKEKLRKEEQEQKAKKKQEAeeneITEKQQKAREEM-EKKESEQAKKEDK------ETSAKRGKE 547
Cdd:COG0488   239 EQRAERLEQEAaayAKQQKKIAKEEEFIRRFRAKA----RKAKQAQSRIKAlEKLEREEPPRRDKtveirfPPPERLGKK 314
                          90
                  ....*....|
gi 410355757  548 ITGVKRQSKS 557
Cdd:COG0488   315 VLELEGLSKS 324
PTZ00121 PTZ00121
MAEBL; Provisional
461-571 1.67e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  461 EKARiHAETALLMEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEEneiTEKQQKAREEMEKKESEQAKKEDKET 540
Cdd:PTZ00121 1143 EEAR-KAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEE---LRKAEDARKAEAARKAEEERKAEEAR 1218
                          90       100       110
                  ....*....|....*....|....*....|.
gi 410355757  541 SAKRGKEITGVKRQSKSEHETSDAKKSVEDR 571
Cdd:PTZ00121 1219 KAEDAKKAEAVKKAEEAKKDAEEAKKAEEER 1249
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
474-531 1.86e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 39.87  E-value: 1.86e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 410355757   474 EKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESE 531
Cdd:pfam03938   34 ELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQE 91
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
459-574 2.01e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  459 DEEKARIHAETALLMEKnkQQKEL---RERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKK 535
Cdd:COG1196   270 EELRLELEELELELEEA--QAEEYellAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 410355757  536 EDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKR 574
Cdd:COG1196   348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
460-548 2.24e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.12  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  460 EEKARIHAETALLMEKNKQQKE-LRERQQEEQKEKLR--KEEQEQKAKKKQEAE--------ENEITEKQQKAREEMEKK 528
Cdd:PRK00409  544 KEAEKLKEELEEKKEKLQEEEDkLLEEAEKEAQQAIKeaKKEADEIIKELRQLQkggyasvkAHELIEARKRLNKANEKK 623
                          90       100
                  ....*....|....*....|
gi 410355757  529 ESEQAKKEDKETSAKRGKEI 548
Cdd:PRK00409  624 EKKKKKQKEKQEELKVGDEV 643
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
471-574 2.41e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 41.86  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   471 LLMEKNKQQKELRERQQEEQKEKLRKEEQE-----------QKAKKKQEAEENEITEKQ-QKAREEMEKKESE-QAKKED 537
Cdd:pfam15709  378 LELEQQRRFEEIRLRKQRLEEERQRQEEEErkqrlqlqaaqERARQQQEEFRRKLQELQrKKQQEEAERAEAEkQRQKEL 457
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 410355757   538 KETSAKRGKEITG------VKRQSKSEHETSDAKKSVEDRGKR 574
Cdd:pfam15709  458 EMQLAEEQKRLMEmaeeerLEYQRQKQEAEEKARLEAEERRQK 500
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
460-548 2.49e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.44  E-value: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   460 EEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRKEEQ----EQKAKKKQEAEENEIT-EKQQKAREEMEK--KESEQ 532
Cdd:pfam13868  225 EEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFErmlrKQAEDEEIEQEEAEKRrMKRLEHRRELEKqiEEREE 304
                           90
                   ....*....|....*.
gi 410355757   533 AKKEDKETSAKRGKEI 548
Cdd:pfam13868  305 QRAAEREEELEEGERL 320
PTZ00121 PTZ00121
MAEBL; Provisional
474-571 2.68e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  474 EKNKQQKELRERQQEEQK-EKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKEDKETSAKRGKEItgvk 552
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARKaEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEV---- 1187
                          90
                  ....*....|....*....
gi 410355757  553 RQSKSEHETSDAKKSVEDR 571
Cdd:PTZ00121 1188 RKAEELRKAEDARKAEAAR 1206
PTZ00121 PTZ00121
MAEBL; Provisional
419-582 2.68e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  419 EEHRIKSESTNHEQQSPQSGKVIPDRSTKPVVFSPTLMLTDEEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRKEE 498
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  499 QEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKEDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKRCPTP 578
Cdd:PTZ00121 1751 KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDS 1830

                  ....
gi 410355757  579 EIQK 582
Cdd:PTZ00121 1831 AIKE 1834
Caldesmon pfam02029
Caldesmon;
416-578 2.70e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 41.78  E-value: 2.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   416 KLPEEHRIKSESTNHEQQ----SPQSGKVIPDRSTKPVVFSPTLMLTDEEKARIHAETALLMEKNKQQKELRERQQEeqk 491
Cdd:pfam02029  183 KIKKEKKVKYESKVFLDQkrghPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQE--- 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   492 ekLRKEEQEQKAKKKQEAEE-----NEITEKQQKAREEME--KKESEQAKKEDKETSAKRGKEITGVKRQSKSEHETSDA 564
Cdd:pfam02029  260 --KESEEFEKLRQKQQEAELeleelKKKREERRKLLEEEEqrRKQEEAERKLREEEEKRRMKEEIERRRAEAAEKRQKLP 337
                          170
                   ....*....|....*.
gi 410355757   565 KKSVEDRGK--RCPTP 578
Cdd:pfam02029  338 EDSSSEGKKpfKCFSP 353
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
475-569 3.14e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 41.40  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  475 KNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQE--------AEENEITEKQQ---KAREEMEKKESEQAKKEDKEtsaK 543
Cdd:COG2268   198 IRDARIAEAEAERETEIAIAQANREAEEAELEQEreietariAEAEAELAKKKaeeRREAETARAEAEAAYEIAEA---N 274
                          90       100
                  ....*....|....*....|....*.
gi 410355757  544 RGKEITGVKRQSKSEHETSDAKKSVE 569
Cdd:COG2268   275 AEREVQRQLEIAEREREIELQEKEAE 300
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
459-568 3.28e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 3.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   459 DEEKARIHAETALLMEKNKQQKELRERQQEEQKEKL-------RKEEQEQKAKKKQEAEENEItekqqkAREEMEKKESE 531
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYalaneisRLEQQKQILRERLANLERQL------EELEAQLEELE 329
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 410355757   532 QAKKEDKETSAKRGKEITGVKRQSKSEHETSDAKKSV 568
Cdd:TIGR02168  330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
459-544 3.38e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 3.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   459 DEEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRKEEQEQ---KAKKKQEAEENEITEKQQKAREEMEKKESEQAKK 535
Cdd:pfam13868   39 KEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQieeREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEA 118

                   ....*....
gi 410355757   536 EDKETSAKR 544
Cdd:pfam13868  119 EEKLEKQRQ 127
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
199-310 3.58e-03

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 38.21  E-value: 3.58e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757    199 LIIMDARRMQDYQDSCILHSLSVPEEAISPGVTASWieaHLPDDSKDTWKKRGNVEYVVLLDwfssakdlqiGTTLRSlk 278
Cdd:smart00450    5 VVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELD---ILEFEELLKRLGLDKDKPVVVYC----------RSGNRS-- 69
                            90       100       110
                    ....*....|....*....|....*....|..
gi 410355757    279 dALFKWESKTVLRNEPLVLEGGYENWLLCYPQ 310
Cdd:smart00450   70 -AKAAWLLRELGFKNVYLLDGGYKEWSAAGPP 100
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
445-612 3.75e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 41.14  E-value: 3.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   445 STKPVVfspTLMLTDEEKARIHAETALLMEKNKQQKELRERQ---QEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKA 521
Cdd:pfam05262  178 SDKKVV---EALREDNEKGVNFRRDMTDLKERESQEDAKRAQqlkEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQ 254
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   522 REE---------MEKKESEQAKKEDKETSAKRGKEITGVKRQSK--SEHETSDAKKSVEDRGKRcptpEIQKKSTGDVPH 590
Cdd:pfam05262  255 QEAknlpkpadtSSPKEDKQVAENQKREIEKAQIEIKKNDEEALkaKDHKAFDLKQESKASEKE----AEDKELEAQKKR 330
                          170       180
                   ....*....|....*....|..
gi 410355757   591 TSVTGDSGSGKPfKIKGQPESG 612
Cdd:pfam05262  331 EPVAEDLQKTKP-QVEAQPTSL 351
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
456-584 3.79e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.50  E-value: 3.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   456 MLTDEEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRKEEQEQKA-------KKKQEAEENEITEKQQKAREEMEKK 528
Cdd:pfam02463  162 AAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKAleyyqlkEKLELEEEYLLYLDYLKLNEERIDL 241
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 410355757   529 ESEQA---KKEDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKRCPTPEIQKKS 584
Cdd:pfam02463  242 LQELLrdeQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKS 300
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
463-571 3.85e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 3.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  463 ARIHAETALLMEKNKQQKELRE-RQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKEDK--E 539
Cdd:PRK02224  592 ERIRTLLAAIADAEDEIERLREkREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKldE 671
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 410355757  540 TSAKRG---KEITGVKRQSKSEHETSDAKKSVEDR 571
Cdd:PRK02224  672 LREERDdlqAEIGAVENELEELEELRERREALENR 706
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
459-574 3.92e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.50  E-value: 3.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   459 DEEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKEDK 538
Cdd:pfam02463  751 EEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKI 830
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 410355757   539 ETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKR 574
Cdd:pfam02463  831 KEEELEELALELKEEQKLEKLAEEELERLEEEITKE 866
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
466-538 4.45e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 4.45e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 410355757  466 HAETALlMEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQ---KAREEMEKKESEQAKKEDK 538
Cdd:COG3883    13 FADPQI-QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAeidKLQAEIAEAEAEIEERREE 87
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
474-536 4.46e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 38.57  E-value: 4.46e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 410355757  474 EKNKQQKELRERQQEEQKEKLRKEEQE--QKAKKKQEAEENEITEkqqKAREEMEKKEsEQAKKE 536
Cdd:cd06503    43 EKAKEEAEELLAEYEEKLAEARAEAQEiiEEARKEAEKIKEEILA---EAKEEAERIL-EQAKAE 103
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
460-613 4.53e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 4.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  460 EEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRKeeQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKEDKE 539
Cdd:COG3883   140 ADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ--QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 410355757  540 TSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKRCPTPEIQKKSTGDVPHTSVTGDSGSGKPFKIKGQPESGI 613
Cdd:COG3883   218 AAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGG 291
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
474-565 4.64e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.11  E-value: 4.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   474 EKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESE-QAKKEDKETSAKrgKEITGVK 552
Cdd:pfam02463  263 EEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEkEKKKAEKELKKE--KEEIEEL 340
                           90
                   ....*....|...
gi 410355757   553 RQSKSEHETSDAK 565
Cdd:pfam02463  341 EKELKELEIKREA 353
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
459-542 5.10e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 5.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  459 DEEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKEDK 538
Cdd:COG4942   163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242

                  ....
gi 410355757  539 ETSA 542
Cdd:COG4942   243 TPAA 246
PRK12704 PRK12704
phosphodiesterase; Provisional
460-567 5.22e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 5.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  460 EEKARihaetALLMEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKEDKE 539
Cdd:PRK12704   37 EEEAK-----RILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEE 111
                          90       100
                  ....*....|....*....|....*...
gi 410355757  540 TSAKRgKEITGVKRQSKSEHETSDAKKS 567
Cdd:PRK12704  112 LEKKE-KELEQKQQELEKKEEELEELIE 138
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
404-634 5.33e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 41.19  E-value: 5.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  404 VPQIDRTKKPAVKLPEEHRIKSESTNHEQQSPQSGKVIPDRSTKPVVFSPTLMLTDE-------EKARIHAETALLMEKN 476
Cdd:PTZ00108 1046 VRFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSYDYLLSMPIWSLTKEkveklnaELEKKEKELEKLKNTT 1125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  477 KQQ------KELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEiTEKQQKAREEMEKKESEqakkEDKETSAKRGKEITG 550
Cdd:PTZ00108 1126 PKDmwledlDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASK-LRKPKLKKKEKKKKKSS----ADKSKKASVVGNSKR 1200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  551 VKRQSKSEHETSDAKKSVEDRGKRCPTPEIQKKSTGDVP------------HTSVTGDSGSGKPFKIKGQPESGILRTGT 618
Cdd:PTZ00108 1201 VDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSvkrlkskknnssKSSEDNDEFSSDDLSKEGKPKNAPKRVSA 1280
                         250
                  ....*....|....*.
gi 410355757  619 FREDTDDTERNKAQRE 634
Cdd:PTZ00108 1281 VQYSPPPPSKRPDGES 1296
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
777-793 6.25e-03

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 40.17  E-value: 6.25e-03
                          10
                  ....*....|....*..
gi 410355757  777 TGLRNLGNTCYMNSILQ 793
Cdd:cd02666     2 AGLDNIGNTCYLNSLLQ 18
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
460-538 7.00e-03

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 39.27  E-value: 7.00e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 410355757   460 EEKARIHAEtallmeknkqqKELRERQQEEQKEKlRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEqAKKEDK 538
Cdd:pfam15927    6 EEEERLRAE-----------EEEAERLEEERREE-EEEERLAAEQDRRAEELEELKHLLEERKEALEKLRAE-AREEAE 71
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
461-567 7.27e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 40.32  E-value: 7.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  461 EKARIHAET--ALLMEKNKQQKELR----ERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAK 534
Cdd:PRK05035  434 AKAEIRAIEqeKKKAEEAKARFEARqarlEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGAR 513
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 410355757  535 KEDKETSAKRgKEITGVKRQSKSEHETS---DAKKS 567
Cdd:PRK05035  514 PDNSAVIAAR-EARKAQARARQAEKQAAaaaDPKKA 548
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
477-556 7.81e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.49  E-value: 7.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   477 KQQKELRERQQEEQKEKLRKEE-QEQKAKKKQEAEENEITEKQQKARE-EMEKKESEQAKKEdkETSAKRGKEITGVKRQ 554
Cdd:pfam17380  279 QHQKAVSERQQQEKFEKMEQERlRQEKEEKAREVERRRKLEEAEKARQaEMDRQAAIYAEQE--RMAMERERELERIRQE 356

                   ..
gi 410355757   555 SK 556
Cdd:pfam17380  357 ER 358
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
460-574 8.00e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 40.02  E-value: 8.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  460 EEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRKEEQEQKAKK-KQEAEENEITEKQQKAREEME-KKESEQAKKED 537
Cdd:COG3064    14 AQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREaKAEAEQRAAELAAEAAKKLAEaEKAAAEAEKKA 93
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 410355757  538 KETSAKRGKEitgVKRQSKSEHETSDAKKSVEDRGKR 574
Cdd:COG3064    94 AAEKAKAAKE---AEAAAAAEKAAAAAEKEKAEEAKR 127
PDCD7 pfam16021
Programmed cell death protein 7;
478-554 8.16e-03

Programmed cell death protein 7;


Pssm-ID: 464979 [Multi-domain]  Cd Length: 305  Bit Score: 39.71  E-value: 8.16e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 410355757   478 QQKELRERQQEEQKEKLRKEEQEQKAKKkqEAEENEITEKQQKaREEMEKKESEQAKKEDKETSAKRGKEITgVKRQ 554
Cdd:pfam16021   75 QKKRLRRKRRKEERKEEKKEEQERRAER--EAKIDKWRRKQIQ-EVEEKKRERELKLAADAVLSEVRKKQAD-AKRM 147
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
457-536 8.17e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 38.22  E-value: 8.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  457 LTDEEKARIHAETAllmeKNKQQKELRERQQEEQK--EKLRKEEQEQKAKKKQEAEEnEITEKQQKAREEMEkKESEQAK 534
Cdd:PRK05759   44 LAAAERAKKELELA----QAKYEAQLAEARAEAAEiiEQAKKRAAQIIEEAKAEAEA-EAARIKAQAQAEIE-QERKRAR 117

                  ..
gi 410355757  535 KE 536
Cdd:PRK05759  118 EE 119
TAF4 pfam05236
Transcription initiation factor TFIID component TAF4 family; This region of similarity is ...
472-521 8.26e-03

Transcription initiation factor TFIID component TAF4 family; This region of similarity is found in Transcription initiation factor TFIID component TAF4.


Pssm-ID: 461598 [Multi-domain]  Cd Length: 264  Bit Score: 39.56  E-value: 8.26e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   472 LMEKNKQQKELRERQQEEQKEKLRKE-------EQEQKAKKKQEAEE---NEITEKQQKA 521
Cdd:pfam05236  116 LKFLAQKDKEEEERRVAEEREGLLKAaksrsnqEDPEQLKLKQEAKEmqkEEDEKMRHRA 175
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
471-554 8.37e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.90  E-value: 8.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   471 LLMEKNKQQKELRERQQEEQKEKL-------RKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKEDKEtsAK 543
Cdd:pfam13868  210 LYQEEQERKERQKEREEAEKKARQrqelqqaREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRR--MK 287
                           90
                   ....*....|.
gi 410355757   544 RGKEITGVKRQ 554
Cdd:pfam13868  288 RLEHRRELEKQ 298
CBP4 pfam07960
CBP4; The CBP4 in S. cerevisiae is essential for the expression and activity of ...
458-548 8.87e-03

CBP4; The CBP4 in S. cerevisiae is essential for the expression and activity of ubiquinol-cytochrome c reductase. This family describes fungal and human proteins..


Pssm-ID: 369619  Cd Length: 125  Bit Score: 37.64  E-value: 8.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   458 TDEEK-ARIHAETALLMEKNKqqkELRERQQEEQKEKLRKEEQEQ----KAKKKQEAEENEiTEKQQKAREEMEKKESEQ 532
Cdd:pfam07960   29 TDEQLiASFSPELRAQYERNR---ELRQKEQQELMKIVKETSKSNdpiwKTGPIKSPWEKN-ADPKLVDREQFQKAKAEE 104
                           90
                   ....*....|....*.
gi 410355757   533 AKKEDKETSAKRGKEI 548
Cdd:pfam07960  105 VQKEELERIRAELEEI 120
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
461-571 9.12e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 9.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757   461 EKARIHAETAL-----LMEKNKQQKELRERQQEEQKEKLRKEEQE-QKAKKKQEAEENEITEKQQKAREEMEKK-ESEQA 533
Cdd:TIGR02168  697 EKALAELRKELeeleeELEQLRKELEELSRQISALRKDLARLEAEvEQLEERIAQLSKELTELEAEIEELEERLeEAEEE 776
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 410355757   534 KKEDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDR 571
Cdd:TIGR02168  777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
460-547 9.22e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 9.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  460 EEKARIHAETALLMEKNKQQKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAREEMEKKESEQAKKEDKE 539
Cdd:COG1196   667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746

                  ....*...
gi 410355757  540 TSAKRGKE 547
Cdd:COG1196   747 LLEEEALE 754
PTZ00121 PTZ00121
MAEBL; Provisional
461-584 9.73e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 9.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410355757  461 EKARiHAETALLMEKNKQQKELR----ERQQEEQK--EKLRKEEQE-QKAKKKQEAEENEITE--------------KQQ 519
Cdd:PTZ00121 1197 EDAR-KAEAARKAEEERKAEEARkaedAKKAEAVKkaEEAKKDAEEaKKAEEERNNEEIRKFEearmahfarrqaaiKAE 1275
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 410355757  520 KAREEMEKKESEQAKKEDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKRcpTPEIQKKS 584
Cdd:PTZ00121 1276 EARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKK--ADAAKKKA 1338
 
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.
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